{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T13:24:19Z","timestamp":1791206659084,"version":"4.1.0"},"reference-count":327,"publisher":"Elsevier BV","issue":"11","license":[{"start":{"date-parts":[[2013,11,1]],"date-time":"2013-11-01T00:00:00Z","timestamp":1383264000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2014,11,1]],"date-time":"2014-11-01T00:00:00Z","timestamp":1414800000000},"content-version":"vor","delay-in-days":365,"URL":"https:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"crossref","award":["FOR855"],"award-info":[{"award-number":["FOR855"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100002342","name":"Finnish Academy of Science","doi-asserted-by":"crossref","award":["128600"],"award-info":[{"award-number":["128600"]}],"id":[{"id":"10.13039\/501100002342","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100011102","name":"European Union Seventh Framework Programme","doi-asserted-by":"crossref","award":["FP7\/2007\u20132013"],"award-info":[{"award-number":["FP7\/2007\u20132013"]}],"id":[{"id":"10.13039\/100011102","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100011102","name":"European Union Seventh Framework Programme","doi-asserted-by":"crossref","award":["n\u00b0281234"],"award-info":[{"award-number":["n\u00b0281234"]}],"id":[{"id":"10.13039\/100011102","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease"],"published-print":{"date-parts":[[2013,11]]},"DOI":"10.1016\/j.bbadis.2013.01.019","type":"journal-article","created":{"date-parts":[[2013,2,8]],"date-time":"2013-02-08T23:11:40Z","timestamp":1360365100000},"page":"1866-1881","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":122,"title":["Cell biology and function of neuronal ceroid lipofuscinosis-related proteins"],"prefix":"10.1016","volume":"1832","author":[{"given":"Katrin","family":"Kollmann","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kristiina","family":"Uusi-Rauva","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Enzo","family":"Scifo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jaana","family":"Tyynel\u00e4","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anu","family":"Jalanko","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thomas","family":"Braulke","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbadis.2013.01.019_bb0005","doi-asserted-by":"crossref","first-page":"684","DOI":"10.1016\/j.bbamcr.2008.12.001","article-title":"Lysosomal disorders: from storage to cellular damage","volume":"1793","author":"Ballabio","year":"2009","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbadis.2013.01.019_bb0010","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1007\/s10048-005-0218-3","article-title":"Correlations between genotype, ultrastructural morphology and clinical phenotype in the neuronal ceroid lipofuscinoses","volume":"6","author":"Mole","year":"2005","journal-title":"Neurogenetics"},{"issue":"Suppl. A","key":"10.1016\/j.bbadis.2013.01.019_bb0015","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1053\/ejpn.2000.0454","article-title":"Clinical and neuroradiological diagnostic aspects of neuronal ceroid lipofuscinoses disorders","volume":"5","author":"Santavuori","year":"2001","journal-title":"Eur. J. Paediatr. Neurol."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0020","doi-asserted-by":"crossref","first-page":"79","DOI":"10.2217\/clp.11.70","article-title":"The juvenile Batten disease protein, CLN3, and its role in regulating anterograde and retrograde post-Golgi trafficking","volume":"7","author":"Cotman","year":"2012","journal-title":"Clin. Lipidol."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0025","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1007\/s00018-010-0468-6","article-title":"Interactions of the proteins of neuronal ceroid lipofuscinosis: clues to function","volume":"68","author":"Getty","year":"2011","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0030","doi-asserted-by":"crossref","first-page":"697","DOI":"10.1016\/j.bbamcr.2008.11.004","article-title":"Neuronal ceroid lipofuscinoses","volume":"1793","author":"Jalanko","year":"2009","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbadis.2013.01.019_bb0035","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1139\/O09-124","article-title":"CSPalpha: the neuroprotective J protein","volume":"88","author":"Johnson","year":"2010","journal-title":"Biochem. Cell Biol."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0040","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1016\/j.brainresbull.2012.03.003","article-title":"Mouse models of neuronal ceroid lipofuscinoses: useful pre-clinical tools to delineate disease pathophysiology and validate therapeutics","volume":"88","author":"Shacka","year":"2012","journal-title":"Brain Res. Bull."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0045","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1212\/WNL.0b013e31825f0547","article-title":"New nomenclature and classification scheme for the neuronal ceroid lipofuscinoses","volume":"79","author":"Williams","year":"2012","journal-title":"Neurology"},{"key":"10.1016\/j.bbadis.2013.01.019_bb0050","doi-asserted-by":"crossref","first-page":"584","DOI":"10.1038\/376584a0","article-title":"Mutations in the palmitoyl protein thioesterase gene causing infantile neuronal ceroid lipofuscinosis","volume":"376","author":"Vesa","year":"1995","journal-title":"Nature"},{"key":"10.1016\/j.bbadis.2013.01.019_bb0055","doi-asserted-by":"crossref","first-page":"22566","DOI":"10.1016\/S0021-9258(18)41567-0","article-title":"Purification and properties of a palmitoyl-protein thioesterase that cleaves palmitate from H-Ras","volume":"268","author":"Camp","year":"1993","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0060","doi-asserted-by":"crossref","first-page":"23212","DOI":"10.1016\/S0021-9258(17)31641-1","article-title":"Molecular cloning and expression of palmitoyl-protein thioesterase","volume":"269","author":"Camp","year":"1994","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0065","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0165-3806(99)00115-7","article-title":"Developmental expression of palmitoyl protein thioesterase in normal mice","volume":"118","author":"Isosomppi","year":"1999","journal-title":"Brain Res. Dev. Brain Res."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0070","doi-asserted-by":"crossref","first-page":"724","DOI":"10.1101\/gr.8.7.724","article-title":"Mouse palmitoyl protein thioesterase: gene structure and expression of cDNA","volume":"8","author":"Salonen","year":"1998","journal-title":"Genome Res."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0075","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1006\/geno.1996.0292","article-title":"cDNA and genomic cloning of human palmitoyl-protein thioesterase (PPT), the enzyme defective in infantile neuronal ceroid lipofuscinosis","volume":"34","author":"Schriner","year":"1996","journal-title":"Genomics"},{"key":"10.1016\/j.bbadis.2013.01.019_bb0080","doi-asserted-by":"crossref","first-page":"406","DOI":"10.1002\/1096-9861(20001023)426:3<406::AID-CNE5>3.0.CO;2-5","article-title":"CLN-1 and CLN-5, genes for infantile and variant late infantile neuronal ceroid lipofuscinoses, are expressed in the embryonic human brain","volume":"426","author":"Heinonen","year":"2000","journal-title":"J. Comp. Neurol."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0085","doi-asserted-by":"crossref","first-page":"290","DOI":"10.1006\/mgme.1999.2839","article-title":"The expression of palmitoyl-protein thioesterase is developmentally regulated in neural tissues but not in nonneural tissues","volume":"66","author":"Suopanki","year":"1999","journal-title":"Mol. Genet. Metab."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0090","doi-asserted-by":"crossref","first-page":"4573","DOI":"10.1073\/pnas.080508097","article-title":"The crystal structure of palmitoyl protein thioesterase 1 and the molecular basis of infantile neuronal ceroid lipofuscinosis","volume":"97","author":"Bellizzi","year":"2000","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0095","doi-asserted-by":"crossref","first-page":"1431","DOI":"10.1093\/hmg\/10.13.1431","article-title":"Biochemical analysis of mutations in palmitoyl-protein thioesterase causing infantile and late-onset forms of neuronal ceroid lipofuscinosis","volume":"10","author":"Das","year":"2001","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0100","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1186\/1471-2121-8-22","article-title":"Glycosylation, transport, and complex formation of palmitoyl protein thioesterase 1 (PPT1)\u2014distinct characteristics in neurons","volume":"8","author":"Lyly","year":"2007","journal-title":"BMC Cell Biol."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0105","doi-asserted-by":"crossref","first-page":"524","DOI":"10.1016\/j.braindev.2009.08.010","article-title":"Structural basis of neuronal ceroid lipofuscinosis 1","volume":"32","author":"Ohno","year":"2010","journal-title":"Brain Dev."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0110","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1002\/(SICI)1097-4547(20000101)59:1<32::AID-JNR5>3.0.CO;2-A","article-title":"In vitro depalmitoylation of neurospecific peptides: implication for infantile neuronal ceroid lipofuscinosis","volume":"59","author":"Cho","year":"2000","journal-title":"J. Neurosci. Res."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0115","doi-asserted-by":"crossref","first-page":"15831","DOI":"10.1074\/jbc.271.26.15831","article-title":"Lysosomal targeting of palmitoyl-protein thioesterase","volume":"271","author":"Verkruyse","year":"1996","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0120","doi-asserted-by":"crossref","first-page":"368","DOI":"10.1002\/cne.10492","article-title":"Palmitoyl protein thioesterase 1 is targeted to the axons in neurons","volume":"455","author":"Ahtiainen","year":"2003","journal-title":"J. Comp. Neurol."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0125","doi-asserted-by":"crossref","first-page":"5240","DOI":"10.1002\/j.1460-2075.1996.tb00909.x","article-title":"Human palmitoyl protein thioesterase: evidence for lysosomal targeting of the enzyme and disturbed cellular routing in infantile neuronal ceroid lipofuscinosis","volume":"15","author":"Hellsten","year":"1996","journal-title":"EMBO J."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0130","doi-asserted-by":"crossref","first-page":"1520","DOI":"10.1002\/pmic.200401054","article-title":"The human brain mannose 6-phosphate glycoproteome: a complex mixture composed of multiple isoforms of many soluble lysosomal proteins","volume":"5","author":"Sleat","year":"2005","journal-title":"Proteomics"},{"key":"10.1016\/j.bbadis.2013.01.019_bb0135","doi-asserted-by":"crossref","first-page":"19191","DOI":"10.1074\/jbc.271.32.19191","article-title":"Rat brain contains high levels of mannose-6-phosphorylated glycoproteins including lysosomal enzymes and palmitoyl-protein thioesterase, an enzyme implicated in infantile neuronal lipofuscinosis","volume":"271","author":"Sleat","year":"1996","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0140","doi-asserted-by":"crossref","first-page":"208","DOI":"10.1002\/jnr.20549","article-title":"Differential regulation of ceramide in lipid-rich microdomains (rafts): antagonistic role of palmitoyl:protein thioesterase and neutral sphingomyelinase 2","volume":"81","author":"Goswami","year":"2005","journal-title":"J. Neurosci. Res."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0145","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1006\/mgme.2000.2961","article-title":"Expression of palmitoyl protein thioesterase in neurons","volume":"69","author":"Heinonen","year":"2000","journal-title":"Mol. Genet. Metab."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0150","doi-asserted-by":"crossref","first-page":"3075","DOI":"10.1172\/JCI33482","article-title":"Palmitoyl protein thioesterase-1 deficiency impairs synaptic vesicle recycling at nerve terminals, contributing to neuropathology in humans and mice","volume":"118","author":"Kim","year":"2008","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0155","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1093\/hmg\/10.1.69","article-title":"Palmitoyl protein thioesterase (PPT) localizes into synaptosomes and synaptic vesicles in neurons: implications for infantile neuronal ceroid lipofuscinosis (INCL)","volume":"10","author":"Lehtovirta","year":"2001","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0160","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1006\/nbdi.2002.0503","article-title":"Status epilepticus induces changes in the expression and localization of endogenous palmitoyl-protein thioesterase 1","volume":"10","author":"Suopanki","year":"2002","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0165","doi-asserted-by":"crossref","first-page":"314","DOI":"10.1016\/j.nbd.2005.03.012","article-title":"Progressively reduced synaptic vesicle pool size in cultured neurons derived from neuronal ceroid lipofuscinosis-1 knockout mice","volume":"20","author":"Virmani","year":"2005","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0170","doi-asserted-by":"crossref","first-page":"4066","DOI":"10.1093\/hmg\/ddp355","article-title":"Molecular correlates of axonal and synaptic pathology in mouse models of Batten disease","volume":"18","author":"Kielar","year":"2009","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0175","doi-asserted-by":"crossref","first-page":"367","DOI":"10.1002\/jnr.22763","article-title":"Altered glutamate receptor function in the cerebellum of the Ppt1(\u2212\/\u2212) mouse, a murine model of infantile neuronal ceroid lipofuscinosis","volume":"90","author":"Finn","year":"2012","journal-title":"J. Neurosci. Res."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0180","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1016\/j.nbd.2007.06.012","article-title":"Palmitoyl protein thioesterase 1 (Ppt1)-deficient mouse neurons show alterations in cholesterol metabolism and calcium homeostasis prior to synaptic dysfunction","volume":"28","author":"Ahtiainen","year":"2007","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0185","doi-asserted-by":"crossref","first-page":"2379","DOI":"10.1534\/genetics.105.053306","article-title":"Palmitoyl-protein thioesterase 1 deficiency in Drosophila melanogaster causes accumulation of abnormal storage material and reduced life span","volume":"172","author":"Hickey","year":"2006","journal-title":"Genetics"},{"key":"10.1016\/j.bbadis.2013.01.019_bb0190","doi-asserted-by":"crossref","first-page":"e14402","DOI":"10.1371\/journal.pone.0014402","article-title":"The Batten disease Palmitoyl Protein Thioesterase 1 gene regulates neural specification and axon connectivity during Drosophila embryonic development","volume":"5","author":"Chu-LaGraff","year":"2010","journal-title":"PLoS One"},{"key":"10.1016\/j.bbadis.2013.01.019_bb0195","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1534\/genetics.106.067983","article-title":"Genetic modifiers of Drosophila palmitoyl-protein thioesterase 1-induced degeneration","volume":"176","author":"Buff","year":"2007","journal-title":"Genetics"},{"key":"10.1016\/j.bbadis.2013.01.019_bb0200","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1186\/1471-2202-4-30","article-title":"An over-expression system for characterizing Ppt1 function in Drosophila","volume":"4","author":"Korey","year":"2003","journal-title":"BMC Neurosci."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0205","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1016\/j.nbd.2010.02.010","article-title":"Identifying cellular pathways modulated by Drosophila palmitoyl-protein thioesterase 1 function","volume":"40","author":"Saja","year":"2010","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0210","doi-asserted-by":"crossref","first-page":"10703","DOI":"10.1523\/JNEUROSCI.2061-10.2010","article-title":"Autophagy-dependent rhodopsin degradation prevents retinal degeneration in Drosophila","volume":"30","author":"Midorikawa","year":"2010","journal-title":"J. Neurosci."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0215","doi-asserted-by":"crossref","first-page":"302","DOI":"10.1128\/EC.3.2.302-310.2004","article-title":"pdf1, a palmitoyl protein thioesterase 1 Ortholog in Schizosaccharomyces pombe: a yeast model of infantile Batten disease","volume":"3","author":"Cho","year":"2004","journal-title":"Eukaryot. Cell"},{"key":"10.1016\/j.bbadis.2013.01.019_bb0220","doi-asserted-by":"crossref","first-page":"5851","DOI":"10.1046\/j.0014-2956.2001.02530.x","article-title":"Elevated lysosomal pH in neuronal ceroid lipofuscinoses (NCLs)","volume":"268","author":"Holopainen","year":"2001","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0225","doi-asserted-by":"crossref","first-page":"1540","DOI":"10.1016\/j.yexcr.2006.01.034","article-title":"Palmitoyl protein thioesterase 1 (PPT1) deficiency causes endocytic defects connected to abnormal saposin processing","volume":"312","author":"Ahtiainen","year":"2006","journal-title":"Exp. Cell Res."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0230","doi-asserted-by":"crossref","first-page":"1478","DOI":"10.1046\/j.1471-4159.2000.0741478.x","article-title":"Palmitoyl protein thioesterase 1 protects against apoptosis mediated by Ras\u2013Akt\u2013caspase pathway in neuroblastoma cells","volume":"74","author":"Cho","year":"2000","journal-title":"J. Neurochem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0235","doi-asserted-by":"crossref","first-page":"234","DOI":"10.1002\/1097-4547(20001015)62:2<234::AID-JNR8>3.0.CO;2-8","article-title":"Antisense palmitoyl protein thioesterase 1 (PPT1) treatment inhibits PPT1 activity and increases cell death in LA-N-5 neuroblastoma cells","volume":"62","author":"Cho","year":"2000","journal-title":"J. Neurosci. Res."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0240","doi-asserted-by":"crossref","first-page":"478","DOI":"10.1038\/86554","article-title":"Lysosomal ceroid depletion by drugs: therapeutic implications for a hereditary neurodegenerative disease of childhood","volume":"7","author":"Zhang","year":"2001","journal-title":"Nat. Med."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0245","doi-asserted-by":"crossref","first-page":"1826","DOI":"10.1093\/hmg\/ddl105","article-title":"Endoplasmic reticulum stress-induced caspase-4 activation mediates apoptosis and neurodegeneration in INCL","volume":"15","author":"Kim","year":"2006","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0250","doi-asserted-by":"crossref","first-page":"1580","DOI":"10.1093\/hmg\/ddl078","article-title":"Palmitoyl-protein thioesterase-1 deficiency leads to the activation of caspase-9 and contributes to rapid neurodegeneration in INCL","volume":"15","author":"Kim","year":"2006","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0255","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1093\/hmg\/ddi451","article-title":"Palmitoyl-protein thioesterase-1 deficiency mediates the activation of the unfolded protein response and neuronal apoptosis in INCL","volume":"15","author":"Zhang","year":"2006","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0260","doi-asserted-by":"crossref","first-page":"1250","DOI":"10.1016\/j.bbamcr.2009.03.007","article-title":"Palmitoyl protein thioesterase 1 modulates tumor necrosis factor alpha-induced apoptosis","volume":"1793","author":"Tardy","year":"2009","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbadis.2013.01.019_bb0265","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1006\/mgme.1999.2811","article-title":"Anomalies of mitochondrial ATP synthase regulation in four different types of neuronal ceroid lipofuscinosis","volume":"66","author":"Das","year":"1999","journal-title":"Mol. Genet. Metab."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0270","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1016\/j.bbrc.2011.11.016","article-title":"Involvement of the mitochondrial compartment in human NCL fibroblasts","volume":"416","author":"Pezzini","year":"2011","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0275","doi-asserted-by":"crossref","first-page":"836","DOI":"10.1002\/jnr.20403","article-title":"Identification and characterization of Caenorhabditis elegans palmitoyl protein thioesterase1","volume":"79","author":"Porter","year":"2005","journal-title":"J. Neurosci. Res."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0280","doi-asserted-by":"crossref","first-page":"1111","DOI":"10.1093\/hmg\/ddq555","article-title":"Disruption of adaptive energy metabolism and elevated ribosomal p-S6K1 levels contribute to INCL pathogenesis: partial rescue by resveratrol","volume":"20","author":"Wei","year":"2011","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0285","doi-asserted-by":"crossref","first-page":"1406","DOI":"10.1093\/hmg\/ddn028","article-title":"Deficiency of the INCL protein Ppt1 results in changes in ectopic F1-ATP synthase and altered cholesterol metabolism","volume":"17","author":"Lyly","year":"2008","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0290","doi-asserted-by":"crossref","first-page":"1051","DOI":"10.1046\/j.1471-4159.2003.01602.x","article-title":"Analysis of phospholipid molecular species in brains from patients with infantile and juvenile neuronal-ceroid lipofuscinosis using liquid chromatography\u2013electrospray ionization mass spectrometry","volume":"84","author":"K\u00e4kel\u00e4","year":"2003","journal-title":"J. Neurochem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0295","first-page":"5925","article-title":"Ecto-F(1)-ATPase: a moonlighting protein complex and an unexpected apoA-I receptor","volume":"16","author":"Vantourout","year":"2010","journal-title":"World J. Gastroenterol."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0300","doi-asserted-by":"crossref","first-page":"1802","DOI":"10.1126\/science.277.5333.1802","article-title":"Association of mutations in a lysosomal protein with classical late-infantile neuronal ceroid lipofuscinosis","volume":"277","author":"Sleat","year":"1997","journal-title":"Science"},{"key":"10.1016\/j.bbadis.2013.01.019_bb0305","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1007\/s00441-011-1252-0","article-title":"Developmental study of tripeptidyl peptidase I activity in the mouse central nervous system and peripheral organs","volume":"346","author":"Dimitrova","year":"2011","journal-title":"Cell Tissue Res."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0310","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1679\/aohc.65.219","article-title":"The expression of tripeptidyl peptidase I in various tissues of rats and mice","volume":"65","author":"Koike","year":"2002","journal-title":"Arch. Histol. Cytol."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0315","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1007\/s004010000321","article-title":"Distribution and development of CLN2 protein, the late-infantile neuronal ceroid lipofuscinosis gene product","volume":"102","author":"Kurachi","year":"2001","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0320","doi-asserted-by":"crossref","first-page":"190","DOI":"10.1006\/mgme.2000.3071","article-title":"Developmental changes in the expression of neuronal ceroid lipofuscinoses-linked proteins","volume":"71","author":"Suopanki","year":"2000","journal-title":"Mol. Genet. Metab."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0325","doi-asserted-by":"crossref","first-page":"2249","DOI":"10.1074\/jbc.M008562200","article-title":"The human CLN2 protein\/tripeptidyl-peptidase I is a serine protease that autoactivates at acidic pH","volume":"276","author":"Lin","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0330","doi-asserted-by":"crossref","first-page":"2573","DOI":"10.1046\/j.1471-4159.1999.0722573.x","article-title":"A lysosomal proteinase, the late infantile neuronal ceroid lipofuscinosis gene (CLN2) product, is essential for degradation of a hydrophobic protein, the subunit c of ATP synthase","volume":"72","author":"Ezaki","year":"1999","journal-title":"J. Neurochem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0335","doi-asserted-by":"crossref","first-page":"7135","DOI":"10.1074\/jbc.M211872200","article-title":"Biosynthesis, glycosylation, and enzymatic processing in vivo of human tripeptidyl-peptidase I","volume":"278","author":"Golabek","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0340","doi-asserted-by":"crossref","first-page":"31058","DOI":"10.1074\/jbc.M400700200","article-title":"Maturation of human tripeptidyl-peptidase I in vitro","volume":"279","author":"Golabek","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0345","doi-asserted-by":"crossref","first-page":"3985","DOI":"10.1074\/jbc.M806943200","article-title":"Crystal structure and autoactivation pathway of the precursor form of human tripeptidyl-peptidase 1, the enzyme deficient in late infantile ceroid lipofuscinosis","volume":"284","author":"Guhaniyogi","year":"2009","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0350","doi-asserted-by":"crossref","first-page":"1383","DOI":"10.1016\/j.febslet.2005.01.035","article-title":"Ser475, Glu272, Asp276, Asp327, and Asp360 are involved in catalytic activity of human tripeptidyl-peptidase I","volume":"579","author":"Walus","year":"2005","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0355","doi-asserted-by":"crossref","first-page":"686","DOI":"10.1074\/mcp.M500343-MCP200","article-title":"Identification of sites of mannose 6-phosphorylation on lysosomal proteins","volume":"5","author":"Sleat","year":"2006","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.bbadis.2013.01.019_bb0360","doi-asserted-by":"crossref","first-page":"12827","DOI":"10.1074\/jbc.M313173200","article-title":"N-glycosylation is crucial for folding, trafficking, and stability of human tripeptidyl-peptidase I","volume":"279","author":"Wujek","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0365","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1074\/mcp.M700217-MCP200","article-title":"Proteomics analysis of serum from mutant mice reveals lysosomal proteins selectively transported by each of the two mannose 6-phosphate receptors","volume":"7","author":"Qian","year":"2008","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.bbadis.2013.01.019_bb0370","doi-asserted-by":"crossref","first-page":"2483","DOI":"10.1093\/hmg\/ddh264","article-title":"Mutations in classical late infantile neuronal ceroid lipofuscinosis disrupt transport of tripeptidyl-peptidase I to lysosomes","volume":"13","author":"Steinfeld","year":"2004","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0375","doi-asserted-by":"crossref","first-page":"1C","DOI":"10.1093\/glycob\/cwh054","article-title":"Mutation of the glycosylated asparagine residue 286 in human CLN2 protein results in loss of enzymatic activity","volume":"14","author":"Tsiakas","year":"2004","journal-title":"Glycobiology"},{"key":"10.1016\/j.bbadis.2013.01.019_bb0380","doi-asserted-by":"crossref","first-page":"16497","DOI":"10.1074\/jbc.M800458200","article-title":"Prosegment of tripeptidyl peptidase I is a potent, slow-binding inhibitor of its cognate enzyme","volume":"283","author":"Golabek","year":"2008","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0385","doi-asserted-by":"crossref","first-page":"7550","DOI":"10.1074\/jbc.M412047200","article-title":"Glycosaminoglycans modulate activation, activity, and stability of tripeptidyl-peptidase I in vitro and in vivo","volume":"280","author":"Golabek","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0390","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1046\/j.1471-4159.2000.0740287.x","article-title":"Purification and characterization of bovine brain lysosomal pepstatin-insensitive proteinase, the gene product deficient in the human late-infantile neuronal ceroid lipofuscinosis","volume":"74","author":"Junaid","year":"2000","journal-title":"J. Neurochem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0395","doi-asserted-by":"crossref","first-page":"1091","DOI":"10.1515\/BC.2006.135","article-title":"Tripeptidyl-peptidase I in health and disease","volume":"387","author":"Golabek","year":"2006","journal-title":"Biol. Chem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0400","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1016\/j.bbrc.2004.04.142","article-title":"The lysosomal degradation of neuromedin B is dependent on tripeptidyl peptidase-I: evidence for the impairment of neuropeptide degradation in late-infantile neuronal ceroid lipofuscinosis","volume":"319","author":"Kopan","year":"2004","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0405","doi-asserted-by":"crossref","first-page":"11507","DOI":"10.1074\/jbc.M807151200","article-title":"Lysosomal serine protease CLN2 regulates tumor necrosis factor-alpha-mediated apoptosis in a Bid-dependent manner","volume":"284","author":"Autefage","year":"2009","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0410","doi-asserted-by":"crossref","first-page":"2410","DOI":"10.1091\/mbc.E02-01-0031","article-title":"Neuronal ceroid lipofuscinoses are connected at molecular level: interaction of CLN5 protein with CLN2 and CLN3","volume":"13","author":"Vesa","year":"2002","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.bbadis.2013.01.019_bb0415","doi-asserted-by":"crossref","first-page":"949","DOI":"10.1016\/0092-8674(95)90274-0","article-title":"Consortium, isolation of a novel gene underlying Batten disease, CLN3. The International Batten Disease Consortium","volume":"82","year":"1995","journal-title":"Cell"},{"key":"10.1016\/j.bbadis.2013.01.019_bb0420","doi-asserted-by":"crossref","first-page":"1296","DOI":"10.1046\/j.1471-4159.2003.02132.x","article-title":"Characterization of Cln3p, the gene product responsible for juvenile neuronal ceroid lipofuscinosis, as a lysosomal integral membrane glycoprotein","volume":"87","author":"Ezaki","year":"2003","journal-title":"J. Neurochem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0425","doi-asserted-by":"crossref","first-page":"1313","DOI":"10.1091\/mbc.E03-02-0120","article-title":"Two motifs target Batten disease protein CLN3 to lysosomes in transfected nonneuronal and neuronal cells","volume":"15","author":"Kytt\u00e4l\u00e4","year":"2004","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.bbadis.2013.01.019_bb0430","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1016\/S0014-5793(03)00284-9","article-title":"Membrane topology of CLN3, the protein underlying Batten disease","volume":"541","author":"Mao","year":"2003","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0435","doi-asserted-by":"crossref","first-page":"1019","DOI":"10.1016\/j.febslet.2008.02.049","article-title":"The transmembrane topology of Batten disease protein CLN3 determined by consensus computational prediction constrained by experimental data","volume":"582","author":"Nugent","year":"2008","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0440","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1111\/j.1600-0854.2007.00537.x","article-title":"C-terminal prenylation of the CLN3 membrane glycoprotein is required for efficient endosomal sorting to lysosomes","volume":"8","author":"Storch","year":"2007","journal-title":"Traffic"},{"key":"10.1016\/j.bbadis.2013.01.019_bb0445","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1006\/mgme.1999.2837","article-title":"Analysis of intracellular distribution and trafficking of the CLN3 protein in fusion with the green fluorescent protein in vitro","volume":"66","author":"Kida","year":"1999","journal-title":"Mol. Genet. Metab."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0450","doi-asserted-by":"crossref","first-page":"2129","DOI":"10.1093\/hmg\/11.18.2129","article-title":"Motifs within the CLN3 protein: modulation of cell growth rates and apoptosis","volume":"11","author":"Persaud-Sawin","year":"2002","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0455","doi-asserted-by":"crossref","first-page":"458","DOI":"10.1006\/bbrc.1998.9210","article-title":"Evidence for phosphorylation of CLN3 protein associated with Batten disease","volume":"253","author":"Michalewski","year":"1998","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0460","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1055\/s-2007-973658","article-title":"Cross-species homology of the CLN3 gene","volume":"28","author":"Taschner","year":"1997","journal-title":"Neuropediatrics"},{"key":"10.1016\/j.bbadis.2013.01.019_bb0465","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1006\/mgme.2000.3056","article-title":"Neural and extraneural expression of the neuronal ceroid lipofuscinoses genes CLN1, CLN2, and CLN3: functional implications for CLN3","volume":"71","author":"Chattopadhyay","year":"2000","journal-title":"Mol. Genet. Metab."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0470","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1006\/mgme.1999.2830","article-title":"Tissue expression and subcellular localization of CLN3, the Batten disease protein","volume":"66","author":"Margraf","year":"1999","journal-title":"Mol. Genet. Metab."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0475","doi-asserted-by":"crossref","first-page":"6062","DOI":"10.1073\/pnas.0400782101","article-title":"A gene atlas of the mouse and human protein-encoding transcriptomes","volume":"101","author":"Su","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0480","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1016\/j.nbd.2010.09.011","article-title":"A knock-in reporter mouse model for Batten disease reveals predominant expression of Cln3 in visual, limbic and subcortical motor structures","volume":"41","author":"Ding","year":"2011","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0485","doi-asserted-by":"crossref","first-page":"9826","DOI":"10.1523\/JNEUROSCI.1710-07.2007","article-title":"A knock-in reporter model of Batten disease","volume":"27","author":"Eliason","year":"2007","journal-title":"J. Neurosci."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0490","doi-asserted-by":"crossref","first-page":"C1388","DOI":"10.1152\/ajpcell.00272.2009","article-title":"Osmoregulation of ceroid neuronal lipofuscinosis type 3 in the renal medulla","volume":"298","author":"Stein","year":"2010","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0495","doi-asserted-by":"crossref","first-page":"2709","DOI":"10.1093\/hmg\/11.22.2709","article-title":"Cln3(Deltaex7\/8) knock-in mice with the common JNCL mutation exhibit progressive neurologic disease that begins before birth","volume":"11","author":"Cotman","year":"2002","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0500","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1093\/hmg\/7.1.85","article-title":"Biosynthesis and intracellular targeting of the CLN3 protein defective in Batten disease","volume":"7","author":"Jarvela","year":"1998","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0505","doi-asserted-by":"crossref","first-page":"573","DOI":"10.1002\/jnr.20367","article-title":"CLN3, the protein associated with batten disease: structure, function and localization","volume":"79","author":"Phillips","year":"2005","journal-title":"J. Neurosci. Res."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0510","doi-asserted-by":"crossref","first-page":"53625","DOI":"10.1074\/jbc.M410930200","article-title":"A dileucine motif and a cluster of acidic amino acids in the second cytoplasmic domain of the batten disease-related CLN3 protein are required for efficient lysosomal targeting","volume":"279","author":"Storch","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0515","doi-asserted-by":"crossref","first-page":"10277","DOI":"10.1074\/jbc.M411862200","article-title":"AP-1 and AP-3 facilitate lysosomal targeting of Batten disease protein CLN3 via its dileucine motif","volume":"280","author":"Kytt\u00e4l\u00e4","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0520","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1186\/1471-2202-5-57","article-title":"Membrane trafficking and mitochondrial abnormalities precede subunit c deposition in a cerebellar cell model of juvenile neuronal ceroid lipofuscinosis","volume":"5","author":"Fossale","year":"2004","journal-title":"BMC Neurosci."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0525","doi-asserted-by":"crossref","first-page":"1091","DOI":"10.1093\/hmg\/8.6.1091","article-title":"Defective intracellular transport of CLN3 is the molecular basis of Batten disease (JNCL)","volume":"8","author":"Jarvela","year":"1999","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0530","doi-asserted-by":"crossref","first-page":"2123","DOI":"10.1093\/hmg\/10.19.2123","article-title":"CLN3 protein is targeted to neuronal synapses but excluded from synaptic vesicles: new clues to Batten disease","volume":"10","author":"Luiro","year":"2001","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0535","doi-asserted-by":"crossref","first-page":"735","DOI":"10.1007\/s00424-003-1103-2","article-title":"The equilibrative nucleoside transporter family, SLC29","volume":"447","author":"Baldwin","year":"2004","journal-title":"Pflugers Arch."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0540","doi-asserted-by":"crossref","first-page":"570","DOI":"10.1002\/ana.20975","article-title":"CLN3P, the Batten's disease protein, is a novel palmitoyl-protein Delta-9 desaturase","volume":"60","author":"Narayan","year":"2006","journal-title":"Ann. Neurol."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0545","doi-asserted-by":"crossref","first-page":"115","DOI":"10.2174\/138920208784139573","article-title":"Analysis of NCL proteins from an evolutionary standpoint","volume":"9","author":"Muzaffar","year":"2008","journal-title":"Curr. Genomics"},{"key":"10.1016\/j.bbadis.2013.01.019_bb0550","doi-asserted-by":"crossref","first-page":"5525","DOI":"10.1242\/jcs.02656","article-title":"btn1, the Schizosaccharomyces pombe homologue of the human Batten disease gene CLN3, regulates vacuole homeostasis","volume":"118","author":"Gachet","year":"2005","journal-title":"J. Cell Sci."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0555","doi-asserted-by":"crossref","first-page":"15458","DOI":"10.1073\/pnas.2136651100","article-title":"A role in vacuolar arginine transport for yeast Btn1p and for human CLN3, the protein defective in Batten disease","volume":"100","author":"Kim","year":"2003","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0560","doi-asserted-by":"crossref","first-page":"6915","DOI":"10.1073\/pnas.95.12.6915","article-title":"A yeast model for the study of Batten disease","volume":"95","author":"Pearce","year":"1998","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0565","doi-asserted-by":"crossref","first-page":"1163","DOI":"10.1242\/jcs.038323","article-title":"S. pombe btn1, the orthologue of the Batten disease gene CLN3, is required for vacuole protein sorting of Cpy1p and Golgi exit of Vps10p","volume":"122","author":"Codlin","year":"2009","journal-title":"J. Cell Sci."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0570","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1083\/jcb.201102115","article-title":"The yeast Batten disease orthologue Btn1 controls endosome-Golgi retrograde transport via SNARE assembly","volume":"195","author":"Kama","year":"2011","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0575","doi-asserted-by":"crossref","first-page":"2075","DOI":"10.1007\/s00018-011-0913-1","article-title":"Neuronal ceroid lipofuscinosis protein CLN3 interacts with motor proteins and modifies location of late endosomal compartments","volume":"69","author":"Uusi-Rauva","year":"2012","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0580","doi-asserted-by":"crossref","first-page":"3017","DOI":"10.1093\/hmg\/ddh321","article-title":"Interconnections of CLN3, Hook1 and Rab proteins link Batten disease to defects in the endocytic pathway","volume":"13","author":"Luiro","year":"2004","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0585","doi-asserted-by":"crossref","first-page":"20483","DOI":"10.1074\/jbc.M602180200","article-title":"Autophagy is disrupted in a knock-in mouse model of juvenile neuronal ceroid lipofuscinosis","volume":"281","author":"Cao","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0590","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1083\/jcb.200907015","article-title":"FYCO1 is a Rab7 effector that binds to LC3 and PI3P to mediate microtubule plus end-directed vesicle transport","volume":"188","author":"Pankiv","year":"2010","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0595","doi-asserted-by":"crossref","first-page":"2895","DOI":"10.1016\/j.yexcr.2008.06.016","article-title":"Novel interactions of CLN3 protein link Batten disease to dysregulation of fodrin-Na+, K+ ATPase complex","volume":"314","author":"Uusi-Rauva","year":"2008","journal-title":"Exp. Cell Res."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0600","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1007\/s00401-010-0696-8","article-title":"CMT2B-associated Rab7 mutants inhibit neurite outgrowth","volume":"120","author":"Cogli","year":"2010","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0605","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1016\/j.neuron.2006.08.018","article-title":"Rab5 and Rab7 control endocytic sorting along the axonal retrograde transport pathway","volume":"52","author":"Deinhardt","year":"2006","journal-title":"Neuron"},{"key":"10.1016\/j.bbadis.2013.01.019_bb0610","doi-asserted-by":"crossref","first-page":"10930","DOI":"10.1523\/JNEUROSCI.2029-05.2005","article-title":"The small GTPase Rab7 controls the endosomal trafficking and neuritogenic signaling of the nerve growth factor receptor TrkA","volume":"25","author":"Saxena","year":"2005","journal-title":"J. Neurosci."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0615","doi-asserted-by":"crossref","first-page":"1255","DOI":"10.1083\/jcb.148.6.1255","article-title":"Kinesin superfamily protein 3 (KIF3) motor transports fodrin-associating vesicles important for neurite building","volume":"148","author":"Takeda","year":"2000","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0620","doi-asserted-by":"crossref","first-page":"284","DOI":"10.1016\/j.nbd.2005.11.008","article-title":"Visual deficits in a mouse model of Batten disease are the result of optic nerve degeneration and loss of dorsal lateral geniculate thalamic neurons","volume":"22","author":"Weimer","year":"2006","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0625","doi-asserted-by":"crossref","first-page":"605","DOI":"10.1128\/MCB.00699-06","article-title":"Btn2, a Hook1 ortholog and potential Batten disease-related protein, mediates late endosome-Golgi protein sorting in yeast","volume":"27","author":"Kama","year":"2007","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0630","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1186\/1471-2121-10-83","article-title":"Novel interactions of CLN5 support molecular networking between Neuronal Ceroid Lipofuscinosis proteins","volume":"10","author":"Lyly","year":"2009","journal-title":"BMC Cell Biol."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0635","doi-asserted-by":"crossref","first-page":"1855","DOI":"10.1128\/MCB.06726-11","article-title":"The role of ceroid lipofuscinosis neuronal protein 5 (CLN5) in endosomal sorting","volume":"32","author":"Mamo","year":"2012","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0640","doi-asserted-by":"crossref","first-page":"1905","DOI":"10.1111\/j.1600-0854.2008.00807.x","article-title":"Loss of the Batten disease gene CLN3 prevents exit from the TGN of the mannose 6-phosphate receptor","volume":"9","author":"Metcalf","year":"2008","journal-title":"Traffic"},{"key":"10.1016\/j.bbadis.2013.01.019_bb0645","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/j.yexcr.2010.09.007","article-title":"A novel interaction of CLN3 with nonmuscle myosin-IIB and defects in cell motility of Cln3(\u2212\/\u2212) cells","volume":"317","author":"Getty","year":"2010","journal-title":"Exp. Cell Res."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0650","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1016\/j.brainres.2009.02.009","article-title":"Cerebellar defects in a mouse model of juvenile neuronal ceroid lipofuscinosis","volume":"1266","author":"Weimer","year":"2009","journal-title":"Brain Res."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0655","doi-asserted-by":"crossref","first-page":"4498","DOI":"10.1523\/JNEUROSCI.6094-08.2009","article-title":"Na, K-ATPase activity regulates AMPA receptor turnover through proteasome-mediated proteolysis","volume":"29","author":"Zhang","year":"2009","journal-title":"J. Neurosci."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0660","doi-asserted-by":"crossref","first-page":"8143","DOI":"10.1523\/JNEUROSCI.1081-09.2009","article-title":"Glutamate transporter coupling to Na, K-ATPase","volume":"29","author":"Rose","year":"2009","journal-title":"J. Neurosci."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0665","doi-asserted-by":"crossref","first-page":"648","DOI":"10.1016\/j.neuint.2011.02.003","article-title":"Altered sensitivity of cerebellar granule cells to glutamate receptor overactivation in the Cln3(Deltaex7\/8)-knock-in mouse model of juvenile neuronal ceroid lipofuscinosis","volume":"58","author":"Finn","year":"2011","journal-title":"Neurochem. Int."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0670","doi-asserted-by":"crossref","first-page":"575","DOI":"10.1016\/j.nbd.2005.12.018","article-title":"Selectively increased sensitivity of cerebellar granule cells to AMPA receptor-mediated excitotoxicity in a mouse model of Batten disease","volume":"22","author":"Kovacs","year":"2006","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0675","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1093\/hmg\/ddl466","article-title":"Neuronal vulnerability of CLN3 deletion to calcium-induced cytotoxicity is mediated by calsenilin","volume":"16","author":"Chang","year":"2007","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0680","doi-asserted-by":"crossref","first-page":"1069","DOI":"10.1212\/WNL.54.5.1069","article-title":"Decreased striatal dopamine transporter density in JNCL patients with parkinsonian symptoms","volume":"54","author":"Aberg","year":"2000","journal-title":"Neurology"},{"key":"10.1016\/j.bbadis.2013.01.019_bb0685","doi-asserted-by":"crossref","first-page":"1857","DOI":"10.1002\/jnr.21630","article-title":"Developmental impairments of select neurotransmitter systems in brains of Cln3(Deltaex7\/8) knock-in mice, an animal model of juvenile neuronal ceroid lipofuscinosis","volume":"86","author":"Herrmann","year":"2008","journal-title":"J. Neurosci. Res."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0690","doi-asserted-by":"crossref","first-page":"138","DOI":"10.1055\/s-2002-33677","article-title":"Positron emission tomography shows reduced striatal dopamine D1 but not D2 receptors in juvenile neuronal ceroid lipofuscinosis","volume":"33","author":"Rinne","year":"2002","journal-title":"Neuropediatrics"},{"key":"10.1016\/j.bbadis.2013.01.019_bb0695","doi-asserted-by":"crossref","first-page":"98","DOI":"10.1016\/j.brainres.2007.05.018","article-title":"Alterations in striatal dopamine catabolism precede loss of substantia nigra neurons in a mouse model of juvenile neuronal ceroid lipofuscinosis","volume":"1162","author":"Weimer","year":"2007","journal-title":"Brain Res."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0700","doi-asserted-by":"crossref","first-page":"1421","DOI":"10.1093\/hmg\/11.12.1421","article-title":"An autoantibody inhibitory to glutamic acid decarboxylase in the neurodegenerative disorder Batten disease","volume":"11","author":"Chattopadhyay","year":"2002","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0705","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1006\/nbdi.1999.0267","article-title":"Targeted disruption of the Cln3 gene provides a mouse model for Batten disease. The Batten Mouse Model Consortium [corrected]","volume":"6","author":"Mitchison","year":"1999","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0710","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1111\/j.1750-3639.2004.tb00077.x","article-title":"Hippocampal pathology in the human neuronal ceroid-lipofuscinoses: distinct patterns of storage deposition, neurodegeneration and glial activation","volume":"14","author":"Tyynel\u00e4","year":"2004","journal-title":"Brain Pathol."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0715","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1016\/j.bbrc.2007.04.064","article-title":"A novel role of the Batten disease gene CLN3: association with BMP synthesis","volume":"358","author":"Hobert","year":"2007","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0720","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1242\/dmm.008490","article-title":"BTN1, the Saccharomyces cerevisiae homolog to the human Batten disease gene, is involved in phospholipid distribution","volume":"5","author":"Padilla-Lopez","year":"2012","journal-title":"Dis. Model. Mech."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0725","doi-asserted-by":"crossref","first-page":"625","DOI":"10.1203\/PDR.0b013e31816fdc17","article-title":"CLN3p impacts galactosylceramide transport, raft morphology, and lipid content","volume":"63","author":"Rusyn","year":"2008","journal-title":"Pediatr. Res."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0730","doi-asserted-by":"crossref","first-page":"2882","DOI":"10.1002\/jnr.21416","article-title":"Progressive oxidative damage in the central nervous system of a murine model for juvenile Batten disease","volume":"85","author":"Benedict","year":"2007","journal-title":"J. Neurosci. Res."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0735","doi-asserted-by":"crossref","first-page":"1124","DOI":"10.1002\/jnr.21015","article-title":"Batten disease (JNCL) is linked to disturbances in mitochondrial, cytoskeletal, and synaptic compartments","volume":"84","author":"Luiro","year":"2006","journal-title":"J. Neurosci. Res."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0740","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1006\/mgme.2000.3006","article-title":"CLN3 protein regulates lysosomal pH and alters intracellular processing of Alzheimer's amyloid-beta protein precursor and cathepsin D in human cells","volume":"70","author":"Golabek","year":"2000","journal-title":"Mol. Genet. Metab."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0745","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1093\/hmg\/ddm306","article-title":"A function retained by the common mutant CLN3 protein is responsible for the late onset of juvenile neuronal ceroid lipofuscinosis","volume":"17","author":"Kitzm\u00fcller","year":"2008","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0750","doi-asserted-by":"crossref","first-page":"10273","DOI":"10.1074\/jbc.M510625200","article-title":"Saccharomyces cerevisiae lacking Btn1p modulate vacuolar ATPase activity to regulate pH imbalance in the vacuole","volume":"281","author":"Padilla-Lopez","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0755","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1038\/8861","article-title":"Action of BTN1, the yeast orthologue of the gene mutated in Batten disease","volume":"22","author":"Pearce","year":"1999","journal-title":"Nat. Genet."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0760","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1111\/j.1365-2990.2008.00984.x","article-title":"Altered arginine metabolism in the central nervous system (CNS) of the Cln3\u2212\/\u2212 mouse model of juvenile Batten disease","volume":"35","author":"Chan","year":"2009","journal-title":"Neuropathol. Appl. Neurobiol."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0765","doi-asserted-by":"crossref","first-page":"3759","DOI":"10.1093\/hmg\/ddi406","article-title":"Defective lysosomal arginine transport in juvenile Batten disease","volume":"14","author":"Ramirez-Montealegre","year":"2005","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0770","doi-asserted-by":"crossref","first-page":"2755","DOI":"10.1091\/mbc.E06-11-1053","article-title":"Nitric oxide signaling is disrupted in the yeast model for Batten disease","volume":"18","author":"Osorio","year":"2007","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.bbadis.2013.01.019_bb0775","doi-asserted-by":"crossref","first-page":"2860","DOI":"10.1242\/jcs.030122","article-title":"Btn1 affects cytokinesis and cell-wall deposition by independent mechanisms, one of which is linked to dysregulation of vacuole pH","volume":"121","author":"Codlin","year":"2008","journal-title":"J. Cell Sci."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0780","doi-asserted-by":"crossref","first-page":"936","DOI":"10.1111\/j.1600-0854.2008.00735.x","article-title":"btn1 affects endocytosis, polarization of sterol-rich membrane domains and polarized growth in Schizosaccharomyces pombe","volume":"9","author":"Codlin","year":"2008","journal-title":"Traffic"},{"key":"10.1016\/j.bbadis.2013.01.019_bb0785","doi-asserted-by":"crossref","first-page":"667","DOI":"10.1093\/hmg\/ddn396","article-title":"Interactions between the juvenile Batten disease gene, CLN3, and the Notch and JNK signalling pathways","volume":"18","author":"Tuxworth","year":"2009","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0790","doi-asserted-by":"crossref","first-page":"2037","DOI":"10.1093\/hmg\/ddr088","article-title":"The Batten disease gene CLN3 is required for the response to oxidative stress","volume":"20","author":"Tuxworth","year":"2011","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0795","doi-asserted-by":"crossref","first-page":"1253","DOI":"10.2119\/molmed.2010.00241","article-title":"Analysis of potential biomarkers and modifier genes affecting the clinical course of CLN3 disease","volume":"17","author":"Lebrun","year":"2011","journal-title":"Mol. Med."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0800","doi-asserted-by":"crossref","first-page":"566","DOI":"10.1016\/j.ajhg.2011.04.004","article-title":"Kufs disease, the major adult form of neuronal ceroid lipofuscinosis, caused by mutations in CLN6","volume":"88","author":"Arsov","year":"2011","journal-title":"Am. J. Hum. Genet."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0805","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1002\/humu.21624","article-title":"Update of the mutation spectrum and clinical correlations of over 360 mutations in eight genes that underlie the neuronal ceroid lipofuscinoses","volume":"33","author":"Kousi","year":"2012","journal-title":"Hum. Mutat."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0810","doi-asserted-by":"crossref","first-page":"e26741","DOI":"10.1371\/journal.pone.0026741","article-title":"Exome-sequencing confirms DNAJC5 mutations as cause of adult neuronal ceroid-lipofuscinosis","volume":"6","author":"Benitez","year":"2011","journal-title":"PLoS One"},{"key":"10.1016\/j.bbadis.2013.01.019_bb0815","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1016\/j.ajhg.2011.07.003","article-title":"Mutations in DNAJC5, encoding cysteine-string protein alpha, cause autosomal-dominant adult-onset neuronal ceroid lipofuscinosis","volume":"89","author":"Noskova","year":"2011","journal-title":"Am. J. Hum. Genet."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0820","doi-asserted-by":"crossref","first-page":"987","DOI":"10.1016\/S0896-6273(01)00427-5","article-title":"A trimeric protein complex functions as a synaptic chaperone machine","volume":"31","author":"Tobaben","year":"2001","journal-title":"Neuron"},{"key":"10.1016\/j.bbadis.2013.01.019_bb0825","doi-asserted-by":"crossref","first-page":"981","DOI":"10.1126\/science.7906056","article-title":"Cysteine string proteins: a potential link between synaptic vesicles and presynaptic Ca2+ channels","volume":"263","author":"Mastrogiacomo","year":"1994","journal-title":"Science"},{"key":"10.1016\/j.bbadis.2013.01.019_bb0830","doi-asserted-by":"crossref","first-page":"1781","DOI":"10.1046\/j.1471-4159.2000.0741781.x","article-title":"Cysteine-string protein: the chaperone at the synapse","volume":"74","author":"Chamberlain","year":"2000","journal-title":"J. Neurochem."},{"issue":"Pt 2","key":"10.1016\/j.bbadis.2013.01.019_bb0835","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1042\/bj3350205","article-title":"The cysteine-string domain of the secretory vesicle cysteine-string protein is required for membrane targeting","volume":"335","author":"Chamberlain","year":"1998","journal-title":"Biochem. J."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0840","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1038\/ncb2131","article-title":"CSPalpha promotes SNARE-complex assembly by chaperoning SNAP-25 during synaptic activity","volume":"13","author":"Sharma","year":"2011","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0845","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1016\/j.neuron.2012.01.029","article-title":"Identification of CSPalpha clients reveals a role in dynamin 1 regulation","volume":"74","author":"Zhang","year":"2012","journal-title":"Neuron"},{"key":"10.1016\/j.bbadis.2013.01.019_bb0850","doi-asserted-by":"crossref","first-page":"829","DOI":"10.1038\/emboj.2011.467","article-title":"CSPalpha knockout causes neurodegeneration by impairing SNAP-25 function","volume":"31","author":"Sharma","year":"2012","journal-title":"EMBO J."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0855","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1016\/j.cell.2005.09.028","article-title":"Alpha-synuclein cooperates with CSPalpha in preventing neurodegeneration","volume":"123","author":"Chandra","year":"2005","journal-title":"Cell"},{"key":"10.1016\/j.bbadis.2013.01.019_bb0860","doi-asserted-by":"crossref","first-page":"977","DOI":"10.1126\/science.8310297","article-title":"Paralysis and early death in cysteine string protein mutants of Drosophila","volume":"263","author":"Zinsmaier","year":"1994","journal-title":"Science"},{"key":"10.1016\/j.bbadis.2013.01.019_bb0865","doi-asserted-by":"crossref","first-page":"6039","DOI":"10.1523\/JNEUROSCI.20-16-06039.2000","article-title":"Cysteine-string protein increases the calcium sensitivity of neurotransmitter exocytosis in Drosophila","volume":"20","author":"Dawson-Scully","year":"2000","journal-title":"J. Neurosci."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0870","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1016\/S0896-6273(04)00190-4","article-title":"The synaptic vesicle protein CSP alpha prevents presynaptic degeneration","volume":"42","author":"Fernandez-Chacon","year":"2004","journal-title":"Neuron"},{"key":"10.1016\/j.bbadis.2013.01.019_bb0875","doi-asserted-by":"crossref","first-page":"7377","DOI":"10.1523\/JNEUROSCI.0924-10.2010","article-title":"Cysteine string protein-alpha prevents activity-dependent degeneration in GABAergic synapses","volume":"30","author":"Garcia-Junco-Clemente","year":"2010","journal-title":"J. Neurosci."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0880","doi-asserted-by":"crossref","first-page":"2926","DOI":"10.1073\/pnas.0510060103","article-title":"CSPalpha-deficiency causes massive and rapid photoreceptor degeneration","volume":"103","author":"Schmitz","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0885","doi-asserted-by":"crossref","first-page":"37330","DOI":"10.1074\/jbc.M112.389098","article-title":"Palmitoylation-induced aggregation of cysteine-string protein mutants that cause neuronal ceroid lipofuscinosis","volume":"287","author":"Greaves","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0890","doi-asserted-by":"crossref","first-page":"5563","DOI":"10.1016\/j.bmcl.2012.07.012","article-title":"Isosteric replacements for benzothiazoles and optimisation to potent Cathepsin K inhibitors free from hERG channel inhibition","volume":"22","author":"Dossetter","year":"2012","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0895","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/j.nbd.2003.12.019","article-title":"The mouse ortholog of the neuronal ceroid lipofuscinosis CLN5 gene encodes a soluble lysosomal glycoprotein expressed in the developing brain","volume":"16","author":"Holmberg","year":"2004","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0900","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/j.nbd.2011.12.009","article-title":"Cln5-deficiency in mice leads to microglial activation, defective myelination and changes in lipid metabolism","volume":"46","author":"Schmiedt","year":"2012","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0905","doi-asserted-by":"crossref","first-page":"286","DOI":"10.1038\/975","article-title":"CLN5, a novel gene encoding a putative transmembrane protein mutated in Finnish variant late infantile neuronal ceroid lipofuscinosis","volume":"19","author":"Savukoski","year":"1998","journal-title":"Nat. Genet."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0910","doi-asserted-by":"crossref","first-page":"885","DOI":"10.1093\/hmg\/11.8.885","article-title":"Lysosomal localization of the neuronal ceroid lipofuscinosis CLN5 protein","volume":"11","author":"Isosomppi","year":"2002","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0915","doi-asserted-by":"crossref","first-page":"3966","DOI":"10.1002\/pmic.200401247","article-title":"Identification of novel lysosomal matrix proteins by proteome analysis","volume":"5","author":"Kollmann","year":"2005","journal-title":"Proteomics"},{"key":"10.1016\/j.bbadis.2013.01.019_bb0920","doi-asserted-by":"crossref","first-page":"E651","DOI":"10.1002\/humu.21010","article-title":"Retention of lysosomal protein CLN5 in the endoplasmic reticulum causes neuronal ceroid lipofuscinosis in Asian sibship","volume":"30","author":"Lebrun","year":"2009","journal-title":"Hum. Mutat."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0925","doi-asserted-by":"crossref","first-page":"356","DOI":"10.1002\/humu.21195","article-title":"The neuronal ceroid lipofuscinosis protein CLN5: new insights into cellular maturation, transport, and consequences of mutations","volume":"31","author":"Schmiedt","year":"2010","journal-title":"Hum. Mutat."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0930","doi-asserted-by":"crossref","first-page":"2893","DOI":"10.1093\/hmg\/ddh312","article-title":"A mouse model for Finnish variant late infantile neuronal ceroid lipofuscinosis, CLN5, reveals neuropathology associated with early aging","volume":"13","author":"Kopra","year":"2004","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0935","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1186\/1471-2164-9-146","article-title":"Brain gene expression profiles of Cln1 and Cln5 deficient mice unravels common molecular pathways underlying neuronal degeneration in NCL diseases","volume":"9","author":"von Schantz","year":"2008","journal-title":"BMC Genomics"},{"key":"10.1016\/j.bbadis.2013.01.019_bb0940","doi-asserted-by":"crossref","first-page":"324","DOI":"10.1086\/338190","article-title":"Mutations in a novel CLN6-encoded transmembrane protein cause variant neuronal ceroid lipofuscinosis in man and mouse","volume":"70","author":"Gao","year":"2002","journal-title":"Am. J. Hum. Genet."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0945","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1086\/338708","article-title":"The gene mutated in variant late-infantile neuronal ceroid lipofuscinosis (CLN6) and in nclf mutant mice encodes a novel predicted transmembrane protein","volume":"70","author":"Wheeler","year":"2002","journal-title":"Am. J. Hum. Genet."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0950","doi-asserted-by":"crossref","first-page":"568","DOI":"10.1002\/jnr.22773","article-title":"High expression of disease-related Cln6 in the cerebral cortex, purkinje cells, dentate gyrus, and hippocampal ca1 neurons","volume":"90","author":"Thelen","year":"2012","journal-title":"J. Neurosci. Res."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0955","doi-asserted-by":"crossref","first-page":"22347","DOI":"10.1074\/jbc.M400643200","article-title":"Defective endoplasmic reticulum-resident membrane protein CLN6 affects lysosomal degradation of endocytosed arylsulfatase A","volume":"279","author":"Heine","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0960","doi-asserted-by":"crossref","first-page":"399","DOI":"10.1016\/j.yexcr.2004.04.042","article-title":"CLN6, which is associated with a lysosomal storage disease, is an endoplasmic reticulum protein","volume":"298","author":"Mole","year":"2004","journal-title":"Exp. Cell Res."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0965","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1080\/09687860600967317","article-title":"Topology and endoplasmic reticulum retention signals of the lysosomal storage disease-related membrane protein CLN6","volume":"24","author":"Heine","year":"2007","journal-title":"Mol. Membr. Biol."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0970","doi-asserted-by":"crossref","first-page":"E1163","DOI":"10.1002\/humu.21184","article-title":"Pathogenic mutations cause rapid degradation of lysosomal storage disease-related membrane protein CLN6","volume":"31","author":"Kurze","year":"2010","journal-title":"Hum. Mutat."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0975","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1042\/BSR20080143","article-title":"Cln6 mutants associated with neuronal ceroid lipofuscinosis are degraded in a proteasome-dependent manner","volume":"29","author":"Oresic","year":"2009","journal-title":"Biosci. Rep."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0980","doi-asserted-by":"crossref","DOI":"10.1371\/annotation\/a4b06d46-8eb9-4d15-a15a-41bf4b5ccb8b","article-title":"Correction: disruption of the autophagy-lysosome pathway is involved in neuropathology of the nclf mouse model of neuronal ceroid lipofuscinosis","volume":"7","author":"Thelen","year":"2012","journal-title":"PLoS One"},{"key":"10.1016\/j.bbadis.2013.01.019_bb0985","doi-asserted-by":"crossref","first-page":"e17118","DOI":"10.1371\/journal.pone.0017118","article-title":"Distinct early molecular responses to mutations causing vLINCL and JNCL presage ATP synthase subunit C accumulation in cerebellar cells","volume":"6","author":"Cao","year":"2011","journal-title":"PLoS One"},{"key":"10.1016\/j.bbadis.2013.01.019_bb0990","doi-asserted-by":"crossref","first-page":"1415","DOI":"10.1111\/j.1471-4159.2008.05497.x","article-title":"Accumulation of bis(monoacylglycero)phosphate and gangliosides in mouse models of neuronal ceroid lipofuscinosis","volume":"106","author":"Jabs","year":"2008","journal-title":"J. Neurochem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb0995","doi-asserted-by":"crossref","first-page":"1773","DOI":"10.1016\/S0021-9258(17)36006-4","article-title":"Ceroid lipofuscinosis in sheep. II. The major component of the lipopigment in liver, kidney, pancreas, and brain is low molecular weight protein","volume":"261","author":"Palmer","year":"1986","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1000","doi-asserted-by":"crossref","first-page":"1766","DOI":"10.1016\/S0021-9258(17)36005-2","article-title":"Ceroid lipofuscinosis in sheep. I. Bis(monoacylglycero)phosphate, dolichol, ubiquinone, phospholipids, fatty acids, and fluorescence in liver lipopigment lipids","volume":"261","author":"Palmer","year":"1986","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1005","doi-asserted-by":"crossref","first-page":"637","DOI":"10.1016\/j.bbadis.2006.06.002","article-title":"Gene expression profiling in vLINCL CLN6-deficient fibroblasts: insights into pathobiology","volume":"1762","author":"Teixeira","year":"2006","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbadis.2013.01.019_bb1010","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1042\/bj20030598","article-title":"Enhanced expression of manganese-dependent superoxide dismutase in human and sheep CLN6 tissues","volume":"376","author":"Heine","year":"2003","journal-title":"Biochem. J."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1015","doi-asserted-by":"crossref","first-page":"2157","DOI":"10.1002\/jnr.22032","article-title":"Protein product of CLN6 gene responsible for variant late-onset infantile neuronal ceroid lipofuscinosis interacts with CRMP-2","volume":"87","author":"Benedict","year":"2009","journal-title":"J. Neurosci. Res."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1020","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1086\/518902","article-title":"The novel neuronal ceroid lipofuscinosis gene MFSD8 encodes a putative lysosomal transporter","volume":"81","author":"Siintola","year":"2007","journal-title":"Am. J. Hum. Genet."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1025","doi-asserted-by":"crossref","first-page":"4497","DOI":"10.1093\/hmg\/ddq381","article-title":"Expression and lysosomal targeting of CLN7, a major facilitator superfamily transporter associated with variant late-infantile neuronal ceroid lipofuscinosis","volume":"19","author":"Sharifi","year":"2010","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1030","doi-asserted-by":"crossref","first-page":"987","DOI":"10.1111\/j.1600-0854.2010.01073.x","article-title":"Lysosomal targeting of the CLN7 membrane glycoprotein and transport via the plasma membrane require a dileucine motif","volume":"11","author":"Steenhuis","year":"2010","journal-title":"Traffic"},{"key":"10.1016\/j.bbadis.2013.01.019_bb1035","doi-asserted-by":"crossref","first-page":"810","DOI":"10.1093\/brain\/awn366","article-title":"Mutations in CLN7\/MFSD8 are a common cause of variant late-infantile neuronal ceroid lipofuscinosis","volume":"132","author":"Kousi","year":"2009","journal-title":"Brain"},{"key":"10.1016\/j.bbadis.2013.01.019_bb1040","doi-asserted-by":"crossref","first-page":"1617","DOI":"10.1016\/j.bbadis.2012.05.015","article-title":"Proteolytic cleavage of the disease-related lysosomal membrane glycoprotein CLN7","volume":"1822","author":"Steenhuis","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbadis.2013.01.019_bb1045","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1128\/MMBR.62.1.1-34.1998","article-title":"Major facilitator superfamily","volume":"62","author":"Pao","year":"1998","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1050","doi-asserted-by":"crossref","first-page":"31233","DOI":"10.1074\/jbc.M110.141150","article-title":"Analysis of the biogenesis of heparan sulfate acetyl-CoA:alpha-glucosaminide N-acetyltransferase provides insights into the mechanism underlying its complete deficiency in mucopolysaccharidosis IIIC","volume":"285","author":"Durand","year":"2010","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1055","doi-asserted-by":"crossref","first-page":"43218","DOI":"10.1074\/jbc.M508210200","article-title":"TRP-ML1 is a lysosomal monovalent cation channel that undergoes proteolytic cleavage","volume":"280","author":"Kiselyov","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1060","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1042\/BJ20110166","article-title":"Disrupted in renal carcinoma 2 (DIRC2), a novel transporter of the lysosomal membrane, is proteolytically processed by cathepsin L","volume":"439","author":"Savalas","year":"2011","journal-title":"Biochem. J."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1065","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1016\/j.brainres.2012.02.006","article-title":"Brain transcriptome perturbations in the Hfe(\u2212\/\u2212) mouse model of genetic iron loading","volume":"1448","author":"Johnstone","year":"2012","journal-title":"Brain Res."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1070","doi-asserted-by":"crossref","first-page":"856","DOI":"10.1016\/j.neuint.2010.03.015","article-title":"Genome-wide microarray analysis of brain gene expression in mice on a short-term high iron diet","volume":"56","author":"Johnstone","year":"2010","journal-title":"Neurochem. Int."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1075","doi-asserted-by":"crossref","first-page":"300","DOI":"10.1002\/humu.20018","article-title":"Variant late infantile neuronal ceroid lipofuscinosis in a subset of Turkish patients is allelic to Northern epilepsy","volume":"23","author":"Ranta","year":"2004","journal-title":"Hum. Mutat."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1080","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1038\/13868","article-title":"The neuronal ceroid lipofuscinoses in human EPMR and mnd mutant mice are associated with mutations in CLN8","volume":"23","author":"Ranta","year":"1999","journal-title":"Nat. Genet."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1085","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1111\/j.1750-3639.2000.tb00255.x","article-title":"Northern epilepsy: a novel form of neuronal ceroid-lipofuscinosis","volume":"10","author":"Herva","year":"2000","journal-title":"Brain Pathol."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1090","doi-asserted-by":"crossref","first-page":"715","DOI":"10.1016\/j.biochi.2010.12.014","article-title":"Molecular organization of the cullin E3 ligase adaptor KCTD11","volume":"93","author":"Correale","year":"2011","journal-title":"Biochimie"},{"key":"10.1016\/j.bbadis.2013.01.019_bb1095","doi-asserted-by":"crossref","first-page":"1691","DOI":"10.1093\/hmg\/9.11.1691","article-title":"The neuronal ceroid lipofuscinosis CLN8 membrane protein is a resident of the endoplasmic reticulum","volume":"9","author":"Lonka","year":"2000","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1100","doi-asserted-by":"crossref","first-page":"862","DOI":"10.1002\/jnr.20133","article-title":"Localization of wild-type and mutant neuronal ceroid lipofuscinosis CLN8 proteins in non-neuronal and neuronal cells","volume":"76","author":"Lonka","year":"2004","journal-title":"J. Neurosci. Res."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1105","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1016\/S0968-0004(02)02154-0","article-title":"TRAM, LAG1 and CLN8: members of a novel family of lipid-sensing domains?","volume":"27","author":"Winter","year":"2002","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1110","doi-asserted-by":"crossref","first-page":"2655","DOI":"10.1093\/emboj\/20.11.2655","article-title":"C26-CoA-dependent ceramide synthesis of Saccharomyces cerevisiae is operated by Lag1p and Lac1p","volume":"20","author":"Guillas","year":"2001","journal-title":"EMBO J."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1115","doi-asserted-by":"crossref","first-page":"3417","DOI":"10.1091\/mbc.12.11.3417","article-title":"Lag1p and Lac1p are essential for the Acyl-CoA-dependent ceramide synthase reaction in Saccharomyces cerevisiae","volume":"12","author":"Schorling","year":"2001","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.bbadis.2013.01.019_bb1120","doi-asserted-by":"crossref","first-page":"43452","DOI":"10.1074\/jbc.M307104200","article-title":"Two mammalian longevity assurance gene (LAG1) family members, trh1 and trh4, regulate dihydroceramide synthesis using different fatty acyl-CoA donors","volume":"278","author":"Riebeling","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1125","doi-asserted-by":"crossref","first-page":"609","DOI":"10.1111\/j.1471-4159.2005.03376.x","article-title":"Mass spectrometric analysis reveals changes in phospholipid, neutral sphingolipid and sulfatide molecular species in progressive epilepsy with mental retardation, EPMR, brain: a case study","volume":"95","author":"Hermansson","year":"2005","journal-title":"J. Neurochem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1130","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1152\/physiolgenomics.00100.2002","article-title":"Vitamin E deficiency and metabolic deficits in neuronal ceroid lipofuscinosis described by bioinformatics","volume":"11","author":"Griffin","year":"2002","journal-title":"Physiol. Genomics"},{"key":"10.1016\/j.bbadis.2013.01.019_bb1135","doi-asserted-by":"crossref","first-page":"286","DOI":"10.1016\/S0005-2760(96)00153-1","article-title":"Abnormalities in mitochondria-associated membranes and phospholipid biosynthetic enzymes in the mnd\/mnd mouse model of neuronal ceroid lipofuscinosis","volume":"1344","author":"Vance","year":"1997","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbadis.2013.01.019_bb1140","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1111\/j.1365-2990.2011.01233.x","article-title":"Galactolipid deficiency in the early pathogenesis of neuronal ceroid lipofuscinosis model Cln8(mnd): implications to delayed myelination and oligodendrocyte maturation","volume":"38","author":"Kuronen","year":"2012","journal-title":"Neuropathol. Appl. Neurobiol."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1145","doi-asserted-by":"crossref","first-page":"258","DOI":"10.1016\/j.neulet.2010.11.041","article-title":"Different early ER-stress responses in the CLN8(mnd) mouse model of neuronal ceroid lipofuscinosis","volume":"488","author":"Galizzi","year":"2011","journal-title":"Neurosci. Lett."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1150","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1016\/j.ceca.2011.08.004","article-title":"Deficient mitochondrial Ca(2+) buffering in the Cln8 (mnd) mouse model of neuronal ceroid lipofuscinosis","volume":"50","author":"Kolikova","year":"2011","journal-title":"Cell Calcium"},{"key":"10.1016\/j.bbadis.2013.01.019_bb1155","doi-asserted-by":"crossref","first-page":"1567","DOI":"10.1111\/j.1471-4159.1993.tb03323.x","article-title":"Synaptosomal glutamate uptake declines progressively in the spinal cord of a mutant mouse with motor neuron disease","volume":"60","author":"Battaglioli","year":"1993","journal-title":"J. Neurochem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1160","doi-asserted-by":"crossref","first-page":"2291","DOI":"10.1046\/j.1460-9568.2002.02299.x","article-title":"Mitochondrial oxidative metabolism in motor neuron degeneration (mnd) mouse central nervous system","volume":"16","author":"Bertamini","year":"2002","journal-title":"Eur. J. Neurosci."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1165","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/S0022-510X(98)00072-0","article-title":"Spinal cord GLT-1 glutamate transporter and blood glutamic acid alterations in motor neuron degeneration (Mnd) mice","volume":"157","author":"Mennini","year":"1998","journal-title":"J. Neurol. Sci."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1170","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1002\/jnr.10420","article-title":"Expression of glutamate receptor subtypes in the spinal cord of control and mnd mice, a model of motor neuron disorder","volume":"70","author":"Mennini","year":"2002","journal-title":"J. Neurosci. Res."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1175","doi-asserted-by":"crossref","first-page":"2784","DOI":"10.1074\/jbc.M509483200","article-title":"The CLN9 protein, a regulator of dihydroceramide synthase","volume":"281","author":"Schulz","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1180","doi-asserted-by":"crossref","first-page":"529","DOI":"10.1016\/j.bbamcr.2012.10.030","article-title":"Identifying protein partners of CLN8, an ER-resident protein involved in neuronal ceroid lipofuscinosis","volume":"1833","author":"Passantino","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbadis.2013.01.019_bb1185","doi-asserted-by":"crossref","first-page":"377","DOI":"10.1002\/ajh.23118","article-title":"Genome-wide association study of N370S homozygous Gaucher disease reveals the candidacy of CLN8 gene as a genetic modifier contributing to extreme phenotypic variation","volume":"87","author":"Zhang","year":"2012","journal-title":"Am. J. Hematol."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1190","doi-asserted-by":"crossref","first-page":"342","DOI":"10.1002\/ana.20187","article-title":"Impaired cell adhesion and apoptosis in a novel CLN9 Batten disease variant","volume":"56","author":"Schulz","year":"2004","journal-title":"Ann. Neurol."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1195","doi-asserted-by":"crossref","first-page":"988","DOI":"10.1086\/504159","article-title":"Cathepsin D deficiency is associated with a human neurodegenerative disorder","volume":"78","author":"Steinfeld","year":"2006","journal-title":"Am. J. Hum. Genet."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1200","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1002\/aja.1001660404","article-title":"The distribution of cathepsin D in rat tissues determined by immunocytochemistry","volume":"166","author":"Whitaker","year":"1983","journal-title":"Am. J. Anat."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1205","doi-asserted-by":"crossref","first-page":"1161","DOI":"10.1111\/j.1471-4159.1983.tb08108.x","article-title":"Postnatal changes in cathepsin D in rat neural tissue","volume":"40","author":"Snyder","year":"1983","journal-title":"J. Neurochem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1210","doi-asserted-by":"crossref","first-page":"4910","DOI":"10.1073\/pnas.82.15.4910","article-title":"Cloning and sequence analysis of cDNA for human cathepsin D","volume":"82","author":"Faust","year":"1985","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1215","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1093\/jb\/mvj037","article-title":"Processing of human cathepsin D is independent of its catalytic function and auto-activation: involvement of cathepsins L and B","volume":"139","author":"Laurent-Matha","year":"2006","journal-title":"J. Biochem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1220","doi-asserted-by":"crossref","first-page":"3215","DOI":"10.1016\/S0021-9258(18)89493-5","article-title":"Processing of human cathepsin D in lysosomes in vitro","volume":"260","author":"Gieselmann","year":"1985","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1225","first-page":"316","article-title":"On the effects of weak bases and monensin on sorting and processing of lysosomal enzymes in human cells","volume":"43","author":"Braulke","year":"1987","journal-title":"Eur. J. Cell Biol."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1230","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1007\/s004410051061","article-title":"Human and hamster procathepsin D, although equally tagged with mannose-6-phosphate, are differentially targeted to lysosomes in transfected BHK cells","volume":"292","author":"Isidoro","year":"1998","journal-title":"Cell Tissue Res."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1235","doi-asserted-by":"crossref","first-page":"2661","DOI":"10.1093\/brain\/aws209","article-title":"Lysosomal dysfunction causes neurodegeneration in mucolipidosis II \u2018knock-in\u2019 mice","volume":"135","author":"Kollmann","year":"2012","journal-title":"Brain"},{"key":"10.1016\/j.bbadis.2013.01.019_bb1240","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1016\/j.critrevonc.2008.02.008","article-title":"Cathepsin D\u2014many functions of one aspartic protease","volume":"68","author":"Benes","year":"2008","journal-title":"Crit. Rev. Oncol. Hematol."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1245","doi-asserted-by":"crossref","first-page":"208","DOI":"10.1016\/j.canlet.2012.04.012","article-title":"Cathepsin D inhibits oxidative stress-induced cell death via activation of autophagy in cancer cells","volume":"323","author":"Hah","year":"2012","journal-title":"Cancer Lett."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1250","doi-asserted-by":"crossref","first-page":"6898","DOI":"10.1523\/JNEUROSCI.20-18-06898.2000","article-title":"Cathepsin D deficiency induces lysosomal storage with ceroid lipofuscin in mouse CNS neurons","volume":"20","author":"Koike","year":"2000","journal-title":"J. Neurosci."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1255","doi-asserted-by":"crossref","first-page":"2081","DOI":"10.1523\/JNEUROSCI.5577-06.2007","article-title":"Cathepsin D deficiency induces persistent neurodegeneration in the absence of Bax-dependent apoptosis","volume":"27","author":"Shacka","year":"2007","journal-title":"J. Neurosci."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1260","doi-asserted-by":"crossref","first-page":"6920","DOI":"10.1038\/sj.onc.1204843","article-title":"A mutated cathepsin-D devoid of its catalytic activity stimulates the growth of cancer cells","volume":"20","author":"Glondu","year":"2001","journal-title":"Oncogene"},{"key":"10.1016\/j.bbadis.2013.01.019_bb1265","doi-asserted-by":"crossref","first-page":"489","DOI":"10.1083\/jcb.200403078","article-title":"Catalytically inactive human cathepsin D triggers fibroblast invasive growth","volume":"168","author":"Laurent-Matha","year":"2005","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1270","doi-asserted-by":"crossref","first-page":"1635","DOI":"10.1016\/j.biochi.2010.05.009","article-title":"Pathophysiological functions of cathepsin D: targeting its catalytic activity versus its protein binding activity?","volume":"92","author":"Masson","year":"2010","journal-title":"Biochimie"},{"key":"10.1016\/j.bbadis.2013.01.019_bb1275","doi-asserted-by":"crossref","first-page":"3135","DOI":"10.1021\/pr060363j","article-title":"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes","volume":"5","author":"Chi","year":"2006","journal-title":"J. Proteome Res."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1280","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1016\/j.bbrc.2008.08.099","article-title":"Cathepsin D: a cellular roadmap","volume":"376","author":"Zaidi","year":"2008","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1285","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1111\/j.1432-1033.1994.00265.x","article-title":"Processing of the pre-beta-amyloid protein by cathepsin D is enhanced by a familial Alzheimer's disease mutation","volume":"224","author":"Dreyer","year":"1994","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1290","doi-asserted-by":"crossref","first-page":"20198","DOI":"10.1016\/S0021-9258(18)54909-7","article-title":"Thyroglobulin processing by thyroidal proteases. Major sites of cleavage by cathepsins B, D, and L","volume":"266","author":"Dunn","year":"1991","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1295","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1042\/BJ20040175","article-title":"Purified recombinant human prosaposin forms oligomers that bind procathepsin D and affect its autoactivation","volume":"383","author":"Gopalakrishnan","year":"2004","journal-title":"Biochem. J."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1300","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1016\/0014-5793(91)80295-E","article-title":"Inactivation of human cystatin C and kininogen by human cathepsin D","volume":"280","author":"Lenarcic","year":"1991","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1305","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1093\/oxfordjournals.jbchem.a022728","article-title":"Lysosomal cysteine protease, cathepsin B, is targeted to lysosomes by the mannose 6-phosphate-independent pathway in rat hepatocytes: site-specific phosphorylation in oligosaccharides of the proregion","volume":"128","author":"Tanaka","year":"2000","journal-title":"J. Biochem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1310","doi-asserted-by":"crossref","first-page":"981","DOI":"10.1038\/nature07767","article-title":"APP binds DR6 to trigger axon pruning and neuron death via distinct caspases","volume":"457","author":"Nikolaev","year":"2009","journal-title":"Nature"},{"key":"10.1016\/j.bbadis.2013.01.019_bb1315","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1007\/BF00915809","article-title":"Neutrophil chemotactic activity is modulated by human cystatin C, an inhibitor of cysteine proteases","volume":"14","author":"Leung-Tack","year":"1990","journal-title":"Inflammation"},{"key":"10.1016\/j.bbadis.2013.01.019_bb1320","doi-asserted-by":"crossref","first-page":"2057","DOI":"10.1016\/j.bbamem.2006.05.027","article-title":"Sphingolipid metabolism diseases","volume":"1758","author":"Kolter","year":"2006","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbadis.2013.01.019_bb1325","doi-asserted-by":"crossref","first-page":"3202","DOI":"10.1038\/onc.2011.501","article-title":"Cathepsin D is partly endocytosed by the LRP1 receptor and inhibits LRP1-regulated intramembrane proteolysis","volume":"31","author":"Derocq","year":"2012","journal-title":"Oncogene"},{"key":"10.1016\/j.bbadis.2013.01.019_bb1330","series-title":"Medical Physiology: A Cellular and Molecular Approach","first-page":"1300","article-title":"Synthesis of thyroid hormones","author":"Boron","year":"2003"},{"key":"10.1016\/j.bbadis.2013.01.019_bb1335","doi-asserted-by":"crossref","first-page":"1102","DOI":"10.1016\/j.ajhg.2012.04.021","article-title":"Strikingly different clinicopathological phenotypes determined by progranulin-mutation dosage","volume":"90","author":"Smith","year":"2012","journal-title":"Am. J. Hum. Genet."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1340","doi-asserted-by":"crossref","first-page":"999","DOI":"10.1177\/002215540004800713","article-title":"Cellular localization of gene expression for progranulin","volume":"48","author":"Daniel","year":"2000","journal-title":"J. Histochem. Cytochem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1345","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1262\/jrd.10-116S","article-title":"Age-dependent changes in progranulin expression in the mouse brain","volume":"57","author":"Matsuwaki","year":"2011","journal-title":"J. Reprod. Dev."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1350","doi-asserted-by":"crossref","first-page":"3931","DOI":"10.1002\/cne.22430","article-title":"Progranulin expression in the developing and adult murine brain","volume":"518","author":"Petkau","year":"2010","journal-title":"J. Comp. Neurol."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1355","doi-asserted-by":"crossref","first-page":"7912","DOI":"10.1073\/pnas.87.20.7912","article-title":"Epithelins 1 and 2: isolation and characterization of two cysteine-rich growth-modulating proteins","volume":"87","author":"Shoyab","year":"1990","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1360","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1007\/s12031-011-9553-z","article-title":"Cellular effects of progranulin in health and disease","volume":"45","author":"De Muynck","year":"2011","journal-title":"J. Mol. Neurosci."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1365","doi-asserted-by":"crossref","first-page":"538","DOI":"10.1007\/s12031-011-9569-4","article-title":"Structure, function, and mechanism of progranulin; the brain and beyond","volume":"45","author":"Toh","year":"2011","journal-title":"J. Mol. Neurosci."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1370","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1038\/nm816","article-title":"Progranulin is a mediator of the wound response","volume":"9","author":"He","year":"2003","journal-title":"Nat. Med."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1375","doi-asserted-by":"crossref","first-page":"1245","DOI":"10.1002\/bies.200900086","article-title":"The granulin gene family: from cancer to dementia","volume":"31","author":"Bateman","year":"2009","journal-title":"Bioessays"},{"key":"10.1016\/j.bbadis.2013.01.019_bb1380","doi-asserted-by":"crossref","first-page":"711","DOI":"10.1016\/j.nbd.2011.10.016","article-title":"Synaptic dysfunction in progranulin-deficient mice","volume":"45","author":"Petkau","year":"2012","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1385","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1084\/jem.20091568","article-title":"Exaggerated inflammation, impaired host defense, and neuropathology in progranulin-deficient mice","volume":"207","author":"Yin","year":"2010","journal-title":"J. Exp. Med."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1390","doi-asserted-by":"crossref","first-page":"1030","DOI":"10.1016\/j.neuron.2011.07.021","article-title":"Functional genomic analyses identify pathways dysregulated by progranulin deficiency, implicating Wnt signaling","volume":"71","author":"Rosen","year":"2011","journal-title":"Neuron"},{"key":"10.1016\/j.bbadis.2013.01.019_bb1395","doi-asserted-by":"crossref","first-page":"478","DOI":"10.1126\/science.1199214","article-title":"The growth factor progranulin binds to TNF receptors and is therapeutic against inflammatory arthritis in mice","volume":"332","author":"Tang","year":"2011","journal-title":"Science"},{"key":"10.1016\/j.bbadis.2013.01.019_bb1400","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0898-6568(00)00130-3","article-title":"Sortilin\/neurotensin receptor-3: a new tool to investigate neurotensin signaling and cellular trafficking?","volume":"13","author":"Mazella","year":"2001","journal-title":"Cell. Signal."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1405","doi-asserted-by":"crossref","first-page":"843","DOI":"10.1038\/nature02319","article-title":"Sortilin is essential for proNGF-induced neuronal cell death","volume":"427","author":"Nykjaer","year":"2004","journal-title":"Nature"},{"key":"10.1016\/j.bbadis.2013.01.019_bb1410","doi-asserted-by":"crossref","first-page":"889","DOI":"10.1111\/j.1600-0854.2006.00429.x","article-title":"The lysosomal trafficking of acid sphingomyelinase is mediated by sortilin and mannose 6-phosphate receptor","volume":"7","author":"Ni","year":"2006","journal-title":"Traffic"},{"key":"10.1016\/j.bbadis.2013.01.019_bb1415","doi-asserted-by":"crossref","first-page":"890","DOI":"10.1016\/j.ajhg.2010.11.002","article-title":"Genome-wide screen identifies rs646776 near sortilin as a regulator of progranulin levels in human plasma","volume":"87","author":"Carrasquillo","year":"2010","journal-title":"Am. J. Hum. Genet."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1420","doi-asserted-by":"crossref","first-page":"654","DOI":"10.1016\/j.neuron.2010.09.034","article-title":"Sortilin-mediated endocytosis determines levels of the frontotemporal dementia protein, progranulin","volume":"68","author":"Hu","year":"2010","journal-title":"Neuron"},{"key":"10.1016\/j.bbadis.2013.01.019_bb1425","doi-asserted-by":"crossref","first-page":"2646","DOI":"10.1093\/hmg\/dds089","article-title":"Mutation of the parkinsonism gene ATP13A2 causes neuronal ceroid-lipofuscinosis","volume":"21","author":"Bras","year":"2012","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1430","doi-asserted-by":"crossref","first-page":"1557","DOI":"10.1212\/01.wnl.0000260963.08711.08","article-title":"ATP13A2 missense mutations in juvenile parkinsonism and young onset Parkinson disease","volume":"68","author":"Di Fonzo","year":"2007","journal-title":"Neurology"},{"key":"10.1016\/j.bbadis.2013.01.019_bb1435","doi-asserted-by":"crossref","first-page":"2104","DOI":"10.1002\/mds.22728","article-title":"ATP13A2 variants in early-onset Parkinson's disease patients and controls","volume":"24","author":"Djarmati","year":"2009","journal-title":"Mov. Disord."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1440","doi-asserted-by":"crossref","first-page":"1491","DOI":"10.1212\/01.wnl.0000310427.72236.68","article-title":"PARK9-linked parkinsonism in eastern Asia: mutation detection in ATP13A2 and clinical phenotype","volume":"70","author":"Ning","year":"2008","journal-title":"Neurology"},{"key":"10.1016\/j.bbadis.2013.01.019_bb1445","doi-asserted-by":"crossref","first-page":"1184","DOI":"10.1038\/ng1884","article-title":"Hereditary parkinsonism with dementia is caused by mutations in ATP13A2, encoding a lysosomal type 5 P-type ATPase","volume":"38","author":"Ramirez","year":"2006","journal-title":"Nat. Genet."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1450","doi-asserted-by":"crossref","first-page":"979","DOI":"10.1002\/mds.22947","article-title":"ATP13A2 mutations (PARK9) cause neurodegeneration with brain iron accumulation","volume":"25","author":"Schneider","year":"2010","journal-title":"Mov. Disord."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1455","doi-asserted-by":"crossref","first-page":"468","DOI":"10.1016\/j.nbd.2011.02.009","article-title":"A truncating mutation in ATP13A2 is responsible for adult-onset neuronal ceroid lipofuscinosis in Tibetan terriers","volume":"42","author":"Farias","year":"2011","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1460","doi-asserted-by":"crossref","first-page":"e1002304","DOI":"10.1371\/journal.pgen.1002304","article-title":"A one base pair deletion in the canine ATP13A2 gene causes exon skipping and late-onset neuronal ceroid lipofuscinosis in the Tibetan terrier","volume":"7","author":"W\u00f6hlke","year":"2011","journal-title":"PLoS Genet."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1465","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1007\/s10048-010-0259-0","article-title":"Novel ATP13A2 (PARK9) homozygous mutation in a family with marked phenotype variability","volume":"12","author":"Santoro","year":"2011","journal-title":"Neurogenetics"},{"key":"10.1016\/j.bbadis.2013.01.019_bb1470","doi-asserted-by":"crossref","first-page":"731","DOI":"10.1016\/j.bbrc.2004.08.156","article-title":"Characterization of the P5 subfamily of P-type transport ATPases in mice","volume":"323","author":"Schultheis","year":"2004","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1475","doi-asserted-by":"crossref","first-page":"308","DOI":"10.1038\/ng.300","article-title":"Alpha-synuclein is part of a diverse and highly conserved interaction network that includes PARK9 and manganese toxicity","volume":"41","author":"Gitler","year":"2009","journal-title":"Nat. Genet."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1480","doi-asserted-by":"crossref","first-page":"1725","DOI":"10.1093\/hmg\/ddr606","article-title":"PARK9-associated ATP13A2 localizes to intracellular acidic vesicles and regulates cation homeostasis and neuronal integrity","volume":"21","author":"Ramonet","year":"2012","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1485","doi-asserted-by":"crossref","first-page":"198","DOI":"10.1016\/j.bbrc.2009.03.151","article-title":"Cd2+, Mn2+, Ni2+ and Se2+ toxicity to Saccharomyces cerevisiae lacking YPK9p the orthologue of human ATP13A2","volume":"383","author":"Schmidt","year":"2009","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1490","doi-asserted-by":"crossref","first-page":"29654","DOI":"10.1074\/jbc.M111.233874","article-title":"Regulation of intracellular manganese homeostasis by Kufor\u2013Rakeb syndrome-associated ATP13A2 protein","volume":"286","author":"Tan","year":"2011","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1495","doi-asserted-by":"crossref","first-page":"3785","DOI":"10.1093\/hmg\/dds206","article-title":"Identification of novel ATP13A2 interactors and their role in alpha-synuclein misfolding and toxicity","volume":"21","author":"Usenovic","year":"2012","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1500","doi-asserted-by":"crossref","first-page":"9611","DOI":"10.1073\/pnas.1112368109","article-title":"Loss of P-type ATPase ATP13A2\/PARK9 function induces general lysosomal deficiency and leads to Parkinson disease neurodegeneration","volume":"109","author":"Dehay","year":"2012","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1505","doi-asserted-by":"crossref","first-page":"4240","DOI":"10.1523\/JNEUROSCI.5575-11.2012","article-title":"Deficiency of ATP13A2 leads to lysosomal dysfunction, alpha-synuclein accumulation, and neurotoxicity","volume":"32","author":"Usenovic","year":"2012","journal-title":"J. Neurosci."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1510","doi-asserted-by":"crossref","DOI":"10.1074\/mcp.M110.003590","article-title":"Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level","volume":"10","author":"Danielsen","year":"2011","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.bbadis.2013.01.019_bb1515","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1016\/j.molcel.2011.08.025","article-title":"Systematic and quantitative assessment of the ubiquitin-modified proteome","volume":"44","author":"Kim","year":"2011","journal-title":"Mol. Cell"},{"key":"10.1016\/j.bbadis.2013.01.019_bb1520","doi-asserted-by":"crossref","first-page":"rs8","DOI":"10.1126\/scisignal.2001699","article-title":"A directed protein interaction network for investigating intracellular signal transduction","volume":"4","author":"Vinayagam","year":"2011","journal-title":"Sci. Signal."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1525","doi-asserted-by":"crossref","DOI":"10.1074\/mcp.M111.013284","article-title":"A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles","volume":"10","author":"Wagner","year":"2011","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.bbadis.2013.01.019_bb1530","doi-asserted-by":"crossref","unstructured":"K.R. Smith, H.H. Dahl, L. Canafoglia, E. Andermann, J. Damiano, M. Morbin, A.C. Bruni, G. Giaccone, P. Cossette, P. Saftig, J. Gr\u00f6tzinger, M. Schwake, F. Andermann, J.F. Staropoli, K.B. Sims, S.E. Mole, S. Franceschetti, N.A. Alexander, J.D. Cooper, H.A. Chapman, S. Carpenter, S.F. Berkovic, M. Bahlo, Cathepsin F mutations cause Type B Kufs disease, an adult-onset neuronal ceroid lipofuscinosis, Hum. Mol. Genet. (in press), http:\/\/dx.doi.org\/10.1093\/hmg\/dds558.","DOI":"10.1093\/hmg\/dds558"},{"key":"10.1016\/j.bbadis.2013.01.019_bb1535","doi-asserted-by":"crossref","first-page":"2309","DOI":"10.1128\/MCB.26.6.2309-2316.2006","article-title":"Murine cathepsin F deficiency causes neuronal lipofuscinosis and late-onset neurological disease","volume":"26","author":"Tang","year":"2006","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1540","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1006\/bbrc.1999.0461","article-title":"Full-length cDNA of human cathepsin F predicts the presence of a cystatin domain at the N-terminus of the cysteine protease zymogen","volume":"257","author":"N\u00e4gler","year":"1999","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1545","doi-asserted-by":"crossref","first-page":"13800","DOI":"10.1074\/jbc.274.20.13800","article-title":"Molecular cloning and structural and functional characterization of human cathepsin F, a new cysteine proteinase of the papain family with a long propeptide domain","volume":"274","author":"Santamaria","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1550","doi-asserted-by":"crossref","first-page":"32000","DOI":"10.1074\/jbc.273.48.32000","article-title":"Human cathepsin F. Molecular cloning, functional expression, tissue localization, and enzymatic characterization","volume":"273","author":"Wang","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1555","doi-asserted-by":"crossref","first-page":"1439","DOI":"10.1515\/BC.1999.185","article-title":"The human cathepsin F gene\u2014a fusion product between an ancestral cathepsin and cystatin gene","volume":"380","author":"Wex","year":"1999","journal-title":"Biol. Chem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1560","doi-asserted-by":"crossref","first-page":"1177","DOI":"10.1084\/jem.191.7.1177","article-title":"Role for cathepsin F in invariant chain processing and major histocompatibility complex class II peptide loading by macrophages","volume":"191","author":"Shi","year":"2000","journal-title":"J. Exp. Med."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1565","doi-asserted-by":"crossref","first-page":"1019","DOI":"10.1016\/j.bbrc.2003.11.020","article-title":"Cathepsins F and S block HDL3-induced cholesterol efflux from macrophage foam cells","volume":"312","author":"Lindstedt","year":"2003","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1570","doi-asserted-by":"crossref","first-page":"34776","DOI":"10.1074\/jbc.M310814200","article-title":"Cysteine protease cathepsin F is expressed in human atherosclerotic lesions, is secreted by cultured macrophages, and modifies low density lipoprotein particles in vitro","volume":"279","author":"O\u00f6rni","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1575","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1007\/s12035-011-8194-0","article-title":"Progressive myoclonic epilepsy-associated gene KCTD7 is a regulator of potassium conductance in neurons","volume":"44","author":"Azizieh","year":"2011","journal-title":"Mol. Neurobiol."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1580","doi-asserted-by":"crossref","first-page":"202","DOI":"10.1016\/j.ajhg.2012.05.023","article-title":"A homozygous mutation in KCTD7 links neuronal ceroid lipofuscinosis to the ubiquitin\u2013proteasome system","volume":"91","author":"Staropoli","year":"2012","journal-title":"Am. J. Hum. Genet."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1585","doi-asserted-by":"crossref","first-page":"1190","DOI":"10.1016\/j.cell.2007.11.025","article-title":"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer","volume":"131","author":"Rikova","year":"2007","journal-title":"Cell"},{"key":"10.1016\/j.bbadis.2013.01.019_bb1590","doi-asserted-by":"crossref","first-page":"579","DOI":"10.1002\/ana.21121","article-title":"Mutation of a potassium channel-related gene in progressive myoclonic epilepsy","volume":"61","author":"Van Bogaert","year":"2007","journal-title":"Ann. Neurol."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1595","doi-asserted-by":"crossref","first-page":"R82","DOI":"10.1186\/gb-2005-6-10-r82","article-title":"Sequence and structural analysis of BTB domain proteins","volume":"6","author":"Stogios","year":"2005","journal-title":"Genome Biol."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1600","doi-asserted-by":"crossref","first-page":"3900","DOI":"10.1111\/j.1742-4658.2008.06537.x","article-title":"KCTD5, a putative substrate adaptor for cullin3 ubiquitin ligases","volume":"275","author":"Bayon","year":"2008","journal-title":"FEBS J."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1605","doi-asserted-by":"crossref","first-page":"5325","DOI":"10.1242\/jcs.02635","article-title":"Downregulation of the HERG (KCNH2) K(+) channel by ceramide: evidence for ubiquitin-mediated lysosomal degradation","volume":"118","author":"Chapman","year":"2005","journal-title":"J. Cell Sci."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1610","doi-asserted-by":"crossref","first-page":"12135","DOI":"10.1074\/jbc.M609385200","article-title":"Regulation of the voltage-gated K(+) channels KCNQ2\/3 and KCNQ3\/5 by ubiquitination. Novel role for Nedd4-2","volume":"282","author":"Ekberg","year":"2007","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1615","doi-asserted-by":"crossref","first-page":"40164","DOI":"10.1074\/jbc.M608194200","article-title":"Actinfilin is a Cul3 substrate adaptor, linking GluR6 kainate receptor subunits to the ubiquitin\u2013proteasome pathway","volume":"281","author":"Salinas","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1620","doi-asserted-by":"crossref","first-page":"4053","DOI":"10.1002\/pmic.201000196","article-title":"The proteome of lysosomes","volume":"10","author":"Schr\u00f6der","year":"2010","journal-title":"Proteomics"},{"key":"10.1016\/j.bbadis.2013.01.019_bb1625","doi-asserted-by":"crossref","first-page":"1228","DOI":"10.1097\/NEN.0b013e3181ffe742","article-title":"Distinct neuropathologic phenotypes after disrupting the chloride transport proteins ClC-6 or ClC-7\/Ostm1","volume":"69","author":"Pressey","year":"2010","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"10.1016\/j.bbadis.2013.01.019_bb1630","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1126\/science.1174447","article-title":"A gene network regulating lysosomal biogenesis and function","volume":"325","author":"Sardiello","year":"2009","journal-title":"Science"},{"key":"10.1016\/j.bbadis.2013.01.019_bb1635","doi-asserted-by":"crossref","first-page":"3852","DOI":"10.1093\/hmg\/ddr306","article-title":"Characterization of the CLEAR network reveals an integrated control of cellular clearance pathways","volume":"20","author":"Palmieri","year":"2011","journal-title":"Hum. Mol. Genet."}],"container-title":["Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0925443913000331?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0925443913000331?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2022,2,8]],"date-time":"2022-02-08T00:25:13Z","timestamp":1644279913000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0925443913000331"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2013,11]]},"references-count":327,"journal-issue":{"issue":"11","published-print":{"date-parts":[[2013,11]]}},"alternative-id":["S0925443913000331"],"URL":"https:\/\/doi.org\/10.1016\/j.bbadis.2013.01.019","relation":{},"ISSN":["0925-4439"],"issn-type":[{"value":"0925-4439","type":"print"}],"subject":[],"published":{"date-parts":[[2013,11]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Cell biology and function of neuronal ceroid lipofuscinosis-related proteins","name":"articletitle","label":"Article Title"},{"value":"Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bbadis.2013.01.019","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2013 Elsevier B.V.","name":"copyright","label":"Copyright"}]}}