{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T03:37:27Z","timestamp":1791171447899,"version":"4.1.0"},"reference-count":95,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2015,6,1]],"date-time":"2015-06-01T00:00:00Z","timestamp":1433116800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/501100002342","name":"Finnish Academy of Science","doi-asserted-by":"publisher","award":["128600"],"award-info":[{"award-number":["128600"]}],"id":[{"id":"10.13039\/501100002342","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004963","name":"European Union Seventh Framework Programme","doi-asserted-by":"publisher","award":["281234"],"award-info":[{"award-number":["281234"]}],"id":[{"id":"10.13039\/501100004963","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Kliinisen kemian tutkimuss\u00e4\u00e4ti\u00f6"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Proteomics"],"published-print":{"date-parts":[[2015,6]]},"DOI":"10.1016\/j.jprot.2015.03.038","type":"journal-article","created":{"date-parts":[[2015,4,11]],"date-time":"2015-04-11T13:48:17Z","timestamp":1428760097000},"page":"42-53","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":63,"special_numbering":"C","title":["Proteomic analysis of the palmitoyl protein thioesterase 1 interactome in SH-SY5Y human neuroblastoma cells"],"prefix":"10.1016","volume":"123","author":[{"given":"Enzo","family":"Scifo","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Agnieszka","family":"Szwajda","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rabah","family":"Soliymani","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Francesco","family":"Pezzini","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marzia","family":"Bianchi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Arvydas","family":"Dapkunas","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Janusz","family":"D\u0119bski","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kristiina","family":"Uusi-Rauva","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Micha\u0142","family":"Dadlez","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anne-Claude","family":"Gingras","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jaana","family":"Tyynel\u00e4","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alessandro","family":"Simonati","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anu","family":"Jalanko","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marc H.","family":"Baumann","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maciej","family":"Lalowski","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jprot.2015.03.038_bb0005","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1038\/415141a","article-title":"Functional organization of the yeast proteome by systematic analysis of protein complexes","volume":"415","author":"Gavin","year":"2002","journal-title":"Nature"},{"key":"10.1016\/j.jprot.2015.03.038_bb0010","doi-asserted-by":"crossref","first-page":"637","DOI":"10.1038\/nature04670","article-title":"Global landscape of protein complexes in the yeast Saccharomyces cerevisiae","volume":"440","author":"Krogan","year":"2006","journal-title":"Nature"},{"key":"10.1016\/j.jprot.2015.03.038_bb0015","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1038\/msb4100134","article-title":"Large-scale mapping of human protein\u2013protein interactions by mass spectrometry","volume":"3","author":"Ewing","year":"2007","journal-title":"Mol Syst Biol"},{"key":"10.1016\/j.jprot.2015.03.038_bb0020","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1016\/S0092-8674(00)80922-8","article-title":"The cell as a collection of protein machines: preparing the next generation of molecular biologists","volume":"92","author":"Alberts","year":"1998","journal-title":"Cell"},{"key":"10.1016\/j.jprot.2015.03.038_bb0025","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1038\/nmeth.1322","article-title":"Universal sample preparation method for proteome analysis","volume":"6","author":"Wisniewski","year":"2009","journal-title":"Nat Methods"},{"key":"10.1016\/j.jprot.2015.03.038_bb0030","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.jprot.2015.03.038_bb0035","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1016\/S0065-2660(01)45004-8","article-title":"Positional candidate gene cloning of CLN1","volume":"45","author":"Hofmann","year":"2001","journal-title":"Adv Genet"},{"key":"10.1016\/j.jprot.2015.03.038_bb0040","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.jprot.2015.03.038_bb0045","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.jprot.2015.03.038_bb0050","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.jprot.2015.03.038_bb0055","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.jprot.2015.03.038_bb0060","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.jprot.2015.03.038_bb0065","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.jprot.2015.03.038_bb0070","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.jprot.2015.03.038_bb0075","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.jprot.2015.03.038_bb0080","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.jprot.2015.03.038_bb0085","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.jprot.2015.03.038_bb0090","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.jprot.2015.03.038_bb0095","doi-asserted-by":"crossref","DOI":"10.4161\/fly.26630","article-title":"Mutations in palmitoyl-protein thioesterase 1 alter exocytosis and endocytosis at synapses in Drosophila larvae","volume":"7","author":"Aby","year":"2013","journal-title":"Fly (Austin)"},{"key":"10.1016\/j.jprot.2015.03.038_bb0100","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.jprot.2015.03.038_bb0105","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.jprot.2015.03.038_bb0110","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1172\/JCI3112","article-title":"Molecular genetics of palmitoyl-protein thioesterase deficiency in the U.S","volume":"102","author":"Das","year":"1998","journal-title":"J Clin Invest"},{"key":"10.1016\/j.jprot.2015.03.038_bb0115","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1186\/1750-1172-8-19","article-title":"Molecular epidemiology of childhood neuronal ceroid-lipofuscinosis in Italy","volume":"8","author":"Santorelli","year":"2013","journal-title":"Orphanet J Rare Dis"},{"key":"10.1016\/j.jprot.2015.03.038_bb0120","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1016\/S0387-7604(88)80075-5","article-title":"Neuronal ceroid-lipofuscinoses in childhood","volume":"10","author":"Santavuori","year":"1988","journal-title":"Brain Dev"},{"key":"10.1016\/j.jprot.2015.03.038_bb0125","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1016\/0014-5793(93)80908-D","article-title":"Storage of saposins A and D in infantile neuronal ceroid-lipofuscinosis","volume":"330","author":"Tyynela","year":"1993","journal-title":"FEBS Lett"},{"key":"10.1016\/j.jprot.2015.03.038_bb0130","doi-asserted-by":"crossref","first-page":"13566","DOI":"10.1073\/pnas.251485198","article-title":"Disruption of PPT1 or PPT2 causes neuronal ceroid lipofuscinosis in knockout mice","volume":"98","author":"Gupta","year":"2001","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.jprot.2015.03.038_bb0135","doi-asserted-by":"crossref","first-page":"226","DOI":"10.1016\/j.nbd.2004.08.013","article-title":"Mice with PPt1Deltaex4 mutation replicate the INCL phenotype and show an inflammation-associated loss of interneurons","volume":"18","author":"Jalanko","year":"2005","journal-title":"Neurobiol Dis"},{"key":"10.1016\/j.jprot.2015.03.038_bb0140","doi-asserted-by":"crossref","first-page":"346","DOI":"10.1016\/j.nbd.2004.02.010","article-title":"Regional and cellular neuropathology in the palmitoyl protein thioesterase-1 null mutant mouse model of infantile neuronal ceroid lipofuscinosis","volume":"16","author":"Bible","year":"2004","journal-title":"Neurobiol Dis"},{"key":"10.1016\/j.jprot.2015.03.038_bb0145","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1093\/hmg\/ddu428","article-title":"The novel Cln1R151X mouse model of infantile neuronal ceroid lipofuscinosis (INCL) for testing nonsense suppression therapy","volume":"24","author":"Miller","year":"2015","journal-title":"Hum Mol Genet"},{"key":"10.1016\/j.jprot.2015.03.038_bb0150","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.jprot.2015.03.038_bb0155","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.jprot.2015.03.038_bb0160","doi-asserted-by":"crossref","first-page":"205","DOI":"10.4161\/cc.6.2.3742","article-title":"Large-scale identification of c-MYC-associated proteins using a combined TAP\/MudPIT approach","volume":"6","author":"Koch","year":"2007","journal-title":"Cell Cycle"},{"key":"10.1016\/j.jprot.2015.03.038_bb0165","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.jprot.2015.03.038_bb0170","doi-asserted-by":"crossref","first-page":"1773","DOI":"10.1021\/pr2010204","article-title":"Proteomic identification of common SCF ubiquitin ligase FBXO6-interacting glycoproteins in three kinds of cells","volume":"11","author":"Liu","year":"2012","journal-title":"J Proteome Res"},{"key":"10.1016\/j.jprot.2015.03.038_bb0175","doi-asserted-by":"crossref","first-page":"1068","DOI":"10.1016\/j.cell.2012.08.011","article-title":"A census of human soluble protein complexes","volume":"150","author":"Havugimana","year":"2012","journal-title":"Cell"},{"key":"10.1016\/j.jprot.2015.03.038_bb0180","doi-asserted-by":"crossref","first-page":"2107","DOI":"10.1002\/pmic.201100487","article-title":"Proteomic analysis of alpha4beta1 integrin adhesion complexes reveals alpha-subunit-dependent protein recruitment","volume":"12","author":"Byron","year":"2012","journal-title":"Proteomics"},{"key":"10.1016\/j.jprot.2015.03.038_bb0185","doi-asserted-by":"crossref","first-page":"536","DOI":"10.1038\/msb.2011.67","article-title":"Toward an understanding of the protein interaction network of the human liver","volume":"7","author":"Wang","year":"2011","journal-title":"Mol Syst Biol"},{"key":"10.1016\/j.jprot.2015.03.038_bb0190","doi-asserted-by":"crossref","first-page":"1243","DOI":"10.1016\/j.cellsig.2014.02.011","article-title":"A systems wide mass spectrometric based linear motif screen to identify dominant in-vivo interacting proteins for the ubiquitin ligase MDM2","volume":"26","author":"Nicholson","year":"2014","journal-title":"Cell Signal"},{"key":"10.1016\/j.jprot.2015.03.038_bb0195","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.jprot.2015.03.038_bb0200","doi-asserted-by":"crossref","first-page":"2101","DOI":"10.1021\/pr301125k","article-title":"Drafting the CLN3 protein interactome in SH-SY5Y human neuroblastoma cells: a label-free quantitative proteomics approach","volume":"12","author":"Scifo","year":"2013","journal-title":"J Proteome Res"},{"key":"10.1016\/j.jprot.2015.03.038_bb0205","series-title":"Data in brief","doi-asserted-by":"crossref","DOI":"10.1016\/j.dib.2015.05.016","article-title":"Quantitative analysis of PPT1 interactome in human neuroblastoma cells","author":"Scifo","year":"2015"},{"key":"10.1016\/j.jprot.2015.03.038_bb0210","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.jprot.2015.03.038_bb0215","doi-asserted-by":"crossref","first-page":"2498","DOI":"10.1101\/gr.1239303","article-title":"Cytoscape: a software environment for integrated models of biomolecular interaction networks","volume":"13","author":"Shannon","year":"2003","journal-title":"Genome Res"},{"key":"10.1016\/j.jprot.2015.03.038_bb0220","doi-asserted-by":"crossref","first-page":"1091","DOI":"10.1093\/bioinformatics\/btp101","article-title":"ClueGO: a cytoscape plug-in to decipher functionally grouped gene ontology and pathway annotation networks","volume":"25","author":"Bindea","year":"2009","journal-title":"Bioinformatics"},{"key":"10.1016\/j.jprot.2015.03.038_bb0225","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1021\/pr8008012","article-title":"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry","volume":"8","author":"Chen","year":"2009","journal-title":"J Proteome Res"},{"key":"10.1016\/j.jprot.2015.03.038_bb0230","doi-asserted-by":"crossref","first-page":"660","DOI":"10.1038\/nbt827","article-title":"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry","volume":"21","author":"Zhang","year":"2003","journal-title":"Nat Biotechnol"},{"key":"10.1016\/j.jprot.2015.03.038_bb0235","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-Akt-caspase pathway in neuroblastoma cells","volume":"74","author":"Cho","year":"2000","journal-title":"J Neurochem"},{"key":"10.1016\/j.jprot.2015.03.038_bb0240","doi-asserted-by":"crossref","first-page":"15830","DOI":"10.1074\/jbc.273.25.15830","article-title":"A cytoplasmic acyl-protein thioesterase that removes palmitate from G protein alpha subunits and p21(RAS)","volume":"273","author":"Duncan","year":"1998","journal-title":"J Biol Chem"},{"key":"10.1016\/j.jprot.2015.03.038_bb0245","doi-asserted-by":"crossref","first-page":"1013","DOI":"10.1038\/nmeth968","article-title":"An efficient tandem affinity purification procedure for interaction proteomics in mammalian cells","volume":"3","author":"Burckstummer","year":"2006","journal-title":"Nat Methods"},{"key":"10.1016\/j.jprot.2015.03.038_bb0250","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1038\/nmeth.1541","article-title":"SAINT: probabilistic scoring of affinity purification-mass spectrometry data","volume":"8","author":"Choi","year":"2011","journal-title":"Nat Methods"},{"key":"10.1016\/j.jprot.2015.03.038_bb0255","doi-asserted-by":"crossref","DOI":"10.1002\/0471250953.bi0815s39","article-title":"Analyzing protein\u2013protein interactions from affinity purification-mass spectrometry data with SAINT","author":"Choi","year":"2012","journal-title":"Curr Protoc Bioinformatics"},{"key":"10.1016\/j.jprot.2015.03.038_bb0260","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/j.jprot.2013.10.023","article-title":"SAINTexpress: improvements and additional features in significance analysis of INTeractome software","volume":"100","author":"Teo","year":"2014","journal-title":"J Proteomics"},{"key":"10.1016\/j.jprot.2015.03.038_bb0265","doi-asserted-by":"crossref","first-page":"9761","DOI":"10.1074\/jbc.273.16.9761","article-title":"Collapsin response mediator protein-2 is associated with neurofibrillary tangles in Alzheimer's disease","volume":"273","author":"Yoshida","year":"1998","journal-title":"J Biol Chem"},{"key":"10.1016\/j.jprot.2015.03.038_bb0270","first-page":"59","article-title":"The molecular mechanism of dopamine-induced apoptosis: identification and characterization of genes that mediate dopamine toxicity","author":"Barzilai","year":"2000","journal-title":"J Neural Transm Suppl"},{"key":"10.1016\/j.jprot.2015.03.038_bb0275","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1002\/ajmg.10196","article-title":"Mutations in the dopamine beta-hydroxylase gene are associated with human norepinephrine deficiency","volume":"108","author":"Kim","year":"2002","journal-title":"Am J Med Genet"},{"key":"10.1016\/j.jprot.2015.03.038_bb0280","doi-asserted-by":"crossref","first-page":"2445","DOI":"10.1002\/pmic.201100668","article-title":"Human and rat brain lipofuscin proteome","volume":"12","author":"Ottis","year":"2012","journal-title":"Proteomics"},{"key":"10.1016\/j.jprot.2015.03.038_bb0285","doi-asserted-by":"crossref","first-page":"433","DOI":"10.1242\/jcs.01622","article-title":"Neurite extension in central neurons: a novel role for the receptor tyrosine kinases Ror1 and Ror2","volume":"118","author":"Paganoni","year":"2005","journal-title":"J Cell Sci"},{"key":"10.1016\/j.jprot.2015.03.038_bb0290","doi-asserted-by":"crossref","first-page":"840","DOI":"10.1016\/j.cub.2004.04.046","article-title":"MAP1B is required for Netrin 1 signaling in neuronal migration and axonal guidance","volume":"14","author":"Del Rio","year":"2004","journal-title":"Curr Biol"},{"key":"10.1016\/j.jprot.2015.03.038_bb0295","series-title":"Proteomic profiling in CLN1 disease brain: an imaging and label-free proteomics approach","author":"Tikka","year":"2014"},{"key":"10.1016\/j.jprot.2015.03.038_bb0300","doi-asserted-by":"crossref","first-page":"D380","DOI":"10.1093\/nar\/gkt984","article-title":"FunCoup 3.0: database of genome-wide functional coupling networks","volume":"42","author":"Schmitt","year":"2014","journal-title":"Nucleic Acids Res"},{"key":"10.1016\/j.jprot.2015.03.038_bb0305","doi-asserted-by":"crossref","first-page":"1508","DOI":"10.1002\/pmic.201000770","article-title":"Label-free quantitative proteomics and SAINT analysis enable interactome mapping for the human Ser\/Thr protein phosphatase 5","volume":"11","author":"Skarra","year":"2011","journal-title":"Proteomics"},{"key":"10.1016\/j.jprot.2015.03.038_bb0310","doi-asserted-by":"crossref","first-page":"4376","DOI":"10.1038\/srep04376","article-title":"Interactome analysis of AMP-activated protein kinase (AMPK)-alpha1 and -beta1 in INS-1 pancreatic beta-cells by affinity purification-mass spectrometry","volume":"4","author":"Moon","year":"2014","journal-title":"Sci Rep"},{"key":"10.1016\/j.jprot.2015.03.038_bb0315","article-title":"Interaction proteomics analysis of polycomb proteins defines distinct PRC1 complexes in mammalian cells","volume":"0","author":"Vandamme","year":"2011","journal-title":"Mol Cell Proteomics"},{"key":"10.1016\/j.jprot.2015.03.038_bb0320","doi-asserted-by":"crossref","first-page":"730","DOI":"10.1038\/nmeth.2557","article-title":"The CRAPome: a contaminant repository for affinity purification-mass spectrometry data","volume":"10","author":"Mellacheruvu","year":"2013","journal-title":"Nat Methods"},{"key":"10.1016\/j.jprot.2015.03.038_bb0325","doi-asserted-by":"crossref","first-page":"589","DOI":"10.1089\/ars.2006.1518","article-title":"Does ORP150\/HSP12A protect dopaminergic neurons against MPTP\/MPP(+)-induced neurotoxicity?","volume":"9","author":"Kitao","year":"2007","journal-title":"Antioxid Redox Signal"},{"key":"10.1016\/j.jprot.2015.03.038_bb0330","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.jprot.2015.03.038_bb0335","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1038\/nature09204","article-title":"Network organization of the human autophagy system","volume":"466","author":"Behrends","year":"2010","journal-title":"Nature"},{"key":"10.1016\/j.jprot.2015.03.038_bb0340","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.jprot.2015.03.038_bb0345","doi-asserted-by":"crossref","first-page":"2786","DOI":"10.1093\/emboj\/19.12.2786","article-title":"A mutation in the ovine cathepsin D gene causes a congenital lysosomal storage disease with profound neurodegeneration","volume":"19","author":"Tyynela","year":"2000","journal-title":"EMBO J"},{"key":"10.1016\/j.jprot.2015.03.038_bb0350","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1007\/s00401-008-0426-7","article-title":"Novel mutation and the first prenatal screening of cathepsin D deficiency (CLN10)","volume":"117","author":"Fritchie","year":"2009","journal-title":"Acta Neuropathol"},{"key":"10.1016\/j.jprot.2015.03.038_bb0355","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.jprot.2015.03.038_bb0360","doi-asserted-by":"crossref","first-page":"639","DOI":"10.1093\/protein\/gzn039","article-title":"CSS-Palm 2.0: an updated software for palmitoylation sites prediction","volume":"21","author":"Ren","year":"2008","journal-title":"Protein Eng Des Sel"},{"key":"10.1016\/j.jprot.2015.03.038_bb0365","doi-asserted-by":"crossref","first-page":"707","DOI":"10.1093\/protein\/gzp055","article-title":"Prediction of palmitoylation sites using the composition of k-spaced amino acid pairs","volume":"22","author":"Wang","year":"2009","journal-title":"Protein Eng Des Sel"},{"key":"10.1016\/j.jprot.2015.03.038_bb0370","doi-asserted-by":"crossref","first-page":"857","DOI":"10.1523\/JNEUROSCI.14-02-00857.1994","article-title":"Microtubule-associated protein 1b (MAP1b) is concentrated in the distal region of growing axons","volume":"14","author":"Black","year":"1994","journal-title":"J Neurosci"},{"key":"10.1016\/j.jprot.2015.03.038_bb0375","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1002\/neu.10283","article-title":"Microtubule-associated protein 1B function during normal development, regeneration, and pathological conditions in the nervous system","volume":"58","author":"Gonzalez-Billault","year":"2004","journal-title":"J Neurobiol"},{"issue":"Pt 2","key":"10.1016\/j.jprot.2015.03.038_bb0380","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1242\/jcs.109.2.467","article-title":"MAP-1B\/TAU functional redundancy during laminin-enhanced axonal growth","volume":"109","author":"DiTella","year":"1996","journal-title":"J Cell Sci"},{"key":"10.1016\/j.jprot.2015.03.038_bb0385","doi-asserted-by":"crossref","first-page":"1134","DOI":"10.1093\/cercor\/bhh213","article-title":"A role of MAP1B in Reelin-dependent neuronal migration","volume":"15","author":"Gonzalez-Billault","year":"2005","journal-title":"Cereb Cortex"},{"key":"10.1016\/j.jprot.2015.03.038_bb0390","doi-asserted-by":"crossref","first-page":"989","DOI":"10.1083\/jcb.150.5.989","article-title":"Defects in axonal elongation and neuronal migration in mice with disrupted tau and map1b genes","volume":"150","author":"Takei","year":"2000","journal-title":"J Cell Biol"},{"key":"10.1016\/j.jprot.2015.03.038_bb0395","doi-asserted-by":"crossref","first-page":"2087","DOI":"10.1091\/mbc.12.7.2087","article-title":"Evidence for the role of MAP1B in axon formation","volume":"12","author":"Gonzalez-Billault","year":"2001","journal-title":"Mol Biol Cell"},{"key":"10.1016\/j.jprot.2015.03.038_bb0400","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1385\/MN:28:1:51","article-title":"Collapsin response mediator proteins (CRMPs): involvement in nervous system development and adult neurodegenerative disorders","volume":"28","author":"Charrier","year":"2003","journal-title":"Mol Neurobiol"},{"key":"10.1016\/j.jprot.2015.03.038_bb0405","doi-asserted-by":"crossref","first-page":"961","DOI":"10.1046\/j.1471-4159.1999.0730961.x","article-title":"Semaphorins as mediators of neuronal apoptosis","volume":"73","author":"Shirvan","year":"1999","journal-title":"J Neurochem"},{"key":"10.1016\/j.jprot.2015.03.038_bb0410","doi-asserted-by":"crossref","first-page":"17917","DOI":"10.1074\/jbc.C000179200","article-title":"Evidence that collapsin response mediator protein-2 is involved in the dynamics of microtubules","volume":"275","author":"Gu","year":"2000","journal-title":"J Biol Chem"},{"key":"10.1016\/j.jprot.2015.03.038_bb0415","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1038\/ncb825","article-title":"CRMP-2 binds to tubulin heterodimers to promote microtubule assembly","volume":"4","author":"Fukata","year":"2002","journal-title":"Nat Cell Biol"},{"key":"10.1016\/j.jprot.2015.03.038_bb0420","doi-asserted-by":"crossref","first-page":"34","DOI":"10.1002\/neu.10269","article-title":"Role of CRMP-2 in neuronal polarity","volume":"58","author":"Arimura","year":"2004","journal-title":"J Neurobiol"},{"key":"10.1016\/j.jprot.2015.03.038_bb0425","doi-asserted-by":"crossref","first-page":"781","DOI":"10.1038\/90476","article-title":"CRMP-2 induces axons in cultured hippocampal neurons","volume":"4","author":"Inagaki","year":"2001","journal-title":"Nat Neurosci"},{"key":"10.1016\/j.jprot.2015.03.038_bb0430","doi-asserted-by":"crossref","first-page":"433","DOI":"10.1016\/j.mcn.2003.11.006","article-title":"Involvement of collapsin response mediator proteins in the neurite extension induced by neurotrophins in dorsal root ganglion neurons","volume":"25","author":"Quach","year":"2004","journal-title":"Mol Cell Neurosci"},{"key":"10.1016\/j.jprot.2015.03.038_bb0435","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1016\/S0925-4773(00)00401-9","article-title":"Repulsive axon guidance molecule Sema3A inhibits branching morphogenesis of fetal mouse lung","volume":"97","author":"Ito","year":"2000","journal-title":"Mech Dev"},{"key":"10.1016\/j.jprot.2015.03.038_bb0440","doi-asserted-by":"crossref","first-page":"6197","DOI":"10.1523\/JNEUROSCI.16-19-06197.1996","article-title":"A family of rat CRMP genes is differentially expressed in the nervous system","volume":"16","author":"Wang","year":"1996","journal-title":"J Neurosci"},{"key":"10.1016\/j.jprot.2015.03.038_bb0445","doi-asserted-by":"crossref","first-page":"1524","DOI":"10.1046\/j.1471-4159.2002.01103.x","article-title":"Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part II: dihydropyrimidinase-related protein 2, alpha-enolase and heat shock cognate 71","volume":"82","author":"Castegna","year":"2002","journal-title":"J Neurochem"},{"key":"10.1016\/j.jprot.2015.03.038_bb0450","doi-asserted-by":"crossref","first-page":"4226","DOI":"10.1046\/j.1460-9568.1999.00864.x","article-title":"Ulip\/CRMP proteins are recognized by autoantibodies in paraneoplastic neurological syndromes","volume":"11","author":"Honnorat","year":"1999","journal-title":"Eur J Neurosci"},{"key":"10.1016\/j.jprot.2015.03.038_bb0455","doi-asserted-by":"crossref","first-page":"2329","DOI":"10.1046\/j.1460-9568.2003.02664.x","article-title":"Axonal morphogenesis controlled by antagonistic roles of two CRMP subtypes in microtubule organization","volume":"17","author":"Yuasa-Kawada","year":"2003","journal-title":"Eur J Neurosci"},{"key":"10.1016\/j.jprot.2015.03.038_bb0460","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1016\/S0014-5793(02)03736-5","article-title":"p80 ROKalpha binding protein is a novel splice variant of CRMP-1 which associates with CRMP-2 and modulates RhoA-induced neuronal morphology","volume":"532","author":"Leung","year":"2002","journal-title":"FEBS Lett"},{"key":"10.1016\/j.jprot.2015.03.038_bb0465","doi-asserted-by":"crossref","first-page":"520","DOI":"10.1196\/annals.1296.064","article-title":"Congenital dopamine-beta-hydroxylase deficiency in humans","volume":"1018","author":"Timmers","year":"2004","journal-title":"Ann N Y Acad Sci"},{"key":"10.1016\/j.jprot.2015.03.038_bb0470","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1136\/bmj.282.6258.93","article-title":"Reduced dopamine-beta-hydroxylase activity in Alzheimer's disease","volume":"282","author":"Cross","year":"1981","journal-title":"Br Med J (Clin Res Ed)"},{"key":"10.1016\/j.jprot.2015.03.038_bb0475","doi-asserted-by":"crossref","first-page":"676","DOI":"10.1038\/nmeth.2019","article-title":"Fiji: an open-source platform for biological-image analysis","volume":"9","author":"Schindelin","year":"2012","journal-title":"Nat Methods"}],"container-title":["Journal of Proteomics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1874391915001608?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1874391915001608?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2022,5,4]],"date-time":"2022-05-04T22:50:06Z","timestamp":1651704606000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1874391915001608"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2015,6]]},"references-count":95,"alternative-id":["S1874391915001608"],"URL":"https:\/\/doi.org\/10.1016\/j.jprot.2015.03.038","relation":{},"ISSN":["1874-3919"],"issn-type":[{"value":"1874-3919","type":"print"}],"subject":[],"published":{"date-parts":[[2015,6]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Proteomic analysis of the palmitoyl protein thioesterase 1 interactome in SH-SY5Y human neuroblastoma cells","name":"articletitle","label":"Article Title"},{"value":"Journal of Proteomics","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jprot.2015.03.038","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2015 Elsevier B.V. All rights reserved.","name":"copyright","label":"Copyright"}]}}