{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,27]],"date-time":"2026-04-27T05:25:28Z","timestamp":1777267528817,"version":"3.51.4"},"reference-count":161,"publisher":"Portland Press Ltd.","issue":"5","license":[{"start":{"date-parts":[[2022,9,16]],"date-time":"2022-09-16T00:00:00Z","timestamp":1663286400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2022,10,31]]},"abstract":"<jats:p>Motor neuron diseases (MNDs) include a broad group of diseases in which neurodegeneration mainly affects upper and\/or lower motor neurons (MNs). Although the involvement of specific MNs, symptoms, age of onset, and progression differ in MNDs, the main pathogenic mechanism common to most MNDs is represented by proteostasis alteration and proteotoxicity. This pathomechanism may be directly related to mutations in genes encoding proteins involved in the protein quality control system, particularly the autophagy-lysosomal pathway (ALP). Alternatively, proteostasis alteration can be caused by aberrant proteins that tend to misfold and to aggregate, two related processes that, over time, cannot be properly handled by the ALP. Here, we summarize the main ALP features, focusing on different routes utilized to deliver substrates to the lysosome and how the various ALP pathways intersect with the intracellular trafficking of membranes and vesicles. Next, we provide an overview of the mutated genes that have been found associated with MNDs, how these gene products are involved in different steps of ALP and related processes. Finally, we discuss how autophagy can be considered a valid therapeutic target for MNDs treatment focusing on traditional autophagy modulators and on emerging approaches to overcome their limitations.<\/jats:p>","DOI":"10.1042\/bst20220778","type":"journal-article","created":{"date-parts":[[2022,9,16]],"date-time":"2022-09-16T12:00:22Z","timestamp":1663329622000},"page":"1489-1503","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":9,"title":["The role of autophagy-lysosomal pathway in motor neuron diseases"],"prefix":"10.1042","volume":"50","author":[{"given":"Barbara","family":"Tedesco","sequence":"first","affiliation":[{"name":"1Dipartimento di Scienze Farmacologiche e Biomolecolari (DiSFeB), Universit\u00e0 degli Studi di Milano, Milano, Italy"},{"name":"2Unit of Medical Genetics and Neurogenetics, Fondazione IRCCS Istituto Neurologico Carlo Besta, Milan, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Veronica","family":"Ferrari","sequence":"additional","affiliation":[{"name":"1Dipartimento di Scienze Farmacologiche e Biomolecolari (DiSFeB), Universit\u00e0 degli Studi di Milano, Milano, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Marta","family":"Cozzi","sequence":"additional","affiliation":[{"name":"1Dipartimento di Scienze Farmacologiche e Biomolecolari (DiSFeB), Universit\u00e0 degli Studi di Milano, Milano, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Marta","family":"Chierichetti","sequence":"additional","affiliation":[{"name":"1Dipartimento di Scienze Farmacologiche e Biomolecolari (DiSFeB), Universit\u00e0 degli Studi di Milano, Milano, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Elena","family":"Casarotto","sequence":"additional","affiliation":[{"name":"1Dipartimento di Scienze Farmacologiche e Biomolecolari (DiSFeB), Universit\u00e0 degli Studi di Milano, Milano, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Paola","family":"Pramaggiore","sequence":"additional","affiliation":[{"name":"1Dipartimento di Scienze Farmacologiche e Biomolecolari (DiSFeB), Universit\u00e0 degli Studi di Milano, Milano, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Francesco","family":"Mina","sequence":"additional","affiliation":[{"name":"1Dipartimento di Scienze Farmacologiche e Biomolecolari (DiSFeB), Universit\u00e0 degli Studi di Milano, Milano, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Margherita","family":"Piccolella","sequence":"additional","affiliation":[{"name":"1Dipartimento di Scienze Farmacologiche e Biomolecolari (DiSFeB), Universit\u00e0 degli Studi di Milano, Milano, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Riccardo","family":"Cristofani","sequence":"additional","affiliation":[{"name":"1Dipartimento di Scienze Farmacologiche e Biomolecolari (DiSFeB), Universit\u00e0 degli Studi di Milano, Milano, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Valeria","family":"Crippa","sequence":"additional","affiliation":[{"name":"1Dipartimento di Scienze Farmacologiche e Biomolecolari (DiSFeB), Universit\u00e0 degli Studi di Milano, Milano, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Paola","family":"Rusmini","sequence":"additional","affiliation":[{"name":"1Dipartimento di Scienze Farmacologiche e Biomolecolari (DiSFeB), Universit\u00e0 degli Studi di Milano, Milano, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mariarita","family":"Galbiati","sequence":"additional","affiliation":[{"name":"1Dipartimento di Scienze Farmacologiche e Biomolecolari (DiSFeB), Universit\u00e0 degli Studi di Milano, Milano, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8883-0468","authenticated-orcid":false,"given":"Angelo","family":"Poletti","sequence":"additional","affiliation":[{"name":"1Dipartimento di Scienze Farmacologiche e Biomolecolari (DiSFeB), Universit\u00e0 degli Studi di Milano, Milano, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","published-online":{"date-parts":[[2022,9,16]]},"reference":[{"key":"2022103116073616600_BST-2022-0778CC1","doi-asserted-by":"publisher","first-page":"225","DOI":"10.1080\/1466082031001128","article-title":"The genetics of motor neuron diseases","volume":"4","year":"2003","journal-title":"Amyotroph. Lateral Scler. Other Motor Neuron Disord."},{"key":"2022103116073616600_BST-2022-0778CC2","doi-asserted-by":"publisher","first-page":"986","DOI":"10.1016\/j.bbadis.2006.04.003","article-title":"The molecular genetics of non-ALS motor neuron diseases","volume":"1762","year":"2006","journal-title":"Biochim. Biophys. Acta"},{"key":"2022103116073616600_BST-2022-0778CC3","doi-asserted-by":"publisher","first-page":"769","DOI":"10.1038\/nrg2680","article-title":"Genetics of motor neuron disorders: new insights into pathogenic mechanisms","volume":"10","year":"2009","journal-title":"Nat. Rev. Genet."},{"key":"2022103116073616600_BST-2022-0778CC4","doi-asserted-by":"publisher","first-page":"2692","DOI":"10.1016\/j.jmb.2020.02.018","article-title":"Pathomechanism heterogeneity in the amyotrophic lateral sclerosis and frontotemporal dementia disease spectrum: providing focus through the lens of autophagy","volume":"432","year":"2020","journal-title":"J. Mol. Biol."},{"key":"2022103116073616600_BST-2022-0778CC5","doi-asserted-by":"publisher","first-page":"417","DOI":"10.3390\/cells11030417","article-title":"Restoring SMN expression: an overview of the therapeutic developments for the treatment of spinal muscular atrophy","volume":"11","year":"2022","journal-title":"Cells"},{"key":"2022103116073616600_BST-2022-0778CC6","doi-asserted-by":"publisher","DOI":"10.1038\/s41434-021-00292-4","article-title":"Systematic review and meta-analysis determining the benefits of in vivo genetic therapy in spinal muscular atrophy rodent models","year":"2021","journal-title":"Gene Ther."},{"key":"2022103116073616600_BST-2022-0778CC7","doi-asserted-by":"publisher","first-page":"146","DOI":"10.1111\/jnc.14974","article-title":"Combinatorial treatment for spinal muscular atrophy: an editorial for \u2018Combined treatment with the histone deacetylase inhibitor LBH589 and a splice-switch antisense oligonucleotide enhances SMN2 splicing and SMN expression in Spinal Muscular Atrophy cells\u2019 on page 264","volume":"153","year":"2020","journal-title":"J. Neurochem."},{"key":"2022103116073616600_BST-2022-0778CC8","doi-asserted-by":"publisher","first-page":"248","DOI":"10.1038\/nrn3430","article-title":"The changing scene of amyotrophic lateral sclerosis","volume":"14","year":"2013","journal-title":"Nat. Rev. Neurosci."},{"key":"2022103116073616600_BST-2022-0778CC9","doi-asserted-by":"publisher","first-page":"935","DOI":"10.1016\/j.neuron.2022.01.017","article-title":"The different autophagy degradation pathways and neurodegeneration","volume":"110","year":"2022","journal-title":"Neuron"},{"key":"2022103116073616600_BST-2022-0778CC10","doi-asserted-by":"publisher","first-page":"101468","DOI":"10.1016\/j.arr.2021.101468","article-title":"Autophagy and the hallmarks of aging","volume":"72","year":"2021","journal-title":"Ageing Res. Rev."},{"key":"2022103116073616600_BST-2022-0778CC11","doi-asserted-by":"publisher","first-page":"254","DOI":"10.1080\/15548627.2021.1926656","article-title":"Autophagy and ALS: mechanistic insights and therapeutic implications","volume":"18","year":"2022","journal-title":"Autophagy"},{"key":"2022103116073616600_BST-2022-0778CC12","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.ceb.2019.12.001","article-title":"The ATG conjugation systems in autophagy","volume":"63","year":"2020","journal-title":"Curr. Opin. Cell Biol."},{"key":"2022103116073616600_BST-2022-0778CC13","doi-asserted-by":"publisher","first-page":"495","DOI":"10.1038\/ncb2979","article-title":"Cargo recognition and trafficking in selective autophagy","volume":"16","year":"2014","journal-title":"Nat. Cell Biol."},{"key":"2022103116073616600_BST-2022-0778CC14","doi-asserted-by":"publisher","first-page":"143","DOI":"10.1146\/annurev-cellbio-120219-035530","article-title":"Mechanisms of selective autophagy","volume":"37","year":"2021","journal-title":"Annu. Rev. Cell Dev. Biol."},{"key":"2022103116073616600_BST-2022-0778CC15","doi-asserted-by":"publisher","first-page":"1552","DOI":"10.1126\/science.292.5521.1552","article-title":"Impairment of the ubiquitin-proteasome system by protein aggregation","volume":"292","year":"2001","journal-title":"Science"},{"key":"2022103116073616600_BST-2022-0778CC16","doi-asserted-by":"publisher","first-page":"351","DOI":"10.1016\/j.molcel.2004.12.021","article-title":"Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation","volume":"17","year":"2005","journal-title":"Mol. Cell"},{"key":"2022103116073616600_BST-2022-0778CC17","doi-asserted-by":"publisher","first-page":"26","DOI":"10.1002\/cm.10057","article-title":"Cytoplasmic dynein\/dynactin mediates the assembly of aggresomes","volume":"53","year":"2002","journal-title":"Cell Motil. Cytoskelet."},{"key":"2022103116073616600_BST-2022-0778CC18","doi-asserted-by":"publisher","first-page":"1883","DOI":"10.1083\/jcb.143.7.1883","article-title":"Aggresomes: a cellular response to misfolded proteins","volume":"143","year":"1998","journal-title":"J. Cell Biol."},{"key":"2022103116073616600_BST-2022-0778CC19","doi-asserted-by":"publisher","first-page":"524","DOI":"10.1016\/S0962-8924(00)01852-3","article-title":"Aggresomes, inclusion bodies and protein aggregation","volume":"10","year":"2000","journal-title":"Trends Cell Biol."},{"key":"2022103116073616600_BST-2022-0778CC20","doi-asserted-by":"publisher","first-page":"143","DOI":"10.1016\/j.cub.2009.11.022","article-title":"Chaperone-assisted selective autophagy is essential for muscle maintenance","volume":"20","year":"2010","journal-title":"Curr. Biol."},{"key":"2022103116073616600_BST-2022-0778CC21","doi-asserted-by":"publisher","first-page":"237","DOI":"10.4161\/auto.5407","article-title":"Hspb8 and Bag3: a new chaperone complex targeting misfolded proteins to macroautophagy","volume":"4","year":"2008","journal-title":"Autophagy"},{"key":"2022103116073616600_BST-2022-0778CC22","doi-asserted-by":"publisher","first-page":"1280","DOI":"10.1080\/15548627.2017.1308985","article-title":"Inhibition of retrograde transport modulates misfolded protein accumulation and clearance in motoneuron diseases","volume":"13","year":"2017","journal-title":"Autophagy"},{"key":"2022103116073616600_BST-2022-0778CC23","doi-asserted-by":"publisher","first-page":"335","DOI":"10.3390\/cells10020335","article-title":"The role of HSPB8, a component of the chaperone-assisted selective autophagy machinery, in cancer","volume":"10","year":"2021","journal-title":"Cells"},{"key":"2022103116073616600_BST-2022-0778CC24","doi-asserted-by":"publisher","first-page":"365","DOI":"10.1038\/s41580-018-0001-6","article-title":"The coming of age of chaperone-mediated autophagy","volume":"19","year":"2018","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"2022103116073616600_BST-2022-0778CC25","doi-asserted-by":"publisher","first-page":"9987","DOI":"10.1074\/jbc.M307905200","article-title":"Determination of four sequential stages during microautophagy in vitro","volume":"279","year":"2004","journal-title":"J. Biol. Chem."},{"key":"2022103116073616600_BST-2022-0778CC26","doi-asserted-by":"publisher","first-page":"131","DOI":"10.1016\/j.devcel.2010.12.003","article-title":"Microautophagy of cytosolic proteins by late endosomes","volume":"20","year":"2011","journal-title":"Dev. Cell"},{"key":"2022103116073616600_BST-2022-0778CC27","doi-asserted-by":"publisher","first-page":"337","DOI":"10.5483\/BMBRep.2016.49.6.212","article-title":"Regulation of amyloid precursor protein processing by its KFERQ motif","volume":"49","year":"2016","journal-title":"BMB Rep."},{"key":"2022103116073616600_BST-2022-0778CC28","doi-asserted-by":"publisher","first-page":"6797","DOI":"10.1016\/S0021-9258(18)68713-7","article-title":"Peptide sequences that target proteins for enhanced degradation during serum withdrawal","volume":"263","year":"1988","journal-title":"J. Biol. Chem."},{"key":"2022103116073616600_BST-2022-0778CC29","doi-asserted-by":"publisher","first-page":"501","DOI":"10.1126\/science.273.5274.501","article-title":"A receptor for the selective uptake and degradation of proteins by lysosomes","volume":"273","year":"1996","journal-title":"Science."},{"key":"2022103116073616600_BST-2022-0778CC30","doi-asserted-by":"publisher","first-page":"1678","DOI":"10.3390\/cells10071678","article-title":"Current knowledge of endolysosomal and autophagy defects in hereditary spastic paraplegia","volume":"10","year":"2021","journal-title":"Cells"},{"key":"2022103116073616600_BST-2022-0778CC31","doi-asserted-by":"publisher","first-page":"18","DOI":"10.1007\/s11910-019-0930-2","article-title":"Update on the genetics of spastic paraplegias","volume":"19","year":"2019","journal-title":"Curr. Neurol. Neurosci. Rep."},{"key":"2022103116073616600_BST-2022-0778CC32","doi-asserted-by":"publisher","first-page":"51","DOI":"10.1002\/jimd.12084","article-title":"Novel insights into the clinical and molecular spectrum of congenital disorders of autophagy","volume":"43","year":"2020","journal-title":"J. Inherit. Metab. Dis."},{"key":"2022103116073616600_BST-2022-0778CC33","doi-asserted-by":"publisher","first-page":"3096","DOI":"10.1080\/15548627.2020.1852727","article-title":"Lysosomal targeting of autophagosomes by the TECPR domain of TECPR2","volume":"17","year":"2021","journal-title":"Autophagy"},{"key":"2022103116073616600_BST-2022-0778CC34","doi-asserted-by":"publisher","first-page":"3082","DOI":"10.1080\/15548627.2020.1852724","article-title":"A tecpr2 knockout mouse exhibits age-dependent neuroaxonal dystrophy associated with autophagosome accumulation","volume":"17","year":"2021","journal-title":"Autophagy"},{"key":"2022103116073616600_BST-2022-0778CC35","doi-asserted-by":"publisher","first-page":"166","DOI":"10.1038\/ng1001-166","article-title":"A gene encoding a putative GTPase regulator is mutated in familial amyotrophic lateral sclerosis 2","volume":"29","year":"2001","journal-title":"Nat. Genet."},{"key":"2022103116073616600_BST-2022-0778CC36","doi-asserted-by":"publisher","first-page":"160","DOI":"10.1038\/ng1001-160","article-title":"The gene encoding alsin, a protein with three guanine-nucleotide exchange factor domains, is mutated in a form of recessive amyotrophic lateral sclerosis","volume":"29","year":"2001","journal-title":"Nat. Genet."},{"key":"2022103116073616600_BST-2022-0778CC37","doi-asserted-by":"publisher","first-page":"eaad9157","DOI":"10.1126\/scitranslmed.aad9157","article-title":"Mutations in the vesicular trafficking protein annexin A11 are associated with amyotrophic lateral sclerosis","volume":"9","year":"2017","journal-title":"Sci. Transl. Med."},{"key":"2022103116073616600_BST-2022-0778CC38","doi-asserted-by":"publisher","first-page":"77","DOI":"10.1038\/352077a0","article-title":"Androgen receptor gene mutations in X-linked spinal and bulbar muscular atrophy","volume":"352","year":"1991","journal-title":"Nature"},{"key":"2022103116073616600_BST-2022-0778CC39","doi-asserted-by":"publisher","first-page":"1069","DOI":"10.1038\/nature09320","article-title":"Ataxin-2 intermediate-length polyglutamine expansions are associated with increased risk for ALS","volume":"466","year":"2010","journal-title":"Nature"},{"key":"2022103116073616600_BST-2022-0778CC40","doi-asserted-by":"publisher","first-page":"1302","DOI":"10.1001\/jamaneurol.2013.443","article-title":"Amyotrophic lateral sclerosis and spinocerebellar ataxia type 2 in a family with full CAG repeat expansions of ATXN2","volume":"70","year":"2013","journal-title":"JAMA Neurol."},{"key":"2022103116073616600_BST-2022-0778CC41","doi-asserted-by":"publisher","first-page":"257","DOI":"10.1016\/j.neuron.2011.09.010","article-title":"A hexanucleotide repeat expansion in C9ORF72 is the cause of chromosome 9p21-linked ALS-FTD","volume":"72","year":"2011","journal-title":"Neuron"},{"key":"2022103116073616600_BST-2022-0778CC42","doi-asserted-by":"publisher","first-page":"245","DOI":"10.1016\/j.neuron.2011.09.011","article-title":"Expanded GGGGCC hexanucleotide repeat in noncoding region of C9ORF72 causes chromosome 9p-linked FTD and ALS","volume":"72","year":"2011","journal-title":"Neuron"},{"key":"2022103116073616600_BST-2022-0778CC43","doi-asserted-by":"publisher","first-page":"11253","DOI":"10.1038\/ncomms11253","article-title":"CCNF mutations in amyotrophic lateral sclerosis and frontotemporal dementia","volume":"7","year":"2016","journal-title":"Nat. Commun."},{"key":"2022103116073616600_BST-2022-0778CC44","doi-asserted-by":"publisher","first-page":"1074","DOI":"10.1212\/01.wnl.0000231510.89311.8b","article-title":"ALS phenotypes with mutations in CHMP2B (charged multivesicular body protein 2B)","volume":"67","year":"2006","journal-title":"Neurology"},{"key":"2022103116073616600_BST-2022-0778CC45","doi-asserted-by":"publisher","first-page":"724","DOI":"10.1212\/01.WNL.0000134608.83927.B1","article-title":"Point mutations of the p150 subunit of dynactin (DCTN1) gene in ALS","volume":"63","year":"2004","journal-title":"Neurology"},{"key":"2022103116073616600_BST-2022-0778CC46","doi-asserted-by":"publisher","first-page":"455","DOI":"10.1038\/ng1123","article-title":"Mutant dynactin in motor neuron disease","volume":"33","year":"2003","journal-title":"Nat. Genet."},{"key":"2022103116073616600_BST-2022-0778CC47","doi-asserted-by":"publisher","first-page":"333","DOI":"10.1007\/s10048-011-0291-8","article-title":"A nullimorphic ERLIN2 mutation defines a complicated hereditary spastic paraplegia locus (SPG18)","volume":"12","year":"2011","journal-title":"Neurogenetics"},{"key":"2022103116073616600_BST-2022-0778CC48","doi-asserted-by":"publisher","first-page":"510","DOI":"10.1002\/ana.23641","article-title":"Loss of ERLIN2 function leads to juvenile primary lateral sclerosis","volume":"72","year":"2012","journal-title":"Ann. Neurol."},{"key":"2022103116073616600_BST-2022-0778CC49","doi-asserted-by":"publisher","first-page":"85","DOI":"10.1016\/j.ajhg.2008.12.010","article-title":"Deleterious variants of FIG4, a phosphoinositide phosphatase, in patients with ALS","volume":"84","year":"2009","journal-title":"Am. J. Hum. Genet."},{"key":"2022103116073616600_BST-2022-0778CC50","doi-asserted-by":"publisher","first-page":"1208","DOI":"10.1126\/science.1165942","article-title":"Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6","volume":"323","year":"2009","journal-title":"Science"},{"key":"2022103116073616600_BST-2022-0778CC51","doi-asserted-by":"publisher","first-page":"1205","DOI":"10.1126\/science.1166066","article-title":"Mutations in the FUS\/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis","volume":"323","year":"2009","journal-title":"Science"},{"key":"2022103116073616600_BST-2022-0778CC52","doi-asserted-by":"publisher","first-page":"1268","DOI":"10.1016\/j.neuron.2018.02.027","article-title":"Genome-wide analyses identify KIF5A as a novel ALS gene","volume":"97","year":"2018","journal-title":"Neuron"},{"key":"2022103116073616600_BST-2022-0778CC53","doi-asserted-by":"publisher","first-page":"688","DOI":"10.1093\/brain\/awx370","article-title":"Hot-spot KIF5A mutations cause familial ALS","volume":"141","year":"2018","journal-title":"Brain"},{"key":"2022103116073616600_BST-2022-0778CC54","doi-asserted-by":"publisher","first-page":"223","DOI":"10.1038\/nature08971","article-title":"Mutations of optineurin in amyotrophic lateral sclerosis","volume":"465","year":"2010","journal-title":"Nature"},{"key":"2022103116073616600_BST-2022-0778CC55","doi-asserted-by":"publisher","first-page":"631","DOI":"10.1093\/hmg\/4.4.631","article-title":"Deletions in the survival motor neuron gene on 5q13 in autosomal recessive spinal muscular atrophy","volume":"4","year":"1995","journal-title":"Hum. Mol. Genet."},{"key":"2022103116073616600_BST-2022-0778CC56","doi-asserted-by":"publisher","first-page":"155","DOI":"10.1016\/0092-8674(95)90460-3","article-title":"Identification and characterization of a spinal muscular atrophy-determining gene","volume":"80","year":"1995","journal-title":"Cell"},{"key":"2022103116073616600_BST-2022-0778CC57","doi-asserted-by":"publisher","first-page":"59","DOI":"10.1038\/362059a0","article-title":"Mutations in Cu\/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis","volume":"362","year":"1993","journal-title":"Nature"},{"key":"2022103116073616600_BST-2022-0778CC58","doi-asserted-by":"publisher","first-page":"366","DOI":"10.1038\/ng1980","article-title":"Mutations in SPG11, encoding spatacsin, are a major cause of spastic paraplegia with thin corpus callosum","volume":"39","year":"2007","journal-title":"Nat. Genet."},{"key":"2022103116073616600_BST-2022-0778CC59","doi-asserted-by":"publisher","first-page":"301","DOI":"10.1007\/s10048-007-0095-z","article-title":"SPG11: a consistent clinical phenotype in a family with homozygous spatacsin truncating mutation","volume":"8","year":"2007","journal-title":"Neurogenetics"},{"key":"2022103116073616600_BST-2022-0778CC60","doi-asserted-by":"publisher","first-page":"591","DOI":"10.1093\/brain\/awp325","article-title":"SPATACSIN mutations cause autosomal recessive juvenile amyotrophic lateral sclerosis","volume":"133","year":"2010","journal-title":"Brain"},{"key":"2022103116073616600_BST-2022-0778CC61","doi-asserted-by":"publisher","first-page":"992","DOI":"10.1016\/j.ajhg.2008.03.004","article-title":"Identification of the SPG15 gene, encoding spastizin, as a frequent cause of complicated autosomal-recessive spastic paraplegia, including Kjellin syndrome","volume":"82","year":"2008","journal-title":"Am. J. Hum. Genet."},{"key":"2022103116073616600_BST-2022-0778CC62","doi-asserted-by":"publisher","first-page":"1230","DOI":"10.1212\/WNL.56.9.1230","article-title":"SPG15, a new locus for autosomal recessive complicated HSP on chromosome 14q","volume":"56","year":"2001","journal-title":"Neurology"},{"key":"2022103116073616600_BST-2022-0778CC63","doi-asserted-by":"publisher","first-page":"307","DOI":"10.1007\/s10048-007-0097-x","article-title":"Refinement of the SPG15 candidate interval and phenotypic heterogeneity in three large Arab families","volume":"8","year":"2007","journal-title":"Neurogenetics"},{"key":"2022103116073616600_BST-2022-0778CC64","doi-asserted-by":"publisher","first-page":"752","DOI":"10.1016\/j.ajhg.2008.11.003","article-title":"A missense mutation in SLC33A1, which encodes the acetyl-CoA transporter, causes autosomal-dominant spastic paraplegia (SPG42)","volume":"83","year":"2008","journal-title":"Am. J. Hum. Genet."},{"key":"2022103116073616600_BST-2022-0778CC65","doi-asserted-by":"publisher","first-page":"788","DOI":"10.1016\/j.ajhg.2011.04.019","article-title":"Adaptor protein complex 4 deficiency causes severe autosomal-recessive intellectual disability, progressive spastic paraplegia, shy character, and short stature","volume":"88","year":"2011","journal-title":"Am. J. Hum. Genet."},{"key":"2022103116073616600_BST-2022-0778CC66","doi-asserted-by":"publisher","first-page":"e1000408","DOI":"10.1371\/journal.pbio.1000408","article-title":"A genome-scale DNA repair RNAi screen identifies SPG48 as a novel gene associated with hereditary spastic paraplegia","volume":"8","year":"2010","journal-title":"PLoS Biol."},{"key":"2022103116073616600_BST-2022-0778CC67","doi-asserted-by":"publisher","first-page":"1065","DOI":"10.1016\/j.ajhg.2012.09.015","article-title":"Mutation in TECPR2 reveals a role for autophagy in hereditary spastic paraparesis","volume":"91","year":"2012","journal-title":"Am. J. Hum. Genet."},{"key":"2022103116073616600_BST-2022-0778CC68","doi-asserted-by":"publisher","first-page":"40","DOI":"10.1016\/j.ajhg.2009.06.004","article-title":"Mutation in the AP4M1 gene provides a model for neuroaxonal injury in cerebral palsy","volume":"85","year":"2009","journal-title":"Am. J. Hum. Genet."},{"key":"2022103116073616600_BST-2022-0778CC69","doi-asserted-by":"publisher","first-page":"141","DOI":"10.1136\/jmg.2010.082263","article-title":"Adaptor protein complex-4 (AP-4) deficiency causes a novel autosomal recessive cerebral palsy syndrome with microcephaly and intellectual disability","volume":"48","year":"2011","journal-title":"J. Med. Genet."},{"key":"2022103116073616600_BST-2022-0778CC70","doi-asserted-by":"publisher","first-page":"462","DOI":"10.1136\/jmedgenet-2012-100742","article-title":"A founder mutation in Vps37A causes autosomal recessive complex hereditary spastic paraparesis","volume":"49","year":"2012","journal-title":"J. Med. Genet."},{"key":"2022103116073616600_BST-2022-0778CC71","doi-asserted-by":"publisher","first-page":"e60","DOI":"10.1212\/NXG.0000000000000060","article-title":"Compound heterozygote mutations in SPG7 in a family with adult-onset primary lateral sclerosis","volume":"2","year":"2016","journal-title":"Neurol. Genet."},{"key":"2022103116073616600_BST-2022-0778CC72","doi-asserted-by":"publisher","first-page":"1904","DOI":"10.1093\/brain\/aww111","article-title":"Genetic and phenotypic characterization of complex hereditary spastic paraplegia","volume":"139","year":"2016","journal-title":"Brain"},{"key":"2022103116073616600_BST-2022-0778CC73","doi-asserted-by":"publisher","first-page":"287","DOI":"10.1093\/brain\/aww307","article-title":"Loss-of-function mutations in the ATP13A2\/PARK9 gene cause complicated hereditary spastic paraplegia (SPG78)","volume":"140","year":"2017","journal-title":"Brain"},{"key":"2022103116073616600_BST-2022-0778CC74","doi-asserted-by":"publisher","first-page":"1440","DOI":"10.1001\/archneurol.2011.250","article-title":"SQSTM1 mutations in familial and sporadic amyotrophic lateral sclerosis","volume":"68","year":"2011","journal-title":"Arch. Neurol."},{"key":"2022103116073616600_BST-2022-0778CC75","doi-asserted-by":"publisher","first-page":"1668","DOI":"10.1126\/science.1154584","article-title":"TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis","volume":"319","year":"2008","journal-title":"Science"},{"key":"2022103116073616600_BST-2022-0778CC76","doi-asserted-by":"publisher","first-page":"409","DOI":"10.1016\/S1474-4422(08)70071-1","article-title":"TARDBP mutations in amyotrophic lateral sclerosis with TDP-43 neuropathology: a genetic and histopathological analysis","volume":"7","year":"2008","journal-title":"Lancet Neurol."},{"key":"2022103116073616600_BST-2022-0778CC77","doi-asserted-by":"publisher","first-page":"572","DOI":"10.1038\/ng.132","article-title":"TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis","volume":"40","year":"2008","journal-title":"Nat. Genet."},{"key":"2022103116073616600_BST-2022-0778CC78","doi-asserted-by":"publisher","first-page":"535","DOI":"10.1002\/ana.21344","article-title":"TDP-43 A315T mutation in familial motor neuron disease","volume":"63","year":"2008","journal-title":"Ann. Neurol."},{"key":"2022103116073616600_BST-2022-0778CC79","doi-asserted-by":"publisher","first-page":"1436","DOI":"10.1126\/science.aaa3650","article-title":"Exome sequencing in amyotrophic lateral sclerosis identifies risk genes and pathways","volume":"347","year":"2015","journal-title":"Science"},{"key":"2022103116073616600_BST-2022-0778CC80","doi-asserted-by":"publisher","first-page":"631","DOI":"10.1038\/nn.4000","article-title":"Haploinsufficiency of TBK1 causes familial ALS and fronto-temporal dementia","volume":"18","year":"2015","journal-title":"Nat. Neurosci."},{"key":"2022103116073616600_BST-2022-0778CC81","doi-asserted-by":"publisher","first-page":"211","DOI":"10.1038\/nature10353","article-title":"Mutations in UBQLN2 cause dominant X-linked juvenile and adult-onset ALS and ALS\/dementia","volume":"477","year":"2011","journal-title":"Nature"},{"key":"2022103116073616600_BST-2022-0778CC82","doi-asserted-by":"publisher","first-page":"822","DOI":"10.1086\/425287","article-title":"A mutation in the vesicle-trafficking protein VAPB causes late-onset spinal muscular atrophy and amyotrophic lateral sclerosis","volume":"75","year":"2004","journal-title":"Am. J. Hum. Genet."},{"key":"2022103116073616600_BST-2022-0778CC83","doi-asserted-by":"publisher","first-page":"857","DOI":"10.1016\/j.neuron.2010.11.036","article-title":"Exome sequencing reveals VCP mutations as a cause of familial ALS","volume":"68","year":"2010","journal-title":"Neuron"},{"key":"2022103116073616600_BST-2022-0778CC84","doi-asserted-by":"publisher","first-page":"273","DOI":"10.1210\/endrev\/bnz005","article-title":"The role of sex and sex hormones in neurodegenerative diseases","volume":"41","year":"2020","journal-title":"Endocr. Rev."},{"key":"2022103116073616600_BST-2022-0778CC85","doi-asserted-by":"publisher","first-page":"1456","DOI":"10.1007\/s12031-022-02029-3","article-title":"Autophagy dysfunction in ALS: from transport to protein degradation","volume":"72","year":"2022","journal-title":"J. Mol. Neurosci."},{"key":"2022103116073616600_BST-2022-0778CC86","doi-asserted-by":"publisher","first-page":"87","DOI":"10.1159\/000500672","article-title":"Exome sequencing identifies a mutation (Y740C) in spastic paraplegia 7 gene associated with adult-onset primary lateral sclerosis in a Chinese family","volume":"81","year":"2019","journal-title":"Eur. Neurol."},{"key":"2022103116073616600_BST-2022-0778CC87","doi-asserted-by":"publisher","first-page":"3877","DOI":"10.1007\/s00018-018-2849-1","article-title":"The role of survival motor neuron protein (SMN) in protein homeostasis","volume":"75","year":"2018","journal-title":"Cell. Mol. Life Sci."},{"key":"2022103116073616600_BST-2022-0778CC88","doi-asserted-by":"publisher","first-page":"287","DOI":"10.1016\/j.expneurol.2016.06.032","article-title":"Autophagy modulators regulate survival motor neuron protein stability in motoneurons","volume":"283","year":"2016","journal-title":"Exp. Neurol."},{"key":"2022103116073616600_BST-2022-0778CC89","doi-asserted-by":"publisher","first-page":"122","DOI":"10.1186\/s40478-021-01223-5","article-title":"Spinal muscular atrophy autophagy profile is tissue-dependent: differential regulation between muscle and motoneurons","volume":"9","year":"2021","journal-title":"Acta Neuropathol. Commun."},{"key":"2022103116073616600_BST-2022-0778CC90","doi-asserted-by":"publisher","first-page":"3008","DOI":"10.1172\/JCI95231","article-title":"Blocking p62-dependent SMN degradation ameliorates spinal muscular atrophy disease phenotypes","volume":"128","year":"2018","journal-title":"J. Clin. Investig."},{"key":"2022103116073616600_BST-2022-0778CC91","doi-asserted-by":"publisher","first-page":"249","DOI":"10.1002\/ana.410440216","article-title":"Nuclear inclusions of the androgen receptor protein in spinal and bulbar muscular atrophy","volume":"44","year":"1998","journal-title":"Ann. Neurol."},{"key":"2022103116073616600_BST-2022-0778CC92","doi-asserted-by":"publisher","first-page":"695","DOI":"10.1016\/S0002-9440(10)65612-X","article-title":"Nonneural nuclear inclusions of androgen receptor protein in spinal and bulbar muscular atrophy","volume":"153","year":"1998","journal-title":"Am. J. Pathol."},{"key":"2022103116073616600_BST-2022-0778CC93","doi-asserted-by":"publisher","first-page":"133","DOI":"10.1093\/hmg\/9.1.133","article-title":"Motoneuronal cell death is not correlated with aggregate formation of androgen receptors containing an elongated polyglutamine tract","volume":"9","year":"2000","journal-title":"Hum. Mol. Genet."},{"key":"2022103116073616600_BST-2022-0778CC94","doi-asserted-by":"publisher","first-page":"731","DOI":"10.1093\/hmg\/8.5.731","article-title":"Polyglutamine-expanded androgen receptors form aggregates that sequester heat shock proteins, proteasome components and SRC-1, and are suppressed by the HDJ-2 chaperone","volume":"8","year":"1999","journal-title":"Hum. Mol. Genet."},{"key":"2022103116073616600_BST-2022-0778CC95","doi-asserted-by":"publisher","first-page":"1418","DOI":"10.1096\/fj.01-1035fje","article-title":"Androgen receptor with elongated polyglutamine tract forms aggregates that alter axonal trafficking and mitochondrial distribution in motor neuronal processes","volume":"16","year":"2002","journal-title":"FASEB J."},{"key":"2022103116073616600_BST-2022-0778CC96","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.yfrne.2004.03.001","article-title":"The polyglutamine tract of androgen receptor: from functions to dysfunctions in motor neurons","volume":"25","year":"2004","journal-title":"Front. Neuroendocrinol."},{"key":"2022103116073616600_BST-2022-0778CC97","doi-asserted-by":"publisher","first-page":"659","DOI":"10.1093\/brain\/awh381","article-title":"Widespread nuclear and cytoplasmic accumulation of mutant androgen receptor in SBMA patients","volume":"128","year":"2005","journal-title":"Brain"},{"key":"2022103116073616600_BST-2022-0778CC98","doi-asserted-by":"publisher","first-page":"135","DOI":"10.1111\/j.1365-2990.2007.00830.x","article-title":"Pathogenesis and molecular targeted therapy of spinal and bulbar muscular atrophy","volume":"33","year":"2007","journal-title":"Neuropathol. Appl. Neurobiol."},{"key":"2022103116073616600_BST-2022-0778CC99","doi-asserted-by":"publisher","first-page":"1376","DOI":"10.1093\/hmg\/ddt527","article-title":"Transcriptional activation of TFEB\/ZKSCAN3 target genes underlies enhanced autophagy in spinobulbar muscular atrophy","volume":"23","year":"2014","journal-title":"Hum. Mol. Genet."},{"key":"2022103116073616600_BST-2022-0778CC100","doi-asserted-by":"publisher","first-page":"569","DOI":"10.3389\/fendo.2019.00569","article-title":"Autophagic and proteasomal mediated removal of mutant androgen receptor in muscle models of spinal and bulbar muscular atrophy","volume":"10","year":"2019","journal-title":"Front. Endocrinol."},{"key":"2022103116073616600_BST-2022-0778CC101","doi-asserted-by":"publisher","first-page":"1180","DOI":"10.1038\/nn.3787","article-title":"Polyglutamine-expanded androgen receptor interferes with TFEB to elicit autophagy defects in SBMA","volume":"17","year":"2014","journal-title":"Nat. Neurosci."},{"key":"2022103116073616600_BST-2022-0778CC102","doi-asserted-by":"publisher","first-page":"64","DOI":"10.1093\/hmg\/ddu419","article-title":"Synergic prodegradative activity of bicalutamide and trehalose on the mutant androgen receptor responsible for spinal and bulbar muscular atrophy","volume":"24","year":"2015","journal-title":"Hum. Mol. Genet."},{"key":"2022103116073616600_BST-2022-0778CC103","doi-asserted-by":"publisher","first-page":"1937","DOI":"10.1093\/hmg\/ddp115","article-title":"Cytoplasmic retention of polyglutamine-expanded androgen receptor ameliorates disease via autophagy in a mouse model of spinal and bulbar muscular atrophy","volume":"18","year":"2009","journal-title":"Hum. Mol. Genet."},{"key":"2022103116073616600_BST-2022-0778CC104","doi-asserted-by":"publisher","first-page":"631","DOI":"10.1080\/15548627.2018.1535292","article-title":"Trehalose induces autophagy via lysosomal-mediated TFEB activation in models of motoneuron degeneration","volume":"15","year":"2019","journal-title":"Autophagy"},{"key":"2022103116073616600_BST-2022-0778CC105","doi-asserted-by":"publisher","first-page":"2585","DOI":"10.1016\/j.neurobiolaging.2013.05.026","article-title":"Clearance of the mutant androgen receptor in motoneuronal models of spinal and bulbar muscular atrophy","volume":"34","year":"2013","journal-title":"Neurobiol. Aging"},{"key":"2022103116073616600_BST-2022-0778CC106","doi-asserted-by":"publisher","first-page":"15174","DOI":"10.1038\/srep15174","article-title":"Aberrant autophagic response in the muscle of A knock-in mouse model of spinal and bulbar muscular atrophy","volume":"5","year":"2015","journal-title":"Sci. Rep."},{"key":"2022103116073616600_BST-2022-0778CC107","doi-asserted-by":"publisher","first-page":"e1002321","DOI":"10.1371\/journal.pgen.1002321","article-title":"Macroautophagy is regulated by the UPR-mediator CHOP and accentuates the phenotype of SBMA mice","volume":"7","year":"2011","journal-title":"PLoS Genet."},{"key":"2022103116073616600_BST-2022-0778CC108","doi-asserted-by":"publisher","first-page":"958","DOI":"10.4161\/auto.6.7.13042","article-title":"A role of small heat shock protein B8 (HspB8) in the autophagic removal of misfolded proteins responsible for neurodegenerative diseases","volume":"6","year":"2010","journal-title":"Autophagy"},{"key":"2022103116073616600_BST-2022-0778CC109","doi-asserted-by":"publisher","first-page":"1598","DOI":"10.1042\/BST20130118","article-title":"Motoneuronal and muscle-selective removal of ALS-related misfolded proteins","volume":"41","year":"2013","journal-title":"Biochem. Soc. Trans."},{"key":"2022103116073616600_BST-2022-0778CC110","doi-asserted-by":"publisher","first-page":"30524","DOI":"10.1074\/jbc.M603337200","article-title":"Degradation of amyotrophic lateral sclerosis-linked mutant Cu,Zn-superoxide dismutase proteins by macroautophagy and the proteasome","volume":"281","year":"2006","journal-title":"J. Biol. Chem."},{"key":"2022103116073616600_BST-2022-0778CC111","doi-asserted-by":"publisher","first-page":"80","DOI":"10.1016\/j.nbd.2013.07.011","article-title":"Autophagy activation and neuroprotection by progesterone in the G93A-SOD1 transgenic mouse model of amyotrophic lateral sclerosis","volume":"59","year":"2013","journal-title":"Neurobiol. Dis."},{"key":"2022103116073616600_BST-2022-0778CC112","doi-asserted-by":"publisher","first-page":"290","DOI":"10.4161\/auto.5524","article-title":"Altered macroautophagy in the spinal cord of SOD1 mutant mice","volume":"4","year":"2008","journal-title":"Autophagy"},{"key":"2022103116073616600_BST-2022-0778CC113","doi-asserted-by":"publisher","first-page":"112","DOI":"10.1016\/j.brainres.2007.06.045","article-title":"Increased autophagy in transgenic mice with a G93A mutant SOD1 gene","volume":"1167","year":"2007","journal-title":"Brain Res."},{"key":"2022103116073616600_BST-2022-0778CC114","doi-asserted-by":"publisher","first-page":"248","DOI":"10.1111\/j.1471-4159.2010.07098.x","article-title":"Regulation of TDP-43 aggregation by phosphorylation and p62\/SQSTM1","volume":"116","year":"2011","journal-title":"J. Neurochem."},{"key":"2022103116073616600_BST-2022-0778CC115","doi-asserted-by":"publisher","first-page":"12390","DOI":"10.1038\/s41598-018-29658-2","article-title":"Tdp-25 routing to autophagy and proteasome ameliorates its aggregation in amyotrophic lateral sclerosis target cells","volume":"8","year":"2018","journal-title":"Sci. Rep."},{"key":"2022103116073616600_BST-2022-0778CC116","doi-asserted-by":"publisher","first-page":"3440","DOI":"10.1093\/hmg\/ddq257","article-title":"The small heat shock protein B8 (HspB8) promotes autophagic removal of misfolded proteins involved in amyotrophic lateral sclerosis (ALS)","volume":"19","year":"2010","journal-title":"Hum. Mol. Genet."},{"key":"2022103116073616600_BST-2022-0778CC117","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1007\/s12192-017-0806-9","article-title":"The small heat shock protein B8 (HSPB8) efficiently removes aggregating species of dipeptides produced in C9ORF72-related neurodegenerative diseases","volume":"23","year":"2018","journal-title":"Cell Stress Chaperones"},{"key":"2022103116073616600_BST-2022-0778CC118","doi-asserted-by":"publisher","first-page":"3187","DOI":"10.1093\/brain\/aww237","article-title":"Exosome secretion is a key pathway for clearance of pathological TDP-43","volume":"139","year":"2016","journal-title":"Brain"},{"key":"2022103116073616600_BST-2022-0778CC119","doi-asserted-by":"publisher","first-page":"875","DOI":"10.1083\/jcb.200908115","article-title":"Valosin-containing protein (VCP) is required for autophagy and is disrupted in VCP disease","volume":"187","year":"2009","journal-title":"J. Cell Biol."},{"key":"2022103116073616600_BST-2022-0778CC120","doi-asserted-by":"publisher","first-page":"19","DOI":"10.3389\/fnmol.2020.00019","article-title":"Chaperone mediated autophagy degrades TDP-43 protein and is affected by TDP-43 aggregation","volume":"13","year":"2020","journal-title":"Front. Mol. Neurosci."},{"key":"2022103116073616600_BST-2022-0778CC121","doi-asserted-by":"publisher","first-page":"784","DOI":"10.1002\/jnr.22243","article-title":"Synergistic effect between proteasome and autophagosome in the clearance of polyubiquitinated TDP-43","volume":"88","year":"2010","journal-title":"J. Neurosci. Res."},{"key":"2022103116073616600_BST-2022-0778CC122","doi-asserted-by":"publisher","first-page":"15024","DOI":"10.1073\/pnas.1206362109","article-title":"Autophagy activators rescue and alleviate pathogenesis of a mouse model with proteinopathies of the TAR DNA-binding protein 43","volume":"109","year":"2012","journal-title":"Proc. Natl Acad. Sci. U.S.A."},{"key":"2022103116073616600_BST-2022-0778CC123","doi-asserted-by":"publisher","first-page":"112","DOI":"10.1016\/j.neulet.2009.11.055","article-title":"Degradation of TDP-43 and its pathogenic form by autophagy and the ubiquitin-proteasome system","volume":"469","year":"2010","journal-title":"Neurosci. Lett."},{"key":"2022103116073616600_BST-2022-0778CC124","doi-asserted-by":"publisher","first-page":"109","DOI":"10.1007\/s12640-018-9865-7","article-title":"Autophagic modulation by trehalose reduces accumulation of TDP-43 in a cell model of amyotrophic lateral sclerosis via TFEB activation","volume":"34","year":"2018","journal-title":"Neurotox Res."},{"key":"2022103116073616600_BST-2022-0778CC125","doi-asserted-by":"publisher","first-page":"84","DOI":"10.3389\/fnmol.2017.00084","article-title":"Granulostasis: protein quality control of RNP granules","volume":"10","year":"2017","journal-title":"Front. Mol. Neurosci."},{"key":"2022103116073616600_BST-2022-0778CC126","doi-asserted-by":"publisher","first-page":"1838","DOI":"10.1038\/cdd.2014.103","article-title":"Inhibition of autophagy, lysosome and VCP function impairs stress granule assembly","volume":"21","year":"2014","journal-title":"Cell Death Diff."},{"key":"2022103116073616600_BST-2022-0778CC127","doi-asserted-by":"publisher","first-page":"217","DOI":"10.4161\/auto.6.2.11014","article-title":"VCP\/p97 is essential for maturation of ubiquitin-containing autophagosomes and this function is impaired by mutations that cause IBMPFD","volume":"6","year":"2010","journal-title":"Autophagy"},{"key":"2022103116073616600_BST-2022-0778CC128","doi-asserted-by":"publisher","first-page":"5673","DOI":"10.1007\/s12035-022-02934-z","article-title":"Recent updates on the genetics of amyotrophic lateral sclerosis and frontotemporal dementia","volume":"59","year":"2022","journal-title":"Mol. Neurobiol."},{"key":"2022103116073616600_BST-2022-0778CC129","doi-asserted-by":"publisher","first-page":"903","DOI":"10.1080\/15548627.2020.1739444","article-title":"KIF5A-dependent axonal transport deficiency disrupts autophagic flux in trimethyltin chloride-induced neurotoxicity","volume":"17","year":"2021","journal-title":"Autophagy"},{"key":"2022103116073616600_BST-2022-0778CC130","doi-asserted-by":"publisher","first-page":"428","DOI":"10.4161\/auto.5.3.7894","article-title":"The stress-inducible HspB8-Bag3 complex induces the eIF2alpha kinase pathway: implications for protein quality control and viral factory degradation?","volume":"5","year":"2009","journal-title":"Autophagy"},{"key":"2022103116073616600_BST-2022-0778CC131","doi-asserted-by":"publisher","first-page":"22827","DOI":"10.1038\/srep22827","article-title":"Transcriptional induction of the heat shock protein B8 mediates the clearance of misfolded proteins responsible for motor neuron diseases","volume":"6","year":"2016","journal-title":"Sci. Rep."},{"key":"2022103116073616600_BST-2022-0778CC132","doi-asserted-by":"publisher","first-page":"796","DOI":"10.3389\/fnins.2019.00796","article-title":"The regulation of the small heat shock protein B8 in misfolding protein diseases causing motoneuronal and muscle cell death","volume":"13","year":"2019","journal-title":"Front. Neurosci."},{"key":"2022103116073616600_BST-2022-0778CC133","doi-asserted-by":"publisher","first-page":"e028486","DOI":"10.1136\/bmjopen-2018-028486","article-title":"Proteostasis and ALS: protocol for a phase II, randomised, double-blind, placebo-controlled, multicentre clinical trial for colchicine in ALS (Co-ALS)","volume":"9","year":"2019","journal-title":"BMJ Open"},{"key":"2022103116073616600_BST-2022-0778CC134","doi-asserted-by":"publisher","first-page":"8755","DOI":"10.1038\/s41598-020-65664-z","article-title":"BAG3 pro209 mutants associated with myopathy and neuropathy relocate chaperones of the CASA-complex to aggresomes","volume":"10","year":"2020","journal-title":"Sci. Rep."},{"key":"2022103116073616600_BST-2022-0778CC135","doi-asserted-by":"publisher","first-page":"412","DOI":"10.4161\/auto.7.4.14541","article-title":"Rapamycin treatment augments motor neuron degeneration in SOD1(G93A) mouse model of amyotrophic lateral sclerosis","volume":"7","year":"2011","journal-title":"Autophagy"},{"key":"2022103116073616600_BST-2022-0778CC136","doi-asserted-by":"publisher","first-page":"e11119","DOI":"10.1097\/MD.0000000000011119","article-title":"Rapamycin treatment for amyotrophic lateral sclerosis: protocol for a phase II randomized, double-blind, placebo-controlled, multicenter, clinical trial (RAP-ALS trial)","volume":"97","year":"2018","journal-title":"Medicine"},{"key":"2022103116073616600_BST-2022-0778CC137","doi-asserted-by":"publisher","first-page":"778","DOI":"10.1002\/mds.28923","article-title":"mTOR inhibition with sirolimus in multiple system atrophy: a randomized, double-blind, placebo-controlled futility trial and 1-year biomarker longitudinal analysis","volume":"37","year":"2022","journal-title":"Mov. Disord."},{"key":"2022103116073616600_BST-2022-0778CC138","doi-asserted-by":"publisher","first-page":"189","DOI":"10.3390\/ijms22010189","article-title":"Is there justification to treat neurodegenerative disorders by repurposing drugs? The case of Alzheimer's disease, lithium, and autophagy","volume":"22","year":"2020","journal-title":"Int. J. Mol. Sci."},{"key":"2022103116073616600_BST-2022-0778CC139","doi-asserted-by":"publisher","first-page":"135","DOI":"10.3390\/pharmaceutics13020135","article-title":"Lack of autophagy induction by lithium decreases neuroprotective effects in the striatum of aged rats","volume":"13","year":"2021","journal-title":"Pharmaceutics"},{"key":"2022103116073616600_BST-2022-0778CC140","doi-asserted-by":"publisher","first-page":"173","DOI":"10.1002\/mus.21423","article-title":"Autophagy, lithium, and amyotrophic lateral sclerosis","volume":"40","year":"2009","journal-title":"Muscle Nerve"},{"key":"2022103116073616600_BST-2022-0778CC141","doi-asserted-by":"publisher","first-page":"434","DOI":"10.1021\/cn500056q","article-title":"Lithium and autophagy","volume":"5","year":"2014","journal-title":"ACS Chem. Neurosci."},{"key":"2022103116073616600_BST-2022-0778CC142","doi-asserted-by":"publisher","first-page":"421","DOI":"10.1016\/j.devcel.2011.07.016","article-title":"Transcriptional activation of lysosomal exocytosis promotes cellular clearance","volume":"21","year":"2011","journal-title":"Dev. Cell"},{"key":"2022103116073616600_BST-2022-0778CC143","doi-asserted-by":"publisher","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","year":"2011","journal-title":"Hum. Mol. Genet."},{"key":"2022103116073616600_BST-2022-0778CC144","doi-asserted-by":"publisher","first-page":"1379","DOI":"10.4161\/auto.7.11.17166","article-title":"TFEB regulates autophagy: an integrated coordination of cellular degradation and recycling processes","volume":"7","year":"2011","journal-title":"Autophagy"},{"key":"2022103116073616600_BST-2022-0778CC145","doi-asserted-by":"publisher","first-page":"970","DOI":"10.1080\/15548627.2015.1047130","article-title":"Lysosomal calcium regulates autophagy","volume":"11","year":"2015","journal-title":"Autophagy"},{"key":"2022103116073616600_BST-2022-0778CC146","doi-asserted-by":"publisher","first-page":"288","DOI":"10.1038\/ncb3114","article-title":"Lysosomal calcium signalling regulates autophagy through calcineurin and TFEB","volume":"17","year":"2015","journal-title":"Nat. Cell Biol."},{"key":"2022103116073616600_BST-2022-0778CC147","doi-asserted-by":"publisher","first-page":"148","DOI":"10.1038\/nm985","article-title":"Trehalose alleviates polyglutamine-mediated pathology in a mouse model of Huntington disease","volume":"10","year":"2004","journal-title":"Nat. Med."},{"key":"2022103116073616600_BST-2022-0778CC148","doi-asserted-by":"publisher","first-page":"74","DOI":"10.1016\/j.nbd.2005.02.003","article-title":"Trehalose differentially inhibits aggregation and neurotoxicity of beta-amyloid 40 and 42","volume":"20","year":"2005","journal-title":"Neurobiol. Dis."},{"key":"2022103116073616600_BST-2022-0778CC149","doi-asserted-by":"publisher","first-page":"23","DOI":"10.1093\/hmg\/ddi422","article-title":"Trehalose reduces aggregate formation and delays pathology in a transgenic mouse model of oculopharyngeal muscular dystrophy","volume":"15","year":"2006","journal-title":"Hum. Mol. Genet."},{"key":"2022103116073616600_BST-2022-0778CC150","doi-asserted-by":"publisher","first-page":"5641","DOI":"10.1074\/jbc.M609532200","article-title":"Trehalose, a novel mTOR-independent autophagy enhancer, accelerates the clearance of mutant huntingtin and alpha-synuclein","volume":"282","year":"2007","journal-title":"J. Biol. Chem."},{"key":"2022103116073616600_BST-2022-0778CC151","doi-asserted-by":"publisher","first-page":"423","DOI":"10.1016\/j.nbd.2010.05.014","article-title":"Trehalose ameliorates dopaminergic and tau pathology in parkin deleted\/tau overexpressing mice through autophagy activation","volume":"39","year":"2010","journal-title":"Neurobiol. Dis."},{"key":"2022103116073616600_BST-2022-0778CC152","doi-asserted-by":"publisher","first-page":"334","DOI":"10.2174\/156720512800107573","article-title":"Trehalose protects from aggravation of amyloid pathology induced by isoflurane anesthesia in APP(swe) mutant mice","volume":"9","year":"2012","journal-title":"Curr. Alzheimer Res."},{"key":"2022103116073616600_BST-2022-0778CC153","doi-asserted-by":"publisher","first-page":"1686","DOI":"10.4161\/auto.21488","article-title":"Stimulation of autophagy is neuroprotective in a mouse model of human tauopathy","volume":"8","year":"2012","journal-title":"Autophagy"},{"key":"2022103116073616600_BST-2022-0778CC154","doi-asserted-by":"publisher","first-page":"2169","DOI":"10.1093\/brain\/aws143","article-title":"Stimulation of autophagy reduces neurodegeneration in a mouse model of human tauopathy","volume":"135","year":"2012","journal-title":"Brain"},{"key":"2022103116073616600_BST-2022-0778CC155","doi-asserted-by":"publisher","first-page":"1308","DOI":"10.4161\/auto.25188","article-title":"Trehalose delays the progression of amyotrophic lateral sclerosis by enhancing autophagy in motoneurons","volume":"9","year":"2013","journal-title":"Autophagy"},{"key":"2022103116073616600_BST-2022-0778CC156","doi-asserted-by":"publisher","first-page":"250","DOI":"10.1016\/j.neuro.2014.07.006","article-title":"Neuroprotective effect of the chemical chaperone, trehalose in a chronic MPTP-induced Parkinson's disease mouse model","volume":"44","year":"2014","journal-title":"Neurotoxicology"},{"key":"2022103116073616600_BST-2022-0778CC157","doi-asserted-by":"publisher","first-page":"12","DOI":"10.1016\/j.neuroscience.2015.03.061","article-title":"Trehalose decreases mutant SOD1 expression and alleviates motor deficiency in early but not end-stage amyotrophic lateral sclerosis in a SOD1-G93A mouse model","volume":"298","year":"2015","journal-title":"Neuroscience"},{"key":"2022103116073616600_BST-2022-0778CC158","doi-asserted-by":"publisher","first-page":"2258","DOI":"10.1007\/s12035-015-9173-7","article-title":"Treatment with trehalose prevents behavioral and neurochemical deficits produced in an AAV alpha-synuclein rat model of Parkinson's disease","volume":"53","year":"2016","journal-title":"Mol. Neurobiol."},{"key":"2022103116073616600_BST-2022-0778CC159","doi-asserted-by":"publisher","first-page":"24126","DOI":"10.1021\/acsami.7b06510","article-title":"Poly(trehalose) nanoparticles prevent amyloid aggregation and suppress polyglutamine aggregation in a Huntington's disease model mouse","volume":"9","year":"2017","journal-title":"ACS Appl. Mater. Interfaces"},{"key":"2022103116073616600_BST-2022-0778CC160","doi-asserted-by":"publisher","first-page":"247","DOI":"10.3390\/jcm11010247","article-title":"Impact of intravenous trehalose administration in patients with Niemann-Pick disease types A and B","volume":"11","year":"2022","journal-title":"J. Clin. Med."},{"key":"2022103116073616600_BST-2022-0778CC161","doi-asserted-by":"publisher","first-page":"3908","DOI":"10.1093\/hmg\/ddw232","article-title":"The chaperone HSPB8 reduces the accumulation of truncated TDP-43 species in cells and protects against TDP-43-mediated toxicity","volume":"25","year":"2016","journal-title":"Hum. Mol. Genet."}],"container-title":["Biochemical Society Transactions"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemsoctrans\/article-pdf\/50\/5\/1489\/938932\/bst-2022-0778c.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemsoctrans\/article-pdf\/50\/5\/1489\/938932\/bst-2022-0778c.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,10,31]],"date-time":"2022-10-31T16:07:55Z","timestamp":1667232475000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemsoctrans\/article\/50\/5\/1489\/231818\/The-role-of-autophagy-lysosomal-pathway-in-motor"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,9,16]]},"references-count":161,"journal-issue":{"issue":"5","published-online":{"date-parts":[[2022,9,16]]},"published-print":{"date-parts":[[2022,10,31]]}},"URL":"https:\/\/doi.org\/10.1042\/bst20220778","relation":{},"ISSN":["0300-5127","1470-8752"],"issn-type":[{"value":"0300-5127","type":"print"},{"value":"1470-8752","type":"electronic"}],"subject":[],"published":{"date-parts":[[2022,9,16]]}}}