{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T20:19:45Z","timestamp":1791404385918,"version":"4.3.3"},"reference-count":108,"publisher":"Frontiers Media SA","funder":[{"DOI":"10.13039\/100009281","name":"Fondation Thierry Latran","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100009281","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000368","name":"Brain Research Trust","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000368","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Mol. Neurosci."],"DOI":"10.3389\/fnmol.2017.00251","type":"journal-article","created":{"date-parts":[[2017,9,8]],"date-time":"2017-09-08T04:18:54Z","timestamp":1504844334000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":56,"title":["Cellular Chaperones As Therapeutic Targets in ALS to Restore Protein Homeostasis and Improve Cellular Function"],"prefix":"10.3389","volume":"10","author":[{"given":"Bernadett","family":"Kalmar","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Linda","family":"Greensmith","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1965","published-online":{"date-parts":[[2017,9,8]]},"reference":[{"key":"B1","doi-asserted-by":"publisher","DOI":"10.1126\/scitranslmed.aad4583","article-title":"Targeting protein homeostasis in sporadic inclusion body myositis.","volume":"8","author":"Ahmed","year":"2016","journal-title":"Sci. Transl. Med."},{"key":"B2","doi-asserted-by":"publisher","first-page":"479","DOI":"10.1016\/j.nbd.2008.08.010","article-title":"Mutant SOD1 from spinal cord of G93A rats is destabilized and binds to inner mitochondrial membrane.","volume":"32","author":"Ahtoniemi","year":"2008","journal-title":"Neurobiol. Dis."},{"key":"B3","doi-asserted-by":"publisher","first-page":"96","DOI":"10.1038\/nrneurol.2016.182","article-title":"Gene discovery in amyotrophic lateral sclerosis: implications for clinical management.","volume":"13","author":"Al-Chalabi","year":"2016","journal-title":"Nat. Rev. Neurol."},{"key":"B4","doi-asserted-by":"publisher","first-page":"602","DOI":"10.1016\/j.bbrc.2006.10.093","article-title":"TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis.","volume":"351","author":"Arai","year":"2006","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"B5","doi-asserted-by":"publisher","first-page":"400","DOI":"10.1016\/j.nbd.2008.02.009","article-title":"Endoplasmic reticulum stress and induction of the unfolded protein response in human sporadic amyotrophic lateral sclerosis.","volume":"30","author":"Atkin","year":"2008","journal-title":"Neurobiol. Dis."},{"key":"B6","doi-asserted-by":"crossref","first-page":"5789","DOI":"10.1523\/JNEUROSCI.23-13-05789.2003","article-title":"High threshold for induction of the stress response in motor neurons is associated with failure to activate HSF1.","volume":"23","author":"Batulan","year":"2003","journal-title":"J. Neurosci."},{"key":"B7","doi-asserted-by":"publisher","first-page":"213","DOI":"10.1016\/j.nbd.2006.06.017","article-title":"Induction of multiple heat shock proteins and neuroprotection in a primary culture model of familial amyotrophic lateral sclerosis.","volume":"24","author":"Batulan","year":"2006","journal-title":"Neurobiol. Dis."},{"key":"B8","doi-asserted-by":"publisher","first-page":"672","DOI":"10.1016\/j.tips.2016.04.007","article-title":"Breaking BAG: the Co-chaperone BAG3 in health and disease.","volume":"37","author":"Behl","year":"2016","journal-title":"Trends Pharmacol. Sci."},{"key":"B9","doi-asserted-by":"publisher","first-page":"9002","DOI":"10.1074\/jbc.272.14.9002","article-title":"Ubiquitin-dependent degradation of certain protein substrates in vitro requires the molecular chaperone Hsc70.","volume":"272","author":"Bercovich","year":"1997","journal-title":"J. Biol. Chem."},{"key":"B10","doi-asserted-by":"publisher","first-page":"39","DOI":"10.1016\/j.neuron.2006.09.018","article-title":"ALS: a disease of motor neurons and their nonneuronal neighbors.","volume":"52","author":"Boill\u00e9e","year":"2006","journal-title":"Neuron"},{"key":"B11","doi-asserted-by":"publisher","first-page":"3256","DOI":"10.1158\/0008-5472.CAN-03-3531","article-title":"Ubiquitination and proteasomal degradation of nucleophosmin-anaplastic lymphoma kinase induced by 17-allylamino-demethoxygeldanamycin: role of the co-chaperone carboxyl heat shock protein 70-interacting protein.","volume":"64","author":"Bonvini","year":"2004","journal-title":"Cancer Res."},{"key":"B12","doi-asserted-by":"publisher","first-page":"3","DOI":"10.1016\/j.neulet.2016.04.065","article-title":"Oxidative stress and mitochondrial damage in the pathogenesis of ALS: new perspectives.","volume":"636","author":"Bozzo","year":"2016","journal-title":"Neurosci. Lett"},{"key":"B13","first-page":"1","article-title":"\u201cGrpE, Hsp110\/Grp170, HspBP1\/Sil1 and BAG domain proteins: nucleotide exchange factors for Hsp70 molecular chaperones,\u201d in","author":"Bracher","year":"2015","journal-title":"Sub-Cellular Biochemistry"},{"key":"B14","doi-asserted-by":"publisher","first-page":"473","DOI":"10.1111\/j.1365-2990.1995.tb01088.x","article-title":"The stress response.","volume":"21","author":"Brown","year":"1995","journal-title":"Neuropathol. Appl. Neurobiol."},{"key":"B15","doi-asserted-by":"publisher","first-page":"693","DOI":"10.1046\/j.1471-4159.1999.0720693.x","article-title":"Up-regulation of protein chaperones preserves viability of cells expressing toxic Cu\/Zn-superoxide dismutase mutants associated with amyotrophic lateral sclerosis.","volume":"72","author":"Bruening","year":"1999","journal-title":"J. Neurochem"},{"key":"B16","doi-asserted-by":"publisher","DOI":"10.4103\/2319-4170.113230","article-title":"Structure, function and regulation of the Hsp90 machinery.","volume":"36","author":"Buchner","year":"2013","journal-title":"Biomed. J."},{"key":"B17","doi-asserted-by":"publisher","first-page":"628","DOI":"10.1016\/j.cell.2009.08.005","article-title":"Importing Mitochondrial proteins: machineries and mechanisms.","volume":"138","author":"Chacinska","year":"2009","journal-title":"Cell"},{"key":"B18","doi-asserted-by":"publisher","first-page":"1417","DOI":"10.1093\/brain\/aww028","article-title":"The heat shock response plays an important role in TDP-43 clearance: evidence for dysfunction in amyotrophic lateral sclerosis.","volume":"139","author":"Chen","year":"2016","journal-title":"Brain"},{"key":"B19","doi-asserted-by":"publisher","first-page":"110","DOI":"10.1111\/j.1750-3639.2011.00546.x","article-title":"Autophagy dysregulation in amyotrophic lateral sclerosis.","volume":"22","author":"Chen","year":"2012","journal-title":"Brain Pathol."},{"key":"B20","doi-asserted-by":"publisher","first-page":"82","DOI":"10.1093\/hmg\/ddn319","article-title":"Functional alterations of the ubiquitin-proteasome system in motor neurons of a mouse model of familial amyotrophic lateral sclerosis.","volume":"18","author":"Cheroni","year":"2009","journal-title":"Hum. Mol. Genet."},{"key":"B21","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","author":"Crippa","year":"2010","journal-title":"Hum. Mol. Genet."},{"key":"B22","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","author":"DeJesus-Hernandez","year":"2011","journal-title":"Neuron"},{"key":"B23","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pgen.1005357","article-title":"FUS Interacts with HSP60 to Promote Mitochondrial Damage.","volume":"11","author":"Deng","year":"2015","journal-title":"PLOS Genet."},{"key":"B24","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1007\/978-3-319-29073-7_11","article-title":"\u201cRNA granules and diseases: a case study of stress granules in ALS and FTLD,\u201d in","author":"Fan","year":"2016","journal-title":"Advances in Experimental Medicine and Biology"},{"key":"B25","doi-asserted-by":"publisher","first-page":"591","DOI":"10.1007\/s12192-013-0413-3","article-title":"Proteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasis.","volume":"18","author":"Finka","year":"2013","journal-title":"Cell Stress Chaperones"},{"key":"B26","doi-asserted-by":"publisher","first-page":"1062","DOI":"10.1111\/j.1471-4159.2009.06388.x","article-title":"Sequestosome 1\/p62 links familial ALS mutant SOD1 to LC3 via an ubiquitin-independent mechanism.","volume":"111","author":"Gal","year":"2009","journal-title":"J. Neurochem."},{"key":"B27","doi-asserted-by":"publisher","first-page":"796","DOI":"10.1016\/j.molcel.2016.07.021","article-title":"A surveillance function of the HSPB8-BAG3-HSP70 chaperone complex ensures stress granule integrity and dynamism.","volume":"63","author":"Ganassi","year":"2016","journal-title":"Mol. Cell"},{"key":"B28","doi-asserted-by":"publisher","first-page":"39","DOI":"10.1111\/j.1365-2990.1991.tb00692.x","article-title":"Ubiquitin and heat shock protein expression in amyotrophic lateral sclerosis.","volume":"17","author":"Garofalo","year":"1991","journal-title":"Neuropathol. Appl. Neurobiol."},{"key":"B29","doi-asserted-by":"publisher","first-page":"394","DOI":"10.1038\/nature10980","article-title":"Hsp72 preserves muscle function and slows progression of severe muscular dystrophy.","volume":"484","author":"Gehrig","year":"2012","journal-title":"Nature"},{"key":"B30","doi-asserted-by":"publisher","first-page":"13173","DOI":"10.1523\/JNEUROSCI.4057-07.2007","article-title":"Exogenous delivery of heat shock protein 70 increases lifespan in a mouse model of amyotrophic lateral sclerosis.","volume":"27","author":"Gifondorwa","year":"2007","journal-title":"J. Neurosci."},{"key":"B31","doi-asserted-by":"publisher","first-page":"3849","DOI":"10.1242\/jcs.075119","article-title":"The mitochondrial UPR - protecting organelle protein homeostasis.","volume":"123","author":"Haynes","year":"2010","journal-title":"J. Cell Sci."},{"key":"B32","doi-asserted-by":"publisher","first-page":"14426","DOI":"10.1074\/jbc.M100266200","article-title":"The yeast hsp70 homologue Ssa is required for translation and interacts with Sis1 and Pab1 on translating ribosomes.","volume":"276","author":"Horton","year":"2001","journal-title":"J. Biol. Chem."},{"key":"B33","doi-asserted-by":"publisher","first-page":"104","DOI":"10.1046\/j.1365-2990.1998.00108.x","article-title":"Amyotrophic lateral sclerosis: current issues in classification, pathogenesis and molecular pathology.","volume":"24","author":"Ince","year":"1998","journal-title":"Neuropathol. Appl. Neurobiol."},{"key":"B34","doi-asserted-by":"publisher","first-page":"367","DOI":"10.3109\/17482968.2012.686511","article-title":"Impaired proteasome function in sporadic amyotrophic lateral sclerosis.","volume":"13","author":"Kabashi","year":"2012","journal-title":"Amyotroph. Lateral Scler."},{"key":"B35","doi-asserted-by":"publisher","first-page":"1325","DOI":"10.1111\/j.1471-4159.2004.02453.x","article-title":"Focal dysfunction of the proteasome: a pathogenic factor in a mouse model of amyotrophic lateral sclerosis.","volume":"89","author":"Kabashi","year":"2004","journal-title":"J. Neurochem."},{"key":"B36","doi-asserted-by":"publisher","first-page":"378","DOI":"10.3109\/17482968.2012.660953","article-title":"Treatment with a coinducer of the heat shock response delays muscle denervation in the SOD1-G93A mouse model of amyotrophic lateral sclerosis.","volume":"13","author":"Kalmar","year":"2012","journal-title":"Amyotroph. Lateral Scler."},{"key":"B37","author":"Kalmar","year":"2008","journal-title":"Heat Shock Proteins and the Brain: Implications for Neurodegeneratice Diseases and Neuroprotection: Section 1: Heat Shock Proteins and Neurodegenerative Diseases"},{"key":"B38","doi-asserted-by":"publisher","first-page":"319","DOI":"10.2478\/s11658-009-0002-8","article-title":"Activation of the heat shock response in a primary cellular model of motoneuron neurodegeneration-evidence for neuroprotective and neurotoxic effects.","volume":"14","author":"Kalmar","year":"2009","journal-title":"Cell. Mol. Biol. Lett."},{"key":"B39","doi-asserted-by":"publisher","first-page":"636","DOI":"10.1016\/S0014-4886(03)00343-1","article-title":"The effect of treatment with BRX-220, a co-inducer of heat shock proteins, on sensory fibers of the rat following peripheral nerve injury.","volume":"184","author":"Kalmar","year":"2003","journal-title":"Exp. Neurol."},{"key":"B40","doi-asserted-by":"publisher","DOI":"10.1093\/hmg\/ddx216","article-title":"Mitochondrial deficits and abnormal mitochondrial retrograde axonal transport play a role in the pathogenesis of mutant Hsp27 induced charcot marie tooth disease.","author":"Kalmar","year":"2017","journal-title":"Hum. Mol. Genet."},{"key":"B41","doi-asserted-by":"publisher","first-page":"339","DOI":"10.1111\/j.1471-4159.2008.05595.x","article-title":"Late stage treatment with arimoclomol delays disease progression and prevents protein aggregation in the SOD1 mouse model of ALS.","volume":"107","author":"Kalmar","year":"2008","journal-title":"J. Neurochem."},{"key":"B42","doi-asserted-by":"publisher","first-page":"81","DOI":"10.1007\/s12035-009-8054-3","article-title":"ER stress and unfolded protein response in amyotrophic lateral sclerosis.","volume":"39","author":"Kanekura","year":"2009","journal-title":"Mol. Neurobiol."},{"key":"B43","doi-asserted-by":"publisher","first-page":"1256","DOI":"10.4161\/auto.7.10.16753","article-title":"Metabolic regulation by HMGB1-mediated autophagy and mitophagy.","volume":"7","author":"Kang","year":"2011","journal-title":"Autophagy"},{"key":"B44","doi-asserted-by":"publisher","first-page":"16801","DOI":"10.1073\/pnas.0506249102","article-title":"Pharmacological induction of heat-shock proteins alleviates polyglutamine-mediated motor neuron disease.","volume":"102","author":"Katsuno","year":"2005","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"B45","doi-asserted-by":"publisher","first-page":"246","DOI":"10.1159\/000090364","article-title":"Celastrol blocks neuronal cell death and extends life in transgenic mouse model of amyotrophic lateral sclerosis.","volume":"2","author":"Kiaei","year":"2005","journal-title":"Neurodegener. Dis."},{"key":"B46","doi-asserted-by":"publisher","first-page":"402","DOI":"10.1038\/nm1021","article-title":"Treatment with arimoclomol, a coinducer of heat shock proteins, delays disease progression in ALS mice.","volume":"10","author":"Kieran","year":"2004","journal-title":"Nat. Med."},{"key":"B47","doi-asserted-by":"publisher","first-page":"6025","DOI":"10.1073\/pnas.0509227103","article-title":"Spinal cord endoplasmic reticulum stress associated with a microsomal accumulation of mutant superoxide dismutase-1 in an ALS model.","volume":"103","author":"Kikuchi","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"B48","doi-asserted-by":"publisher","first-page":"1399","DOI":"10.1016\/j.febslet.2009.12.025","article-title":"Chaperone-mediated autophagy in health and disease.","volume":"584","author":"Kon","year":"2010","journal-title":"FEBS Lett."},{"key":"B49","doi-asserted-by":"publisher","first-page":"532","DOI":"10.1111\/j.1742-4658.2011.08456.x","article-title":"Molecular chaperones in targeting misfolded proteins for ubiquitin-dependent degradation.","volume":"279","author":"Kriegenburg","year":"2012","journal-title":"FEBS J."},{"key":"B50","doi-asserted-by":"publisher","first-page":"2170","DOI":"10.1111\/j.1471-4159.2008.05545.x","article-title":"Over-expression of Hsp27 does not influence disease in the mutant SOD1(G93A) mouse model of amyotrophic lateral sclerosis.","volume":"106","author":"Krishnan","year":"2008","journal-title":"J. Neurochem."},{"key":"B51","doi-asserted-by":"publisher","DOI":"10.1186\/2051-5960-1-24","article-title":"Amyotrophic lateral sclerosis (ALS)-associated VAPB-P56S inclusions represent an ER quality control compartment.","volume":"1","author":"Kuijpers","year":"2013","journal-title":"Acta Neuropathol. Commun."},{"key":"B52","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","author":"Kwiatkowski","year":"2009","journal-title":"Science"},{"key":"B53","doi-asserted-by":"publisher","first-page":"1488","DOI":"10.1038\/nn.3230","article-title":"artICleS Divergent roles of ALS-linked proteins FUS \/ TLS and TDP-43 intersect in processing long pre-mRNAs.","volume":"15","author":"Lagier-tourenne","year":"2012","journal-title":"Nat. Neurosci."},{"key":"B54","doi-asserted-by":"publisher","first-page":"775","DOI":"10.1093\/brain\/114.2.775","article-title":"Ubiquitin-immunoreactive intraneuronal inclusions in amyotrophic lateral sclerosis. Morphology, distribution, and specificity.","volume":"114","author":"Leigh","year":"1991","journal-title":"Brain"},{"key":"B55","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","author":"Li","year":"2008","journal-title":"Autophagy"},{"key":"B56","doi-asserted-by":"publisher","first-page":"21146","DOI":"10.1073\/pnas.1014862107","article-title":"ALS-linked mutant superoxide dismutase 1 (SOD1) alters mitochondrial protein composition and decreases protein import.","volume":"107","author":"Li","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"B57","doi-asserted-by":"publisher","first-page":"5089","DOI":"10.1074\/jbc.M116.753913","article-title":"Heat Shock-induced Phosphorylation of TAR DNA-binding Protein 43 (TDP-43) by MAPK\/ERK kinase regulates TDP-43 Function.","volume":"292","author":"Li","year":"2017","journal-title":"J. Biol. Chem."},{"key":"B58","doi-asserted-by":"publisher","first-page":"671","DOI":"10.1002\/jnr.23725","article-title":"Overexpression of heat shock factor 1 maintains TAR DNA binding protein 43 solubility via induction of inducible heat shock protein 70 in cultured cells.","volume":"94","author":"Lin","year":"2016","journal-title":"J. Neurosci. Res."},{"key":"B59","doi-asserted-by":"publisher","first-page":"5","DOI":"10.1016\/j.neuron.2004.06.016","article-title":"Toxicity of familial ALS-linked SOD1 mutants from selective recruitment to spinal mitochondria.","volume":"43","author":"Liu","year":"2004","journal-title":"Neuron"},{"key":"B60","doi-asserted-by":"publisher","first-page":"4613","DOI":"10.1074\/jbc.275.7.4613","article-title":"The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70\/Hsp70 and the proteasome.","volume":"275","author":"L\u00fcders","year":"2000","journal-title":"J. Biol. Chem."},{"key":"B61","doi-asserted-by":"publisher","first-page":"926","DOI":"10.1093\/brain\/aws343","article-title":"Co-induction of the heat shock response ameliorates disease progression in a mouse model of human spinal and bulbar muscular atrophy: implications for therapy.","volume":"136","author":"Malik","year":"2013","journal-title":"Brain"},{"key":"B62","doi-asserted-by":"publisher","first-page":"99","DOI":"10.1111\/j.1749-6632.1998.tb08982.x","article-title":"Role of the heat-shock response in the life and death of proteins.","volume":"851","author":"Mathew","year":"1998","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"B63","doi-asserted-by":"publisher","first-page":"670","DOI":"10.1007\/s00018-004-4464-6","article-title":"Hsp70 chaperones: cellular functions and molecular mechanism.","volume":"62","author":"Mayer","year":"2005","journal-title":"Cell. Mol. Life Sci."},{"key":"B64","doi-asserted-by":"publisher","first-page":"3877","DOI":"10.1242\/jcs.093831","article-title":"The VCP\/p97 system at a glance: connecting cellular function to disease pathogenesis.","volume":"127","author":"Meyer","year":"2014","journal-title":"J. Cell Sci."},{"key":"B65","doi-asserted-by":"publisher","first-page":"1277","DOI":"10.1007\/s10072-016-2582-1","article-title":"Elevation of serum heat-shock protein levels in amyotrophic lateral sclerosis.","volume":"37","author":"Miyazaki","year":"2016","journal-title":"Neurol. Sci."},{"key":"B66","doi-asserted-by":"publisher","first-page":"1192","DOI":"10.1126\/science.1256800","article-title":"C9orf72 repeat expansions cause neurodegeneration in Drosophila through arginine-rich proteins.","volume":"345","author":"Mizielinska","year":"2014","journal-title":"Science"},{"key":"B67","doi-asserted-by":"publisher","first-page":"E3349","DOI":"10.1073\/pnas.1523810113","article-title":"Dynamic recruitment and activation of ALS-associated TBK1 with its target optineurin are required for efficient mitophagy.","volume":"113","author":"Moore","year":"2016","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"B68","doi-asserted-by":"publisher","first-page":"1427","DOI":"10.1101\/gad.1657108","article-title":"Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging.","volume":"22","author":"Morimoto","year":"2008","journal-title":"Genes Dev."},{"key":"B69","doi-asserted-by":"publisher","first-page":"1975","DOI":"10.1093\/hmg\/ddt594","article-title":"The amyotrophic lateral sclerosis 8 protein, VAP, is required for ER protein quality control.","volume":"23","author":"Moustaqim-Barrette","year":"2014","journal-title":"Hum. Mol. Genet."},{"key":"B70","doi-asserted-by":"publisher","first-page":"710","DOI":"10.1038\/nature18302","article-title":"Mitochondrial unfolded protein response controls matrix pre-RNA processing and translation.","volume":"534","author":"M\u00fcnch","year":"2016","journal-title":"Nature"},{"key":"B71","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pbio.1000291","article-title":"Modulation of heat shock transcription factor 1 as a therapeutic target for small molecule intervention in neurodegenerative disease.","volume":"8","author":"Neef","year":"2010","journal-title":"PLOS Biol."},{"key":"B72","doi-asserted-by":"publisher","first-page":"130","DOI":"10.1126\/science.1134108","article-title":"Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis.","volume":"314","author":"Neumann","year":"2006","journal-title":"Science"},{"key":"B73","doi-asserted-by":"publisher","first-page":"9010","DOI":"10.1073\/pnas.132260399","article-title":"Amyotrophic lateral sclerosis: a proposed mechanism.","volume":"99","author":"Okado-Matsumoto","year":"2002","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"B74","doi-asserted-by":"publisher","first-page":"324","DOI":"10.1016\/j.bbrc.2016.02.107","article-title":"Disturbance of proteasomal and autophagic protein degradation pathways by amyotrophic lateral sclerosis-linked mutations in ubiquilin 2.","volume":"472","author":"Osaka","year":"2016","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"B75","doi-asserted-by":"publisher","DOI":"10.1038\/cddis.2014.214","article-title":"The heat-shock response co-inducer arimoclomol protects against retinal degeneration in rhodopsin retinitis pigmentosa.","volume":"5","author":"Parfitt","year":"2014","journal-title":"Cell Death Dis."},{"key":"B76","doi-asserted-by":"publisher","first-page":"415","DOI":"10.1016\/j.neuint.2012.01.019","article-title":"Endogenous TDP-43 localized to stress granules can subsequently form protein aggregates.","volume":"60","author":"Parker","year":"2012","journal-title":"Neurochem. Int."},{"key":"B77","doi-asserted-by":"publisher","first-page":"19","DOI":"10.1016\/j.neuron.2004.06.021","article-title":"Amyotrophic lateral sclerosis-associated SOD1 mutant proteins bind and aggregate with Bcl-2 in spinal cord mitochondria.","volume":"43","author":"Pasinelli","year":"2004","journal-title":"Neuron"},{"key":"B78","doi-asserted-by":"publisher","first-page":"1066","DOI":"10.1016\/j.cell.2015.07.047","article-title":"A Liquid-to-solid phase transition of the ALS protein FUS accelerated by disease mutation.","volume":"162","author":"Patel","year":"2015","journal-title":"Cell"},{"key":"B79","doi-asserted-by":"publisher","first-page":"256","DOI":"10.1016\/j.molbrainres.2004.10.028","article-title":"Hsp27 and Hsp70 administered in combination have a potent protective effect against FALS-associated SOD1-mutant-induced cell death in mammalian neuronal cells.","volume":"134","author":"Patel","year":"2005","journal-title":"Brain Res. Mol. Brain Res."},{"key":"B80","doi-asserted-by":"publisher","first-page":"87","DOI":"10.2174\/1874609811205020087","article-title":"Longevity pathways: HSF1 and FoxO pathways, a new therapeutic target to prevent age-related diseases.","volume":"5","author":"Perez","year":"2012","journal-title":"Curr. Aging Sci."},{"key":"B81","doi-asserted-by":"publisher","DOI":"10.3389\/fcell.2015.00080","article-title":"The unfolded protein response and the role of protein disulfide isomerase in neurodegeneration.","volume":"3","author":"Perri","year":"2016","journal-title":"Front. Cell Dev. Biol."},{"key":"B82","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0035050","article-title":"Aberrant localization of FUS and TDP43 is associated with misfolding of SOD1 in amyotrophic lateral sclerosis.","volume":"7","author":"Pokrishevsky","year":"2012","journal-title":"PLOS ONE"},{"key":"B83","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pbio.0050172","article-title":"PINK1 protects against oxidative stress by phosphorylating mitochondrial chaperone TRAP1.","volume":"5","author":"Pridgeon","year":"2007","journal-title":"PLOS Biol."},{"key":"B84","doi-asserted-by":"publisher","first-page":"379","DOI":"10.1007\/s12192-016-0676-6","article-title":"The human HSP70 family of chaperones: where do we stand?","volume":"21","author":"Radons","year":"2016","journal-title":"Cell Stress Chaperones"},{"key":"B85","doi-asserted-by":"publisher","first-page":"4039","DOI":"10.1073\/pnas.1523926113","article-title":"Phosphorylation of OPTN by TBK1 enhances its binding to Ub chains and promotes selective autophagy of damaged mitochondria.","volume":"113","author":"Richter","year":"2016","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"B86","doi-asserted-by":"publisher","first-page":"9735","DOI":"10.1523\/JNEUROSCI.1912-05.2005","article-title":"Extracellular heat shock protein 70: a critical component for motoneuron survival.","volume":"25","author":"Robinson","year":"2005","journal-title":"J. Neurosci."},{"key":"B87","doi-asserted-by":"publisher","first-page":"326","DOI":"10.1038\/35014014","article-title":"Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response.","volume":"2","author":"Ron","year":"2000","journal-title":"Nat. Cell Biol."},{"key":"B88","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","author":"Rosen","year":"1993","journal-title":"Nature"},{"key":"B89","doi-asserted-by":"publisher","first-page":"443","DOI":"10.1038\/nature21695","article-title":"Cytosolic proteostasis through importing of misfolded proteins into mitochondria.","volume":"543","author":"Ruan","year":"2017","journal-title":"Nature"},{"key":"B90","doi-asserted-by":"publisher","first-page":"571","DOI":"10.1016\/j.brainres.2016.03.032","article-title":"Proteostasis impairment in ALS.","volume":"1648","author":"Ruegsegger","year":"2016","journal-title":"Brain Res."},{"key":"B91","doi-asserted-by":"publisher","DOI":"10.1038\/ncomms6705","article-title":"The small-molecule BGP-15 protects against heart failure and atrial fibrillation in mice.","volume":"5","author":"Sapra","year":"2014","journal-title":"Nat. Commun."},{"key":"B92","doi-asserted-by":"publisher","first-page":"627","DOI":"10.1038\/nn.2297","article-title":"A role for motoneuron subtype-selective ER stress in disease manifestations of FALS mice.","volume":"12","author":"Saxena","year":"2009","journal-title":"Nat. Neurosci."},{"key":"B93","doi-asserted-by":"publisher","DOI":"10.3389\/fnmol.2017.00119","article-title":"Protein Quality control and the amyotrophic lateral sclerosis\/frontotemporal dementia continuum.","volume":"10","author":"Shahheydari","year":"2017","journal-title":"Front. Mol. Neurosci."},{"key":"B94","doi-asserted-by":"publisher","first-page":"42","DOI":"10.1016\/j.nbd.2007.12.002","article-title":"Protective effects of heat shock protein 27 in a model of ALS occur in the early stages of disease progression.","volume":"30","author":"Sharp","year":"2008","journal-title":"Neurobiol. Dis."},{"key":"B95","doi-asserted-by":"publisher","first-page":"8340","DOI":"10.1074\/jbc.M707751200","article-title":"Detergent-insoluble aggregates associated with amyotrophic lateral sclerosis in transgenic mice contain primarily full-length, unmodified superoxide dismutase-1.","volume":"283","author":"Shaw","year":"2008","journal-title":"J. Biol. Chem."},{"key":"B96","doi-asserted-by":"publisher","first-page":"704","DOI":"10.3390\/biom4030704","article-title":"Chaperoning proteins for destruction: diverse roles of Hsp70 chaperones and their co-chaperones in targeting misfolded proteins to the proteasome.","volume":"4","author":"Shiber","year":"2014","journal-title":"Biomolecules"},{"key":"B97","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","author":"Sreedharan","year":"2008","journal-title":"Science"},{"key":"B98","doi-asserted-by":"publisher","first-page":"515","DOI":"10.1038\/nrm2918","article-title":"HSP90 at the hub of protein homeostasis: emerging mechanistic insights.","volume":"11","author":"Taipale","year":"2010","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"B99","doi-asserted-by":"publisher","first-page":"1815","DOI":"10.1002\/dneu.20559","article-title":"Regulation of heat shock protein 70 release in astrocytes: role of signaling kinases.","volume":"67","author":"Taylor","year":"2007","journal-title":"Dev. Neurobiol."},{"key":"B100","doi-asserted-by":"publisher","first-page":"197","DOI":"10.1038\/nature20413","article-title":"Decoding ALS: from genes to mechanism.","volume":"539","author":"Taylor","year":"2016","journal-title":"Nature"},{"key":"B101","doi-asserted-by":"publisher","first-page":"285","DOI":"10.1016\/j.cbpa.2010.02.015","article-title":"Celastrol can inhibit proteasome activity and upregulate the expression of heat shock protein genes, hsp30 and hsp70, in Xenopus laevis A6 cells.","volume":"156","author":"Walcott","year":"2010","journal-title":"Comp. Biochem. Physiol. A Mol. Integr. Physiol."},{"key":"B102","doi-asserted-by":"publisher","first-page":"552","DOI":"10.1016\/j.tibs.2015.08.004","article-title":"Coupling of ribostasis and proteostasis: Hsp70 proteins in mRNA metabolism.","volume":"40","author":"Walters","year":"2015","journal-title":"Trends Biochem. Sci."},{"key":"B103","doi-asserted-by":"publisher","first-page":"933","DOI":"10.1006\/nbdi.2001.0443","article-title":"Histological evidence of protein aggregation in mutant SOD1 transgenic mice and in amyotrophic lateral sclerosis neural tissues.","volume":"8","author":"Watanabe","year":"2001","journal-title":"Neurobiol. Dis."},{"key":"B104","doi-asserted-by":"publisher","first-page":"56053","DOI":"10.1074\/jbc.M409267200","article-title":"Celastrols as inducers of the heat shock response and cytoprotection.","volume":"279","author":"Westerheide","year":"2004","journal-title":"J. Biol. Chem."},{"key":"B105","doi-asserted-by":"publisher","first-page":"1058","DOI":"10.1016\/j.cub.2005.04.058","article-title":"HSJ1 is a neuronal shuttling factor for the sorting of chaperone clients to the proteasome.","volume":"15","author":"Westhoff","year":"2005","journal-title":"Curr. Biol."},{"key":"B106","doi-asserted-by":"publisher","first-page":"E4439","DOI":"10.1073\/pnas.1405752111","article-title":"Optineurin is an autophagy receptor for damaged mitochondria in parkin-mediated mitophagy that is disrupted by an ALS-linked mutation.","volume":"111","author":"Wong","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"B107","doi-asserted-by":"publisher","first-page":"291","DOI":"10.1139\/O09-175","article-title":"Mechanisms of the Hsp70 chaperone system This paper is one of a selection of papers published in this special issue entitled \u201cCanadian society of biochemistry, molecular & cellular biology 52nd annual meeting \u2014 protein folding: principles and diseases\u201d and has undergone the Journal\u2019s usual peer review process.","volume":"88","author":"Young","year":"2010","journal-title":"Biochem. Cell Biol."},{"key":"B108","first-page":"1628","article-title":"Analysis of sequence-specific binding of RNA to Hsp70 and its various homologs indicates the involvement of N- and C-terminal interactions.","volume":"7","author":"Zimmer","year":"2001","journal-title":"RNA"}],"container-title":["Frontiers in Molecular Neuroscience"],"original-title":[],"link":[{"URL":"http:\/\/journal.frontiersin.org\/article\/10.3389\/fnmol.2017.00251\/full","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2019,10,3]],"date-time":"2019-10-03T07:24:25Z","timestamp":1570087465000},"score":1,"resource":{"primary":{"URL":"http:\/\/journal.frontiersin.org\/article\/10.3389\/fnmol.2017.00251\/full"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,9,8]]},"references-count":108,"alternative-id":["10.3389\/fnmol.2017.00251"],"URL":"https:\/\/doi.org\/10.3389\/fnmol.2017.00251","relation":{},"ISSN":["1662-5099"],"issn-type":[{"value":"1662-5099","type":"electronic"}],"subject":[],"published":{"date-parts":[[2017,9,8]]},"article-number":"251"}}