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H\u00f6glund","year":"2006","journal-title":"Bioinformatics"},{"key":"ref50","doi-asserted-by":"crossref","first-page":"785","DOI":"10.1038\/nmeth.1701","article-title":"SignalP 4.0: discriminating signal peptides from transmembrane regions","volume":"8","author":"TN Petersen","year":"2011","journal-title":"Nat Methods"},{"key":"ref51","doi-asserted-by":"crossref","first-page":"W585","DOI":"10.1093\/nar\/gkm259","article-title":"WoLF PSORT: Protein localization predictor","volume":"35","author":"P Horton","year":"2007","journal-title":"Nucleic Acids Res"},{"key":"ref52","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1146\/annurev.ge.22.120188.003215","article-title":"The heat shock proteins","volume":"22","author":"S Lindquist","year":"1988","journal-title":"Ann. 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exogenous stimuli","volume":"23","author":"KM Edwards","year":"2004","journal-title":"Oncogene"},{"key":"ref88","doi-asserted-by":"crossref","first-page":"1475","DOI":"10.1016\/j.str.2003.10.012","article-title":"The Crystal Structure of the Yeast Hsp40 Ydj1 Complexed with Its Peptide Substrate","volume":"11","author":"J Li","year":"2003","journal-title":"Structure"},{"issue":"8","key":"ref89","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1016\/S0968-0004(98)01215-8","article-title":"The J-domain family and the recruitment of chaperone power","volume":"23","author":"WL Kelley","year":"1998","journal-title":"Trends Biochem Sci"},{"key":"ref90","doi-asserted-by":"crossref","first-page":"2825","DOI":"10.1016\/j.febslet.2015.07.040","article-title":"Functionality of Class A and Class B J-protein co-chaperones with Hsp70","volume":"589","author":"HY Yu","year":"2015","journal-title":"FEBS Lett"},{"key":"ref91","doi-asserted-by":"crossref","first-page":"e833","DOI":"10.1038\/cddis.2013.351","article-title":"Suppression of polyglutamine protein toxicity by co-expression of a heat-shock protein 40 and a heat-shock protein 110","volume":"4","author":"Y Kuo","year":"2013","journal-title":"Cell Death Dis"},{"key":"ref92","doi-asserted-by":"crossref","first-page":"24984","DOI":"10.1074\/jbc.M000739200","article-title":"HEDJ, an Hsp40 co-chaperone localized to the endoplasmic reticulum of human cells","volume":"275","author":"M Yu","year":"2000","journal-title":"J Biol Chem"},{"key":"ref93","doi-asserted-by":"crossref","first-page":"15947","DOI":"10.1074\/jbc.M112214200","article-title":"Identification and characterization of a novel endoplasmic reticulum (ER) DnaJ homologue, which stimulates ATPase activity of BiP in vitro and is induced by ER stress","volume":"277","author":"Y Shen","year":"2002","journal-title":"J. Biol. Chem"},{"issue":"6","key":"ref94","doi-asserted-by":"crossref","first-page":"1429","DOI":"10.1242\/jcs.118182","article-title":"ERdj3 regulates BiP occupancy in living cells","volume":"126","author":"F Guo","year":"2013","journal-title":"J Cell Sci"},{"key":"ref95","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1007\/s12192-011-0285-3","article-title":"Reactivation of protein aggregates by mortalin and Tid1-the human mitochondrial Hsp70 chaperone system","volume":"17","author":"O Iosefson","year":"2012","journal-title":"Cell Stress Chaperones"},{"key":"ref96","doi-asserted-by":"crossref","first-page":"785","DOI":"10.1007\/s00109-009-0471-2","article-title":"The role of redox modulation of class II histone deacetylases in mediating pathological cardiac hypertrophy","volume":"87","author":"SI Oka","year":"2009","journal-title":"J Mol Med"},{"key":"ref97","doi-asserted-by":"crossref","first-page":"34341","DOI":"10.1074\/jbc.M114.606392","article-title":"Class IIa histone deacetylases are conserved regulators of circadian function","volume":"289","author":"PCM Fogg","year":"2014","journal-title":"J Biol Chem"},{"key":"ref98","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1371\/journal.pone.0083903","article-title":"The histone deacetylase HDAC4 regulates long-term memory in Drosophila","volume":"8","author":"HL Fitzsimons","year":"2013","journal-title":"PLoS One"},{"issue":"24","key":"ref99","doi-asserted-by":"crossref","first-page":"17225","DOI":"10.1074\/jbc.M112.421685","article-title":"The DNAJB6 and DNAJB8 protein chaperones prevent intracellular aggregation of polyglutamine peptides","volume":"288","author":"J Gillis","year":"2013","journal-title":"J Biol Chem"},{"key":"ref100","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1016\/j.semcdb.2015.03.008","article-title":"Cysteine string protein (CSP) and its role in preventing neurodegeneration","volume":"40","author":"RD Burgoyne","year":"2015","journal-title":"Semin Cell Dev Biol"},{"key":"ref101","doi-asserted-by":"crossref","first-page":"899","DOI":"10.1016\/0896-6273(94)90255-0","article-title":"Presynaptic dysfunction in Drosophila csp mutants","volume":"13","author":"JA Umbach","year":"1994","journal-title":"Neuron"},{"issue":"22","key":"ref102","doi-asserted-by":"crossref","first-page":"2560","DOI":"10.1007\/s00018-006-6192-6","article-title":"The diversity of the DnaJ\/Hsp40 family, the crucial partners for Hsp70 chaperones","volume":"63","author":"XB Qiu","year":"2006","journal-title":"Cell Mol Life Sci"},{"issue":"9","key":"ref103","doi-asserted-by":"crossref","first-page":"1379","DOI":"10.1002\/mrd.20874","article-title":"A heat-shock protein 40, DNAJB13, is an axoneme-associated component in mouse spermatozoa","volume":"75","author":"J Guan","year":"2008","journal-title":"Mol Reprod Dev"},{"issue":"38","key":"ref104","article-title":"DNAJB13, a type II HSP40 family member, localizes to the spermatids and spermatozoa during mouse spermatogenesis","volume":"14","author":"W Li","year":"2014","journal-title":"BMC Dev Biol"},{"issue":"1","key":"ref105","doi-asserted-by":"crossref","first-page":"971","DOI":"10.1186\/s12864-016-3283-0","article-title":"Tsetse fly tolerance to T. brucei infection: transcriptome analysis of trypanosome-associated changes in the tsetse fly salivary gland","volume":"17","author":"I Matetovic","year":"2016","journal-title":"BMC Genomics"},{"issue":"6","key":"ref106","doi-asserted-by":"crossref","first-page":"915","DOI":"10.1101\/gr.115089.110","article-title":"High-throughput phenotyping using parallel sequencing of RNA interference targets in the African trypanosome","volume":"21","author":"S Alsford","year":"2011","journal-title":"Genome Res"},{"issue":"5","key":"ref107","doi-asserted-by":"crossref","first-page":"335","DOI":"10.4161\/chan.4.5.13090","article-title":"Channel triage: Emerging insights into the processing and quality control of hERG potassium channels by DnaJA proteins 1, 2 and 4","volume":"4","author":"E Ahrendt","year":"2010","journal-title":"Channels (Austin)"},{"key":"ref108","doi-asserted-by":"crossref","first-page":"682","DOI":"10.18632\/aging.100599","article-title":"Increased expression of Drosophila Sir2 extends life span in a dose-dependent manner","volume":"5","author":"R Whitaker","year":"2013","journal-title":"Aging"},{"issue":"12","key":"ref109","doi-asserted-by":"crossref","first-page":"2969","DOI":"10.1002\/j.1460-2075.1996.tb00660.x","article-title":"The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding","volume":"15","author":"BC Freeman","year":"1996","journal-title":"EMBO J"},{"issue":"12","key":"ref110","doi-asserted-by":"crossref","first-page":"825","DOI":"10.1093\/jnci\/djj229","article-title":"A new tumor suppressor DnaJ-like heat shock protein, HLJ1, and survival of patients with non-small-cell lung carcinoma","volume":"98","author":"MF Tsai","year":"2006","journal-title":"J Natl Cancer Inst"},{"key":"ref111","doi-asserted-by":"crossref","first-page":"978","DOI":"10.1016\/j.cell.2008.04.041","article-title":"A Redox-Dependent Pathway for Regulating Class II HDACs and Cardiac Hypertrophy","volume":"133","author":"T Ago","year":"2008","journal-title":"Cell"},{"issue":"1","key":"ref112","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1021\/bi8015923","article-title":"ERdj3, a luminal ER DnaJ homologue, binds directly to unfolded proteins in the mammalian ER: identification of critical residues","volume":"48","author":"Y Jin","year":"2009","journal-title":"Biochemistry"},{"key":"ref113","doi-asserted-by":"crossref","first-page":"19620","DOI":"10.1074\/jbc.M001333200","article-title":"Interaction of murine BiP\/GRP78 with the DnaJ homologue MTJ1","volume":"275","author":"M Chevalier","year":"2000","journal-title":"J Biol Chem"},{"issue":"12","key":"ref114","doi-asserted-by":"crossref","first-page":"11432","DOI":"10.1074\/jbc.M310903200","article-title":"The SANT2 domain of the murine tumor cell DnaJ-like protein 1 human homologue interacts with alpha1-antichymotrypsin and kinetically interferes with its serpin inhibitory activity","volume":"279","author":"B Kroczynska","year":"2004","journal-title":"J Biol Chem"},{"issue":"29","key":"ref115","doi-asserted-by":"crossref","first-page":"10064","DOI":"10.1073\/pnas.0504400102","article-title":"The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complex","volume":"102","author":"H Otto","year":"2005","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"25","key":"ref116","doi-asserted-by":"crossref","first-page":"15920","DOI":"10.1073\/pnas.252341799","article-title":"Control of PERK eIF2alpha kinase activity by the endoplasmic reticulum stress-induced molecular chaperone P58IPK","volume":"99","author":"W Yan","year":"2002","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"1","key":"ref117","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/j.virol.2011.04.020","article-title":"Virus infection rapidly activates the P58(IPK) pathway, delaying peak kinase activation to enhance viral replication","volume":"417","author":"AG Goodman","year":"2011","journal-title":"Virology"},{"issue":"10","key":"ref118","first-page":"1177","article-title":"The DnaJ60 gene of Drosophila melanogaster encodes a new member of the DnaJ family of proteins","volume":"378","author":"I Iliopoulos","year":"1997","journal-title":"Biol Chem"},{"key":"ref119","doi-asserted-by":"crossref","first-page":"2204","DOI":"10.1523\/JNEUROSCI.3610-04.2005","article-title":"The multiple functions of cysteine-string protein analyzed at Drosophila nerve terminals","volume":"25","author":"P Bronk","year":"2005","journal-title":"J Neurosci"},{"key":"ref120","doi-asserted-by":"crossref","first-page":"632","DOI":"10.1038\/378632a0","article-title":"Role of auxilin in uncoating clathrin-coated vesicles","volume":"378","author":"E Ungewickell","year":"1995","journal-title":"Nature"},{"issue":"14","key":"ref121","doi-asserted-by":"crossref","first-page":"3613","DOI":"10.1093\/emboj\/cdg362","article-title":"Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70\/Hsp90 chaperone system","volume":"22","author":"A Brychzy","year":"2003","journal-title":"EMBO J"},{"issue":"2","key":"ref122","doi-asserted-by":"crossref","first-page":"280","DOI":"10.1016\/j.bbrc.2006.12.013","article-title":"HDJC9, a novel human type C DnaJ\/HSP40 member interacts with and cochaperones HSP70 through the J domain","volume":"353","author":"C Han","year":"2007","journal-title":"Biochem Biophys Res Commun"},{"issue":"18","key":"ref123","doi-asserted-by":"crossref","first-page":"3545","DOI":"10.1016\/j.febslet.2007.06.052","article-title":"The mitochondrial inner membrane protein mitofilin exists as a complex with SAM50, metaxins 1 and 2, coiled-coil-helix coiled-coil-helix domain-containing protein 3 and 6 and DnaJC11","volume":"581","author":"J Xie","year":"2007","journal-title":"FEBS Lett"},{"issue":"3","key":"ref124","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1007\/s12192-013-0471-6","article-title":"The co-chaperone DNAJC12 binds to Hsc70 and is upregulated by endoplasmic reticulum stress","volume":"19","author":"J Choi","year":"2014","journal-title":"Cell Stress Chaperones"},{"key":"ref125","doi-asserted-by":"crossref","first-page":"40135","DOI":"10.1074\/jbc.M505036200","article-title":"The DnaJ-domain protein RME-8 functions in endosomal trafficking","volume":"280","author":"M Girard","year":"2005","journal-title":"J Biol Chem"},{"issue":"6","key":"ref126","doi-asserted-by":"crossref","first-page":"961","DOI":"10.1016\/j.febslet.2008.02.042","article-title":"RME-8 regulates trafficking of the epidermal growth factor receptor","volume":"582","author":"M Girard","year":"2008","journal-title":"FEBS Lett"},{"issue":"1","key":"ref127","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1038\/75556","article-title":"Gene ontology: tool for the unification of biology. The Gene Ontology Consortium","volume":"25","author":"M Ashburner","year":"2000","journal-title":"Nat Genet"},{"key":"ref128","doi-asserted-by":"crossref","first-page":"816","DOI":"10.1093\/emboj\/cdg090","article-title":"Tim50, a novel component of the TIM23 preprotein translocase of mitochondria","volume":"22","author":"D Mokranjac","year":"2003","journal-title":"EMBO J"},{"issue":"19","key":"ref129","doi-asserted-by":"crossref","first-page":"3816","DOI":"10.1093\/hmg\/ddq301","article-title":"Characterization of the human HSC20, an unusual DnaJ type III protein, involved in iron-sulfur cluster biogenesis","volume":"19","author":"H Uhrigshardt","year":"2010","journal-title":"Hum Mol Genet"},{"issue":"15","key":"ref130","doi-asserted-by":"crossref","first-page":"2783","DOI":"10.1016\/j.febslet.2007.05.013","article-title":"Nuclear export and cytoplasmic maturation of ribosomal subunits","volume":"581","author":"I Zemp","year":"2007","journal-title":"FEBS Lett"},{"issue":"9","key":"ref131","doi-asserted-by":"crossref","first-page":"1133","DOI":"10.1515\/BC.1999.142","article-title":"Molecular characterization of a novel mammalian DnaJ-like Sec63p homolog","volume":"380","author":"MH Skowronek","year":"1999","journal-title":"Biol Chem"},{"issue":"21","key":"ref132","doi-asserted-by":"crossref","first-page":"9487","DOI":"10.1128\/MCB.24.21.9487-9497.2004","article-title":"Identification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2","volume":"24","author":"S Liu","year":"2004","journal-title":"Mol Cell Biol"},{"issue":"2","key":"ref133","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1247\/csf.12017","article-title":"A novel mammalian ER-located J-protein, DNAJB14, can accelerate ERAD of misfolded membrane proteins","volume":"37","author":"P Sopha","year":"2012","journal-title":"Cell Struct Funct"}],"container-title":["PLOS ONE"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/dx.plos.org\/10.1371\/journal.pone.0183858","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,8,25]],"date-time":"2023-08-25T20:34:37Z","timestamp":1692995677000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pone.0183858"}},"subtitle":[],"editor":[{"given":"Nikolas","family":"Nikolaidis","sequence":"first","affiliation":[],"role":[{"role":"editor","vocabulary":"crossref"}]}],"short-title":[],"issued":{"date-parts":[[2017,9,13]]},"references-count":133,"journal-issue":{"issue":"9","published-online":{"date-parts":[[2017,9,13]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pone.0183858","relation":{},"ISSN":["1932-6203"],"issn-type":[{"type":"electronic","value":"1932-6203"}],"subject":[],"published":{"date-parts":[[2017,9,13]]}}}