{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T03:19:46Z","timestamp":1791083986873,"version":"4.1.0"},"reference-count":85,"publisher":"Elsevier BV","issue":"24","license":[{"start":{"date-parts":[[2020,6,1]],"date-time":"2020-06-01T00:00:00Z","timestamp":1590969600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,11,15]],"date-time":"2020-11-15T00:00:00Z","timestamp":1605398400000},"content-version":"vor","delay-in-days":167,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100002855","name":"Ministry of Science and Technology of the People's Republic of China","doi-asserted-by":"publisher","award":["2017YFA0504000"],"award-info":[{"award-number":["2017YFA0504000"]}],"id":[{"id":"10.13039\/501100002855","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["31570780"],"award-info":[{"award-number":["31570780"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["31770829"],"award-info":[{"award-number":["31770829"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["21673278"],"award-info":[{"award-number":["21673278"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["31920103011"],"award-info":[{"award-number":["31920103011"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["31470747"],"award-info":[{"award-number":["31470747"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["91849203"],"award-info":[{"award-number":["91849203"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["31570857"],"award-info":[{"award-number":["31570857"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004826","name":"Natural Science Foundation of Beijing Municipality","doi-asserted-by":"publisher","award":["5172026"],"award-info":[{"award-number":["5172026"]}],"id":[{"id":"10.13039\/501100004826","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2020,6]]},"DOI":"10.1074\/jbc.ra119.012372","type":"journal-article","created":{"date-parts":[[2020,4,24]],"date-time":"2020-04-24T20:49:29Z","timestamp":1587761369000},"page":"8302-8324","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":35,"title":["S-Glutathionylation of human inducible Hsp70 reveals a regulatory mechanism involving the C-terminal \u03b1-helical lid"],"prefix":"10.1016","volume":"295","author":[{"given":"Jie","family":"Yang","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9204-2547","authenticated-orcid":false,"given":"Hong","family":"Zhang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7130-4093","authenticated-orcid":false,"given":"Weibin","family":"Gong","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhenyan","family":"Liu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Huiwen","family":"Wu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wanhui","family":"Hu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xinxin","family":"Chen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5071-5800","authenticated-orcid":false,"given":"Lei","family":"Wang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7743-8236","authenticated-orcid":false,"given":"Si","family":"Wu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1008-1062","authenticated-orcid":false,"given":"Chang","family":"Chen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0137-0997","authenticated-orcid":false,"given":"Sarah","family":"Perrett","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.RA119.012372_bib1","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1146\/annurev-biochem-060208-092442","article-title":"Molecular chaperone functions in protein folding and proteostasis","volume":"82","author":"Kim","year":"2013","journal-title":"Annu. Rev. Biochem"},{"key":"10.1074\/jbc.RA119.012372_bib2","doi-asserted-by":"crossref","first-page":"1575","DOI":"10.1016\/j.jmb.2015.02.004","article-title":"How hsp70 molecular machines interact with their substrates to mediate diverse physiological functions","volume":"427","author":"Clerico","year":"2015","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.RA119.012372_bib3","doi-asserted-by":"crossref","first-page":"4585","DOI":"10.1021\/jm100054f","article-title":"Heat shock protein 70 (hsp70) as an emerging drug target","volume":"53","author":"Evans","year":"2010","journal-title":"J. Med. Chem"},{"key":"10.1074\/jbc.RA119.012372_bib4","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1080\/152165401317190770","article-title":"Insights into the function of Hsp70 chaperones","volume":"51","author":"Zylicz","year":"2001","journal-title":"IUBMB Life"},{"key":"10.1074\/jbc.RA119.012372_bib5","doi-asserted-by":"crossref","first-page":"e78443","DOI":"10.1371\/journal.pone.0078443","article-title":"Functional analysis of Hsp70 inhibitors","volume":"8","author":"Schlecht","year":"2013","journal-title":"PLoS ONE"},{"key":"10.1074\/jbc.RA119.012372_bib6","doi-asserted-by":"crossref","first-page":"8471","DOI":"10.1073\/pnas.0903503106","article-title":"Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate","volume":"106","author":"Bertelsen","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.RA119.012372_bib7","doi-asserted-by":"crossref","first-page":"6987","DOI":"10.1073\/pnas.1014448108","article-title":"Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones","volume":"108","author":"Zhuravleva","year":"2011","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.RA119.012372_bib8","doi-asserted-by":"crossref","first-page":"e103518","DOI":"10.1371\/journal.pone.0103518","article-title":"Crystal structure of the stress-inducible human heat shock protein 70 substrate-binding domain in complex with peptide substrate","volume":"9","author":"Zhang","year":"2014","journal-title":"PLoS ONE"},{"key":"10.1074\/jbc.RA119.012372_bib9","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1007\/128_2012_323","article-title":"Allostery in the Hsp70 chaperone proteins","volume":"328","author":"Zuiderweg","year":"2013","journal-title":"Top. Curr. Chem"},{"key":"10.1074\/jbc.RA119.012372_bib10","doi-asserted-by":"crossref","first-page":"38705","DOI":"10.1074\/jbc.M609020200","article-title":"Allosteric regulation of Hsp70 chaperones involves a conserved interdomain linker","volume":"281","author":"Vogel","year":"2006","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA119.012372_bib11","doi-asserted-by":"crossref","first-page":"1296","DOI":"10.1016\/j.cell.2012.11.002","article-title":"An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones","volume":"151","author":"Zhuravleva","year":"2012","journal-title":"Cell"},{"key":"10.1074\/jbc.RA119.012372_bib12","doi-asserted-by":"crossref","first-page":"900","DOI":"10.1038\/nsmb.2583","article-title":"Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP","volume":"20","author":"Qi","year":"2013","journal-title":"Nat. Struct. Mol. Biol"},{"key":"10.1074\/jbc.RA119.012372_bib13","doi-asserted-by":"crossref","first-page":"863","DOI":"10.1016\/j.molcel.2012.09.023","article-title":"Structure and dynamics of the ATP-bound open conformation of Hsp70 chaperones","volume":"48","author":"Kityk","year":"2012","journal-title":"Mol. Cell"},{"key":"10.1074\/jbc.RA119.012372_bib14","doi-asserted-by":"crossref","first-page":"1308","DOI":"10.1016\/j.cell.2012.10.051","article-title":"CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abundance and cell-cycle progression","volume":"151","author":"Truman","year":"2012","journal-title":"Cell"},{"key":"10.1074\/jbc.RA119.012372_bib15","doi-asserted-by":"crossref","first-page":"834","DOI":"10.1126\/science.1175371","article-title":"Lysine acetylation targets protein complexes and co-regulates major cellular functions","volume":"325","author":"Choudhary","year":"2009","journal-title":"Science"},{"key":"10.1074\/jbc.RA119.012372_bib16","doi-asserted-by":"crossref","first-page":"e0128240","DOI":"10.1371\/journal.pone.0128240","article-title":"Biochemical and proteomic analysis of ubiquitination of Hsc70 and Hsp70 by the E3 ligase CHIP","volume":"10","author":"Soss","year":"2015","journal-title":"PLoS ONE"},{"key":"10.1074\/jbc.RA119.012372_bib17","doi-asserted-by":"crossref","first-page":"27752","DOI":"10.1074\/jbc.M113.483248","article-title":"Identification and characterization of a novel human methyltransferase modulating Hsp70 protein function through lysine methylation","volume":"288","author":"Jakobsson","year":"2013","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA119.012372_bib18","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1111\/sji.12078","article-title":"The antioxidative effect of heat-shock protein 70 in dendritic cells","volume":"78","author":"Je","year":"2013","journal-title":"Scand. J. Immunol"},{"key":"10.1074\/jbc.RA119.012372_bib19","doi-asserted-by":"crossref","first-page":"536","DOI":"10.1093\/cvr\/cvp154","article-title":"Shear flow increases S-nitrosylation of proteins in endothelial cells","volume":"83","author":"Huang","year":"2009","journal-title":"Cardiovasc. Res"},{"key":"10.1074\/jbc.RA119.012372_bib20","doi-asserted-by":"crossref","first-page":"3066","DOI":"10.1002\/pmic.200700254","article-title":"Human spermatozoa contain multiple targets for protein S-nitrosylation: an alternative mechanism of the modulation of sperm function by nitric oxide?","volume":"7","author":"Lefi\u00e8vre","year":"2007","journal-title":"Proteomics"},{"key":"10.1074\/jbc.RA119.012372_bib21","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1586\/14789450.1.3.365","article-title":"Redox proteomics: identification and functional role of glutathionylated proteins","volume":"1","author":"Fratelli","year":"2004","journal-title":"Expert Rev. Proteomics"},{"key":"10.1074\/jbc.RA119.012372_bib22","doi-asserted-by":"crossref","first-page":"1085","DOI":"10.1016\/j.exer.2004.02.001","article-title":"Protein S-glutathionylation in retinal pigment epithelium converts heat shock protein 70 to an active chaperone","volume":"78","author":"Hoppe","year":"2004","journal-title":"Exp. Eye Res"},{"key":"10.1074\/jbc.RA119.012372_bib23","doi-asserted-by":"crossref","first-page":"21571","DOI":"10.1074\/jbc.M802331200","article-title":"In vivo targets of S-thiolation in Chlamydomonas reinhardtii","volume":"283","author":"Michelet","year":"2008","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA119.012372_bib24","doi-asserted-by":"crossref","first-page":"591","DOI":"10.1007\/s12192-009-0110-4","article-title":"The ambiguous role of the Na+-H+ exchanger isoform 1 (NHE1) in leptin-induced oxidative stress in human monocytes","volume":"14","author":"Konstantinidis","year":"2009","journal-title":"Cell Stress Chaperones"},{"key":"10.1074\/jbc.RA119.012372_bib25","doi-asserted-by":"crossref","first-page":"10153","DOI":"10.1073\/pnas.1221210110","article-title":"Top-down proteomics reveals a unique protein S-thiolation switch in Salmonella Typhimurium in response to infection-like conditions","volume":"110","author":"Ansong","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.RA119.012372_bib26","doi-asserted-by":"crossref","first-page":"6967","DOI":"10.1074\/jbc.M115.673608","article-title":"Glutathionylation of the bacterial Hsp70 chaperone DnaK provides a link between oxidative stress and the heat shock response","volume":"291","author":"Zhang","year":"2016","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA119.012372_bib27","doi-asserted-by":"crossref","first-page":"7541","DOI":"10.1074\/jbc.M115.694810","article-title":"Formation and reversibility of BiP protein cysteine oxidation facilitate cell survival during and post oxidative stress","volume":"291","author":"Wang","year":"2016","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA119.012372_bib28","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1016\/j.tibs.2013.08.001","article-title":"Hsp70 chaperone dynamics and molecular mechanism","volume":"38","author":"Mayer","year":"2013","journal-title":"Trends Biochem. Sci"},{"key":"10.1074\/jbc.RA119.012372_bib29","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1074\/mcp.O115.056051","article-title":"The expanding landscape of the thiol redox proteome","volume":"15","author":"Yang","year":"2016","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1074\/jbc.RA119.012372_bib30","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1016\/j.tibs.2008.11.002","article-title":"Protein S-glutathionylation: a regulatory device from bacteria to humans","volume":"34","author":"Dalle-Donne","year":"2009","journal-title":"Trends Biochem. Sci"},{"key":"10.1074\/jbc.RA119.012372_bib31","doi-asserted-by":"crossref","first-page":"1555","DOI":"10.1038\/sj.cdd.4401754","article-title":"Disulfide relays and phosphorylative cascades: partners in redox-mediated signaling pathways","volume":"12","author":"Filomeni","year":"2005","journal-title":"Cell Death Differ"},{"key":"10.1074\/jbc.RA119.012372_bib32","doi-asserted-by":"crossref","first-page":"204","DOI":"10.1016\/j.freeradbiomed.2018.03.038","article-title":"An evolving understanding of the S-glutathionylation cycle in pathways of redox regulation","volume":"120","author":"Zhang","year":"2018","journal-title":"Free Radic. Biol. Med"},{"key":"10.1074\/jbc.RA119.012372_bib33","doi-asserted-by":"crossref","first-page":"460","DOI":"10.1016\/j.freeradbiomed.2013.12.004","article-title":"Proteomic identification and quantification of S-glutathionylation in mouse macrophages using resin-assisted enrichment and isobaric labeling","volume":"67","author":"Su","year":"2014","journal-title":"Free Radic. Biol. Med"},{"key":"10.1074\/jbc.RA119.012372_bib34","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1016\/j.ejps.2012.03.010","article-title":"S-Glutathionylation signaling in cell biology: progress and prospects","volume":"46","author":"Pastore","year":"2012","journal-title":"Eur. J. Pharm. Sci"},{"key":"10.1074\/jbc.RA119.012372_bib35","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1089\/ars.2011.4454","article-title":"Posttranslational modification of cysteine in redox signaling and oxidative stress: Focus on S-glutathionylation","volume":"16","author":"Mieyal","year":"2012","journal-title":"Antioxid. Redox Signal"},{"key":"10.1074\/jbc.RA119.012372_bib36","doi-asserted-by":"crossref","first-page":"216","DOI":"10.3389\/fphys.2018.00216","article-title":"Redox aspects of chaperones in cardiac function","volume":"9","author":"Penna","year":"2018","journal-title":"Front. Physiol"},{"key":"10.1074\/jbc.RA119.012372_bib37","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1016\/j.molcel.2004.12.027","article-title":"Severe oxidative stress causes inactivation of DnaK and activation of the redox-regulated chaperone Hsp33","volume":"17","author":"Winter","year":"2005","journal-title":"Mol. Cell"},{"key":"10.1074\/jbc.RA119.012372_bib38","doi-asserted-by":"crossref","first-page":"524","DOI":"10.1021\/acsnano.5b05524","article-title":"Quantitative profiling of protein S-glutathionylation reveals redox-dependent regulation of macrophage function during nanoparticle-induced oxidative stress","volume":"10","author":"Duan","year":"2016","journal-title":"ACS Nano"},{"key":"10.1074\/jbc.RA119.012372_bib39","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1038\/nprot.2013.161","article-title":"Resin-assisted enrichment of thiols as a general strategy for proteomic profiling of cysteine-based reversible modifications","volume":"9","author":"Guo","year":"2014","journal-title":"Nat. Protoc"},{"key":"10.1074\/jbc.RA119.012372_bib40","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1016\/bs.mie.2016.10.006","article-title":"Biotin switch assays for quantitation of reversible cysteine oxidation","volume":"585","author":"Li","year":"2017","journal-title":"Methods Enzymol"},{"key":"10.1074\/jbc.RA119.012372_bib41","doi-asserted-by":"crossref","first-page":"2026","DOI":"10.1021\/acs.jproteome.5b00133","article-title":"Identification of total reversible cysteine oxidation in an atherosclerosis model using a modified biotin switch assay","volume":"14","author":"Li","year":"2015","journal-title":"J. Proteome Res"},{"key":"10.1074\/jbc.RA119.012372_bib42","doi-asserted-by":"crossref","first-page":"9427","DOI":"10.1074\/jbc.274.14.9427","article-title":"Nitric oxide-induced S-glutathionylation and inactivation of glyceraldehyde-3-phosphate dehydrogenase","volume":"274","author":"Mohr","year":"1999","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA119.012372_bib43","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1042\/BJ20100164","article-title":"Role of nitric oxide-mediated glutathionylation in neuronal function: potential regulation of energy utilization","volume":"428","author":"Yap","year":"2010","journal-title":"Biochem. J"},{"key":"10.1074\/jbc.RA119.012372_bib44","doi-asserted-by":"crossref","first-page":"541","DOI":"10.1006\/jmbi.1998.2444","article-title":"NMR structure of Escherichia coli glutaredoxin 3-glutathione mixed disulfide complex: implications for the enzymatic mechanism","volume":"286","author":"Nordstrand","year":"1999","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.RA119.012372_bib45","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/0076-6879(95)51116-4","article-title":"Diamide: an oxidant probe for thiols","volume":"251","author":"Kosower","year":"1995","journal-title":"Methods Enzymol"},{"key":"10.1074\/jbc.RA119.012372_bib46","doi-asserted-by":"crossref","first-page":"9513","DOI":"10.1073\/pnas.88.21.9513","article-title":"DnaK as a thermometer: threonine-199 is site of autophosphorylation and is critical for ATPase activity","volume":"88","author":"McCarty","year":"1991","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.RA119.012372_bib47","doi-asserted-by":"crossref","first-page":"4028","DOI":"10.1021\/bi035924o","article-title":"Protein S-glutathiolation triggered by decomposed S-nitrosoglutathione","volume":"43","author":"Tao","year":"2004","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA119.012372_bib48","doi-asserted-by":"crossref","first-page":"6044","DOI":"10.1074\/jbc.M111.294728","article-title":"The C-terminal helices of heat shock protein 70 are essential for J-domain binding and ATPase activation","volume":"287","author":"Gao","year":"2012","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA119.012372_bib49","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1016\/j.chembiol.2014.11.007","article-title":"The novolactone natural product disrupts the allosteric regulation of Hsp70","volume":"22","author":"Hassan","year":"2015","journal-title":"Chem. Biol"},{"key":"10.1074\/jbc.RA119.012372_bib50","doi-asserted-by":"crossref","first-page":"1387","DOI":"10.1006\/jmbi.1999.2776","article-title":"High-resolution solution structure of the 18 kDa substrate-binding domain of the mammalian chaperone protein Hsc70","volume":"289","author":"Morshauser","year":"1999","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.RA119.012372_bib51","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1016\/j.molcel.2005.09.028","article-title":"Structural basis of interdomain communication in the Hsc70 chaperone","volume":"20","author":"Jiang","year":"2005","journal-title":"Mol. Cell"},{"key":"10.1074\/jbc.RA119.012372_bib52","doi-asserted-by":"crossref","first-page":"7929","DOI":"10.1021\/bi9800855","article-title":"NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: a preview of chaperone-protein interaction","volume":"37","author":"Wang","year":"1998","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA119.012372_bib53","doi-asserted-by":"crossref","first-page":"1153","DOI":"10.1101\/gad.6.7.1153","article-title":"The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression","volume":"6","author":"Abravaya","year":"1992","journal-title":"Genes Dev"},{"key":"10.1074\/jbc.RA119.012372_bib54","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1016\/0022-2836(82)90515-0","article-title":"A simple method for displaying the hydropathic character of a protein","volume":"157","author":"Kyte","year":"1982","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.RA119.012372_bib55","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1007\/978-1-4939-6783-4_9","article-title":"Analysis of cysteine redox post-translational modifications in cell biology and drug pharmacology","volume":"1558","author":"Wani","year":"2017","journal-title":"Methods Mol. Biol"},{"key":"10.1074\/jbc.RA119.012372_bib56","doi-asserted-by":"crossref","first-page":"3290","DOI":"10.1091\/mbc.e12-06-0447","article-title":"The yeast Hsp70 Ssa1 is a sensor for activation of the heat shock response by thiol-reactive compounds","volume":"23","author":"Wang","year":"2012","journal-title":"Mol. Biol. Cell"},{"key":"10.1074\/jbc.RA119.012372_bib57","doi-asserted-by":"crossref","first-page":"1391","DOI":"10.1016\/j.chembiol.2012.07.026","article-title":"Cysteine reactivity distinguishes redox sensing by the heat-inducible and constitutive forms of heat shock protein 70","volume":"19","author":"Miyata","year":"2012","journal-title":"Chem. Biol"},{"key":"10.1074\/jbc.RA119.012372_bib58","doi-asserted-by":"crossref","first-page":"33604","DOI":"10.1074\/jbc.M202890200","article-title":"Differential acquisition of antigenic peptides by Hsp70 and Hsc70 under oxidative conditions","volume":"277","author":"Callahan","year":"2002","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA119.012372_bib59","doi-asserted-by":"crossref","first-page":"e03496","DOI":"10.7554\/eLife.03496","article-title":"Redox signaling via the molecular chaperone BiP protects cells against endoplasmic reticulum-derived oxidative stress","volume":"3","author":"Wang","year":"2014","journal-title":"Elife"},{"key":"10.1074\/jbc.RA119.012372_bib60","doi-asserted-by":"crossref","first-page":"12675","DOI":"10.3390\/ijms140612675","article-title":"Tracking the interplay between bound peptide and the lid domain of DnaK, using molecular dynamics","volume":"14","author":"Azoulay","year":"2013","journal-title":"Int. J. Mol. Sci"},{"key":"10.1074\/jbc.RA119.012372_bib61","doi-asserted-by":"crossref","first-page":"E2865","DOI":"10.1073\/pnas.1506692112","article-title":"Substrate-binding domain conformational dynamics mediate Hsp70 allostery","volume":"112","author":"Zhuravleva","year":"2015","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.RA119.012372_bib62","doi-asserted-by":"crossref","first-page":"16493","DOI":"10.1074\/jbc.M600847200","article-title":"Amide hydrogen exchange reveals conformational changes in hsp70 chaperones important for allosteric regulation","volume":"281","author":"Rist","year":"2006","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA119.012372_bib63","doi-asserted-by":"crossref","first-page":"114","DOI":"10.1016\/j.pharmthera.2014.11.016","article-title":"Glycogen synthase kinase-3 (GSK3): regulation, actions, and diseases","volume":"148","author":"Beurel","year":"2015","journal-title":"Pharmacol. Ther"},{"key":"10.1074\/jbc.RA119.012372_bib64","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1016\/S0003-9861(02)00468-X","article-title":"Identification of S-glutathionylated cellular proteins during oxidative stress and constitutive metabolism by affinity purification and proteomic analysis","volume":"406","author":"Lind","year":"2002","journal-title":"Arch. Biochem. Biophys"},{"key":"10.1074\/jbc.RA119.012372_bib65","doi-asserted-by":"crossref","first-page":"9321","DOI":"10.1007\/s00216-013-7376-1","article-title":"Specific biotinylation and sensitive enrichment of citrullinated peptides","volume":"405","author":"Tutturen","year":"2013","journal-title":"Anal. Bioanal. Chem"},{"key":"10.1074\/jbc.RA119.012372_bib66","doi-asserted-by":"crossref","first-page":"D442","DOI":"10.1093\/nar\/gky1106","article-title":"The PRIDE database and related tools and resources in 2019: improving support for quantification data","volume":"47","author":"Perez-Riverol","year":"2019","journal-title":"Nucleic Acids Res"},{"key":"10.1074\/jbc.RA119.012372_bib67","doi-asserted-by":"crossref","first-page":"6455","DOI":"10.1073\/pnas.82.19.6455","article-title":"Conserved features of eukaryotic hsp70 genes revealed by comparison with the nucleotide sequence of human hsp70","volume":"82","author":"Hunt","year":"1985","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.RA119.012372_bib68","doi-asserted-by":"crossref","first-page":"865","DOI":"10.1016\/S1097-2765(00)80326-3","article-title":"Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast","volume":"5","author":"Mossessova","year":"2000","journal-title":"Mol. Cell"},{"key":"10.1074\/jbc.RA119.012372_bib69","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/0003-2697(79)90792-9","article-title":"Ellman's reagent: 5,5\u2032-dithiobis(2-nitrobenzoic acid)\u2014a reexamination","volume":"94","author":"Riddles","year":"1979","journal-title":"Anal. Biochem"},{"key":"10.1074\/jbc.RA119.012372_bib70","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1007\/BF00197809","article-title":"NMRPipe: a multidimensional spectral processing system based on UNIX pipes","volume":"6","author":"Delaglio","year":"1995","journal-title":"J. Biomol. NMR"},{"key":"10.1074\/jbc.RA119.012372_bib71","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1007\/BF00404272","article-title":"NMR View: A computer program for the visualization and analysis of NMR data","volume":"4","author":"Johnson","year":"1994","journal-title":"J. Biomol. NMR"},{"key":"10.1074\/jbc.RA119.012372_bib72","doi-asserted-by":"crossref","first-page":"933","DOI":"10.1006\/jmbi.1998.1852","article-title":"Recommendations for the presentation of NMR structures of proteins and nucleic acids","volume":"280","author":"Markley","year":"1998","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.RA119.012372_bib73","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1016\/S0022-2836(02)00241-3","article-title":"Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA","volume":"319","author":"Herrmann","year":"2002","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.RA119.012372_bib74","doi-asserted-by":"crossref","first-page":"905","DOI":"10.1107\/S0907444998003254","article-title":"Crystallography & NMR system: A new software suite for macromolecular structure determination","volume":"54","author":"Br\u00fcnger","year":"1998","journal-title":"Acta Crystallogr. D Biol. Crystallogr"},{"key":"10.1074\/jbc.RA119.012372_bib75","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1023\/A:1011227824104","article-title":"SANE (Structure Assisted NOE Evaluation): an automated model-based approach for NOE assignment","volume":"19","author":"Duggan","year":"2001","journal-title":"J. Biomol. NMR"},{"key":"10.1074\/jbc.RA119.012372_bib76","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1007\/BF00175245","article-title":"The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data","volume":"4","author":"Wishart","year":"1994","journal-title":"J. Biomol. NMR"},{"key":"10.1074\/jbc.RA119.012372_bib77","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1007\/s10858-013-9741-y","article-title":"Protein backbone and sidechain torsion angles predicted from NMR chemical shifts using artificial neural networks","volume":"56","author":"Shen","year":"2013","journal-title":"J. Biomol. NMR"},{"key":"10.1074\/jbc.RA119.012372_bib78","doi-asserted-by":"crossref","first-page":"662","DOI":"10.1002\/prot.20408","article-title":"RECOORD: a recalculated coordinate database of 500+ proteins from the PDB using restraints from the BioMagResBank","volume":"59","author":"Nederveen","year":"2005","journal-title":"Proteins"},{"key":"10.1074\/jbc.RA119.012372_bib79","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1007\/BF00228148","article-title":"AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR","volume":"8","author":"Laskowski","year":"1996","journal-title":"J. Biomol. NMR"},{"key":"10.1074\/jbc.RA119.012372_bib80","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/0263-7855(96)00009-4","article-title":"MOLMOL: a program for display and analysis of macromolecular structures","volume":"14","author":"Koradi","year":"1996","journal-title":"J. Mol. Graph"},{"key":"10.1074\/jbc.RA119.012372_bib81","series-title":"The PyMOL Molecular Graphics System","author":"DeLano","year":"2012"},{"key":"10.1074\/jbc.RA119.012372_bib82","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1016\/j.ab.2007.08.020","article-title":"High-throughput screen for small molecules that modulate the ATPase activity of the molecular chaperone DnaK","volume":"372","author":"Chang","year":"2008","journal-title":"Anal. Biochem"},{"key":"10.1074\/jbc.RA119.012372_bib83","doi-asserted-by":"crossref","first-page":"702","DOI":"10.1111\/j.1365-2958.2008.06557.x","article-title":"Alcohol oxidase (AOX1) from Pichia pastoris is a novel inhibitor of prion propagation and a potential ATPase","volume":"71","author":"Zhang","year":"2009","journal-title":"Mol. Microbiol"},{"key":"10.1074\/jbc.RA119.012372_bib84","doi-asserted-by":"crossref","first-page":"90","DOI":"10.2174\/1875397300802010090","article-title":"Development of fluorescence polarization assays for the molecular chaperone Hsp70 family members: Hsp72 and DnaK","volume":"2","author":"Ricci","year":"2008","journal-title":"Curr. Chem. Genomics"},{"key":"10.1074\/jbc.RA119.012372_bib85","doi-asserted-by":"crossref","first-page":"1694","DOI":"10.1128\/JB.01197-13","article-title":"DnaJ-promoted binding of DnaK to multiple sites on \u03c332 in the presence of ATP","volume":"196","author":"Noguchi","year":"2014","journal-title":"J. Bacteriol"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S002192581749418X?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S002192581749418X?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.RA119.012372","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,12,18]],"date-time":"2021-12-18T05:54:20Z","timestamp":1639806860000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S002192581749418X"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,6]]},"references-count":85,"journal-issue":{"issue":"24","published-print":{"date-parts":[[2020,6]]}},"alternative-id":["S002192581749418X"],"URL":"https:\/\/doi.org\/10.1074\/jbc.ra119.012372","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2020,6]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"S-Glutathionylation of human inducible Hsp70 reveals a regulatory mechanism involving the C-terminal \u03b1-helical lid","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1074\/jbc.RA119.012372","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2020 Yang et al.","name":"copyright","label":"Copyright"}]}}