{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,23]],"date-time":"2026-07-23T13:11:17Z","timestamp":1784812277600,"version":"3.55.0"},"reference-count":59,"publisher":"Springer Science and Business Media LLC","issue":"7564","license":[{"start":{"date-parts":[[2015,8,5]],"date-time":"2015-08-05T00:00:00Z","timestamp":1438732800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springer.com\/tdm"},{"start":{"date-parts":[[2015,8,5]],"date-time":"2015-08-05T00:00:00Z","timestamp":1438732800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Nature"],"published-print":{"date-parts":[[2015,8,13]]},"DOI":"10.1038\/nature14884","type":"journal-article","created":{"date-parts":[[2015,8,4]],"date-time":"2015-08-04T15:58:32Z","timestamp":1438703912000},"page":"247-251","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":359,"title":["Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation"],"prefix":"10.1038","volume":"524","author":[{"given":"Nadinath B.","family":"Nillegoda","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Janine","family":"Kirstein","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anna","family":"Szlachcic","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mykhaylo","family":"Berynskyy","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Antonia","family":"Stank","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Florian","family":"Stengel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kristin","family":"Arnsburg","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xuechao","family":"Gao","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Annika","family":"Scior","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ruedi","family":"Aebersold","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"D. Lys","family":"Guilbride","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rebecca C.","family":"Wade","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Richard I.","family":"Morimoto","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Matthias P.","family":"Mayer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bernd","family":"Bukau","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2015,8,5]]},"reference":[{"key":"BFnature14884_CR1","doi-asserted-by":"publisher","first-page":"506","DOI":"10.1016\/j.tcb.2014.05.003","volume":"24","author":"MS Hipp","year":"2014","unstructured":"Hipp, M. S., Park, S. H. & Hartl, F. U. Proteostasis impairment in protein-misfolding and -aggregation diseases. Trends Cell Biol. 24, 506\u2013514 (2014)","journal-title":"Trends Cell Biol."},{"key":"BFnature14884_CR2","doi-asserted-by":"publisher","first-page":"1427","DOI":"10.1101\/gad.1657108","volume":"22","author":"RI Morimoto","year":"2008","unstructured":"Morimoto, R. I. Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging. Genes Dev. 22, 1427\u20131438 (2008)","journal-title":"Genes Dev."},{"key":"BFnature14884_CR3","doi-asserted-by":"publisher","first-page":"1451","DOI":"10.1038\/emboj.2013.87","volume":"32","author":"J Kirstein-Miles","year":"2013","unstructured":"Kirstein-Miles, J., Scior, A., Deuerling, E. & Morimoto, R. I. The nascent polypeptide-associated complex is a key regulator of proteostasis. EMBO J. 32, 1451\u20131468 (2013)","journal-title":"EMBO J."},{"key":"BFnature14884_CR4","doi-asserted-by":"publisher","first-page":"4221","DOI":"10.1038\/emboj.2012.264","volume":"31","author":"H Rampelt","year":"2012","unstructured":"Rampelt, H. et al. Metazoan Hsp70 machines use Hsp110 to power protein disaggregation. EMBO J. 31, 4221\u20134235 (2012)","journal-title":"EMBO J."},{"key":"BFnature14884_CR5","doi-asserted-by":"publisher","first-page":"13732","DOI":"10.1073\/pnas.96.24.13732","volume":"96","author":"P Goloubinoff","year":"1999","unstructured":"Goloubinoff, P., Mogk, A., Zvi, A. P., Tomoyasu, T. & Bukau, B. Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network. Proc. Natl Acad. Sci. USA 96, 13732\u201313737 (1999)","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BFnature14884_CR6","doi-asserted-by":"publisher","first-page":"475","DOI":"10.1038\/372475a0","volume":"372","author":"DA Parsell","year":"1994","unstructured":"Parsell, D. A., Kowal, A. S., Singer, M. A. & Lindquist, S. Protein disaggregation mediated by heat-shock protein HSP104. Nature 372, 475\u2013478 (1994)","journal-title":"Nature"},{"key":"BFnature14884_CR7","doi-asserted-by":"publisher","first-page":"e26319","DOI":"10.1371\/journal.pone.0026319","volume":"6","author":"J Shorter","year":"2011","unstructured":"Shorter, J. The mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free system. PLoS ONE 6, e26319 (2011)","journal-title":"PLoS ONE"},{"key":"BFnature14884_CR8","doi-asserted-by":"publisher","first-page":"670","DOI":"10.1007\/s00018-004-4464-6","volume":"62","author":"MP Mayer","year":"2005","unstructured":"Mayer, M. P. & Bukau, B. Hsp70 chaperones: cellular functions and molecular mechanism. Cell. Mol. Life Sci. 62, 670\u2013684 (2005)","journal-title":"Cell. Mol. Life Sci."},{"key":"BFnature14884_CR9","doi-asserted-by":"publisher","first-page":"579","DOI":"10.1038\/nrm2941","volume":"11","author":"HH Kampinga","year":"2010","unstructured":"Kampinga, H. H. & Craig, E. A. The HSP70 chaperone machinery: J proteins as drivers of functional specificity. Nature Rev. Mol. Cell Biol. 11, 579\u2013592 (2010)","journal-title":"Nature Rev. Mol. Cell Biol."},{"key":"BFnature14884_CR10","doi-asserted-by":"publisher","first-page":"91","DOI":"10.1007\/978-3-319-11731-7_4","volume":"78","author":"DM Cyr","year":"2015","unstructured":"Cyr, D. M. & Ramos, C. H. Specification of Hsp70 function by type I and type II HSP40. Subcell. Biochem. 78, 91\u2013102 (2015)","journal-title":"Subcell. Biochem."},{"key":"BFnature14884_CR11","doi-asserted-by":"publisher","first-page":"7163","DOI":"10.1073\/pnas.0702357104","volume":"104","author":"C Sahi","year":"2007","unstructured":"Sahi, C. & Craig, E. A. Network of general and specialty J protein chaperones of the yeast cytosol. Proc. Natl Acad. Sci. USA 104, 7163\u20137168 (2007)","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BFnature14884_CR12","doi-asserted-by":"publisher","first-page":"27100","DOI":"10.1074\/jbc.M803923200","volume":"283","author":"S Tzankov","year":"2008","unstructured":"Tzankov, S., Wong, M. J., Shi, K., Nassif, C. & Young, J. C. Functional divergence between co-chaperones of Hsc70. J. Biol. Chem. 283, 27100\u201327109 (2008)","journal-title":"J. Biol. Chem."},{"key":"BFnature14884_CR13","doi-asserted-by":"publisher","first-page":"1402","DOI":"10.1074\/jbc.M113.521997","volume":"289","author":"JN Rauch","year":"2014","unstructured":"Rauch, J. N. & Gestwicki, J. E. Binding of human nucleotide exchange factors to heat shock protein 70 (Hsp70) generates functionally distinct complexes in vitro . J. Biol. Chem. 289, 1402\u20131414 (2014)","journal-title":"J. Biol. Chem."},{"key":"BFnature14884_CR14","doi-asserted-by":"publisher","first-page":"27824","DOI":"10.1074\/jbc.273.43.27824","volume":"273","author":"Z Lu","year":"1998","unstructured":"Lu, Z. & Cyr, D. M. Protein folding activity of HSP70 is modified differentially by the Hsp40 co-chaperones Sis1 and Ydj1. J. Biol. Chem. 273, 27824\u201327830 (1998)","journal-title":"J. Biol. Chem."},{"key":"BFnature14884_CR15","doi-asserted-by":"publisher","first-page":"653","DOI":"10.1016\/j.cell.2004.11.027","volume":"119","author":"J Weibezahn","year":"2004","unstructured":"Weibezahn, J. et al. Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB. Cell 119, 653\u2013665 (2004)","journal-title":"Cell"},{"key":"BFnature14884_CR16","doi-asserted-by":"publisher","first-page":"155","DOI":"10.1016\/j.jmb.2008.08.019","volume":"383","author":"CH Ramos","year":"2008","unstructured":"Ramos, C. H., Oliveira, C. L., Fan, C. Y., Torriani, I. L. & Cyr, D. M. Conserved central domains control the quaternary structure of type I and type II HSP40 molecular chaperones. J. Mol. Biol. 383, 155\u2013166 (2008)","journal-title":"J. Mol. Biol."},{"key":"BFnature14884_CR17","doi-asserted-by":"publisher","first-page":"13671","DOI":"10.1074\/jbc.M408349200","volume":"280","author":"JC Borges","year":"2005","unstructured":"Borges, J. C., Fischer, H., Craievich, A. F. & Ramos, C. H. Low resolution structural study of two human HSP40 chaperones in solution. DJA1 from subfamily A and DJB4 from subfamily B have different quaternary structures. J. Biol. Chem. 280, 13671\u201313681 (2005)","journal-title":"J. Biol. Chem."},{"key":"BFnature14884_CR18","doi-asserted-by":"publisher","first-page":"9347","DOI":"10.1074\/jbc.271.16.9347","volume":"271","author":"J Tsai","year":"1996","unstructured":"Tsai, J. & Douglas, M. G. A conserved HPD sequence of the J-domain is necessary for YDJ1 stimulation of Hsp70 ATPase activity at a site distinct from substrate binding. J. Biol. Chem. 271, 9347\u20139354 (1996)","journal-title":"J. Biol. Chem."},{"key":"BFnature14884_CR19","doi-asserted-by":"publisher","first-page":"30534","DOI":"10.1074\/jbc.274.43.30534","volume":"274","author":"WC Suh","year":"1999","unstructured":"Suh, W. C., Lu, C. Z. & Gross, C. A. Structural features required for the interaction of the Hsp70 molecular chaperone DnaK with its cochaperone DnaJ. J. Biol. Chem. 274, 30534\u201330539 (1999)","journal-title":"J. Biol. Chem."},{"key":"BFnature14884_CR20","doi-asserted-by":"publisher","first-page":"1045","DOI":"10.1093\/genetics\/162.3.1045","volume":"162","author":"P Genevaux","year":"2002","unstructured":"Genevaux, P., Schwager, F., Georgopoulos, C. & Kelley, W. L. Scanning mutagenesis identifies amino acid residues essential for the in vivo activity of the Escherichia coli DnaJ (Hsp40) J-domain. Genetics 162, 1045\u20131053 (2002)","journal-title":"Genetics"},{"key":"BFnature14884_CR21","doi-asserted-by":"publisher","first-page":"6166","DOI":"10.1073\/pnas.0510496103","volume":"103","author":"P De Los Rios","year":"2006","unstructured":"De Los Rios, P., Ben-Zvi, A., Slutsky, O., Azem, A. & Goloubinoff, P. Hsp70 chaperones accelerate protein translocation and the unfolding of stable protein aggregates by entropic pulling. Proc. Natl Acad. Sci. USA 103, 6166\u20136171 (2006)","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BFnature14884_CR22","doi-asserted-by":"publisher","first-page":"267","DOI":"10.1146\/annurev.neuro.26.010302.081142","volume":"26","author":"B Caughey","year":"2003","unstructured":"Caughey, B. & Lansbury, P. T. Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu. Rev. Neurosci. 26, 267\u2013298 (2003)","journal-title":"Annu. Rev. Neurosci."},{"key":"BFnature14884_CR23","doi-asserted-by":"publisher","first-page":"28","DOI":"10.1379\/1466-1268(1998)003<0028:SFAEOD>2.3.CO;2","volume":"3","author":"ME Cheetham","year":"1998","unstructured":"Cheetham, M. E. & Caplan, A. J. Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function. Cell Stress Chaperones 3, 28\u201336 (1998)","journal-title":"Cell Stress Chaperones"},{"key":"BFnature14884_CR24","doi-asserted-by":"publisher","first-page":"1475","DOI":"10.1016\/j.str.2003.10.012","volume":"11","author":"J Li","year":"2003","unstructured":"Li, J., Qian, X. & Sha, B. The crystal structure of the yeast Hsp40 Ydj1 complexed with its peptide substrate. Structure 11, 1475\u20131483 (2003)","journal-title":"Structure"},{"key":"BFnature14884_CR25","doi-asserted-by":"publisher","first-page":"5970","DOI":"10.1074\/jbc.273.10.5970","volume":"273","author":"Z Lu","year":"1998","unstructured":"Lu, Z. & Cyr, D. M. The conserved carboxyl terminus and zinc finger-like domain of the co-chaperone Ydj1 assist Hsp70 in protein folding. J. Biol. Chem. 273, 5970\u20135978 (1998)","journal-title":"J. Biol. Chem."},{"key":"BFnature14884_CR26","doi-asserted-by":"publisher","first-page":"8877","DOI":"10.1074\/jbc.M710063200","volume":"283","author":"C Andr\u00e9asson","year":"2008","unstructured":"Andr\u00e9asson, C., Fiaux, J., Rampelt, H., Mayer, M. P. & Bukau, B. Hsp110 is a nucleotide-activated exchange factor for Hsp70. J. Biol. Chem. 283, 8877\u20138884 (2008)","journal-title":"J. Biol. Chem."},{"key":"BFnature14884_CR27","doi-asserted-by":"publisher","first-page":"23869","DOI":"10.1074\/jbc.M502854200","volume":"280","author":"AG Cashikar","year":"2005","unstructured":"Cashikar, A. G., Duennwald, M. & Lindquist, S. L. A chaperone pathway in protein disaggregation. Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104. J. Biol. Chem. 280, 23869\u201323875 (2005)","journal-title":"J. Biol. Chem."},{"key":"BFnature14884_CR28","doi-asserted-by":"publisher","first-page":"23861","DOI":"10.1074\/jbc.M502697200","volume":"280","author":"M Haslbeck","year":"2005","unstructured":"Haslbeck, M., Miess, A., Stromer, T., Walter, S. & Buchner, J. Disassembling protein aggregates in the yeast cytosol. The cooperation of Hsp26 with Ssa1 and Hsp104. J. Biol. Chem. 280, 23861\u201323868 (2005)","journal-title":"J. Biol. Chem."},{"key":"BFnature14884_CR29","doi-asserted-by":"publisher","first-page":"20110409","DOI":"10.1098\/rstb.2011.0409","volume":"368","author":"S Carra","year":"2013","unstructured":"Carra, S. et al. Different anti-aggregation and pro-degradative functions of the members of the mammalian sHSP family in neurological disorders. Phil. Trans. R. Soc. Lond. B 368, 20110409 (2013)","journal-title":"Phil. Trans. R. Soc. Lond. B"},{"key":"BFnature14884_CR30","doi-asserted-by":"publisher","first-page":"4677","DOI":"10.1093\/hmg\/ddq398","volume":"19","author":"MJ Vos","year":"2010","unstructured":"Vos, M. J. et al. HSPB7 is the most potent polyQ aggregation suppressor within the HSPB family of molecular chaperones. Hum. Mol. Genet. 19, 4677\u20134693 (2010)","journal-title":"Hum. Mol. Genet."},{"key":"BFnature14884_CR31","doi-asserted-by":"publisher","first-page":"975","DOI":"10.1016\/j.biochi.2011.12.018","volume":"94","author":"F Skouri-Panet","year":"2012","unstructured":"Skouri-Panet, F., Michiel, M., Ferard, C., Duprat, E. & Finet, S. Structural and functional specificity of small heat shock protein HspB1 and HspB4, two cellular partners of HspB5: role of the in vitro hetero-complex formation in chaperone activity. Biochimie 94, 975\u2013984 (2012)","journal-title":"Biochimie"},{"key":"BFnature14884_CR32","doi-asserted-by":"publisher","first-page":"E3780","DOI":"10.1073\/pnas.1308898110","volume":"110","author":"J Peschek","year":"2013","unstructured":"Peschek, J. et al. Regulated structural transitions unleash the chaperone activity of \u03b1B-crystallin. Proc. Natl Acad. Sci. USA 110, E3780\u2013E3789 (2013)","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BFnature14884_CR33","doi-asserted-by":"publisher","first-page":"M111.014126","DOI":"10.1074\/mcp.M111.014126","volume":"11","author":"A Leitner","year":"2012","unstructured":"Leitner, A. et al. Expanding the chemical cross-linking toolbox by the use of multiple proteases and enrichment by size exclusion chromatography. Mol. Cell. Proteomics 11, M111.014126 (2012)","journal-title":"Mol. Cell. Proteomics"},{"key":"BFnature14884_CR34","doi-asserted-by":"publisher","first-page":"315","DOI":"10.1038\/nmeth.1192","volume":"5","author":"O Rinner","year":"2008","unstructured":"Rinner, O. et al. Identification of cross-linked peptides from large sequence databases. Nature Methods 5, 315\u2013318 (2008)","journal-title":"Nature Methods"},{"key":"BFnature14884_CR35","doi-asserted-by":"publisher","first-page":"901","DOI":"10.1038\/nmeth.2103","volume":"9","author":"T Walzthoeni","year":"2012","unstructured":"Walzthoeni, T. et al. False discovery rate estimation for cross-linked peptides identified by mass spectrometry. Nature Methods 9, 901\u2013903 (2012)","journal-title":"Nature Methods"},{"key":"BFnature14884_CR36","doi-asserted-by":"publisher","first-page":"6063","DOI":"10.1021\/ja017687n","volume":"124","author":"SR Adams","year":"2002","unstructured":"Adams, S. R. et al. New biarsenical ligands and tetracysteine motifs for protein labeling in vitro and in vivo: synthesis and biological applications. J. Am. Chem. Soc. 124, 6063\u20136076 (2002)","journal-title":"J. Am. Chem. Soc."},{"key":"BFnature14884_CR37","doi-asserted-by":"publisher","first-page":"12040","DOI":"10.1021\/ja063212q","volume":"128","author":"CC Spagnuolo","year":"2006","unstructured":"Spagnuolo, C. C., Vermeij, R. J. & Jares-Erijman, E. A. Improved photostable FRET-competent biarsenical-tetracysteine probes based on fluorinated fluoresceins. J. Am. Chem. Soc. 128, 12040\u201312041 (2006)","journal-title":"J. Am. Chem. Soc."},{"key":"BFnature14884_CR38","doi-asserted-by":"publisher","first-page":"18878","DOI":"10.1074\/jbc.M111.222828","volume":"286","author":"A Dixit","year":"2011","unstructured":"Dixit, A., Ray, K., Lakowicz, J. R. & Black, L. W. Dynamics of the T4 bacteriophage DNA packasome motor: endonuclease VII resolvase release of arrested Y-DNA substrates. J. Biol. Chem. 286, 18878\u201318889 (2011)","journal-title":"J. Biol. Chem."},{"issue":"suppl. 1","key":"BFnature14884_CR39","doi-asserted-by":"publisher","first-page":"S162","DOI":"10.1002\/elps.200900140","volume":"30","author":"N Guex","year":"2009","unstructured":"Guex, N., Peitsch, M. C. & Schwede, T. Automated comparative protein structure modeling with SWISS-MODEL and Swiss-PdbViewer: a historical perspective. Electrophoresis 30 (suppl. 1). S162\u2013S173 (2009)","journal-title":"Electrophoresis"},{"key":"BFnature14884_CR40","doi-asserted-by":"publisher","first-page":"D230","DOI":"10.1093\/nar\/gkh008","volume":"32","author":"J Kopp","year":"2004","unstructured":"Kopp, J. & Schwede, T. The SWISS-MODEL Repository of annotated three-dimensional protein structure homology models. Nucleic Acids Res. 32, D230\u2013D234 (2004)","journal-title":"Nucleic Acids Res."},{"key":"BFnature14884_CR41","doi-asserted-by":"publisher","first-page":"D387","DOI":"10.1093\/nar\/gkn750","volume":"37","author":"F Kiefer","year":"2009","unstructured":"Kiefer, F., Arnold, K., Kunzli, M., Bordoli, L. & Schwede, T. The SWISS-MODEL Repository and associated resources. Nucleic Acids Res. 37, D387\u2013D392 (2009)","journal-title":"Nucleic Acids Res."},{"key":"BFnature14884_CR42","doi-asserted-by":"publisher","first-page":"195","DOI":"10.1093\/bioinformatics\/bti770","volume":"22","author":"K Arnold","year":"2006","unstructured":"Arnold, K., Bordoli, L., Kopp, J. & Schwede, T. The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 22, 195\u2013201 (2006)","journal-title":"Bioinformatics"},{"key":"BFnature14884_CR43","doi-asserted-by":"publisher","first-page":"8577","DOI":"10.1021\/bi100876n","volume":"49","author":"H Suzuki","year":"2010","unstructured":"Suzuki, H. et al. Peptide-binding sites as revealed by the crystal structures of the human Hsp40 Hdj1 C-terminal domain in complex with the octapeptide from human Hsp70. Biochemistry 49, 8577\u20138584 (2010)","journal-title":"Biochemistry"},{"key":"BFnature14884_CR44","doi-asserted-by":"publisher","first-page":"224","DOI":"10.1006\/jmbi.1996.0394","volume":"260","author":"YQ Qian","year":"1996","unstructured":"Qian, Y. Q., Patel, D., Hartl, F. U. & McColl, D. J. Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain. J. Mol. Biol. 260, 224\u2013235 (1996)","journal-title":"J. Mol. Biol."},{"key":"BFnature14884_CR45","doi-asserted-by":"publisher","first-page":"1631","DOI":"10.1002\/jcc.23971","volume":"36","author":"M Martinez","year":"2015","unstructured":"Martinez, M. et al. SDA7: a modular and parallel implementation of the simulation of diffusional association software. J. Comput. Chem. 36, 1631\u20131645 (2015)","journal-title":"J. Comput. Chem."},{"key":"BFnature14884_CR46","doi-asserted-by":"publisher","first-page":"1917","DOI":"10.1016\/S0006-3495(97)78838-6","volume":"72","author":"RR Gabdoulline","year":"1997","unstructured":"Gabdoulline, R. R. & Wade, R. C. Simulation of the diffusional association of barnase and barstar. Biophys. J. 72, 1917\u20131929 (1997)","journal-title":"Biophys. J."},{"key":"BFnature14884_CR47","doi-asserted-by":"publisher","first-page":"52","DOI":"10.1016\/0263-7855(90)80070-V","volume":"8","author":"G Vriend","year":"1990","unstructured":"Vriend, G. WHAT IF: a molecular modeling and drug design program. J. Mol. Graph. 8, 52\u201356 (1990)","journal-title":"J. Mol. Graph."},{"key":"BFnature14884_CR48","doi-asserted-by":"publisher","first-page":"57","DOI":"10.1016\/0010-4655(95)00043-F","volume":"91","author":"JD Madura","year":"1995","unstructured":"Madura, J. D. et al. Electrostatics and diffusion of molecules in solution: simulations with the University of Houston Brownian Dynamics Program. Comp. Phys. Comm. 91, 57\u201395 (1995)","journal-title":"Comp. Phys. Comm."},{"key":"BFnature14884_CR49","doi-asserted-by":"publisher","first-page":"11225","DOI":"10.1021\/ja9621760","volume":"118","author":"WL Jorgensen","year":"1996","unstructured":"Jorgensen, W. L., Maxwell, D. S. & Tirado-Rives, J. Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids. J. Am. Chem. Soc. 118, 11225\u201311236 (1996)","journal-title":"J. Am. Chem. Soc."},{"key":"BFnature14884_CR50","doi-asserted-by":"publisher","first-page":"3868","DOI":"10.1021\/jp953109f","volume":"100","author":"RR Gabdoulline","year":"1996","unstructured":"Gabdoulline, R. R. & Wade, R. C. Effective charges for macromolecules in solvent. J. Phys. Chem. 100, 3868\u20133878 (1996)","journal-title":"J. Phys. Chem."},{"key":"BFnature14884_CR51","doi-asserted-by":"publisher","first-page":"149","DOI":"10.1006\/jmbi.1999.2919","volume":"291","author":"AH Elcock","year":"1999","unstructured":"Elcock, A. H., Gabdoulline, R. R., Wade, R. C. & McCammon, J. A. Computer simulation of protein-protein association kinetics: acetylcholinesterase-fasciculin. J. Mol. Biol. 291, 149\u2013162 (1999)","journal-title":"J. Mol. Biol."},{"key":"BFnature14884_CR52","doi-asserted-by":"publisher","first-page":"9230","DOI":"10.1021\/ja809567k","volume":"131","author":"RR Gabdoulline","year":"2009","unstructured":"Gabdoulline, R. R. & Wade, R. C. On the contributions of diffusion and thermal activation to electron transfer between Phormidium laminosum plastocyanin and cytochrome f: Brownian dynamics simulations with explicit modeling of nonpolar desolvation interactions and electron transfer events. J. Am. Chem. Soc. 131, 9230\u20139238 (2009)","journal-title":"J. Am. Chem. Soc."},{"key":"BFnature14884_CR53","doi-asserted-by":"publisher","first-page":"1540","DOI":"10.1107\/S0907444913010640","volume":"69","author":"TR Barends","year":"2013","unstructured":"Barends, T. R. et al. Combining crystallography and EPR: crystal and solution structures of the multidomain cochaperone DnaJ. Acta Crystallogr. D 69, 1540\u20131552 (2013)","journal-title":"Acta Crystallogr. D"},{"key":"BFnature14884_CR54","doi-asserted-by":"publisher","first-page":"2519","DOI":"10.1038\/sj.emboj.7601138","volume":"25","author":"Z Dragovic","year":"2006","unstructured":"Dragovic, Z., Broadley, S. A., Shomura, Y., Bracher, A. & Hartl, F. U. Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s. EMBO J. 25, 2519\u20132528 (2006)","journal-title":"EMBO J."},{"key":"BFnature14884_CR55","doi-asserted-by":"publisher","first-page":"2510","DOI":"10.1038\/sj.emboj.7601139","volume":"25","author":"H Raviol","year":"2006","unstructured":"Raviol, H., Sadlish, H., Rodriguez, F., Mayer, M. P. & Bukau, B. Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor. EMBO J. 25, 2510\u20132518 (2006)","journal-title":"EMBO J."},{"key":"BFnature14884_CR56","doi-asserted-by":"publisher","first-page":"721","DOI":"10.1038\/90443","volume":"8","author":"J Chen","year":"2001","unstructured":"Chen, J., Walter, S., Horwich, A. L. & Smith, D. L. Folding of malate dehydrogenase inside the GroEL-GroES cavity. Nature Struct. Biol. 8, 721\u2013728 (2001)","journal-title":"Nature Struct. Biol."},{"key":"BFnature14884_CR57","doi-asserted-by":"publisher","first-page":"44457","DOI":"10.1074\/jbc.M307491200","volume":"278","author":"K Linke","year":"2003","unstructured":"Linke, K., Wolfram, T., Bussemer, J. & Jakob, U. The roles of the two zinc binding sites in DnaJ. J. Biol. Chem. 278, 44457\u201344466 (2003)","journal-title":"J. Biol. Chem."},{"key":"BFnature14884_CR58","doi-asserted-by":"publisher","first-page":"6917","DOI":"10.1021\/bi060411d","volume":"45","author":"R Garimella","year":"2006","unstructured":"Garimella, R. et al. Hsc70 contacts helix III of the J domain from polyomavirus T antigens: addressing a dilemma in the chaperone hypothesis of how they release E2F from pRb. Biochemistry 45, 6917\u20136929 (2006)","journal-title":"Biochemistry"},{"key":"BFnature14884_CR59","doi-asserted-by":"publisher","first-page":"6108","DOI":"10.1073\/pnas.95.11.6108","volume":"95","author":"MK Greene","year":"1998","unstructured":"Greene, M. K. et al. Role of the J-domain in the cooperation of Hsp40 with Hsp70. Proc. Natl Acad. Sci. USA 95, 6108\u20136113 (1998)","journal-title":"Proc. Natl Acad. Sci. USA"}],"container-title":["Nature"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.nature.com\/articles\/nature14884.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/nature14884","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/nature14884.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,4,15]],"date-time":"2022-04-15T14:11:02Z","timestamp":1650031862000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/nature14884"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2015,8,5]]},"references-count":59,"journal-issue":{"issue":"7564","published-print":{"date-parts":[[2015,8,13]]}},"alternative-id":["BFnature14884"],"URL":"https:\/\/doi.org\/10.1038\/nature14884","relation":{},"ISSN":["0028-0836","1476-4687"],"issn-type":[{"value":"0028-0836","type":"print"},{"value":"1476-4687","type":"electronic"}],"subject":[],"published":{"date-parts":[[2015,8,5]]},"assertion":[{"value":"25 October 2014","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"8 July 2015","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"5 August 2015","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"The authors declare no competing financial interests.","order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}]}}