{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,6]],"date-time":"2026-07-06T23:26:33Z","timestamp":1783380393544,"version":"3.54.6"},"reference-count":84,"publisher":"Public Library of Science (PLoS)","issue":"10","license":[{"start":{"date-parts":[[2014,10,9]],"date-time":"2014-10-09T00:00:00Z","timestamp":1412812800000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["www.plosone.org"],"crossmark-restriction":false},"short-container-title":["PLoS ONE"],"DOI":"10.1371\/journal.pone.0110115","type":"journal-article","created":{"date-parts":[[2014,10,9]],"date-time":"2014-10-09T18:21:31Z","timestamp":1412878891000},"page":"e110115","update-policy":"https:\/\/doi.org\/10.1371\/journal.pone.corrections_policy","source":"Crossref","is-referenced-by-count":19,"title":["Suramin Inhibits Hsp104 ATPase and Disaggregase Activity"],"prefix":"10.1371","volume":"9","author":[{"given":"Mariana P.","family":"Torrente","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Laura M.","family":"Castellano","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"James","family":"Shorter","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2014,10,9]]},"reference":[{"key":"ref1","doi-asserted-by":"crossref","first-page":"884","DOI":"10.1038\/nature02261","article-title":"Protein folding and misfolding","volume":"426","author":"CM Dobson","year":"2003","journal-title":"Nature"},{"key":"ref2","first-page":"1","article-title":"Applying Hsp104 to protein-misfolding disorders","volume":"88","author":"S Vashist","year":"2010","journal-title":"Biochem Cell Biol"},{"key":"ref3","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1159\/000109760","article-title":"Hsp104: a weapon to combat diverse neurodegenerative disorders","volume":"16","author":"J Shorter","year":"2008","journal-title":"Neurosignals"},{"key":"ref4","doi-asserted-by":"crossref","first-page":"1533","DOI":"10.1101\/gad.241125.114","article-title":"Organismal proteostasis: role of cell-nonautonomous regulation and transcellular chaperone signaling","volume":"28","author":"P van Oosten-Hawle","year":"2014","journal-title":"Genes Dev"},{"key":"ref5","doi-asserted-by":"crossref","first-page":"324","DOI":"10.1038\/nature10317","article-title":"Molecular chaperones in protein folding and proteostasis","volume":"475","author":"FU Hartl","year":"2011","journal-title":"Nature"},{"key":"ref6","doi-asserted-by":"crossref","first-page":"1793","DOI":"10.1126\/science.1098007","article-title":"Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers","volume":"304","author":"J Shorter","year":"2004","journal-title":"Science"},{"key":"ref7","doi-asserted-by":"crossref","first-page":"475","DOI":"10.1038\/372475a0","article-title":"Protein disaggregation mediated by heat-shock protein Hsp104","volume":"372","author":"DA Parsell","year":"1994","journal-title":"Nature"},{"key":"ref8","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1016\/S0092-8674(00)81223-4","article-title":"Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins","volume":"94","author":"JR Glover","year":"1998","journal-title":"Cell"},{"key":"ref9","doi-asserted-by":"crossref","first-page":"778","DOI":"10.1016\/j.cell.2012.09.038","article-title":"Operational plasticity enables Hsp104 to disaggregate diverse amyloid and nonamyloid clients","volume":"151","author":"ME DeSantis","year":"2012","journal-title":"Cell"},{"key":"ref10","doi-asserted-by":"crossref","first-page":"4","DOI":"10.1038\/nsmb0105-4","article-title":"Navigating the ClpB channel to solution","volume":"12","author":"J Shorter","year":"2005","journal-title":"Nat Struct Mol Biol"},{"key":"ref11","doi-asserted-by":"crossref","first-page":"1366","DOI":"10.1016\/j.cell.2007.10.047","article-title":"Atypical AAA+ subunit packing creates an expanded cavity for disaggregation by the protein-remodeling factor Hsp104","volume":"131","author":"P Wendler","year":"2007","journal-title":"Cell"},{"key":"ref12","doi-asserted-by":"crossref","first-page":"653","DOI":"10.1016\/j.cell.2004.11.027","article-title":"Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB","volume":"119","author":"J Weibezahn","year":"2004","journal-title":"Cell"},{"key":"ref13","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1111\/j.1365-2958.2008.06135.x","article-title":"Substrate threading through the central pore of the Hsp104 chaperone as a common mechanism for protein disaggregation and prion propagation","volume":"68","author":"P Tessarz","year":"2008","journal-title":"Mol Microbiol"},{"key":"ref14","doi-asserted-by":"crossref","first-page":"30139","DOI":"10.1074\/jbc.M804849200","article-title":"Peptide and protein binding in the axial channel of Hsp104. Insights into the mechanism of protein unfolding","volume":"283","author":"R Lum","year":"2008","journal-title":"J Biol Chem"},{"key":"ref15","doi-asserted-by":"crossref","first-page":"29139","DOI":"10.1074\/jbc.M403777200","article-title":"Evidence for an unfolding\/threading mechanism for protein disaggregation by Saccharomyces cerevisiae Hsp104","volume":"279","author":"R Lum","year":"2004","journal-title":"J Biol Chem"},{"key":"ref16","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/j.bbamcr.2011.07.014","article-title":"The elusive middle domain of Hsp104 and ClpB: location and function","volume":"1823","author":"ME DeSantis","year":"2012","journal-title":"Biochim Biophys Acta"},{"key":"ref17","doi-asserted-by":"crossref","first-page":"17992","DOI":"10.1074\/jbc.M110.216176","article-title":"Regulatory circuits of the AAA+ disaggregase Hsp104","volume":"286","author":"TM Franzmann","year":"2011","journal-title":"J Biol Chem"},{"key":"ref18","doi-asserted-by":"crossref","first-page":"15546","DOI":"10.1074\/jbc.273.25.15546","article-title":"The ATPase activity of Hsp104, effects of environmental conditions and mutations","volume":"273","author":"EC Schirmer","year":"1998","journal-title":"J Biol Chem"},{"key":"ref19","doi-asserted-by":"crossref","first-page":"252","DOI":"10.1002\/bip.21301","article-title":"Structure and function of the molecular chaperone Hsp104 from yeast","volume":"93","author":"V Grimminger-Marquardt","year":"2010","journal-title":"Biopolymers"},{"key":"ref20","doi-asserted-by":"crossref","first-page":"e1001346","DOI":"10.1371\/journal.pbio.1001346","article-title":"Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humans","volume":"10","author":"ML Duennwald","year":"2012","journal-title":"PLoS Biol"},{"key":"ref21","doi-asserted-by":"crossref","first-page":"23869","DOI":"10.1074\/jbc.M502854200","article-title":"A chaperone pathway in protein disaggregation. Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104","volume":"280","author":"AG Cashikar","year":"2005","journal-title":"J Biol Chem"},{"key":"ref22","doi-asserted-by":"crossref","first-page":"23861","DOI":"10.1074\/jbc.M502697200","article-title":"Disassembling protein aggregates in the yeast cytosol. The cooperation of Hsp26 with Ssa1 and Hsp104","volume":"280","author":"M Haslbeck","year":"2005","journal-title":"J Biol Chem"},{"key":"ref23","doi-asserted-by":"crossref","first-page":"e26319","DOI":"10.1371\/journal.pone.0026319","article-title":"The mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free system","volume":"6","author":"J Shorter","year":"2011","journal-title":"PLoS One"},{"key":"ref24","doi-asserted-by":"crossref","first-page":"457","DOI":"10.4161\/pri.27531","article-title":"The metazoan protein disaggregase and amyloid depolymerase system: Hsp110, Hsp70, Hsp40, and small heat shock proteins","volume":"7","author":"MP Torrente","year":"2013","journal-title":"Prion"},{"key":"ref25","doi-asserted-by":"crossref","first-page":"114","DOI":"10.1038\/nsmb1198","article-title":"Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling activity","volume":"14","author":"SM Doyle","year":"2007","journal-title":"Nat Struct Mol Biol"},{"key":"ref26","doi-asserted-by":"crossref","first-page":"1112","DOI":"10.1126\/science.2188365","article-title":"HSP104 required for induced thermotolerance","volume":"248","author":"Y Sanchez","year":"1990","journal-title":"Science"},{"key":"ref27","doi-asserted-by":"crossref","first-page":"2357","DOI":"10.1002\/j.1460-2075.1992.tb05295.x","article-title":"Hsp104 is required for tolerance to many forms of stress","volume":"11","author":"Y Sanchez","year":"1992","journal-title":"EMBO J"},{"key":"ref28","doi-asserted-by":"crossref","first-page":"587","DOI":"10.1038\/nature13555","article-title":"PTEX is an essential nexus for protein export in malaria parasites","volume":"511","author":"B Elsworth","year":"2014","journal-title":"Nature"},{"key":"ref29","doi-asserted-by":"crossref","first-page":"592","DOI":"10.1038\/nature13574","article-title":"PTEX component HSP101 mediates export of diverse malaria effectors into host erythrocytes","volume":"511","author":"JR Beck","year":"2014","journal-title":"Nature"},{"key":"ref30","doi-asserted-by":"crossref","first-page":"7378","DOI":"10.1074\/jbc.M312403200","article-title":"The prion curing agent guanidinium chloride specifically inhibits ATP hydrolysis by Hsp104","volume":"279","author":"V Grimminger","year":"2004","journal-title":"J Biol Chem"},{"key":"ref31","doi-asserted-by":"crossref","first-page":"7065","DOI":"10.1074\/jbc.M112.432583","article-title":"The molecular mechanism of Hsp100 chaperone inhibition by the prion curing agent guanidinium chloride","volume":"288","author":"C Zeymer","year":"2013","journal-title":"J Biol Chem"},{"key":"ref32","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":"L Chang","year":"2008","journal-title":"Anal Biochem"},{"key":"ref33","doi-asserted-by":"crossref","first-page":"1939","DOI":"10.1016\/j.bmc.2007.01.004","article-title":"High-throughput assay for the identification of Hsp90 inhibitors based on Hsp90-dependent refolding of firefly luciferase","volume":"15","author":"L Galam","year":"2007","journal-title":"Bioorg Med Chem"},{"key":"ref34","doi-asserted-by":"crossref","first-page":"4834","DOI":"10.1073\/pnas.1015312108","article-title":"Reversible inhibitor of p97, DBeQ, impairs both ubiquitin-dependent and autophagic protein clearance pathways","volume":"108","author":"TF Chou","year":"2011","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref35","doi-asserted-by":"crossref","first-page":"7177","DOI":"10.1021\/jm400499k","article-title":"Screening and evaluation of small organic molecules as ClpB inhibitors and potential antimicrobials","volume":"56","author":"I Martin","year":"2013","journal-title":"J Med Chem"},{"key":"ref36","doi-asserted-by":"crossref","first-page":"548","DOI":"10.1038\/nchembio.1313","article-title":"Covalent and allosteric inhibitors of the ATPase VCP\/p97 induce cancer cell death","volume":"9","author":"P Magnaghi","year":"2013","journal-title":"Nat Chem Biol"},{"key":"ref37","doi-asserted-by":"crossref","first-page":"848","DOI":"10.1074\/jbc.M113.520759","article-title":"Conserved distal loop residues in the Hsp104 and ClpB middle domain contact nucleotide-binding domain 2 and enable Hsp70-dependent protein disaggregation","volume":"289","author":"ME DeSantis","year":"2014","journal-title":"J Biol Chem"},{"key":"ref38","first-page":"e3190","article-title":"Purification of hsp104, a protein disaggregase","volume":"55","author":"EA Sweeny","year":"2011","journal-title":"J Vis Exp"},{"key":"ref39","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1093\/emboj\/21.1.12","article-title":"Cooperative kinetics of both Hsp104 ATPase domains and interdomain communication revealed by AAA sensor-1 mutants","volume":"21","author":"DA Hattendorf","year":"2002","journal-title":"EMBO J"},{"key":"ref40","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1016\/j.cell.2013.11.047","article-title":"Potentiated Hsp104 variants antagonize diverse proteotoxic misfolding events","volume":"156","author":"ME Jackrel","year":"2014","journal-title":"Cell"},{"key":"ref41","doi-asserted-by":"crossref","first-page":"1899","DOI":"10.1110\/ps.8.9.1899","article-title":"Nucleotide-dependent oligomerization of ClpB from Escherichia coli","volume":"8","author":"M Zolkiewski","year":"1999","journal-title":"Protein Sci"},{"key":"ref42","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1177\/108705719900400206","article-title":"A Simple Statistical Parameter for Use in Evaluation and Validation of High Throughput Screening Assays","volume":"4","author":"JH Zhang","year":"1999","journal-title":"J Biomol Screen"},{"key":"ref43","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1016\/j.devcel.2008.08.005","article-title":"An Afg2\/Spaf-related Cdc48-like AAA ATPase regulates the stability and activity of the C. elegans Aurora B kinase AIR-2","volume":"15","author":"TR Heallen","year":"2008","journal-title":"Dev Cell"},{"key":"ref44","doi-asserted-by":"crossref","first-page":"e1000105","DOI":"10.1371\/journal.pbio.1000105","article-title":"Stress-dependent coordination of transcriptome and translatome in yeast","volume":"7","author":"RE Halbeisen","year":"2009","journal-title":"PLoS Biol"},{"key":"ref45","doi-asserted-by":"crossref","first-page":"674","DOI":"10.1016\/j.jmb.2007.04.070","article-title":"Processing of proteins by the molecular chaperone Hsp104","volume":"370","author":"A Schaupp","year":"2007","journal-title":"J Mol Biol"},{"key":"ref46","doi-asserted-by":"crossref","first-page":"2719","DOI":"10.1021\/jm901137j","article-title":"New substructure filters for removal of pan assay interference compounds (PAINS) from screening libraries and for their exclusion in bioassays","volume":"53","author":"JB Baell","year":"2010","journal-title":"J Med Chem"},{"key":"ref47","doi-asserted-by":"crossref","first-page":"1712","DOI":"10.1021\/jm010533y","article-title":"A common mechanism underlying promiscuous inhibitors from virtual and high-throughput screening","volume":"45","author":"SL McGovern","year":"2002","journal-title":"J Med Chem"},{"key":"ref48","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1038\/nchembio718","article-title":"High-throughput assays for promiscuous inhibitors","volume":"1","author":"BY Feng","year":"2005","journal-title":"Nat Chem Biol"},{"key":"ref49","doi-asserted-by":"crossref","first-page":"550","DOI":"10.1038\/nprot.2006.77","article-title":"A detergent-based assay for the detection of promiscuous inhibitors","volume":"1","author":"BY Feng","year":"2006","journal-title":"Nat Protoc"},{"key":"ref50","doi-asserted-by":"crossref","first-page":"e77073","DOI":"10.1371\/journal.pone.0077073","article-title":"The beneficial effect of suramin on monocrotaline-induced pulmonary hypertension in rats","volume":"8","author":"M Izikki","year":"2013","journal-title":"PLoS One"},{"key":"ref51","doi-asserted-by":"crossref","first-page":"242","DOI":"10.1179\/2047773213Y.0000000105","article-title":"A current analysis of chemotherapy strategies for the treatment of human African trypanosomiasis","volume":"107","author":"P Babokhov","year":"2013","journal-title":"Pathog Glob Health"},{"key":"ref52","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1007\/s10549-014-2857-2","article-title":"A combination treatment with DNA methyltransferase inhibitors and suramin decreases invasiveness of breast cancer cells","volume":"144","author":"S Borges","year":"2014","journal-title":"Breast Cancer Res Treat"},{"key":"ref53","doi-asserted-by":"crossref","first-page":"e57380","DOI":"10.1371\/journal.pone.0057380","article-title":"Antipurinergic therapy corrects the autism-like features in the poly(IC) mouse model","volume":"8","author":"RK Naviaux","year":"2013","journal-title":"PLoS One"},{"key":"ref54","doi-asserted-by":"crossref","first-page":"e400","DOI":"10.1038\/tp.2014.33","article-title":"Reversal of autism-like behaviors and metabolism in adult mice with single-dose antipurinergic therapy","volume":"4","author":"JC Naviaux","year":"2014","journal-title":"Transl Psychiatry"},{"key":"ref55","doi-asserted-by":"crossref","first-page":"2241","DOI":"10.1093\/brain\/awl150","article-title":"A systematic review of prion therapeutics in experimental models","volume":"129","author":"CR Trevitt","year":"2006","journal-title":"Brain"},{"key":"ref56","doi-asserted-by":"crossref","first-page":"4959","DOI":"10.1242\/jcs.02609","article-title":"Charged bipolar suramin derivatives induce aggregation of the prion protein at the cell surface and inhibit PrPSc replication","volume":"118","author":"M Nunziante","year":"2005","journal-title":"J Cell Sci"},{"key":"ref57","first-page":"2239","article-title":"Suramin: a novel antineoplastic agent with multiple potential mechanisms of action","volume":"53","author":"CA Stein","year":"1993","journal-title":"Cancer Res"},{"key":"ref58","doi-asserted-by":"crossref","first-page":"1478","DOI":"10.1021\/jm020427b","article-title":"Kinase inhibitors: not just for kinases anymore","volume":"46","author":"SL McGovern","year":"2003","journal-title":"J Med Chem"},{"key":"ref59","doi-asserted-by":"crossref","first-page":"31232","DOI":"10.1074\/jbc.M110.212613","article-title":"The trypanocidal drug suramin and other trypan blue mimetics are inhibitors of pyruvate kinases and bind to the adenosine site","volume":"286","author":"HP Morgan","year":"2011","journal-title":"J Biol Chem"},{"key":"ref60","doi-asserted-by":"crossref","first-page":"3249","DOI":"10.1016\/j.bmcl.2007.04.013","article-title":"Directed molecular screening for RecA ATPase inhibitors","volume":"17","author":"TJ Wigle","year":"2007","journal-title":"Bioorg Med Chem Lett"},{"key":"ref61","doi-asserted-by":"crossref","first-page":"1839","DOI":"10.1517\/14656566.2013.813934","article-title":"Cisplatin: an old drug with a newfound efficacy \u2013 from mechanisms of action to cytotoxicity","volume":"14","author":"A Maccio","year":"2013","journal-title":"Expert Opin Pharmacother"},{"key":"ref62","doi-asserted-by":"crossref","first-page":"7265","DOI":"10.1038\/sj.onc.1206933","article-title":"Cisplatin: mode of cytotoxic action and molecular basis of resistance","volume":"22","author":"ZH Siddik","year":"2003","journal-title":"Oncogene"},{"key":"ref63","doi-asserted-by":"crossref","first-page":"14721","DOI":"10.1074\/jbc.273.24.14721","article-title":"Cisplatin binding sites on human albumin","volume":"273","author":"AI Ivanov","year":"1998","journal-title":"J Biol Chem"},{"key":"ref64","doi-asserted-by":"crossref","first-page":"9936","DOI":"10.1073\/pnas.152333299","article-title":"Amino acid residue 184 of yeast Hsp104 chaperone is critical for prion-curing by guanidine, prion propagation, and thermotolerance","volume":"99","author":"G Jung","year":"2002","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref65","doi-asserted-by":"crossref","first-page":"1357","DOI":"10.1046\/j.1365-2958.2001.02478.x","article-title":"The elimination of the yeast [PSI+] prion by guanidine hydrochloride is the result of Hsp104 inactivation","volume":"40","author":"PC Ferreira","year":"2001","journal-title":"Mol Microbiol"},{"key":"ref66","doi-asserted-by":"crossref","first-page":"697","DOI":"10.1038\/10754","article-title":"Co-translational domain folding as the structural basis for the rapid de novo folding of firefly luciferase","volume":"6","author":"J Frydman","year":"1999","journal-title":"Nat Struct Biol"},{"key":"ref67","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1016\/j.molcel.2006.05.042","article-title":"Destruction or potentiation of different prions catalyzed by similar Hsp104 remodeling activities","volume":"23","author":"J Shorter","year":"2006","journal-title":"Mol Cell"},{"key":"ref68","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1007\/BF02110333","article-title":"Yeast multidrug resistance: the PDR network","volume":"27","author":"E Balzi","year":"1995","journal-title":"J Bioenerg Biomembr"},{"key":"ref69","doi-asserted-by":"crossref","first-page":"880","DOI":"10.1126\/science.7754373","article-title":"Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]","volume":"268","author":"YO Chernoff","year":"1995","journal-title":"Science"},{"key":"ref70","doi-asserted-by":"crossref","first-page":"137","DOI":"10.2174\/157488411796151174","article-title":"Tissue protective and anti-fibrotic actions of suramin: new uses of an old drug","volume":"6","author":"N Liu","year":"2011","journal-title":"Curr Clin Pharmacol"},{"key":"ref71","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1038\/43481","article-title":"Global unfolding of a substrate protein by the Hsp100 chaperone ClpA","volume":"401","author":"EU Weber-Ban","year":"1999","journal-title":"Nature"},{"key":"ref72","doi-asserted-by":"crossref","first-page":"914","DOI":"10.1073\/pnas.98.3.914","article-title":"Subunit interactions influence the biochemical and biological properties of Hsp104","volume":"98","author":"EC Schirmer","year":"2001","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref73","doi-asserted-by":"crossref","first-page":"2732","DOI":"10.1073\/pnas.261693199","article-title":"Analysis of the AAA sensor-2 motif in the C-terminal ATPase domain of Hsp104 with a site-specific fluorescent probe of nucleotide binding","volume":"99","author":"DA Hattendorf","year":"2002","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref74","doi-asserted-by":"crossref","first-page":"17615","DOI":"10.1074\/jbc.M209686200","article-title":"Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP hydrolysis, and chaperone activity","volume":"278","author":"A Mogk","year":"2003","journal-title":"J Biol Chem"},{"key":"ref75","doi-asserted-by":"crossref","first-page":"4480","DOI":"10.1016\/S0021-9258(17)41804-7","article-title":"Saccharomyces cerevisiae Hsp104 protein. Purification and characterization of ATP-induced structural changes","volume":"269","author":"DA Parsell","year":"1994","journal-title":"J Biol Chem"},{"key":"ref76","doi-asserted-by":"crossref","first-page":"1400","DOI":"10.1016\/j.chembiol.2012.09.013","article-title":"Hsp104 drives \u201cprotein-only\u201d positive selection of Sup35 prion strains encoding strong [PSI(+)]","volume":"19","author":"ME DeSantis","year":"2012","journal-title":"Chem Biol"},{"key":"ref77","doi-asserted-by":"crossref","first-page":"e02481","DOI":"10.7554\/eLife.02481","article-title":"Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation","volume":"3","author":"M Carroni","year":"2014","journal-title":"Elife (Cambridge)"},{"key":"ref78","doi-asserted-by":"crossref","first-page":"3957","DOI":"10.1093\/emboj\/20.15.3957","article-title":"Intracellular re-routing of prion protein prevents propagation of PrP(Sc) and delays onset of prion disease","volume":"20","author":"S Gilch","year":"2001","journal-title":"EMBO J"},{"key":"ref79","doi-asserted-by":"crossref","first-page":"270","DOI":"10.1038\/353270a0","article-title":"Hsp104 is a highly conserved protein with two essential nucleotide-binding sites","volume":"353","author":"DA Parsell","year":"1991","journal-title":"Nature"},{"key":"ref80","doi-asserted-by":"crossref","first-page":"1379","DOI":"10.4161\/cc.28709","article-title":"Reversing deleterious protein aggregation with re-engineered protein disaggregases","volume":"13","author":"ME Jackrel","year":"2014","journal-title":"Cell Cycle"},{"key":"ref81","doi-asserted-by":"crossref","unstructured":"Jackrel ME, Shorter J (2014) Potentiated Hsp104 variants suppress toxicity of diverse neurodegenerative disease-linked proteins. Dis Model Mech doi:10.1242\/dmm.016113.","DOI":"10.1242\/dmm.016113"},{"key":"ref82","doi-asserted-by":"crossref","first-page":"751","DOI":"10.1016\/S1097-2765(02)00499-9","article-title":"Defining a pathway of communication from the C-terminal peptide binding domain to the N-terminal ATPase domain in a AAA protein","volume":"9","author":"AG Cashikar","year":"2002","journal-title":"Mol Cell"},{"key":"ref83","doi-asserted-by":"crossref","first-page":"2061","DOI":"10.1091\/mbc.E02-08-0502","article-title":"Dominant gain-of-function mutations in Hsp104p reveal crucial roles for the middle region","volume":"15","author":"EC Schirmer","year":"2004","journal-title":"Mol Biol Cell"},{"key":"ref84","doi-asserted-by":"crossref","first-page":"810","DOI":"10.1016\/j.febslet.2013.02.011","article-title":"Mechanism of Hsp104\/ClpB inhibition by prion curing Guanidinium hydrochloride","volume":"587","author":"E Kummer","year":"2013","journal-title":"FEBS Lett"}],"container-title":["PLoS ONE"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/dx.plos.org\/10.1371\/journal.pone.0110115","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,4,19]],"date-time":"2022-04-19T18:24:15Z","timestamp":1650392655000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pone.0110115"}},"subtitle":[],"editor":[{"given":"Koichi M.","family":"Iijima","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"editor"}]}],"short-title":[],"issued":{"date-parts":[[2014,10,9]]},"references-count":84,"journal-issue":{"issue":"10","published-online":{"date-parts":[[2014,10,9]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pone.0110115","relation":{},"ISSN":["1932-6203"],"issn-type":[{"value":"1932-6203","type":"electronic"}],"subject":[],"published":{"date-parts":[[2014,10,9]]}}}