{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,5]],"date-time":"2026-11-05T10:24:54Z","timestamp":1793874294194,"version":"4.6.1"},"reference-count":34,"publisher":"Elsevier BV","issue":"12","license":[{"start":{"date-parts":[[2026,12,1]],"date-time":"2026-12-01T00:00:00Z","timestamp":1796083200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,12,1]],"date-time":"2026-12-01T00:00:00Z","timestamp":1796083200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,12,1]],"date-time":"2026-12-01T00:00:00Z","timestamp":1796083200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2026,12,1]],"date-time":"2026-12-01T00:00:00Z","timestamp":1796083200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,12,1]],"date-time":"2026-12-01T00:00:00Z","timestamp":1796083200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2026,12,1]],"date-time":"2026-12-01T00:00:00Z","timestamp":1796083200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,12,1]],"date-time":"2026-12-01T00:00:00Z","timestamp":1796083200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100006769","name":"Russian Science Foundation","doi-asserted-by":"publisher","award":["23-74-00021"],"award-info":[{"award-number":["23-74-00021"]}],"id":[{"id":"10.13039\/501100006769","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochimica et Biophysica Acta (BBA) - General Subjects"],"published-print":{"date-parts":[[2026,12]]},"DOI":"10.1016\/j.bbagen.2026.131012","type":"journal-article","created":{"date-parts":[[2026,10,2]],"date-time":"2026-10-02T15:24:11Z","timestamp":1790954651000},"page":"131012","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"title":["D90N and D90K mutations in the chaperonin OBP reduce its ability to induce fibrillation of the prion protein by decreasing ATPase activity"],"prefix":"10.1016","volume":"1870","author":[{"given":"Denis V.","family":"Pozdyshev","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Victor N.","family":"Orlov","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maria V.","family":"Kirpichenko","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sofiya S.","family":"Kudryavtseva","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ilya P.","family":"Oleynikov","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sergei A.","family":"Golyshev","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vladimir I.","family":"Muronetz","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lidia P.","family":"Kurochkina","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbagen.2026.131012_bb0005","doi-asserted-by":"crossref","DOI":"10.3390\/ijms25105483","article-title":"Molecular chaperonin HSP60: current understanding and future prospects","volume":"25","author":"Singh","year":"2024","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.bbagen.2026.131012_bb0010","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1146\/annurev-biophys-082521-113418","article-title":"Chaperonin mechanisms: multiple and (mis)understood?","volume":"51","author":"Horovitz","year":"2022","journal-title":"Annu. Rev. Biophys."},{"key":"10.1016\/j.bbagen.2026.131012_bb0015","doi-asserted-by":"crossref","DOI":"10.1017\/S0033583519000143","article-title":"Chaperonin-assisted protein folding: a chronologue","volume":"53","author":"Horwich","year":"2020","journal-title":"Q. Rev. Biophys."},{"key":"10.1016\/j.bbagen.2026.131012_bb0020","doi-asserted-by":"crossref","first-page":"1852","DOI":"10.1126\/science.1068408","article-title":"Molecular chaperones in the cytosol: from nascent chain to folded protein","volume":"295","author":"Hartl","year":"2002","journal-title":"Science"},{"key":"10.1016\/j.bbagen.2026.131012_bb0025","doi-asserted-by":"crossref","DOI":"10.3389\/fgene.2020.00172","article-title":"The molecular chaperone CCT\/TRiC: an essential component of proteostasis and a potential modulator of protein aggregation","volume":"11","author":"Grantham","year":"2020","journal-title":"Front. Genet."},{"key":"10.1016\/j.bbagen.2026.131012_bb0030","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1146\/annurev.biophys.30.1.245","article-title":"Chaperonin-mediated protein folding","volume":"30","author":"Thirumalai","year":"2001","journal-title":"Annu. Rev. Biophys. Biomol. Struct."},{"key":"10.1016\/j.bbagen.2026.131012_bb0035","doi-asserted-by":"crossref","first-page":"536","DOI":"10.1016\/j.jmb.2005.08.075","article-title":"Genome comparison of Pseudomonas aeruginosa large Phages","volume":"354","author":"Hertveldt","year":"2005","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbagen.2026.131012_bb0040","doi-asserted-by":"crossref","first-page":"1844","DOI":"10.1128\/JVI.06330-11","article-title":"Complete genome sequence of the Giant virus OBP and comparative genome analysis of the diverse \u03d5KZ-related Phages","volume":"86","author":"Cornelissen","year":"2012","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2026.131012_bb0045","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1016\/j.virol.2016.04.030","article-title":"The genome of AR9, a giant transducing Bacillus phage encoding two multisubunit RNA polymerases","volume":"495","author":"Lavysh","year":"2016","journal-title":"Virology"},{"key":"10.1016\/j.bbagen.2026.131012_bb0050","doi-asserted-by":"crossref","DOI":"10.1128\/JVI.02391-20","article-title":"Comparative genomics of three novel jumbo bacteriophages infecting Staphylococcus aureus","volume":"95","author":"Korn","year":"2021","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2026.131012_bb0055","doi-asserted-by":"crossref","first-page":"544","DOI":"10.1016\/j.ijbiomac.2020.04.189","article-title":"Structural and functional diversity of novel and known bacteriophage-encoded chaperonins","volume":"157","author":"Semenyuk","year":"2020","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.bbagen.2026.131012_bb0060","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1134\/S0006297922010011","article-title":"Structural and functional features of viral chaperonins","volume":"87","author":"Kurochkina","year":"2022","journal-title":"Biochemistry (Mosc)"},{"key":"10.1016\/j.bbagen.2026.131012_bb0065","doi-asserted-by":"crossref","DOI":"10.1016\/j.jsb.2019.107439","article-title":"Cryo-EM reveals an asymmetry in a novel single-ring viral chaperonin","volume":"209","author":"Stanishneva-Konovalova","year":"2020","journal-title":"J. Struct. Biol."},{"key":"10.1016\/j.bbagen.2026.131012_bb0070","doi-asserted-by":"crossref","first-page":"614","DOI":"10.1038\/371614a0","article-title":"Residues in chaperonin GroEL required for polypeptide binding and release","volume":"371","author":"Fenton","year":"1994","journal-title":"Nature"},{"key":"10.1016\/j.bbagen.2026.131012_bb0075","doi-asserted-by":"crossref","first-page":"13956","DOI":"10.1074\/jbc.270.23.13956","article-title":"A mutant at position 87 of the GroEL chaperonin is affected in protein binding and ATP hydrolysis","volume":"270","author":"Weiss","year":"1995","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2026.131012_bb0080","doi-asserted-by":"crossref","first-page":"2383","DOI":"10.1042\/BCJ20160367","article-title":"New GroEL-like chaperonin of bacteriophage OBP Pseudomonas fluorescens suppresses thermal protein aggregation in an ATP-dependent manner","volume":"473","author":"Semenyuk","year":"2016","journal-title":"Biochem. J."},{"key":"10.1016\/j.bbagen.2026.131012_bb0085","doi-asserted-by":"crossref","DOI":"10.1016\/j.bbapap.2023.140965","article-title":"Bacteriophage-encoded chaperonins stimulate prion protein fibrillation in an ATP-dependent manner","volume":"1872","author":"Leisi","year":"2024","journal-title":"Biochim. Biophys. Acta, Proteins Proteomics"},{"key":"10.1016\/j.bbagen.2026.131012_bb0090","doi-asserted-by":"crossref","DOI":"10.1016\/j.abb.2025.110493","article-title":"Interaction of phage chaperonin OBP domains with amyloidogenic proteins","volume":"771","author":"Leisi","year":"2025","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.bbagen.2026.131012_bb0095","doi-asserted-by":"crossref","first-page":"10103","DOI":"10.1128\/JVI.00940-12","article-title":"Expression and functional characterization of the first bacteriophage-encoded chaperonin","volume":"86","author":"Robben","year":"2012","journal-title":"J. Virol."},{"key":"10.1016\/j.bbagen.2026.131012_bb0100","doi-asserted-by":"crossref","DOI":"10.3389\/fnagi.2020.581374","article-title":"Molecular chaperones: a double-edged sword in neurodegenerative diseases","volume":"12","author":"Tittelmeier","year":"2020","journal-title":"Front. Aging Neurosci."},{"key":"10.1016\/j.bbagen.2026.131012_bb0105","doi-asserted-by":"crossref","first-page":"S164","DOI":"10.1134\/S0006297924604003","article-title":"Factors affecting pathological amyloid protein transformation: from post-translational modifications to chaperones","volume":"90","author":"Muronets","year":"2025","journal-title":"Biochemistry (Mosc)"},{"key":"10.1016\/j.bbagen.2026.131012_bb0110","doi-asserted-by":"crossref","first-page":"680","DOI":"10.1038\/227680a0","article-title":"Cleavage of structural proteins during the assembly of the head of bacteriophage T4","volume":"227","author":"Laemmli","year":"1970","journal-title":"Nature"},{"key":"10.1016\/j.bbagen.2026.131012_bb0115","first-page":"2833","article-title":"High yield purification and physico-chemical properties of full-length recombinant allelic variants of sheep prion protein linked to scrapie susceptibility","volume":"267","author":"Rezaei","year":"2000","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.bbagen.2026.131012_bb0120","doi-asserted-by":"crossref","first-page":"266","DOI":"10.1016\/0003-2697(88)90484-8","article-title":"A malachite green procedure for orthophosphate determination and its use in alkaline phosphatase-based enzyme immunoassay","volume":"171","author":"Baykov","year":"1988","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.bbagen.2026.131012_bb0125","doi-asserted-by":"crossref","first-page":"3448","DOI":"10.1529\/biophysj.106.098608","article-title":"A three-stage kinetic model of amyloid fibrillation","volume":"92","author":"Lee","year":"2007","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbagen.2026.131012_bb0130","doi-asserted-by":"crossref","DOI":"10.1016\/j.str.2024.02.001","article-title":"Cryo-EM structure and molecular dynamic simulations explain the enhanced stability and ATP activity of the pathological chaperonin mutant","volume":"32","author":"Syed","year":"2024","journal-title":"Structure"},{"key":"10.1016\/j.bbagen.2026.131012_bb0135","doi-asserted-by":"crossref","DOI":"10.3390\/biomedicines9111649","article-title":"Structural and computational study of the GroEL\u2013prion protein complex","volume":"9","author":"Mamchur","year":"2021","journal-title":"Biomedicines"},{"key":"10.1016\/j.bbagen.2026.131012_bb0140","doi-asserted-by":"crossref","first-page":"2373","DOI":"10.1074\/jbc.M510840200","article-title":"Annealing prion protein amyloid fibrils at high temperature results in extension of a proteinase K-resistant core","volume":"281","author":"Bocharova","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2026.131012_bb0145","doi-asserted-by":"crossref","first-page":"1586","DOI":"10.1021\/bi00220a020","article-title":"GroE facilitates refolding of citrate synthase by suppressing aggregation","volume":"30","author":"Buchner","year":"1991","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbagen.2026.131012_bb0150","doi-asserted-by":"crossref","first-page":"11609","DOI":"10.1021\/bi00114a001","article-title":"Reconstitution of a heat shock effect in vitro: influence of GroE on the thermal aggregation of alpha-glucosidase from yeast","volume":"30","author":"Hoell-Neugebauer","year":"1991","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbagen.2026.131012_bb0155","doi-asserted-by":"crossref","first-page":"1213","DOI":"10.1134\/S0006297916100199","article-title":"Inhibition of chaperonin GroEL by a monomer of ovine prion protein and its oligomeric forms","volume":"81","author":"Kudryavtseva","year":"2016","journal-title":"Biochem. Mosc."},{"key":"10.1016\/j.bbagen.2026.131012_bb0160","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1021\/bi011393x","article-title":"Molecular mechanisms of chaperonin GroEL\u2212GroES function","volume":"41","author":"Keskin","year":"2002","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbagen.2026.131012_bb0165","doi-asserted-by":"crossref","DOI":"10.3390\/biomedicines10123276","article-title":"Amyloid disassembly: what can we learn from chaperones?","volume":"10","author":"Almeida","year":"2022","journal-title":"Biomedicines"},{"key":"10.1016\/j.bbagen.2026.131012_bb0170","doi-asserted-by":"crossref","first-page":"848","DOI":"10.1039\/D3MD00040K","article-title":"Amyloid inhibition by molecular chaperones in vitro can be translated to Alzheimer\u2019s pathology in vivo","volume":"14","author":"Abelein","year":"2023","journal-title":"RSC Med. Chem."}],"container-title":["Biochimica et Biophysica Acta (BBA) - General Subjects"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0304416526001121?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0304416526001121?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,11,5]],"date-time":"2026-11-05T09:28:21Z","timestamp":1793870901000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0304416526001121"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,12]]},"references-count":34,"journal-issue":{"issue":"12","published-print":{"date-parts":[[2026,12]]}},"alternative-id":["S0304416526001121"],"URL":"https:\/\/doi.org\/10.1016\/j.bbagen.2026.131012","relation":{},"ISSN":["0304-4165"],"issn-type":[{"value":"0304-4165","type":"print"}],"subject":[],"published":{"date-parts":[[2026,12]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"D90N and D90K mutations in the chaperonin OBP reduce its ability to induce fibrillation of the prion protein by decreasing ATPase activity","name":"articletitle","label":"Article Title"},{"value":"Biochimica et Biophysica Acta (BBA) - General Subjects","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bbagen.2026.131012","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 Published by Elsevier B.V.","name":"copyright","label":"Copyright"}],"article-number":"131012"}}