Protein folding assisted by chaperones

dc.creatorBorges, JC
dc.creatorRamos, CHI
dc.date2005
dc.dateAPR
dc.date2014-11-16T13:12:28Z
dc.date2015-11-26T17:25:05Z
dc.date2014-11-16T13:12:28Z
dc.date2015-11-26T17:25:05Z
dc.date.accessioned2018-03-29T00:12:22Z
dc.date.available2018-03-29T00:12:22Z
dc.identifierProtein And Peptide Letters. Bentham Science Publ Ltd, v. 12, n. 3, n. 257, n. 261, 2005.
dc.identifier0929-8665
dc.identifierWOS:000227740500009
dc.identifier10.2174/0929866053587165
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/58327
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/58327
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/58327
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1284242
dc.descriptionMolecular chaperones are one of the most important cell defense mechanisms against protein aggregation and misfolding. These specialized proteins bind non-native states of other proteins and assist them in reaching a correctly folded and functional conformation. Chaperones also participate in protein translocation by membranes, in the stabilization of unstable protein conformers and regulatory factors, in the delivery of substrates for proteolysis and in the recovery of proteins from aggregates.
dc.description12
dc.description3
dc.description257
dc.description261
dc.languageen
dc.publisherBentham Science Publ Ltd
dc.publisherSharjah
dc.publisherEmirados Árabes Unidos
dc.relationProtein And Peptide Letters
dc.relationProtein Pept. Lett.
dc.rightsfechado
dc.sourceWeb of Science
dc.subjectmolecular chaperones
dc.subjectheat shock proteins
dc.subjectHsp70
dc.subjectchaperonin
dc.subjectHeat-shock-protein
dc.subjectNucleotide Exchange Factor
dc.subjectCrystal-structure
dc.subjectMolecular Chaperone
dc.subjectSubstrate-binding
dc.subjectMitochondrial Grpe
dc.subjectNonnative Protein
dc.subjectAlpha-crystallin
dc.subjectAtpase Activity
dc.subjectDnak Chaperone
dc.titleProtein folding assisted by chaperones
dc.typeArtículos de revistas


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