dc.contributorUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2019-10-06T15:36:47Z
dc.date.accessioned2022-12-19T18:31:14Z
dc.date.available2019-10-06T15:36:47Z
dc.date.available2022-12-19T18:31:14Z
dc.date.created2019-10-06T15:36:47Z
dc.date.issued2019-05-01
dc.identifierInternational Journal of Biochemistry and Cell Biology, v. 110, p. 140-142.
dc.identifier1878-5875
dc.identifier1357-2725
dc.identifierhttp://hdl.handle.net/11449/187460
dc.identifier10.1016/j.biocel.2019.03.007
dc.identifier2-s2.0-85062893393
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/5368498
dc.description.abstractSome mechanisms of cellular stress, aging, and apoptosis are related to proteolysis. With respect to ClpP, little is known about the mechanical manner in which the substrate is hydrolyzed in and released from the degradation chamber. Furthermore, what would be the real influence of ClpP in mammalian UPR mt ?
dc.languageeng
dc.relationInternational Journal of Biochemistry and Cell Biology
dc.rightsAcesso aberto
dc.sourceScopus
dc.subjectCellular function
dc.subjectChaperone
dc.subjectProtease
dc.subjectProteostasis
dc.titleControlling proteolysis of Clp peptidase: a possible target for combating mitochondrial diseases
dc.typeOtros


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