dc.creatorBicev, Renata Naporano
dc.creatorOliveira, Cristiano Luis Pinto de
dc.creatorDemasi, M.
dc.date.accessioned2014-04-01T14:09:33Z
dc.date.accessioned2018-07-04T16:45:08Z
dc.date.available2014-04-01T14:09:33Z
dc.date.available2018-07-04T16:45:08Z
dc.date.created2014-04-01T14:09:33Z
dc.date.issued2013-02-26
dc.identifierReunião Anual de Usuários do LNLS RAU, XXIII, 2013, Campinas
dc.identifierhttp://www.producao.usp.br/handle/BDPI/44349
dc.identifierhttp://lnls.cnpem.br/rau/files/2013/04/Livro-Resumos-23RAU.pdf
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1639876
dc.description.abstractThe process of intracellular proteolysis (protein degradation) is a regulatory mechanism of cellular homeostasis with the same level of importance as gene expression.The proteasome is a proteolytic complex responsible for protein degradation and consists of a catalytic core unit called the 20S(20SPT) where the hydrolysis occurs, engaged in one or both ends by regulatory units, called 19S, responsible for the recognition of poly-ubiquitylated proteins, unfolding and translocation of them to the 20S catalytic chamber. However, the catalytic unit (20SPT) can also degrade not marked proteins with poly-ubiquitin tail, as in the case of oxidized proteins. Oxidized proteins have a tendency to form aggregates (a phenomenon that underlies human neurodegenerative diseases), and therefore they must be effectively removed from the living cell. Interestingly, the cells have approximately 1/3 of proteasome without regulatory units, i.e. only the 20S catalytic unit.
dc.languageeng
dc.publisherComitê dos Usuários do LNLS
dc.publisherCNPEM/LNLS
dc.publisherCampinas
dc.relationReunião Anual de Usuários do LNLS RAU, XXIII
dc.rightsRenata Naporano Bicev
dc.rightsopenAccess
dc.subject20S proteasome
dc.subjectStructural study
dc.subjectSAXS
dc.title20S Proteasome: Structural study using SAXS.
dc.typeActas de congresos


Este ítem pertenece a la siguiente institución