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dc.contributor.author
Caramelo, Julio Javier
dc.contributor.author
Parodi, Armando José A.
dc.contributor.other
Lennarz, William J.
dc.contributor.other
Lanes, M. Daniel
dc.date.available
2021-06-18T02:23:18Z
dc.date.issued
2013
dc.identifier.citation
Caramelo, Julio Javier; Parodi, Armando José A.; Glycoprotein Folding and Processing Reactions; Academic Press Inc Elsevier Science; 2013; 448-452
dc.identifier.isbn
978-0-12-378631-9
dc.identifier.uri
http://hdl.handle.net/11336/134488
dc.description.abstract
The N-glycan-dependent quality control of glycoprotein folding occurring in the endoplasmic reticulum prevents exit to Golgi of folding intermediates, irreparably misfolded glycoproteins, and incompletely assembled multimeric complexes. It also enhances folding efficiency by preventing aggregation and facilitating formation of proper disulfide bonds. The control mechanism essentially involves four components, two resident lectin-chaperones, calnexin and calreticulin, that recognize monoglucosylated polymannose protein-linked glycans, a lectin-associated oxidoreductase acting on monoglucosylated glycoproteins, a glucosyltransferase that creates monoglucosytlated epitopes in protein-linked glycans, and a glucosidase that removes the glucose units added by the glucosyltransferase. The glucosyltransferase is the only mechanism component sensing glycoprotein conformations as it creates monoglucosylated glycans exclusively in not properly folded species or in not completely assembled complexes. The glucosidase is a heterodimer composed of a catalytic subunit and an additional one that is responsible for the ER localization of the enzyme. The glucosyltransferase, the glucosidase, and calreticulin, but not calnexin, are soluble proteins.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Academic Press Inc Elsevier Science
dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Quality control
dc.subject
Glycoprotein folding
dc.subject
endoplasmic reticulum
dc.subject.classification
Bioquímica y Biología Molecular
dc.subject.classification
Ciencias Biológicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
Glycoprotein Folding and Processing Reactions
dc.type
info:eu-repo/semantics/publishedVersion
dc.type
info:eu-repo/semantics/bookPart
dc.type
info:ar-repo/semantics/parte de libro
dc.date.updated
2020-04-24T19:01:43Z
dc.journal.pagination
448-452
dc.journal.pais
Estados Unidos
dc.description.fil
Fil: Caramelo, Julio Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
dc.description.fil
Fil: Parodi, Armando José A.. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/B9780123786302001109
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/B978-0-12-378630-2.00110-9
dc.conicet.paginas
3015
dc.source.titulo
The Encyclopedia of Biological Chemistry
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