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dc.contributor.author
Trombetta, E. Sergio
dc.contributor.author
Parodi, Armando José A.
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dc.contributor.other
Buchner, Johannes
dc.contributor.other
Kiefhaber, Thomas
dc.date.available
2021-07-30T00:34:19Z
dc.date.issued
2005
dc.identifier.citation
Trombetta, E. Sergio; Parodi, Armando José A.; Quality Control in Glycoprotein Folding; Wiley-VCH; II; 2005; 617-648
dc.identifier.isbn
9783527307845
dc.identifier.uri
http://hdl.handle.net/11336/137408
dc.description.abstract
The concept of quality control of protein folding in the secretory pathway emerged in the late 1970s and early 1980s when it was noticed that not in all cases did insertion of proteins in the endoplasmic reticulum (ER) result in their appearance at the expected final destination, intra- or extracellular. Several experimental results showed that cells displayed mechanisms that ensured that only proteins in their native conformations could be produced by the secretory pathway. Those mechanisms received the collective denomination of ‘‘quality control’’. Protein folding in living cells is a complex, error-prone process. Numerous mechanisms are in place to ensure that newly synthesized proteins reach their folded functional form. One such mechanism is the addition of glycans occurring in the ER lumen. Covalently linked N-glycans affect protein folding in cell-free assays, as they provide bulky, highly hydrophilic substituents that maintain molecules in solution while protein moieties successively adopt a variety of different conformations before reaching their final structures. In addition, the highly hydrophilic nature of N-glycans forces the asparagine units to which they are linked and neighboring amino acids to be in or close to the water-protein interphase. This chapter will not deal with those effects, which certainly also occur in vivo, but with folding-efficiency enhancement and ER retention of folding intermediates and irreparably misfolded species mediated by the interaction of a specific glycan structure (monoglucosylated polymannose-type compounds) with the ER lectins calnexin (CNX) and calreticulin (CRT). Recent evidence suggesting a role for a specific putative lectin (EDEM/Htm1p/Man1p) on the disposal of irreparably misfolded glycoproteins will be discussed also.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Wiley-VCH
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dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
GLYCOPROTEIN FOLDING
dc.subject.classification
Bioquímica y Biología Molecular
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dc.subject.classification
Ciencias Biológicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
Quality Control in Glycoprotein Folding
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
2020-06-23T15:15:03Z
dc.journal.volume
II
dc.journal.pagination
617-648
dc.journal.pais
Estados Unidos
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dc.journal.ciudad
Weinham
dc.description.fil
Fil: Trombetta, E. Sergio. Yale Medical School; Estados Unidos
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://onlinelibrary.wiley.com/doi/10.1002/9783527619498.ch50
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/https://doi.org/10.1002/9783527619498.ch50
dc.conicet.paginas
1365
dc.source.titulo
Protein Folding Handbook
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