Registro completo de metadatos
| Campo DC | Valor | Lengua/Idioma |
|---|---|---|
| dc.creator | Olson, Linda J. | - |
| dc.creator | Orsi, Ramiro | - |
| dc.creator | Alculumbre, Solana G. | - |
| dc.creator | Peterson, Francis C. | - |
| dc.creator | Stigliano, Ivan Daniel | - |
| dc.creator | Parodi, Armando Jose A. | - |
| dc.creator | D'alessio, Cecilia | - |
| dc.creator | Dahms, Nancy M. | - |
| dc.date | 2017-07-06T14:34:11Z | - |
| dc.date | 2017-07-06T14:34:11Z | - |
| dc.date | 2013-06 | - |
| dc.date | 2016-09-05T13:18:41Z | - |
| dc.date.accessioned | 2019-04-29T15:48:34Z | - |
| dc.date.available | 2019-04-29T15:48:34Z | - |
| dc.date.issued | 2013-06 | - |
| dc.identifier | Olson, Linda J.; Orsi, Ramiro; Alculumbre, Solana G.; Peterson, Francis C.; Stigliano, Ivan Daniel; et al.; Structure of the lectin mannose 6-phosphate receptor homology (MRH) domain of glucosidase II an enzyme that regulates glycoprotein folding quality control in the endoplasmic reticulum; American Society for Biochemistry and Molecular Biology; Journal Of Biological Chemistry (online); 288; 23; 6-2013; 16460-16475 | - |
| dc.identifier | 0021-9258 | - |
| dc.identifier | http://hdl.handle.net/11336/19717 | - |
| dc.identifier | 1083-351X | - |
| dc.identifier | CONICET Digital | - |
| dc.identifier | CONICET | - |
| dc.identifier.uri | http://rodna.bn.gov.ar:8080/jspui/handle/bnmm/302619 | - |
| dc.description | Here we report for the first time the three-dimensional structure of a mannose 6-phosphate receptor homology (MRH) domain present in a protein with enzymatic activity, glucosidase II (GII). GII is involved in glycoprotein folding in the endoplasmic reticulum. GII removes the two innermost glucose residues from the Glc3Man9GlcNAc2 transferred to nascent proteins and the glucose added by UDP-Glc:glycoprotein glucosyltransferase. GII is composed of a catalytic GIIα subunit and a regulatory GIIβ subunit. GIIβ participates in the endoplasmic reticulum localization of GIIα and mediates in vivo enhancement of N-glycan trimming by GII through its C-terminal MRH domain. We determined the structure of a functional GIIβ MRH domain by NMR spectroscopy. It adopts a β-barrel fold similar to that of other MRH domains, but its binding pocket is the most shallow known to date as it accommodates a single mannose residue. In addition, we identified a conserved residue outside the binding pocket (Trp-409) present in GIIβ but not in other MRHs that influences GII glucose trimming activity. | - |
| dc.description | Fil: Olson, Linda J.. Medical College Of Wisconsin; Estados Unidos | - |
| dc.description | Fil: Orsi, Ramiro. 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: Alculumbre, Solana G.. 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: Peterson, Francis C.. Medical College Of Wisconsin; Estados Unidos | - |
| dc.description | Fil: Stigliano, Ivan Daniel. 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: Parodi, Armando Jose 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.description | Fil: D'alessio, Cecilia. 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. Universidad de Buenos Aires; Argentina | - |
| dc.description | Fil: Dahms, Nancy M.. Medical College Of Wisconsin; Estados Unidos | - |
| dc.format | application/pdf | - |
| dc.format | application/pdf | - |
| dc.format | application/pdf | - |
| dc.format | application/pdf | - |
| dc.language | eng | - |
| dc.publisher | American Society for Biochemistry and Molecular Biology | - |
| dc.relation | info:eu-repo/semantics/altIdentifier/url/http://www.jbc.org/content/288/23/16460.long | - |
| dc.relation | info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1074/jbc.M113.450239 | - |
| dc.rights | info:eu-repo/semantics/openAccess | - |
| dc.rights | https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ | - |
| dc.source | reponame:CONICET Digital (CONICET) | - |
| dc.source | instname:Consejo Nacional de Investigaciones Científicas y Técnicas | - |
| dc.source | instacron:CONICET | - |
| dc.source.uri | http://hdl.handle.net/11336/17347 | - |
| dc.subject | Endoplasmic Reticulum | - |
| dc.subject | Glucosidase II B | - |
| dc.subject | Glycobiology | - |
| dc.subject | MRH Domain | - |
| dc.subject | Bioquímica y Biología Molecular | - |
| dc.subject | Ciencias Biológicas | - |
| dc.subject | CIENCIAS NATURALES Y EXACTAS | - |
| dc.title | Structure of the lectin mannose 6-phosphate receptor homology (MRH) domain of glucosidase II an enzyme that regulates glycoprotein folding quality control in the endoplasmic reticulum | - |
| dc.type | info:eu-repo/semantics/article | - |
| dc.type | info:eu-repo/semantics/publishedVersion | - |
| dc.type | info:ar-repo/semantics/articulo | - |
| Aparece en las colecciones: | CONICET | |
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