Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Esther, Guarinos"'
Publikováno v:
Molecular Microbiology. 50:703-712
The analysis of the not well understood composition of the stalk, a key ribosomal structure, in eukaryotes having multiple 12 kDa P1/P2 acidic protein components has been approached using these proteins tagged with a histidine tail at the C-terminus.
Autor:
Juan P. G. Ballesta, Esther Guarinos, Vassiliki Lalioti, J. Zurdo, Gretel Nusspaumer, Jorge Perez-Fernandez, Pilar Parada, Miguel Remacha
The stalk of the large ribosomal subunit is involved in the interaction of the elongation factors with the ribosome, as biochemical data have clearly indicated and as has been directly confirmed by electron microscopy. The eukaryotic ribosomal-stalk
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0e976c80de80daa681b4ce46283226a7
https://doi.org/10.1128/9781555818142.ch12
https://doi.org/10.1128/9781555818142.ch12
Publikováno v:
Journal of Biological Chemistry. 276:32474-32479
The Saccharomyces cerevisiae ribosomal stalk is made of five components, the 32-kDa P0 and four 12-kDa acidic proteins, P1alpha, P1beta, P2alpha, and P2beta. The P0 carboxyl-terminal domain is involved in the interaction with the acidic proteins and
Autor:
Antonio Morreale, Juan P. G. Ballesta, Alberto García-Marcos, Angel R. Ortiz, Esther Guarinos, Miguel Remacha, Elisa Briones
Publikováno v:
Nucleic Acids Research
Biblos-e Archivo. Repositorio Institucional de la UAM
instname
Digital.CSIC. Repositorio Institucional del CSIC
Biblos-e Archivo. Repositorio Institucional de la UAM
instname
Digital.CSIC. Repositorio Institucional del CSIC
Article available at http://dx.doi.org/10.1093/nar/gkm773
Eukaryotic ribosomal stalk protein L12 and its bacterial orthologue L11 play a central role on ribosomal conformational changes during translocation. Deletion of the two genes encoding L1
Eukaryotic ribosomal stalk protein L12 and its bacterial orthologue L11 play a central role on ribosomal conformational changes during translocation. Deletion of the two genes encoding L1
Autor:
Esther, Guarinos, Cruz, Santos, Arancha, Sánchez, De-Yi, Qiu, Miguel, Remacha, Juan P G, Ballesta
Publikováno v:
Molecular microbiology. 50(2)
The analysis of the not well understood composition of the stalk, a key ribosomal structure, in eukaryotes having multiple 12 kDa P1/P2 acidic protein components has been approached using these proteins tagged with a histidine tail at the C-terminus.
Autor:
Miguel Remacha, Esther Guarinos, Antonio Jimenez-Diaz, Cruz Santos, Elisa Briones, Juan P. G. Ballesta, M. A. Rodriguez Gabriel, Reina Zambrano
Publikováno v:
Scopus-Elsevier
The eukaryoic ribosomal stalk is thought to consist of the phosphoproteins P1 and P2, which form a complex with protein P0. This complex interacts at the GTPase domain in the large subunit rRNA, overlapping the binding site of the protein L11-like eu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c2044787c1c1fd16988bd710fbfb09c7
http://www.scopus.com/inward/record.url?eid=2-s2.0-0029402485&partnerID=MN8TOARS
http://www.scopus.com/inward/record.url?eid=2-s2.0-0029402485&partnerID=MN8TOARS
Autor:
Juan P. G. Ballesta, Esther Guarinos, Miguel Remacha, Antonio Jimenez-Diaz, B. Bermejo, Miguel Ángel Rodríguez-Gabriel
Publikováno v:
Scopus-Elsevier
Saccharomyces cerevisiae strains with either three inactivated genes (triple disruptants) or four inactivated genes (quadruple disruptants) encoding the four acidic ribosomal phosphoproteins, YP1 alpha, YP1 beta, YP2 alpha, and YP2 beta, present in t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::39e8eab81523d45671bb11182a6963fc
http://www.scopus.com/inward/record.url?eid=2-s2.0-0028981381&partnerID=MN8TOARS
http://www.scopus.com/inward/record.url?eid=2-s2.0-0028981381&partnerID=MN8TOARS