Zobrazeno 1 - 10
of 29
pro vyhledávání: '"Rosa M. Ríos"'
Autor:
Francisco Rivero-Rodríguez, Antonio Díaz-Quintana, Alejandro Velázquez-Cruz, Katiuska González-Arzola, Maria P. Gavilan, Adrián Velázquez-Campoy, Rosa M. Ríos, Miguel A. De la Rosa, Irene Díaz-Moreno
Publikováno v:
Redox Biology, Vol 43, Iss , Pp 101967- (2021)
Repair of injured DNA relies on nucleosome dismantling by histone chaperones and de-phosphorylation events carried out by Protein Phosphatase 2A (PP2A). Typical histone chaperones are the Acidic leucine-rich Nuclear Phosphoprotein 32 family (ANP32) m
Externí odkaz:
https://doaj.org/article/c70cdc896df04b2f83aeef2d8a00e8fe
Autor:
Fernando R Balestra, Andrés Domínguez-Calvo, Benita Wolf, Coralie Busso, Alizée Buff, Tessa Averink, Marita Lipsanen-Nyman, Pablo Huertas, Rosa M Ríos, Pierre Gönczy
Publikováno v:
eLife, Vol 10 (2021)
TRIM37 is an E3 ubiquitin ligase mutated in Mulibrey nanism, a disease with impaired organ growth and increased tumor formation. TRIM37 depletion from tissue culture cells results in supernumerary foci bearing the centriolar protein Centrin. Here, we
Externí odkaz:
https://doaj.org/article/43c73efe37f44b62a2ac44ad88b4b1c6
Autor:
Fernando R. Balestra, Benita Wolf, Andrés Domínguez-Calvo, Alizée Buff, Tessa Averink, Marita Lipsanen-Nyman, Coralie Busso, Pablo Huertas, Rosa M. Ríos, Pierre Gönczy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b511b5a5802a5c1550f563317ed39e4b
https://doi.org/10.15252/rc.2022383751
https://doi.org/10.15252/rc.2022383751
Autor:
Katiuska González-Arzola, Antonio Díaz-Quintana, Noelia Bernardo-García, Jonathan Martínez-Fábregas, Francisco Rivero-Rodríguez, Miguel Á. Casado-Combreras, Carlos A. Elena-Real, Alejandro Velázquez-Cruz, Sergio Gil-Caballero, Adrián Velázquez-Campoy, Elzbieta Szulc, María P. Gavilán, Isabel Ayala, Rocío Arranz, Rosa M. Ríos, Xavier Salvatella, José M. Valpuesta, Juan A. Hermoso, Miguel A. De la Rosa, Irene Díaz-Moreno
Publikováno v:
Nature Structural and Molecular Biology
Nature Structural and Molecular Biology, 2022, 29 (10), pp.1024-1036. ⟨10.1038/s41594-022-00842-3⟩
Nature Structural and Molecular Biology, 2022, 29 (10), pp.1024-1036. ⟨10.1038/s41594-022-00842-3⟩
32 pags., 17 figs., 1 tab.
The regular functioning of the nucleolus and nucleus-mitochondria crosstalk are considered unrelated processes, yet cytochrome c (Cc) migrates to the nucleus and even the nucleolus under stress conditions. Nucleolar li
The regular functioning of the nucleolus and nucleus-mitochondria crosstalk are considered unrelated processes, yet cytochrome c (Cc) migrates to the nucleus and even the nucleolus under stress conditions. Nucleolar li
Autor:
Pablo Huertas, Fernando R. Balestra, Benita Wolf, Marita Lipsanen-Nyman, Rosa M. Ríos, Alizée Buff, Pierre Gönczy, Coralie Busso, Tessa Averink, Andrés Domínguez-Calvo
Publikováno v:
idUS: Depósito de Investigación de la Universidad de Sevilla
Universidad de Sevilla (US)
idUS. Depósito de Investigación de la Universidad de Sevilla
instname
eLife
eLife, Vol 10 (2021)
Universidad de Sevilla (US)
idUS. Depósito de Investigación de la Universidad de Sevilla
instname
eLife
eLife, Vol 10 (2021)
TRIM37 is an E3 ubiquitin ligase mutated in Mulibrey nanism, a disease with impaired organ growth and increased tumor formation. TRIM37 depletion from tissue culture cells results in supernumerary foci bearing the centriolar protein Centrin. Here, we
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::402a491220967dd6432b7190f679458f
Autor:
Tessa Averink, Pablo Huertas, Marita Lipsanen-Nyman, Alizée Buff, Fernando R. Balestra, Andrés Domínguez-Calvo, Rosa M. Ríos, Pierre Gönczy, Coralie Busso, Benita Wolf
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::551357c05fddd737c0f162abac5dafe1
https://doi.org/10.7554/elife.62640.sa2
https://doi.org/10.7554/elife.62640.sa2
Autor:
Antonio Díaz-Quintana, Rosa M. Ríos, Irene Díaz-Moreno, Miguel A. De la Rosa, Alejandro Velázquez-Cruz, Katiuska González-Arzola, Francisco Rivero-Rodríguez, Adrián Velázquez-Campoy, Maria P. Gavilan
Publikováno v:
Redox Biology
Redox Biology, Vol 43, Iss, Pp 101967-(2021)
Zaguán. Repositorio Digital de la Universidad de Zaragoza
instname
idUS. Depósito de Investigación de la Universidad de Sevilla
Digital.CSIC. Repositorio Institucional del CSIC
Redox Biology, Vol 43, Iss, Pp 101967-(2021)
Zaguán. Repositorio Digital de la Universidad de Zaragoza
instname
idUS. Depósito de Investigación de la Universidad de Sevilla
Digital.CSIC. Repositorio Institucional del CSIC
17 pags., 9 figs., 1 tab.
Repair of injured DNA relies on nucleosome dismantling by histone chaperones and de-phosphorylation events carried out by Protein Phosphatase 2A (PP2A). Typical histone chaperones are the Acidic leucine-rich Nuclear Pho
Repair of injured DNA relies on nucleosome dismantling by histone chaperones and de-phosphorylation events carried out by Protein Phosphatase 2A (PP2A). Typical histone chaperones are the Acidic leucine-rich Nuclear Pho
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bff76eab6460b646f7099b403c216fe6
http://zaguan.unizar.es/record/112040
http://zaguan.unizar.es/record/112040
Autor:
Fernando R. Balestra, Marita Lipsanen-Nyman, Andrés Domínguez-Calvo, Alizée Buff, Tessa Averink, Rosa M. Ríos, Pablo Huertas, Benita Wolf, Pierre Gönczy, Coralie Busso
TRIM37 is an E3 ubiquitin ligase mutated in Mulibrey nanism, a disease characterized by impaired growth and increased tumorigenesis, whose cellular etiology is poorly understood. TRIM37 depletion from tissue culture cells results in supernumerary foc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0c0d5159e377a840c38f7415f270ba8e
https://doi.org/10.1101/2020.09.03.281097
https://doi.org/10.1101/2020.09.03.281097
Autor:
Mathieu Maurin, Gregory J. Pazour, Rosa M. Ríos, Andrés Ernesto Zucchetti, Mabel San Roman-Jouve, Michael W. Stuck, Jean-Marie Carpier, Claire Hivroz, Stéphanie Dogniaux, Laurence Bataille, Cosima T. Baldari
Publikováno v:
Nature Communications
Nature Communications, Nature Publishing Group, 2019, 10 (1), pp.2864. ⟨10.1038/s41467-019-10891-w⟩
Nature Communications, Vol 10, Iss 1, Pp 1-17 (2019)
Digital.CSIC. Repositorio Institucional del CSIC
instname
Nature Communications, Nature Publishing Group, 2019, 10 (1), pp.2864. ⟨10.1038/s41467-019-10891-w⟩
Nature Communications, Vol 10, Iss 1, Pp 1-17 (2019)
Digital.CSIC. Repositorio Institucional del CSIC
instname
The T cell immune synapse is a site of intense vesicular trafficking. Here we show that the golgin GMAP210, known to capture vesicles and organize membrane traffic at the Golgi, is involved in the vesicular transport of LAT to the immune synapse. Upo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d56c06a9f8d6cf2917eebdec7a44bd26
https://www.hal.inserm.fr/inserm-02446810/document
https://www.hal.inserm.fr/inserm-02446810/document
Autor:
Maria P. Gavilan, Michel Bornens, Rosa M. Ríos, Fernando R. Balestra, Francisco Arias, Pablo Gandolfo
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
instname
Here, we address the regulation of microtubule nucleation during interphase by genetically ablating one, or two, of three major mammalian γ‐TuRC‐binding factors namely pericentrin, CDK5Rap2, and AKAP450. Unexpectedly, we find that while all of t