Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Rachid Boutoual"'
Autor:
Rachid Boutoual, Hyunsun Jo, Indra Heckenbach, Ritesh Tiwari, Herbert Kasler, Chad A. Lerner, Samah Shah, Birgit Schilling, Vincenzo Calvanese, Matthew J. Rardin, Morten Scheibye-Knudsen, Eric Verdin
Publikováno v:
Scientific Reports, Vol 12, Iss 1, Pp 1-14 (2022)
Abstract Post-translational modifications, such as lysine acetylation, regulate the activity of diverse proteins across many cellular compartments. Protein deacetylation in mitochondria is catalyzed by the enzymatic activity of the NAD+-dependent dea
Externí odkaz:
https://doaj.org/article/b028fc2b6f7e4beeb56bfa8dbba5cc9e
Autor:
Salvador Meseguer, Olga Boix, Carmen Navarro-González, Magda Villarroya, Rachid Boutoual, Sonia Emperador, Elena García-Arumí, Julio Montoya, M.-Eugenia Armengod
Publikováno v:
Scientific Reports, Vol 7, Iss 1, Pp 1-16 (2017)
Abstract Mitochondrial diseases due to mutations in the mitochondrial (mt) DNA are heterogeneous in clinical manifestations but usually include OXPHOS dysfunction. Mechanisms by which OXPHOS dysfunction contributes to the disease phenotype invoke, ap
Externí odkaz:
https://doaj.org/article/8373d498e1a446ffb1debbb300c1e96f
Autor:
Rachid Boutoual, Hyunsun Jo, Indra Heckenbach, Ritesh Tiwari, Herbert Kasler, Chad A. Lerner, Samah Shah, Birgit Schilling, Vincenzo Calvanese, Matthew J. Rardin, Morten Scheibye-Knudsen, Eric Verdin
Post-translational modifications, such as lysine acetylation, regulate the activity of diverse proteins across many cellular compartments. Protein deacetylation in mitochondria is catalyzed by the enzymatic activity of the NAD+-dependent deacetylase
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::40987a70136da768018c1476d0800456
https://doi.org/10.1101/2022.03.24.485634
https://doi.org/10.1101/2022.03.24.485634
Autor:
Salvador Meseguer, José Antonio Sánchez-Alcázar, Joaquin Panadero, Rachid Boutoual, M.-Eugenia Armengod, Carmen Navarro-González, Magda Villarroya
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
instname
Recent evidences highlight the importance of mitochondria-nucleus communication for the clinical phenotype of oxidative phosphorylation (OXPHOS) diseases. However, the participation of small non-coding RNAs (sncRNAs) in this communication has been po
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2eb22f8ef7604e24ae127598bddb383f
http://hdl.handle.net/10261/202477
http://hdl.handle.net/10261/202477
Autor:
Carmen Navarro-González, M-Eugenia Armengod, Rachid Boutoual, Magda Villarroya, Salvador Meseguer, Giacomo P. Comi, Joaquin Panadero
Publikováno v:
Biochimica et biophysica acta. Molecular basis of disease. 1864(9 Pt)
The pathomechanisms underlying oxidative phosphorylation (OXPHOS) diseases are not well-understood, but they involve maladaptive changes in mitochondria-nucleus communication. Many studies on the mitochondria-nucleus cross-talk triggered by mitochond
Autor:
Salvador Meseguer, Elena Martín-Hernández, Rachid Boutoual, Magda Villarroya, Mohammed Errami, Miguel Martín, M.-Eugenia Armengod, Marta Casado
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
Scientific Reports
Scientific Reports, Vol 8, Iss 1, Pp 1-18 (2018)
instname
Scientific Reports
Scientific Reports, Vol 8, Iss 1, Pp 1-18 (2018)
18 páginas 8 figuras. Supplementary information accompanies this paper at https://doi.org/10.1038/s41598-018-19587-5.
Human proteins MTO1 and GTPBP3 are thought to jointly catalyze the modification of the wobble uridine in mitochondrial tRNAs.
Human proteins MTO1 and GTPBP3 are thought to jointly catalyze the modification of the wobble uridine in mitochondrial tRNAs.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b6fd11408dcd33c6fae23c0ee454c07
http://hdl.handle.net/10261/159468
http://hdl.handle.net/10261/159468
Autor:
Olga Boix, Salvador Meseguer, Julio Montoya, Sonia Emperador, Magda Villarroya, Rachid Boutoual, Elena García-Arumí, Carmen Navarro-González, M.-Eugenia Armengod
Publikováno v:
Scientific Reports
r-CIPF: Repositorio Institucional Producción Científica del Centro de Investigación Principe Felipe (CIPF)
Centro de Investigación Principe Felipe (CIPF)
Zaguán. Repositorio Digital de la Universidad de Zaragoza
instname
Scientific Reports, Vol 7, Iss 1, Pp 1-16 (2017)
r-CIPF. Repositorio Institucional Producción Científica del Centro de Investigación Principe Felipe (CIPF)
r-CIPF: Repositorio Institucional Producción Científica del Centro de Investigación Principe Felipe (CIPF)
Centro de Investigación Principe Felipe (CIPF)
Zaguán. Repositorio Digital de la Universidad de Zaragoza
instname
Scientific Reports, Vol 7, Iss 1, Pp 1-16 (2017)
r-CIPF. Repositorio Institucional Producción Científica del Centro de Investigación Principe Felipe (CIPF)
Mitochondrial diseases due to mutations in the mitochondrial (mt) DNA are heterogeneous in clinical manifestations but usually include OXPHOS dysfunction. Mechanisms by which OXPHOS dysfunction contributes to the disease phenotype invoke, apart from
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b9c8791bd0994c33967b643c74d2ff69
https://fundanet.cipf.es/Publicaciones/ProdCientif/PublicacionFrw.aspx?id=1316
https://fundanet.cipf.es/Publicaciones/ProdCientif/PublicacionFrw.aspx?id=1316