Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Julia M. Fraile"'
Autor:
Diana Campos-Iglesias, Julia M. Fraile, Gabriel Bretones, Alejandro A. Montero, Elena Bonzon-Kulichenko, Jesús Vázquez, Carlos López-Otín, José M. P. Freije
Publikováno v:
Cell Death and Disease, Vol 14, Iss 1, Pp 1-7 (2023)
Abstract The spindle assembly checkpoint (SAC) is an essential mechanism that ensures the accurate chromosome segregation during mitosis, thus preventing genomic instability. Deubiquitinases have emerged as key regulators of the SAC, mainly by determ
Externí odkaz:
https://doaj.org/article/494225a6be484efc921f890a1b484580
Publikováno v:
Frontiers in Oncology, Vol 1 (2011)
The oncogene addiction concept refers to the dependence of cancer cells on the function of the oncogenes responsible for their transformed phenotype, while the term non-oncogene addiction has been introduced to define the exacerbated necessity of the
Externí odkaz:
https://doaj.org/article/7440b7375b75412b8d2f09bb34f60948
Publikováno v:
Drug Design, Development and Therapy
Non-alcoholic steatohepatitis (NASH) is a progressive form of non-alcoholic fatty liver disease (NAFLD), characterized by chronic inflammation and accumulation of fat in liver tissue. Affecting estimated 35 million people globally, NASH is the most c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6108afd1cef96d763e7cebd31038918d
https://pubmed.ncbi.nlm.nih.gov/34675485
https://pubmed.ncbi.nlm.nih.gov/34675485
Publikováno v:
Oncotarget
Scopus
RUO. Repositorio Institucional de la Universidad de Oviedo
instname
Scopus
RUO. Repositorio Institucional de la Universidad de Oviedo
instname
// Julia M. Fraile 1 , Diana Campos-Iglesias 1 , Francisco Rodriguez 1 , Yaiza Espanol 1 and Jose M.P. Freije 1 1 Departamento de Bioquimica y Biologia Molecular, Facultad de Medicina, Instituto Universitario de Oncologia, Universidad de Oviedo, Ovie
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b4f76fdad1b688e1cf6fa470375af2a2
https://doi.org/10.18632/oncotarget.12769
https://doi.org/10.18632/oncotarget.12769
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1731
Proteases play key roles in the execution and regulation of most if not all biological functions, and alterations in their activity, expression, or location are associated with multiple pathological conditions, including cancer and aging. In this reg
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::8e568dd7b6decdaf3c28d6d604d2b3c8
https://pubmed.ncbi.nlm.nih.gov/29318560
https://pubmed.ncbi.nlm.nih.gov/29318560
Autor:
Aurora Astudillo, Steven P. Gygi, José I. Martín-Subero, Diana Campos-Iglesias, Carlos López-Otín, Roser Vilarrasa-Blasi, Francisco Rodríguez, Núria Verdaguer-Dot, José M.P. Freije, Julia M. Fraile, Joao A. Paulo, Miguel A. Prado
Publikováno v:
Scopus
RUO. Repositorio Institucional de la Universidad de Oviedo
instname
RUO. Repositorio Institucional de la Universidad de Oviedo
instname
Deubiquitinases are proteases with a wide functional diversity that profoundly impact multiple biological processes. Among them, the ubiquitin-specific protease 36 (USP36) has been implicated in the regulation of nucleolar activity. However, its func
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fe2bfe949f621009af74f6f5c9118496
http://hdl.handle.net/10651/47153
http://hdl.handle.net/10651/47153
Publikováno v:
Methods in Molecular Biology ISBN: 9781493975945
Proteases play key roles in the execution and regulation of most if not all biological functions, and alterations in their activity, expression, or location are associated with multiple pathological conditions, including cancer and aging. In this reg
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8e3923017100d59cc6019083d352a112
https://doi.org/10.1007/978-1-4939-7595-2_23
https://doi.org/10.1007/978-1-4939-7595-2_23
Autor:
Julia M. Fraile, Diana Campos-Iglesias, Eusebio Manchado, Thomas R. Webb, Carlos López-Otín, Amaia Lujambio, José M.P. Freije, Scott W. Lowe, Víctor Quesada
Publikováno v:
WOS:000404672500003
RUO. Repositorio Institucional de la Universidad de Oviedo
instname
RUO: Repositorio Institucional de la Universidad de Oviedo
Universidad de Oviedo (UNIOVI)
RUO. Repositorio Institucional de la Universidad de Oviedo
instname
RUO: Repositorio Institucional de la Universidad de Oviedo
Universidad de Oviedo (UNIOVI)
KRAS is the most frequently mutated oncogene in human cancer, but its therapeutic targeting remains challenging. Here, we report a synthetic lethal screen with a library of deubiquitinases and identify USP39, which encodes an essential splicing facto
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7eda6361ef99db38f84ec3e654ee81f2
http://hdl.handle.net/10651/44757
http://hdl.handle.net/10651/44757
Publikováno v:
Proteases in Physiology and Pathology ISBN: 9789811025129
Deubiquitinases (DUBs) are critical regulators of ubiquitin-mediated signaling pathways through their ability to cleave the isopeptide bond that links ubiquitin to target proteins. The human genome encodes at least 100 DUBs, grouped into six families
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4c0cef0ca22c340820ecfbc24f6c5272
https://doi.org/10.1007/978-981-10-2513-6_16
https://doi.org/10.1007/978-981-10-2513-6_16
Autor:
Julia M, Fraile, Eusebio, Manchado, Amaia, Lujambio, Víctor, Quesada, Diana, Campos-Iglesias, Thomas R, Webb, Scott W, Lowe, Carlos, López-Otín, José M P, Freije
Publikováno v:
The Journal of biological chemistry. 292(10)
KRAS is the most frequently mutated oncogene in human cancer, but its therapeutic targeting remains challenging. Here, we report a synthetic lethal screen with a library of deubiquitinases and identify USP39, which encodes an essential splicing facto
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::31994f624bfbe2f6d179f5a82ccf8421
https://pubmed.ncbi.nlm.nih.gov/28154181
https://pubmed.ncbi.nlm.nih.gov/28154181