Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Laura Merino-Cacho"'
Autor:
Orhi Barroso-Gomila, Laura Merino-Cacho, Veronica Muratore, Coralia Perez, Vincenzo Taibi, Elena Maspero, Mikel Azkargorta, Ibon Iloro, Fredrik Trulsson, Alfred C. O. Vertegaal, Ugo Mayor, Felix Elortza, Simona Polo, Rosa Barrio, James D. Sutherland
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-19 (2023)
Abstract Hundreds of E3 ligases play a critical role in recognizing specific substrates for modification by ubiquitin (Ub). Separating genuine targets of E3s from E3-interactors remains a challenge. We present BioE3, a powerful approach for matching
Externí odkaz:
https://doaj.org/article/4ccb7e7077984547931c1b4504e71284
Autor:
Orhi Barroso-Gomila, Fredrik Trulsson, Veronica Muratore, Iñigo Canosa, Laura Merino-Cacho, Ana Rosa Cortazar, Coralia Pérez, Mikel Azkargorta, Ibon Iloro, Arkaitz Carracedo, Ana M. Aransay, Felix Elortza, Ugo Mayor, Alfred C. O. Vertegaal, Rosa Barrio, James D. Sutherland
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-19 (2021)
Several proteomic approaches allow the analysis of covalent protein SUMOylation, but it remains challenging to systematically study the consequences of a substrate being modified. Here, the authors combine proximity biotinylation and protein-fragment
Externí odkaz:
https://doaj.org/article/a373110170724930bd012a7ad3fa350e
Autor:
Iñigo Canosa, James D. Sutherland, Ugo Mayor, Rosa Barrio, Alfred C.O. Vertegaal, Ibon Iloro, Ana R. Cortazar, Fredrik Trulsson, Coralia Pérez, Laura Merino-Cacho, Arkaitz Carracedo, Veronica Muratore, Orhi Barroso-Gomila, Ana M. Aransay, Mikel Azkargorta, Felix Elortza
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-19 (2021)
Nature Communications, 12(1). NATURE PORTFOLIO
Nature Communications
Addi. Archivo Digital para la Docencia y la Investigación
instname
bioRxiv
Nature Communications, 12(1). NATURE PORTFOLIO
Nature Communications
Addi. Archivo Digital para la Docencia y la Investigación
instname
bioRxiv
The fast dynamics and reversibility of posttranslational modifications by the ubiquitin family pose significant challenges for research. Here we present SUMO-ID, a technology that merges proximity biotinylation by TurboID and protein-fragment complem