Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Maria G. Füzesi-Levi"'
Autor:
Fanindra Kumar Deshmukh, Gili Ben-Nissan, Maya A. Olshina, Maria G. Füzesi-Levi, Caley Polkinghorn, Galina Arkind, Yegor Leushkin, Irit Fainer, Sarel J. Fleishman, Dan Tawfik, Michal Sharon
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-24 (2023)
Abstract Controlled degradation of proteins is necessary for ensuring their abundance and sustaining a healthy and accurately functioning proteome. One of the degradation routes involves the uncapped 20S proteasome, which cleaves proteins with a part
Externí odkaz:
https://doaj.org/article/efa8f7774d4c40b7b1bee774b5fa6164
Autor:
Shelly Rozen, Maria G. Füzesi-Levi, Gili Ben-Nissan, Limor Mizrachi, Alexandra Gabashvili, Yishai Levin, Shifra Ben-Dor, Miriam Eisenstein, Michal Sharon
Publikováno v:
Cell Reports, Vol 13, Iss 3, Pp 585-598 (2015)
The highly conserved COP9 signalosome (CSN) complex is a key regulator of all cullin-RING-ubiquitin ligases (CRLs), the largest family of E3 ubiquitin ligases. Until now, it was accepted that the CSN is composed of eight canonical components. Here, w
Externí odkaz:
https://doaj.org/article/dcacfbac55394c26a7dce4e1d4c69287
Autor:
Maria G. Füzesi-Levi, Gili Ben-Nissan, Dina Listov, Zvi Hayouka, Sarel Fleishman, Michal Sharon
Protein degradation is one of the essential mechanisms that enables reshaping of the proteome landscape in response to various stimuli. The largest E3 ubiquitin ligase family that targets proteins to degradation by catalyzing ubiquitnation is the cul
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::32f2058640537c76aa86c560e8761892
https://doi.org/10.1101/2022.07.18.500399
https://doi.org/10.1101/2022.07.18.500399
Autor:
Maria G. Füzesi-Levi, Tomer-Meir Salame, Michal Sharon, Matthias Peter, Gili Ben-Nissan, Yishai Levin, Gilgi Friedlander, Meital Kupervaser, Radoslav I. Enchev, Reinat Nevo
The cullin-RING ubiquitin E3 ligase (CRL) family consists of ~250 complexes that catalyze ubiquitylation of proteins to achieve cellular regulation. All CRLs are inhibited by the COP9 signalosome complex (CSN) through both enzymatic (deneddylation) a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c7c601849d7d078943b3365c3befc54
Autor:
Maria G. Füzesi-Levi, Shelly Rozen, Gili Ben-Nissan, Michal Sharon, Miriam Eisenstein, Limor Mizrachi, Alexandra Gabashvili, Shifra Ben-Dor, Yishai Levin
Publikováno v:
Cell Reports
Cell Reports, Vol 13, Iss 3, Pp 585-598 (2015)
Cell Reports, Vol 13, Iss 3, Pp 585-598 (2015)
The highly conserved COP9 signalosome (CSN) complex is a key regulator of all cullin-RING-ubiquitin ligases (CRLs), the largest family of E3 ubiquitin ligases. Until now it was accepted that the CSN is comprised of eight canonical components. Here, w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::72075e0558447887831be44dbe185f3e
https://doi.org/10.1016/j.celrep.2015.09.021
https://doi.org/10.1016/j.celrep.2015.09.021
Autor:
Elisabetta Bianchi, Gili Ben-Nissan, Yishai Levin, Maria G. Füzesi-Levi, Houjiang Zhou, Kathryn S. Lilley, Michael J. Deery, Michal Sharon
Publikováno v:
Molecular and Cellular Biology
The COP9 signalosome (CSN) is an evolutionarily conserved protein complex that participates in the regulation of the ubiquitin/26S proteasome pathway by controlling the function of cullin-RING-ubiquitin ligases. Impressive progress has been made in d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::513c289a0a52daa4fe789bb954af6060
Autor:
Gilgi Friedlander, Reinat Nevo, Radoslav I. Enchev, Tomer-Meir Salame, Yishai Levin, Irit Fainer, Maria G. Füzesi-Levi, Matthias Peter, Gili Ben-Nissan, Michal Sharon, Meital Kupervaser
Publikováno v:
Cell Death & Differentiation
Cell Death Differ
Cell Death Differ
The cullin-RING ubiquitin E3 ligase (CRL) family consists of ~250 complexes that catalyze ubiquitylation of proteins to achieve cellular regulation. All CRLs are inhibited by the COP9 signalosome complex (CSN) through both enzymatic (deneddylation) a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6cc5f6af0c0c5b514a6bfd2d2eaaef5d