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Cullin 5-RING E3 ubiquitin ligases, new therapeutic targets?
Lamsoul, Isabelle; Uttenweiler-Joseph, Sandrine; Moog-Lutz, Christel; Lutz, Pierre G.
Afiliación
  • Lamsoul I; CNRS, IPBS (Institut de Pharmacologie et de Biologie Structurale), 205 route de Narbonne, BP 64182, F-31077 Toulouse, France; Université de Toulouse, UPS, IPBS, F-31077 Toulouse, France.
  • Uttenweiler-Joseph S; CNRS, IPBS (Institut de Pharmacologie et de Biologie Structurale), 205 route de Narbonne, BP 64182, F-31077 Toulouse, France; Université de Toulouse, UPS, IPBS, F-31077 Toulouse, France.
  • Moog-Lutz C; CNRS, IPBS (Institut de Pharmacologie et de Biologie Structurale), 205 route de Narbonne, BP 64182, F-31077 Toulouse, France; Université de Toulouse, UPS, IPBS, F-31077 Toulouse, France.
  • Lutz PG; CNRS, IPBS (Institut de Pharmacologie et de Biologie Structurale), 205 route de Narbonne, BP 64182, F-31077 Toulouse, France; Université de Toulouse, UPS, IPBS, F-31077 Toulouse, France. Electronic address: Pierre.Lutz@ipbs.fr.
Biochimie ; 122: 339-47, 2016 Mar.
Article en En | MEDLINE | ID: mdl-26253693
ABSTRACT
Ubiquitylation is a reversible post-translational modification of proteins that controls a myriad of functions and cellular processes. It occurs through the sequential action of three distinct enzymes. E3 ubiquitin ligases (E3s) play the role of conductors of the ubiquitylation pathway making them attractive therapeutic targets. This review is dedicated to the largest family of multimeric E3s, the Cullin-RING E3 (CRL) family and more specifically to cullin 5 based CRLs that remains poorly characterized.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Ubiquitina-Proteína Ligasas / Proteínas Cullin / Complejo de la Endopetidasa Proteasomal / Ubiquitinación Tipo de estudio: Prognostic_studies Límite: Humans Idioma: En Revista: Biochimie Año: 2016 Tipo del documento: Article País de afiliación: Francia

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Ubiquitina-Proteína Ligasas / Proteínas Cullin / Complejo de la Endopetidasa Proteasomal / Ubiquitinación Tipo de estudio: Prognostic_studies Límite: Humans Idioma: En Revista: Biochimie Año: 2016 Tipo del documento: Article País de afiliación: Francia
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