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(ADP-ribosyl)hydrolases: structure, function, and biology.
Rack, Johannes Gregor Matthias; Palazzo, Luca; Ahel, Ivan.
Afiliación
  • Rack JGM; Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, United Kingdom.
  • Palazzo L; Institute for the Experimental Endocrinology and Oncology, National Research Council of Italy, 80145 Naples, Italy.
  • Ahel I; Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, United Kingdom.
Genes Dev ; 34(5-6): 263-284, 2020 03 01.
Article en En | MEDLINE | ID: mdl-32029451
ABSTRACT
ADP-ribosylation is an intricate and versatile posttranslational modification involved in the regulation of a vast variety of cellular processes in all kingdoms of life. Its complexity derives from the varied range of different chemical linkages, including to several amino acid side chains as well as nucleic acids termini and bases, it can adopt. In this review, we provide an overview of the different families of (ADP-ribosyl)hydrolases. We discuss their molecular functions, physiological roles, and influence on human health and disease. Together, the accumulated data support the increasingly compelling view that (ADP-ribosyl)hydrolases are a vital element within ADP-ribosyl signaling pathways and they hold the potential for novel therapeutic approaches as well as a deeper understanding of ADP-ribosylation as a whole.
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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Adenosina Difosfato / ADP-Ribosilación / Hidrolasas Límite: Humans Idioma: En Revista: Genes Dev Asunto de la revista: BIOLOGIA MOLECULAR Año: 2020 Tipo del documento: Article País de afiliación: Reino Unido

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Adenosina Difosfato / ADP-Ribosilación / Hidrolasas Límite: Humans Idioma: En Revista: Genes Dev Asunto de la revista: BIOLOGIA MOLECULAR Año: 2020 Tipo del documento: Article País de afiliación: Reino Unido