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(ADP-ribosyl)hydrolases: structure, function, and biology

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 a...

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Detalles Bibliográficos
Autores principales: Rack, Johannes Gregor Matthias, Palazzo, Luca, Ahel, Ivan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Cold Spring Harbor Laboratory Press 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7050489/
https://www.ncbi.nlm.nih.gov/pubmed/32029451
http://dx.doi.org/10.1101/gad.334631.119
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author Rack, Johannes Gregor Matthias
Palazzo, Luca
Ahel, Ivan
author_facet Rack, Johannes Gregor Matthias
Palazzo, Luca
Ahel, Ivan
author_sort Rack, Johannes Gregor Matthias
collection PubMed
description 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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spelling pubmed-70504892020-03-16 (ADP-ribosyl)hydrolases: structure, function, and biology Rack, Johannes Gregor Matthias Palazzo, Luca Ahel, Ivan Genes Dev Special Section: Review 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. Cold Spring Harbor Laboratory Press 2020-03-01 /pmc/articles/PMC7050489/ /pubmed/32029451 http://dx.doi.org/10.1101/gad.334631.119 Text en © 2020 Rack et al.; Published by Cold Spring Harbor Laboratory Press http://creativecommons.org/licenses/by/4.0/ This article, published in Genes & Development, is available under a Creative Commons License (Attribution 4.0 International), as described at http://creativecommons.org/licenses/by/4.0/.
spellingShingle Special Section: Review
Rack, Johannes Gregor Matthias
Palazzo, Luca
Ahel, Ivan
(ADP-ribosyl)hydrolases: structure, function, and biology
title (ADP-ribosyl)hydrolases: structure, function, and biology
title_full (ADP-ribosyl)hydrolases: structure, function, and biology
title_fullStr (ADP-ribosyl)hydrolases: structure, function, and biology
title_full_unstemmed (ADP-ribosyl)hydrolases: structure, function, and biology
title_short (ADP-ribosyl)hydrolases: structure, function, and biology
title_sort (adp-ribosyl)hydrolases: structure, function, and biology
topic Special Section: Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7050489/
https://www.ncbi.nlm.nih.gov/pubmed/32029451
http://dx.doi.org/10.1101/gad.334631.119
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