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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...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Cold Spring Harbor Laboratory Press
2020
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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. |
format | Online Article Text |
id | pubmed-7050489 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Cold Spring Harbor Laboratory Press |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT rackjohannesgregormatthias adpribosylhydrolasesstructurefunctionandbiology AT palazzoluca adpribosylhydrolasesstructurefunctionandbiology AT ahelivan adpribosylhydrolasesstructurefunctionandbiology |