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The seven faces of SIRT7

SIRT7, a member of the sirtuin family of NAD(+)-dependent protein deacetylases, is a key mediator of many cellular activities. SIRT7 expression is linked to cell proliferation and oncogenic activity, connecting SIRT7-dependent regulation of ribosome biogenesis with checkpoints controlling cell cycle...

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Detalles Bibliográficos
Autores principales: Blank, Maximilian F., Grummt, Ingrid
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Taylor & Francis 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5423475/
https://www.ncbi.nlm.nih.gov/pubmed/28067587
http://dx.doi.org/10.1080/21541264.2016.1276658
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author Blank, Maximilian F.
Grummt, Ingrid
author_facet Blank, Maximilian F.
Grummt, Ingrid
author_sort Blank, Maximilian F.
collection PubMed
description SIRT7, a member of the sirtuin family of NAD(+)-dependent protein deacetylases, is a key mediator of many cellular activities. SIRT7 expression is linked to cell proliferation and oncogenic activity, connecting SIRT7-dependent regulation of ribosome biogenesis with checkpoints controlling cell cycle progression, metabolic homeostasis, stress resistance, aging and tumorigenesis. Despite this important functional link, the enzymatic activity, the molecular targets and physiological functions of SIRT7 are poorly defined. Here, we review recent progress in SIRT7 research and elaborate the main pathways in which SIRT7 participates.
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spelling pubmed-54234752017-05-17 The seven faces of SIRT7 Blank, Maximilian F. Grummt, Ingrid Transcription Review SIRT7, a member of the sirtuin family of NAD(+)-dependent protein deacetylases, is a key mediator of many cellular activities. SIRT7 expression is linked to cell proliferation and oncogenic activity, connecting SIRT7-dependent regulation of ribosome biogenesis with checkpoints controlling cell cycle progression, metabolic homeostasis, stress resistance, aging and tumorigenesis. Despite this important functional link, the enzymatic activity, the molecular targets and physiological functions of SIRT7 are poorly defined. Here, we review recent progress in SIRT7 research and elaborate the main pathways in which SIRT7 participates. Taylor & Francis 2017-01-09 /pmc/articles/PMC5423475/ /pubmed/28067587 http://dx.doi.org/10.1080/21541264.2016.1276658 Text en © 2017 The Author(s). Published with license by Taylor & Francis http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivatives License (http://creativecommons.org/licenses/by-nc-nd/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited, and is not altered, transformed, or built upon in any way.
spellingShingle Review
Blank, Maximilian F.
Grummt, Ingrid
The seven faces of SIRT7
title The seven faces of SIRT7
title_full The seven faces of SIRT7
title_fullStr The seven faces of SIRT7
title_full_unstemmed The seven faces of SIRT7
title_short The seven faces of SIRT7
title_sort seven faces of sirt7
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5423475/
https://www.ncbi.nlm.nih.gov/pubmed/28067587
http://dx.doi.org/10.1080/21541264.2016.1276658
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