Skip to search form
Skip to main content
Skip to account menu
Semantic Scholar
Semantic Scholar's Logo
Search 222,933,251 papers from all fields of science
Search
Sign In
Create Free Account
Sirtuins
Known as:
Sirtuins [Chemical/Ingredient]
, Sir2-like Proteins
, Silent Mating Type Information Regulator 2 like Proteins
Expand
A homologous family of regulatory enzymes that are structurally related to the protein silent mating type information regulator 2 (Sir2) found in…
Expand
National Institutes of Health
Create Alert
Alert
Related topics
Related topics
8 relations
In Blood
Process of secretion
Silent Information Regulator Proteins, Saccharomyces cerevisiae
antagonists & inhibitors
Expand
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Review
2017
Review
2017
Sirtuins as modifiers of Parkinson's disease pathology
B. Tang
Journal of Neuroscience Research
2017
Corpus ID: 22473240
Parkinson's disease (PD) is the most common movement disorder associated with the elderly which, other than symptomatic therapies…
Expand
Review
2014
Review
2014
Systemic regulation of mammalian ageing and longevity by brain sirtuins
A. Satoh
,
S. Imai
Nature Communications
2014
Corpus ID: 22146333
Sirtuins have been implicated in the ageing process in a variety of organisms, but their role in mammalian ageing remains…
Expand
Highly Cited
2014
Highly Cited
2014
Overexpression of Mitochondrial Sirtuins Alters Glycolysis and Mitochondrial Function in HEK293 Cells
Michelle Barbi de Moura
,
R. Uppala
,
Yuxun Zhang
,
B. Van Houten
,
E. Goetzman
PLoS ONE
2014
Corpus ID: 18473218
SIRT3, SIRT4, and SIRT5 are mitochondrial deacylases that impact multiple facets of energy metabolism and mitochondrial function…
Expand
Review
2010
Review
2010
Sirtuins and their relevance to the kidney.
C. Hao
,
V. Haase
Journal of the American Society of Nephrology
2010
Corpus ID: 7491337
Sirtuins (silent information regulator 2 [Sir2] proteins) belong to an ancient family of evolutionary conserved nicotinamide…
Expand
Review
2010
Review
2010
Sirtuins: common targets in aging and in neurodegeneration.
R. M. de Oliveira
,
T. F. Pais
,
T. Outeiro
Current Drug Targets
2010
Corpus ID: 22043009
Aging has been a subject of interest since primordial times. More recently, it became clear that aging is the major known risk…
Expand
2009
2009
Sirtuins at the Breaking Point: SIRT6 in DNA Repair
D. Lombard
Aging
2009
Corpus ID: 17508648
Aging is the accumulation of unrepaired damage to cellular and organismal components over time. Damage to nuclear DNA likely…
Expand
Review
2009
Review
2009
Pharmaceutical strategies for activating sirtuins.
A. Sauve
Current pharmaceutical design
2009
Corpus ID: 30282565
The sirtuins are protein modifying enzymes widely distributed in all forms of life. The sirtuins are principally NAD(+)-dependent…
Expand
2009
2009
A fluorometric assay of SIRT1 deacetylation activity through quantification of nicotinamide adenine dinucleotide.
Yu Feng
,
Jiahui Wu
,
+5 authors
Dongxiang Liu
Analytical Biochemistry
2009
Corpus ID: 5340718
Highly Cited
2008
Highly Cited
2008
Mammalian sirtuin 1 is involved in the protective action of dietary saturated fat against alcoholic fatty liver in mice.
Min You
,
Q. Cao
,
Xiaomei Liang
,
Joanne M. Ajmo
,
G. Ness
Journal of NutriLife
2008
Corpus ID: 4458593
This study was undertaken to elucidate the mechanism underlying the protective effect of a high saturated fat (HSF) diet against…
Expand
Highly Cited
2006
Highly Cited
2006
The structural basis of sirtuin substrate affinity.
M. Cosgrove
,
K. Bever
,
J. Avalos
,
S. Muhammad
,
Xiangbin Zhang
,
C. Wolberger
Biochemistry
2006
Corpus ID: 42146833
Sirtuins comprise a family of enzymes that catalyze the deacetylation of acetyllysine side chains in a reaction that consumes NAD…
Expand
By clicking accept or continuing to use the site, you agree to the terms outlined in our
Privacy Policy
(opens in a new tab)
,
Terms of Service
(opens in a new tab)
, and
Dataset License
(opens in a new tab)
ACCEPT & CONTINUE