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Nicotinamide adenine dinucleotide, a metabolic regulator of transcription, longevity and disease
scientific journal article
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scholarly article
1 reference
stated in
PubMed
PubMed ID
12648681
retrieved
3 February 2017
review article
1 reference
stated in
Europe PubMed Central
title
Nicotinamide adenine dinucleotide, a metabolic regulator of transcription, longevity and disease
(English)
1 reference
stated in
PubMed
PubMed ID
12648681
retrieved
3 February 2017
main subject
NAD salvage
1 reference
stated in
Gene Ontology release 2020-05-02
Gene Ontology ID
GO:0034355
adenine
0 references
niacinamide
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based on heuristic
inferred from title
author name string
Su-Ju Lin
series ordinal
1
1 reference
stated in
PubMed
PubMed ID
12648681
retrieved
3 February 2017
Leonard Guarente
series ordinal
2
1 reference
stated in
PubMed
PubMed ID
12648681
retrieved
3 February 2017
publication date
1 April 2003
1 reference
stated in
PubMed
PubMed ID
12648681
retrieved
3 February 2017
published in
Current Opinion in Cell Biology
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stated in
PubMed
PubMed ID
12648681
retrieved
3 February 2017
volume
15
1 reference
stated in
PubMed
PubMed ID
12648681
retrieved
3 February 2017
page(s)
241–246
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stated in
PubMed
PubMed ID
12648681
retrieved
3 February 2017
issue
2
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stated in
PubMed
PubMed ID
12648681
retrieved
3 February 2017
cites work
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Requirement of NAD and SIR2 for life-span extension by calorie restriction in Saccharomyces cerevisiae
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The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms
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Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans
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Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
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The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases
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Energy coupling through molecular discrimination: nicotinate phosphoribosyltransferase.
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Manipulation of a nuclear NAD+ salvage pathway delays aging without altering steady-state NAD+ levels
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Aerobic and anaerobic NAD+ metabolism in Saccharomyces cerevisiae
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Regulation of clock and NPAS2 DNA binding by the redox state of NAD cofactors
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hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase
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Negative control of p53 by Sir2alpha promotes cell survival under stress
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Stoichiometry and compartmentation of NADH metabolism inSaccharomyces cerevisiae
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Intracellular compartmentation of pyruvate in primary cultures of cortical neurons as detected by (13)C NMR spectroscopy with multiple (13)C labels
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In vivo role of NAD(P)H:quinone oxidoreductase 1 (NQO1) in the regulation of intracellular redox state and accumulation of abdominal adipose tissue
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Pyruvate improves redox status and decreases indicators of hepatic apoptosis during hemorrhagic shock in swine
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Mouse lacking NAD+-linked glycerol phosphate dehydrogenase has normal pancreatic beta cell function but abnormal metabolite pattern in skeletal muscle
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Role of NAD in regulating the adhE gene of Escherichia coli
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7 January 2021
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Levels of nicotinamide adenine dinucleotide and reduced nicotinamide adenine dinucleotide in facultative bacteria and the effect of oxygen
1 reference
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Crossref
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7 January 2021
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Enhanced gluconeogenesis and increased energy storage as hallmarks of aging in Saccharomyces cerevisiae
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7 January 2021
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Calorie restriction extends Saccharomyces cerevisiae lifespan by increasing respiration
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7 January 2021
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p53 mutant mice that display early ageing-associated phenotypes
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Biomarkers of caloric restriction may predict longevity in humans
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Transcriptional regulation of the Saccharomyces cerevisiae DAL5 gene family and identification of the high affinity nicotinic acid permease TNA1 (YGR260w).
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Structure of human nicotinamide/nicotinic acid mononucleotide adenylyltransferase. Basis for the dual substrate specificity and activation of the oncolytic agent tiazofurin
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https://api.crossref.org/works/10.1016%2FS0955-0674%2803%2900006-1
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Identifiers
DOI
10.1016/S0955-0674(03)00006-1
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1580176
Fatcat ID
release_ytjq32slgrafrig2wptwhnvbqe
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Fatcat
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https://api.fatcat.wiki/v0/release/ytjq32slgrafrig2wptwhnvbqe
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based on heuristic
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OpenCitations bibliographic resource ID
1580176
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1580176
PubMed ID
12648681
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1580176
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