CoChat
Sign Up
Cited by 200Sirtuins and Resveratrol in MedicineBiochemical and Molecular ResearchAutophagy in Disease and Therapy

The DOI matches its Crossref record; 69 of the 69 references it cites were found in a registry or an index.

The role of sirtuins in cellular homeostasis

Open access
Kupis, Wioleta, Pałyga, Jan, Tomal, Ewa, Niewiadomska, Ewa·2016·Journal of Physiology and Biochemistry
DOI 10.1007/s13105-016-0492-6PMC PMC4992043
Open this paper in CoChat — free accountOpen PDF

Abstract

Sirtuins are evolutionarily conserved nicotinamide adenine dinucleotide (NAD(+))-dependent lysine deacylases or ADP-ribosyltransferases. These cellular enzymes are metabolic sensors sensitive to NAD(+) levels that maintain physiological homeostasis in the animal and plant cells.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1007/s13105-016-0492-6

Cites

69 of 69 references verified0 citation errors · 0 not checkable

Statistics

Figures

Fig. 1 Deacetylation of acetylated proteins by sirtuins and the conversion of resulting nicotinamide into NAD+. NAM nicotinamide, NMN nicotinamide mononucleotide. The enzymes involved are boxed: NAMPT nicotinamide phosphoribosyltransferase, NMNAT nicotinamide mononucleotide adenylyltransferase
Fig. 1 Deacetylation of acetylated proteins by sirtuins and the conversion of resulting nicotinamide into NAD+. NAM nicotinamide, NMN nicotinamide mononucleotide. The enzymes involved are boxed: NAMPT nicotinamide phosphoribosyltransferase, NMNAT nicotinamide mononucleotide adenylyltransferaseCC BY · PubMed Central
Fig. 2 Deacylation reaction performed by sirtuins; 2′-O-succinyl-ADP-ribose is shown as the product of deacylation reaction catalyzed by SIRT5. The long-chain fatty acid moieties can be removed by SIRT2 or SIRT6
Fig. 2 Deacylation reaction performed by sirtuins; 2′-O-succinyl-ADP-ribose is shown as the product of deacylation reaction catalyzed by SIRT5. The long-chain fatty acid moieties can be removed by SIRT2 or SIRT6CC BY · PubMed Central
Fig. 3 ADP-ribosylation conducted by SIRT4 and SIRT6. Nu nucleophilic group of the amino acid side chain, R/D/E Arg/Asp/Glu; the letter R in the NAD+ and ADP-ribosylated protein denotes ADP moiety
Fig. 3 ADP-ribosylation conducted by SIRT4 and SIRT6. Nu nucleophilic group of the amino acid side chain, R/D/E Arg/Asp/Glu; the letter R in the NAD+ and ADP-ribosylated protein denotes ADP moietyCC BY · PubMed Central

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Show all 69 references

Cited by

Sorted by citations

See all 200

Related

Metadata

Authors
Kupis, W., Pałyga, J., Tomal, E., & Niewiadomska, E.
Affiliations
  • Jan Kochanowski University (PL)
  • Franciszek Górski Institute of Plant Physiology (PL)
Corresponding author
Pałyga, Jan
ORCID
Venue
Journal of Physiology and Biochemistry
Publisher
Springer Science and Business Media LLC
Published
2016-05-06
Volume
72
Issue
3
Pages
371-380
ISSN
  • 1138-7548 (ISSN-L)
  • 1877-8755
DOI
10.1007/s13105-016-0492-6
PMC
PMC4992043
OpenAlex
W2345900051
Cited by
200
References
69
Citations by year
2026: 13 · 2025: 16 · 2024: 20 · 2023: 19 · 2022: 27 · 2021: 35 · 2020: 28 · 2019: 11 · 2018: 11 · 2017: 14 · 2016: 6
FWCI
1.41
Type
journal article
Language
en
Open access
Licence
Locations
  • Journal of Physiology and Biochemistry (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
Topics
  • Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Keywords
sirtuins, NAD+-dependent deacylases, ADP-ribosyltransferase, cellular homeostasis, metabolic sensing, NAD levels, plant cells, animal cells
MeSH terms
Acetylation, Animals, Enzyme Activation, Enzyme Inhibitors, Homeostasis, Humans, Isoenzymes, Models, Biological, NAD, Plant Proteins, Species Specificity, Substrate Specificity, Conserved Sequence, Catalytic Domain, Protein Transport, Sirtuins

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review