Reference health
Negative Control of p53 by Sir2α Promotes Cell Survival under Stress
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1 of 47 checkable references need attention · checked 2026-07-23
At the dated check, the references listed below either did not resolve in Crossref or DataCite, or carried a retraction notice. Each one is shown with the registry record that put it there.
3 without a DOI — not checked. A reference deposited without a DOI is never matched by title or guessed at; it stays outside the checked set, and this line discloses that.
References needing attention
does not resolve to a known work10.1042/0264-6021:3470543
The 46 checked references that resolve
resolves10.1093/emboj/19.18.4967
p53 transcriptional activity is essential for p53‐dependent apoptosis following DNA damage
resolves10.1126/science.285.5436.2122
Impaired Fas Response and Autoimmunity in
<i>Pten</i>
<sup>+/−</sup>
Mice
resolves10.1101/gad.14.16.2015
PML is induced by oncogenic<i>ras</i>and promotes premature senescence
resolves10.1006/bbrc.1999.0897
Characterization of Five Human cDNAs with Homology to the Yeast SIR2 Gene: Sir2-like Proteins (Sirtuins) Metabolize NAD and May Have Protein ADP-Ribosyltransferase Activity
resolves10.1006/bbrc.2000.3000
Phylogenetic Classification of Prokaryotic and Eukaryotic Sir2-like Proteins
resolves10.1016/S0092-8674(00)80521-8
Activation of p53 Sequence-Specific DNA Binding by Acetylation of the p53 C-Terminal Domain
resolves10.1016/S1097-2765(00)80178-1
A Novel Human SRB/MED-Containing Cofactor Complex, SMCC, Involved in Transcription Regulation
resolves10.1038/35001622
Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
resolves10.1093/emboj/20.6.1331
p300/CBP‐mediated p53 acetylation is commonly induced by p53‐activating agents and inhibited by MDM2
resolves10.1038/79152
A transactivation-deficient mouse model provides insights into Trp53 regulation and function
resolves10.1073/pnas.110148297
The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases
resolves10.1126/science.289.5487.2126
Requirement of NAD and
<i>SIR2</i>
for Life-Span Extension by Calorie Restriction in
<i>Saccharomyces cerevisiae</i>
resolves10.1038/nm0796-804
A functionally inactive p53 protein interatocarcinoma cells is activated by either DNA damage or cellular differentiation
resolves10.1101/gad.886901
ATM-dependent phosphorylation of Mdm2 on serine 395: role in p53 activation by DNA damage
resolves10.1038/46311
The p66shc adaptor protein controls oxidative stress response and life span in mammals
resolves10.1128/MCB.20.24.9391-9398.2000
Multiple Lysine Mutations in the C-Terminal Domain of p53 Interfere with MDM2-Dependent Protein Degradation and Ubiquitination
resolves10.1128/MCB.20.22.8458-8467.2000
Multiple C-Terminal Lysine Residues Target p53 for Ubiquitin-Proteasome-Mediated Degradation
resolves10.1016/S0092-8674(00)80416-X
DNA Damage-Induced Phosphorylation of p53 Alleviates Inhibition by MDM2
resolves10.1073/pnas.011506198
The Sir2 protein family: A novel deacetylase for gene silencing and more
resolves10.1073/pnas.97.12.6658
A phylogenetically conserved NAD
<sup>+</sup>
-dependent protein deacetylase activity in the Sir2 protein family
resolves10.1073/pnas.250422697
Silent information regulator 2 family of NAD- dependent histone/protein deacetylases generates a unique product, 1-
<i>O-</i>
acetyl-ADP-ribose
resolves10.1073/pnas.98.2.415
Coupling of histone deacetylation to NAD breakdown by the yeast silencing protein Sir2: Evidence for acetyl transfer from substrate to an NAD breakdown product
resolves10.1093/emboj/16.19.6018
ATM‐dependent telomere loss in aging human diploid fibroblasts and DNA damage lead to the post‐translational activation of p53 protein involving poly(ADP‐ribose) polymerase
resolves10.1002/bies.950170510
Trichostatin A and trapoxin: Novel chemical probes for the role of histone acetylation in chromatin structure and function
resolves10.1016/S1097-2765(00)80320-2
Activation of p53 or Loss of the Cockayne Syndrome Group B Repair Protein Causes Metaphase Fragility of Human U1, U2, and 5S Genes
The 3 references without a DOI — listed, not checked
no DOI — not checkedSignaling to p53
no DOI — not checkedSuberoylanilide hydroxamic acid, an inhibitor of histone deacetylase suppresses the growth of prostate cancer cells in vitro and in vivo
no DOI — not checkedInhibitors of histone deacetylase are potentially effective anticancer agents
What this badge says. CiteStamped means the CHECKABLE references of this
work were clean at the dated check: each resolved to a known work in a public registry, and none
carried a retraction notice at that time. It says nothing about the quality, findings,
or importance of the work itself, and nothing about references deposited without a DOI.
checked 2026-07-23 — re-checked daily as this page is visited; titles and statuses come from Crossref and DataCite and are not part of the signed record
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