Cited by 111Sirtuins and Resveratrol in MedicineHistone Deacetylase Inhibitors ResearchNuclear Structure and Function

The DOI matches its Crossref record; 44 of the 44 references it cites were found in a registry or an index.

The seven faces of SIRT7

Open access
Blank, Maximilian F., Grummt, Ingrid·2017·Transcription

Abstract

-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.

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 · 10.1080/21541264.2016.1276658

Cites

44 of 44 references verified0 citation errors · 0 not checkable

Statistics

Figures

Figure 1. The sirtuin family of NAD+-dependent deacetylases. The seven mammalian sirtuins (SIRT1–7) share a conserved catalytic core domain (HDAC domain) with varying N- and C-terminal sequences. They localize to different cellular compartments, use NAD+ as a co-factor and serve functions in multiple cellular processes.
Figure 1. The sirtuin family of NAD+-dependent deacetylases. The seven mammalian sirtuins (SIRT1–7) share a conserved catalytic core domain (HDAC domain) with varying N- and C-terminal sequences. They localize to different cellular compartments, use NAD+ as a co-factor and serve functions in multiple cellular processes.CC BY-NC-ND · PubMed Central
Figure 2. Reversible acetylation of PAF53 and U3–55k regulates pre-rRNA synthesis and processing. In normal growth conditions, SIRT7 keeps the Pol I-associated factor PAF53 hypoacetylated, which is required for rDNA transcription. Deacetylation of the U3–55k protein by SIRT7 facilitates the interaction of U3–55k with U3 snoRNA, thus promoting pre-rRNA cleavage. Nucleolar release of SIRT7 in response to environmental or metabolic stress enhances acetylation of PAF53 and U3–55k, which impairs Pol I transcription and pre-rRNA processing and attenuates ribosome biogenesis.
Figure 2. Reversible acetylation of PAF53 and U3–55k regulates pre-rRNA synthesis and processing. In normal growth conditions, SIRT7 keeps the Pol I-associated factor PAF53 hypoacetylated, which is required for rDNA transcription. Deacetylation of the U3–55k protein by SIRT7 facilitates the interaction of U3–55k with U3 snoRNA, thus promoting pre-rRNA cleavage. Nucleolar release of SIRT7 in response to environmental or metabolic stress enhances acetylation of PAF53 and U3–55k, which impairs Pol I transcription and pre-rRNA processing and attenuates ribosome biogenesis.CC BY-NC-ND · PubMed Central
Figure 3. The seven faces of SIRT7. The cartoon depicts the main pathways in which SIRT7 is involved. The proteins that are targeted by SIRT7 or mediate SIRT7 function are highlighted.
Figure 3. The seven faces of SIRT7. The cartoon depicts the main pathways in which SIRT7 is involved. The proteins that are targeted by SIRT7 or mediate SIRT7 function are highlighted.CC BY-NC-ND · 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

1 retracted

Show all 44 references

Research works printed but not linked: 1

  1. 10.1074/mcp.A111.01515 · DOI

Cited by

Sorted by citations

Metadata

Authors
Blank, M. F., & Grummt, I.
Affiliations
German Cancer Research Center (DE)
Corresponding author
Grummt, Ingrid
Venue
Transcription
Published
2017-01-23
Volume
8
Issue
2
Pages
67-74
ISSN
  • 2154-1264 (ISSN-L)
  • 2154-1272
OpenAlex
W2571520146
Cited by
111
References
44
Citations by year
2026: 5 · 2025: 8 · 2024: 9 · 2023: 14 · 2022: 21 · 2021: 12 · 2020: 15 · 2019: 13 · 2018: 9 · 2017: 5
FWCI
1.31
Type
journal article
Language
en
Open access
Locations
  • Transcription (publishedVersion, cc-by-nc-nd)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-nd)
  • PubMed Central (publishedVersion, cc-by-nc-nd)
  • PubMed (publishedVersion)
Topics
  • Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
Keywords
SIRT7, ribosome biogenesis, cell cycle checkpoints, metabolic homeostasis, stress tolerance, aging, carcinogenesis, cell proliferation, molecular targets
MeSH terms
Animals, Cell Transformation, Neoplastic, Energy Metabolism, Humans, Ribosomes, DNA-Directed RNA Polymerases, Stress, Physiological, Transcription, Genetic, Sirtuins, Genomic Instability, Cell Cycle Checkpoints

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