Evidence map›Paper›PMID 24169447›Full record

ArticleScientific reports2013

Proteomic analysis of the SIRT6 interactome: novel links to genome maintenance and cellular stress signaling.

Federica Simeoni, Luisa Tasselli, Shinji Tanaka, Lidia Villanova, Mayumi Hayashi, Kazuishi Kubota, Fujio Isono, Benjamin A Garcia, Eriko Michishita-Kioi, Katrin F Chua

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.1field-weighted citation impact, top 14% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

22 citing papers in PubMed, 44 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. The many faces of SIRT6 in the retina and retinal pigment epithelium.Frontiers in cell and developmental biology · 2023
    Review
  6. Review
  7. Review
  8. Emerging Roles of SIRT3 in Cardiac Metabolism.Frontiers in cardiovascular medicine · 2022
    Review
  9. Review
  10. Article
  11. Article
  12. Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Sirtuins: guardians of mammalian healthspan.Trends in genetics : TIG · 2014
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 6 institutions in 3 countries.

Federica Simeoni1] Department of Medicine, Division of Endocrinology, Gerontology and Metabolism, School of Medicine, Stanford University, Stanford, California 94305, USA [2] Geriatric Research, Education, and Clinical Center, VA Palo Alto Health Care System, Palo Alto, California 94304, USA.
Luisa Tasselli
Shinji Tanaka
Lidia Villanova
Mayumi Hayashi
Kazuishi Kubota
Fujio Isono
Benjamin A Garcia
Eriko Michishita-Kioi
Katrin F Chua
Daiichi-Sankyo (Japan) · JPGeriatric Research Education and Clinical Center · USSapienza University of Rome · ITStanford University · USUniversity of Pennsylvania · USVA Palo Alto Health Care System · US

Funding

Molecular Mechanisms of Mammalian SIRT6 FunctionR01AG028867 · NIA · STANFORD UNIVERSITY · PI CHUA, KATRIN F · 2006 to 2010
$1.6M
NIA NIH HHS R01 AG028867
6 · The paper itself

Abstract

The chromatin regulatory factor SIRT6 plays pivotal roles in metabolism, tumor suppression, and aging biology. Despite the fundamental roles of SIRT6 in physiology and disease, only a handful of molecular and functional interactions of SIRT6 have been reported. Here, we characterize the SIRT6 interactome and identify 80+ novel SIRT6-interacting proteins. The discovery of these SIRT6-associations considerably expands knowledge of the SIRT6 interaction network, and suggests previously unknown functional interactions of SIRT6 in fundamental cellular processes. These include chromatin remodeling, mitotic chromosome segregation, protein homeostasis, and transcriptional elongation. Extended analysis of the SIRT6 interaction with G3BP1, a master stress response factor, uncovers an unexpected role and mechanism of SIRT6 in regulating stress granule assembly and cellular stress resistance.

Indexed as

Protein Interaction MapsAnimalsCarrier ProteinsCell Cycle ProteinsCell Line, TumorDNA HelicasesHEK293 CellsHeLa CellsHumansMicePoly-ADP-Ribose Binding ProteinsProtein BindingProteomicsRNA HelicasesRNA InterferenceRNA Recognition Motif ProteinsCAPRIN1 protein, humanCarrier ProteinsCell Cycle ProteinsDNA HelicasesG3BP1 protein, humanPoly-ADP-Ribose Binding ProteinsRNA HelicasesRNA Recognition Motif ProteinsRNA, Small InterferingSIRT6 protein, humanSirtuinsUbiquitin ThiolesteraseUSP10 protein, human

Identifiers

PMID24169447
PMCPMC3812651
OpenAlexW1989810319

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.