Evidence map›Paper›PMID 16079181›Full record

ArticleMolecular biology of the cell2005

Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins.

Eriko Michishita, Jean Y Park, Jenna M Burneskis, J Carl Barrett, Izumi Horikawa

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 714 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
714citing papers in PubMed, 1 pooled it
28.1field-weighted citation impact, top 1% 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

714 citing papers in PubMed, 1 synthesis or guideline pooled it, 1,354 citations in OpenAlex.

  1. Pooled it
  2. Advances in sirtuin research in lung diseases (Review).International journal of molecular medicine · 2026
    Review
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  4. Tuning epigenetics to enhance cancer virotherapy.Acta pharmaceutica Sinica. B · 2026
    Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Facile Synthesis of H-L-Photo-Lysine and Its Genetic Incorporation Into Proteins.Chembiochem : a European journal of chemical biology · 2026
    Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. From Pharmacophore to Warhead: NADAngewandte Chemie (International ed. in English) · 2025
    Article
  18. Review
  19. Article
  20. Review

654 more citing papers are in PubMed but not listed here.

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

5 authors at 3 institutions in 1 country.

Eriko MichishitaLaboratory of Biosystems and Cancer, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Jean Y Park
Jenna M Burneskis
J Carl Barrett
Izumi Horikawa
Center for Cancer Research · USNational Cancer Institute · USNational Institutes of Health · US

Funding

Intramural NIH HHS
6 · The paper itself

Abstract

Sir2 is a NAD+-dependent protein deacetylase that extends lifespan in yeast and worms. This study examines seven human proteins homologous to Sir2 (SIRT1 through SIRT7) for cellular localization, expression profiles, protein deacetylation activity, and effects on human cell lifespan. We found that: 1) three nuclear SIRT proteins (SIRT1, SIRT6, and SIRT7) show different subnuclear localizations: SIRT6 and SIRT7 are associated with heterochromatic regions and nucleoli, respectively, where yeast Sir2 functions; 2) SIRT3, SIRT4, and SIRT5 are localized in mitochondria, an organelle that links aging and energy metabolism; 3) cellular p53 is a major in vivo substrate of SIRT1 deacetylase, but not the other six SIRT proteins; 4) SIRT1, but not the other two nuclear SIRT proteins, shows an in vitro deacetylase activity on histone H4 and p53 peptides; and 5) overexpression of any one of the seven SIRT proteins does not extend cellular replicative lifespan in normal human fibroblasts or prostate epithelial cells. This study supports the notion that multiple human SIRT proteins have evolutionarily conserved and nonconserved functions at different cellular locations and reveals that the lifespan of normal human cells, in contrast to that of lower eukaryotes, cannot be manipulated by increased expression of a single SIRT protein.

Indexed as

Cell LineCell NucleolusCellular SenescenceFibroblastsGreen Fluorescent ProteinsHeterochromatinHistonesHumansMitochondriaOrgan SpecificityRecombinant Fusion ProteinsSirtuinsSubstrate SpecificityTumor Suppressor Protein p53Green Fluorescent ProteinsHeterochromatinHistonesRecombinant Fusion ProteinsSirtuinsTumor Suppressor Protein p53

Identifiers

PMID16079181
PMCPMC1237069
OpenAlexW2106715610

What OpenQuestion holds

Textmetadata
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.