Evidence map›Paper›PMID 23585919›Full record

ArticleThe journal of physical chemistry letters2013

Sirtuin Deacetylation Mechanism and Catalytic Role of the Dynamic Cofactor Binding Loop.

Yawei Shi, Yanzi Zhou, Shenglong Wang, Yingkai Zhang

Abstract read
In one paragraph

Article in The journal of physical chemistry letters, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.0field-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

17 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. The Role of NADBiomedicines · 2023
    Review
  6. A Molecular Perspective on Sirtuin Activity.International journal of molecular sciences · 2020
    Review
  7. Review
  8. Evolved, Selective Erasers of Distinct Lysine Acylations.Angewandte Chemie (International ed. in English) · 2020
    Article
  9. Article
  10. Mechanism of activation for the sirtuin 6 protein deacylase.The Journal of biological chemistry · 2020
    Article
  11. Two symmetric arginine residues play distinct roles inProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
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

4 authors at 2 institutions in 2 countries.

Yawei ShiDepartment of Chemistry, New York University, New York, New York 10003.
Yanzi Zhou
Shenglong Wang
Yingkai Zhang
New York University · USNanjing University · CN

Funding

Computational Studies of Histone ModificationsR01GM079223 · NIGMS · NEW YORK UNIVERSITY · PI ZHANG, YINGKAI · 2007 to 2016
$2.4M
NIGMS NIH HHS R01 GM079223
6 · The paper itself

Abstract

Sirtuins constitute a novel family of protein deacetylases and play critical roles in epigenetics, cell death, and metabolism. In spite of numerous experimental studies, the key and most complicated stage of its NAD

Indexed as

ab initio QM/MM molecular dynamics simulationenzyme catalysisfree energy and umbrella samplingprotein deacetylationreaction mechanisms

Identifiers

PMID23585919
PMCPMC3621114
OpenAlexW2324233696

What OpenQuestion holds

Textmetadata
LicenceTDM
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.