Evidence map›Paper›PMID 20559317›Full record

ReviewNature chemical biology2010

The chemical toolbox for monitoring protein fatty acylation and prenylation.

Rami N Hannoush, Jinglucy Sun

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature chemical biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
8.1field-weighted citation impact, top 2% 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

85 citing papers in PubMed, 163 citations in OpenAlex.

  1. Structural basis of GSDME pore formation and its regulation by S-palmitoylation.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Biochemistry · 2026
    Review
  3. Article
  4. Article
  5. Review
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  7. Article
  8. Article
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  11. Review
  12. Regulation of Ras Signaling by S-Nitrosylation.Antioxidants (Basel, Switzerland) · 2023
    Review
  13. Article
  14. Review
  15. Regulation of Cell Polarity by Posttranslational Protein Palmitoylation.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  16. Review
  17. Review
  18. Review
  19. Article
  20. Article

25 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

2 authors at 1 institution in 1 country.

Rami N HannoushDepartment of Protein Engineering, Genentech, Inc., South San Francisco, California, USA. hannoush.rami@gene.com
Jinglucy Sun
Gene Therapy Laboratory · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lipid modification of cellular proteins plays diverse roles in the regulation of such proteins' trafficking, signaling and behavior. Owing to a lack of robust detection technologies, the mechanisms by which lipids regulate proteins are poorly understood. Recently, various groups have developed innovative chemical probes in conjunction with bio-orthogonal chemistry for the detection of lipid-modified proteins in vitro and in vivo. These new methods enable further understanding of the mechanisms of protein lipidation and its function in physiology and disease. Here we present a comprehensive summary of these detection probes for monitoring fatty acylation and prenylation, and we provide a perspective on their current and future applications.

Indexed as

AcylationLipid MetabolismLipidsMolecular StructurePrenylationProteinsLipidsProteins

Identifiers

PMID20559317
OpenAlexW2059407885

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.