Evidence map›Paper›PMID 26790532›Full record

ReviewNature reviews. Molecular cell biology2016

Protein prenylation: unique fats make their mark on biology.

Mei Wang, Patrick J Casey

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature reviews. Molecular cell biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 316 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
316citing papers in PubMed, 1 pooled it
25.2field-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

316 citing papers in PubMed, 1 synthesis or guideline pooled it, 535 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Review
  10. Review
  11. Prelamin A in anArteriosclerosis, thrombosis, and vascular biology · 2026
    Article
  12. Article
  13. Article
  14. Host prenylation promotes membrane association of theMicrobiology (Reading, England) · 2026
    Article
  15. Article
  16. Sortase A-Mediated Farnesylation of Cdc42ACS synthetic biology · 2026
    Article
  17. Article
  18. Article
  19. Review
  20. Renaissance of farnesyltransferase inhibitors in cancer.Journal of translational medicine · 2026
    Review

256 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 2 institutions in 2 countries.

Mei WangProgram in Cancer and Stem Cell Biology, Duke-NUS Medical School, Singapore 169857.
Patrick J CaseyProgram in Cancer and Stem Cell Biology, Duke-NUS Medical School, Singapore 169857.
Duke Medical Center · USDuke-NUS Medical School · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The modification of eukaryotic proteins by isoprenoid lipids, which is known as prenylation, controls the localization and activity of a range of proteins that have crucial functions in biological regulation. The roles of prenylated proteins in cells are well conserved across species, underscoring the biological and evolutionary importance of this lipid modification pathway. Genetic suppression and pharmacological inhibition of the protein prenylation machinery have provided insights into several cellular processes and into the aetiology of diseases in which prenylation is involved. The functional dependence of prenylation substrates, such as RAS proteins, on this modification and the therapeutic potential of targeting the prenylation process in pathological conditions accentuate the need to fully understand this form of post-translational modification.

Indexed as

Protein PrenylationProtein Processing, Post-TranslationalAgingAlkyl and Aryl TransferasesAnimalsAntineoplastic AgentsCell Transformation, NeoplasticEndopeptidasesEnzyme InhibitorsHumansHydroxymethylglutaryl-CoA Reductase InhibitorsNeoplasmsProtein Transportras ProteinsTerpenesAlkyl and Aryl TransferasesAntineoplastic AgentsEndopeptidasesEnzyme Inhibitorsgeranylgeranyltransferase type-IHydroxymethylglutaryl-CoA Reductase Inhibitorsp21(ras) farnesyl-protein transferaseras ProteinsRCE1 protein, humanTerpenes

Identifiers

PMID26790532
OpenAlexW2272329318

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.