Evidence map›Paper›PMID 29861273›Full record

ReviewCell chemical biology2018

Protein Lipidation in Cell Signaling and Diseases: Function, Regulation, and Therapeutic Opportunities.

Baoen Chen, Yang Sun, Jixiao Niu, Gopala K Jarugumilli, Xu Wu

Open access · bronzeAbstract readReview
In one paragraph

Review in Cell chemical biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 144 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
144citing papers in PubMed, 1 pooled it
10.6field-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

144 citing papers in PubMed, 1 synthesis or guideline pooled it, 252 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Article
  5. Article
  6. Subcellular localization as a driver of protein function.Nature reviews. Molecular cell biology · 2026
    Review
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Crosstalk between protein lipidation and ubiquitination in tumor biology.Apoptosis : an international journal on programmed cell death · 2026
    Review
  16. Review
  17. Review
  18. Article
  19. Review
  20. Article

84 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 2 institutions in 1 country.

Baoen ChenCutaneous Biology Research Center, Massachusetts General Hospital, Harvard Medical School, 149, 13th St., Charlestown, MA 02129, USA.
Yang SunCutaneous Biology Research Center, Massachusetts General Hospital, Harvard Medical School, 149, 13th St., Charlestown, MA 02129, USA.
Jixiao NiuCutaneous Biology Research Center, Massachusetts General Hospital, Harvard Medical School, 149, 13th St., Charlestown, MA 02129, USA.
Gopala K JarugumilliCutaneous Biology Research Center, Massachusetts General Hospital, Harvard Medical School, 149, 13th St., Charlestown, MA 02129, USA.
Xu WuCutaneous Biology Research Center, Massachusetts General Hospital, Harvard Medical School, 149, 13th St., Charlestown, MA 02129, USA. Electronic address: xwu@cbrc2.mgh.harvard.edu.
Massachusetts General Hospital · USHarvard University · US

Funding

Chemical approach to study autopalmitoylation of transcription factorsR01DK107651 · NIDDK · MASSACHUSETTS GENERAL HOSPITAL · PI LUO, XUELIAN, WU, XU · 2016 to 2020
$1.9M
Metabolic regulation of cellular junction proteinsR01CA181537 · NCI · MASSACHUSETTS GENERAL HOSPITAL · PI WU, XU · 2014 to 2018
$1.8M
NCI NIH HHS R01 CA181537NIDDK NIH HHS R01 DK107651
6 · The paper itself

Abstract

Protein lipidation is an important co- or posttranslational modification in which lipid moieties are covalently attached to proteins. Lipidation markedly increases the hydrophobicity of proteins, resulting in changes to their conformation, stability, membrane association, localization, trafficking, and binding affinity to their co-factors. Various lipids and lipid metabolites serve as protein lipidation moieties. The intracellular concentrations of these lipids and their derivatives are tightly regulated by cellular metabolism. Therefore, protein lipidation links the output of cellular metabolism to the regulation of protein function. Importantly, deregulation of protein lipidation has been linked to various diseases, including neurological disorders, metabolic diseases, and cancers. In this review, we highlight recent progress in our understanding of protein lipidation, in particular, S-palmitoylation and lysine fatty acylation, and we describe the importance of these modifications for protein regulation, cell signaling, and diseases. We further highlight opportunities and new strategies for targeting protein lipidation for therapeutic applications.

Indexed as

Lipid MetabolismSignal TransductionHumansLipidsNeoplasmsProteinsLipidsProteinsbioorthogonal chemical reporterscancerdrug discoveryfatty acylationinfectious diseasespalmitoylationprotein lipidationsignal transduction

Identifiers

PMID29861273
PMCPMC6054547
OpenAlexW2806826548

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.