Evidence map›Paper›PMID 27233110›Full record

ReviewProgress in lipid research2016

Fatty acylation of proteins: The long and the short of it.

Marilyn D Resh

Open access · greenAbstract readReview
In one paragraph

Review in Progress in lipid research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 159 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
159citing papers in PubMed, 1 pooled it
13.8field-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

159 citing papers in PubMed, 1 synthesis or guideline pooled it, 274 citations in OpenAlex.

  1. Pooled it
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  5. ACS medicinal chemistry letters · 2026
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99 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

1 author at 1 institution in 1 country.

Marilyn D ReshCell Biology Program, Memorial Sloan Kettering Cancer Center, 1275 York Avenue, Box 143, New York, NY 10075, United States. Electronic address: reshm@mskcc.org.
Memorial Sloan Kettering Cancer Center · US

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Hongbiao Carl Lekaye · 1985 to 2026
$347.4M
Fatty Acylation of Hedgehog and Wnt ProteinsR01GM116860 · NIGMS · SLOAN-KETTERING INST CAN RESEARCH · PI RESH, MARILYN D · 2016 to 2019
$2.0M
Hedgehog Acyltransferase as a target in cancerR21CA186957 · NCI · SLOAN-KETTERING INST CAN RESEARCH · PI RESH, MARILYN D · 2014 to 2015
$420k
NCI NIH HHS P30 CA008748NCI NIH HHS R21 CA186957NIGMS NIH HHS R01 GM116860
6 · The paper itself

Abstract

Long, short and medium chain fatty acids are covalently attached to hundreds of proteins. Each fatty acid confers distinct biochemical properties, enabling fatty acylation to regulate intracellular trafficking, subcellular localization, protein-protein and protein-lipid interactions. Myristate and palmitate represent the most common fatty acid modifying groups. New insights into how fatty acylation reactions are catalyzed, and how fatty acylation regulates protein structure and function continue to emerge. Myristate is typically linked to an N-terminal glycine, but recent studies reveal that lysines can also be myristoylated. Enzymes that remove N-terminal myristoyl-glycine or myristate from lysines have now been identified. DHHC proteins catalyze S-palmitoylation, but the mechanisms that regulate substrate recognition by individual DHHC family members remain to be determined. New studies continue to reveal thioesterases that remove palmitate from S-acylated proteins. Another area of rapid expansion is fatty acylation of the secreted proteins hedgehog, Wnt and Ghrelin, by Hhat, Porcupine and GOAT, respectively. Understanding how these membrane bound O-acyl transferases recognize their protein and fatty acyl CoA substrates is an active area of investigation, and is punctuated by the finding that these enzymes are potential drug targets in human diseases.

Indexed as

AcylationAcyltransferasesAnimalsFatty AcidsGhrelinHedgehog ProteinsHumansProteinsWnt ProteinsAcyltransferasesFatty AcidsGhrelinHedgehog ProteinsProteinsWnt ProteinsDepalmitoylationLipid raftsMBOAT familyMyristoylationMyristoyl switchPalmitoylation

Identifiers

PMID27233110
PMCPMC4975971
OpenAlexW2401035952

What OpenQuestion holds

Textmetadata
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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.