Evidence map›Paper›PMID 33878949›Full record

ArticleOpen biology2021

Substrate recruitment by zDHHC protein acyltransferases.

Martin Ian P Malgapo, Maurine E Linder

Open access · goldAbstract read
In one paragraph

Article in Open biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed, 1 pooled it
4.1field-weighted citation impact, top 5% 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

58 citing papers in PubMed, 1 synthesis or guideline pooled it, 75 citations in OpenAlex.

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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.

Martin Ian P MalgapoDepartment of Molecular Medicine, College of Veterinary Medicine, Cornell University, Ithaca, NY, USA.
Maurine E LinderDepartment of Molecular Medicine, College of Veterinary Medicine, Cornell University, Ithaca, NY, USA.
Cornell University · US

Funding

A Novel Regulatory Mechanism for the Ras Family of GTPasesR01GM121540 · NIGMS · CORNELL UNIVERSITY · PI LINDER, MAURINE E · 2017 to 2020
$1.5M
NIGMS NIH HHS R01 GM121540
6 · The paper itself

Abstract

Protein palmitoylation is the post-translational attachment of fatty acids, most commonly palmitate (C16 : 0), onto a cysteine residue of a protein. This reaction is catalysed by a family of integral membrane proteins, the zDHHC protein acyltransferases (PATs), so-called due to the presence of an invariant Asp-His-His-Cys (DHHC) cysteine-rich domain harbouring the catalytic centre of the enzyme. Conserved throughout eukaryotes, the zDHHC PATs are encoded by multigene families and mediate palmitoylation of thousands of protein substrates. In humans, a number of zDHHC proteins are associated with human diseases, including intellectual disability, Huntington's disease, schizophrenia and cancer. Key to understanding the physiological and pathophysiological importance of individual zDHHC proteins is the identification of their protein substrates. Here, we will describe the approaches and challenges in assigning substrates for individual zDHHCs, highlighting key mechanisms that underlie substrate recruitment.

Indexed as

AcyltransferasesAmino Acid SequenceConserved SequenceFatty AcidsHumansIsoenzymesLigandsMultigene FamilyPhylogenyProtein BindingProtein ConformationProtein Interaction Domains and MotifsProtein Processing, Post-TranslationalProtein TransportStructure-Activity RelationshipSubstrate SpecificityAcyltransferasesFatty AcidsIsoenzymesLigandsZDHHC1 protein, humanfatty acylationpalmitoylationpost-translational modificationzDHHC enzyme

Identifiers

PMID33878949
PMCPMC8059564
OpenAlexW3154350377

What OpenQuestion holds

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LicenceCC BY
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.