Evidence map›Paper›PMID 15613341›Full record

ArticleJournal of virology2005

Human N-myristoyltransferases form stable complexes with lentiviral nef and other viral and cellular substrate proteins.

Brian T Hill, Jacek Skowronski

Abstract read
In one paragraph

Article in Journal of virology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
0.3field-weighted citation impact, top 50% 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

17 citing papers in PubMed, 31 citations in OpenAlex.

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  15. Protein myristoylation in health and disease.Journal of chemical biology · 2010
    Article
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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 2 institutions in 1 country.

Brian T HillCold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724, USA.
Jacek Skowronski
Cold Spring Harbor Laboratory · USStony Brook University · US

Funding

MOLECULAR INTERACTIONS OF NEF AND AIDS PATHOGENESISR01AI042561 · NIAID · COLD SPRING HARBOR LABORATORY · PI SKOWRONSKI, JACEK · 1998 to 2007
$4.7M
NIAID NIH HHS AI-42561NIAID NIH HHS R01 AI042561
6 · The paper itself

Abstract

Nef is a multifunctional virulence factor of primate lentiviruses that facilitates viral replication in the infected host. All known functions of Nef require that it be myristoylated at its N terminus. This reaction is catalyzed by N-myristoyltransferases (NMTs), which transfer myristate from myristoyl coenzyme A (myristoyl-CoA) to the N-terminal glycine of substrate proteins. Two NMT isoforms (NMT-1 and NMT-2) are expressed in mammalian cells. To provide a better mechanistic understanding of Nef function, we used biochemical and microsequencing techniques to isolate and identify Nef-associated proteins. Through these studies, NMT-1 was identified as an abundant Nef-associated protein. The Nef-NMT-1 complex is most likely a transient intermediate of the myristoylation reaction of Nef and is modulated by agents which affect the size of the myristoyl-CoA pool in the cell. We also examined two other proteins that bear an N-terminal myristoylation signal, human immunodeficiency virus type 1 Gag and Hck protein tyrosine kinase, and found that Gag bound preferentially the NMT-2 isoform, while Hck bound mostly to NMT-1. Recognition of different NMT isoforms by these viral and cellular substrate proteins suggests nonoverlapping roles for these enzymes in vivo and reveals a potential for the development of inhibitors that target the myristoylation of specific viral substrates more selectively.

Indexed as

Acyl Coenzyme AAcyltransferasesAmino Acid SequenceAnimalsCOS CellsGene Products, nefHIV-1HumansIsoenzymesJurkat CellsMolecular Sequence Datanef Gene Products, Human Immunodeficiency VirusAcyl Coenzyme AAcyltransferasesGene Products, nefglycylpeptide N-tetradecanoyltransferaseIsoenzymesnef Gene Products, Human Immunodeficiency VirusS-tetradecanoyl-coenzyme A

Identifiers

PMID15613341
PMCPMC538564
OpenAlexW2099025150

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.