Evidence map›Paper›PMID 1402651›Full record

ArticleThe Journal of experimental medicine1992

Myristyl acylation of the tumor necrosis factor alpha precursor on specific lysine residues.

F T Stevenson, S L Bursten, R M Locksley, D H Lovett

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Journal of experimental medicine, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
1.5field-weighted citation impact, top 16% 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

53 citing papers in PubMed, 115 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Review
  9. Chemical Proteomics Reveals NMolecular & cellular proteomics : MCP · 2024
    Article
  10. Chemische Synthese und Semisynthese von lipidierten Proteinen.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2022
    Review
  11. Chemical Synthesis and Semisynthesis of Lipidated Proteins.Angewandte Chemie (International ed. in English) · 2022
    Review
  12. Reversible lysine fatty acylation of an anchoring protein mediates adipocyte adrenergic signaling.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  13. Review
  14. Protein Lipidation by Palmitoylation and Myristoylation in Cancer.Frontiers in cell and developmental biology · 2021
    Review
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article
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

4 authors at 1 institution in 1 country.

F T StevensonMedical Service, San Francisco Veterans Administration Medical Center, California 94121.
S L Bursten
R M Locksley
D H Lovett
San Francisco VA Medical Center · US

Funding

NIDDK NIH HHS DK AI-26918
6 · The paper itself

Abstract

NH2-terminal glycine myristyl acylation is a cotranslational modification that affects both protein localization and function. However, several proteins that lack NH2-terminal glycine residues, including the interleukin 1 (IL-1) precursors, also contain covalently linked myristate. To date, the site(s) of acylation of these proteins has not been determined. During an evaluation of IL-1 acylation, it was observed that [3H]myristate-labeled human monocyte lysates contained a prominent 26-kD myristylated protein, which was identified as the tumor necrosis factor alpha (TNF) precursor protein on the basis of specific immune precipitation. Radioimmunoprecipitates from the supernates of labeled monocytes indicated that the processed or mature 17-kD form of TNF does not contain myristate, suggesting that the site of acylation occurs within the 76-amino acid propiece of the precursor molecule. As the TNF precursor does not contain an NH2-terminal glycine, we hypothesized that myristyl acylation occurs on the N-epsilon-NH2 groups of lysine, of which two are present in the propiece (K19K20). Synthetic peptides were designed to include all seven lysine residues present within the entire 26-kD TNF precursor, and used in an in vitro myristyl acylation assay containing peptide, myristyl-CoA, and monocyte lysate as a source of enzyme. Analysis of reaction products by reverse phase high performance liquid chromatography and gas phase sequencing demonstrated the exclusive myristyl acylation of K19 and K20, consistent with the presence in monocytes of a specific lysyl N-epsilon-NH2-myristyl transferase activity. The acylated lysine residues are located immediately downstream from a hydrophobic, probable membrane-spanning segment of the propiece. Specific myristyl acylation of the TNF propiece may facilitate membrane insertion or anchoring of this critical inflammatory mediator.

Indexed as

LysineAcylationAmino Acid SequenceAnimalsCytosolElectrophoresis, Gel, Two-DimensionalHumansKineticsMolecular Sequence DataMonocytesMyristic AcidMyristic AcidsOligopeptidesProtein PrecursorsProtein Processing, Post-TranslationalRecombinant ProteinsLysineMyristic AcidMyristic AcidsOligopeptidesProtein PrecursorsRecombinant ProteinsTumor Necrosis Factor-alphatumor necrosis factor precursor

Identifiers

PMID1402651
PMCPMC2119375
OpenAlexW2186750753

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.