Evidence map›Paper›PMID 2199457›Full record

ArticleThe Journal of cell biology1990

A rapid posttranslational myristylation of a 68-kD protein in D. discoideum.

A M da Silva, C Klein

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

6 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Pheromone action regulates G-protein alpha-subunit myristoylation in the yeast Saccharomyces cerevisiae.Proceedings of the National Academy of Sciences of the United States of America · 1993
    Article
  4. Article
  5. Article
  6. 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

2 authors at 1 institution in 1 country.

A M da SilvaE. A. Doisy Department of Biochemistry and Molecular Biology, St. Louis University School of Medicine, Missouri 63104.
C Klein
Saint Louis University · US

Funding

CELL SPECIFIC COHESION IN D. DISCOIDEUMR01GM034561 · NIGMS · SAINT LOUIS UNIVERSITY · PI KLEIN, CLAUDETTE · 1985 to 1993
–
NIGMS NIH HHS GM 34561
6 · The paper itself

Abstract

Cells incubated with [3H]myristate were shown to rapidly and specifically acylate a 68-kD protein, p68, in a developmentally-regulated manner. The fatty acid incorporated into p68 was identified as myristate, and is linked to the protein via an amide bond, apparently to an NH2-terminal glycine. The acylation of p68 in D. discoideum displays some unusual properties. Unexpectedly, myristylation of p68 is a posttranslational event and occurs in the presence of inhibitors of protein synthesis. Another unusual finding was that although p68 is a stable protein, the acyl moiety is removed with a half time of approximately 15 min.

Indexed as

Protein Processing, Post-TranslationalAcylationCycloheximideDictyosteliumElectrophoresis, Polyacrylamide GelFungal ProteinsHydroxylamineHydroxylaminesMolecular WeightMyristic AcidMyristic AcidsPeptide HydrolasesCycloheximideFungal ProteinsHydroxylamineHydroxylaminesMyristic AcidMyristic AcidsPeptide Hydrolases

Identifiers

PMID2199457
PMCPMC2116220
OpenAlexW2110552447

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.