Evidence map›Paper›PMID 8475115›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1993

Lipid modifications of G proteins: alpha subunits are palmitoylated.

M E Linder, P Middleton, J R Hepler, R Taussig, A G Gilman, S M Mumby

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 116 papers.

0numbers the graph read from it
0cells of the map it votes in
116citing papers in PubMed
13.1field-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

116 citing papers in PubMed, 351 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Altered Protein Palmitoylation as Disease Mechanism in Neurodegenerative Disorders.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024
    Review
  8. Article
  9. Review
  10. Impact of Protein NLife (Basel, Switzerland) · 2023
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Measuring Smoothened (SMO)-Mediated Activation of the GMethods in molecular biology (Clifton, N.J.) · 2022
    Article
  17. Review
  18. Article
  19. Article
  20. Article

56 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

6 authors at 1 institution in 1 country.

M E LinderDepartment of Pharmacology, University of Texas Southwestern Medical Center, Dallas 75235.
P Middleton
J R Hepler
R Taussig
A G Gilman
S M Mumby
The University of Texas Southwestern Medical Center · US

Funding

REGULATION OF CYCLIC NUCLEOTIDE METABOLISMR01GM034497 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI GILMAN, ALFRED G · 1985 to 2007
$5.8M
REGULATION OF CYCLIC NUCLEOTIDE METABOLISMR37GM034497 · NIGMS · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI GILMAN, ALFRED G · 1990 to 1998
–
NIGMS NIH HHS GM34497
6 · The paper itself

Abstract

A small number of membrane-associated proteins are reversibly and covalently modified with palmitic acid. Palmitoylation of G-protein alpha and beta subunits was assessed by metabolic labeling of subunits expressed in simian COS cells or insect Sf9 cells. The fatty acid was incorporated into all of the alpha subunits examined (alpha s, alpha o, alpha i1, alpha i2, alpha i3, alpha z, and alpha q), including those that are also myristoylated (alpha o, alpha i, and alpha z). Palmitate was released by treatment with base, suggesting attachment to the protein through a thioester or ester bond. Limited tryptic digestion of activated alpha o and alpha s resulted in release of the amino-terminal portions of the proteins and radioactive palmitate. These data are consistent with palmitoylation of the proteins near their amino termini, most likely on Cys-3. Reversible acylation of G-protein alpha subunits may provide an additional mechanism for regulation of signal transduction.

Indexed as

Protein Processing, Post-TranslationalAnimalsAutoradiographyBase SequenceCell LineCell MembraneChlorocebus aethiopsCytosolGTP-Binding ProteinsGuanosine 5'-O-(3-Thiotriphosphate)Macromolecular SubstancesMethionineMolecular Sequence DataMothsMyristic AcidMyristic AcidsGTP-Binding ProteinsGuanosine 5'-O-(3-Thiotriphosphate)Macromolecular SubstancesMethionineMyristic AcidMyristic AcidsOligodeoxyribonucleotidesPalmitic AcidPalmitic AcidsRecombinant ProteinsTritium

Identifiers

PMID8475115
PMCPMC46364
OpenAlexW1978686382

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.