Evidence map›Paper›PMID 3132707›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1988

Identification of cDNA encoding an additional alpha subunit of a human GTP-binding protein: expression of three alpha i subtypes in human tissues and cell lines.

S Y Kim, S L Ang, D B Bloch, K D Bloch, Y Kawahara, C Tolman, R Lee, J G Seidman, E J Neer

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1988. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
5.3field-weighted citation impact, top 4% 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

26 citing papers in PubMed, 66 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. AGS3 and GαMolecules (Basel, Switzerland) · 2020
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. G proteins: critical control points for transmembrane signals.Protein science : a publication of the Protein Society · 1994
    Review
  13. Article
  14. Article
  15. Embryonic stem cells lacking a functional inhibitory G-protein subunit (alpha i2) produced by gene targeting of both alleles.Proceedings of the National Academy of Sciences of the United States of America · 1991
    Article
  16. Heterologously expressed serotonin 1A receptors couple to muscarinic K+ channels in heart.Proceedings of the National Academy of Sciences of the United States of America · 1991
    Article
  17. Article
  18. Guanine nucleotide-binding regulatory proteins in retinal pigment epithelial cells.Proceedings of the National Academy of Sciences of the United States of America · 1991
    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

9 authors at 2 institutions in 1 country.

S Y KimDepartment of Medicine, Brigham and Women's Hospital, Boston, MA 02115.
S L Ang
D B Bloch
K D Bloch
Y Kawahara
C Tolman
R Lee
J G Seidman
E J Neer
Brigham and Women's Hospital · USHarvard University · US

Funding

SENSITIVITY OF THE CALCIUM CHANNEL TO ISCHEMIAK11HL001835 · NHLBI · BRIGHAM AND WOMEN'S HOSPITAL · PI LEE, RICHARD T · 1986 to 1991
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THE MOLECULAR ORGANIZATION OF THE MURINE I-A GENESR01AI018436 · NIAID · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI SEIDMAN, JONATHAN G · 1985 to 1989
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THE MOLECULAR BASIS OF H-2 POLYMORPHISMR01AI019148 · NIAID · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI SEIDMAN, JONATHAN G · 1985 to 1991
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NHLBI NIH HHS HL01835NIAID NIH HHS AI 18436NIAID NIH HHS AI 19148
6 · The paper itself

Abstract

The guanine nucleotide-binding proteins (G proteins), which mediate hormonal regulation of many membrane functions, are composed of alpha, beta, and gamma subunits. We have cloned and characterized cDNA from a human T-cell library encoding a form of alpha i that is different from the human alpha i subtypes previously reported [Didsbury, J. R., Ho, Y.-S. & Snyderman, R. (1987) FEBS Lett. 211, 160-164 and Bray, P., Carter, A., Guo, V., Puckett, C., Kamholz, J., Spiegel, A. & Nirenberg, M. (1987) Proc. Natl. Acad. Sci. USA 84, 5115-5119]. alpha i is the alpha subunit of a class of G proteins that inhibits adenylate cyclase and regulates other enzymes and ion channels. This cDNA encodes a polypeptide of 354 amino acids and is assigned to encode the alpha i-3 subtype of G proteins on the basis of its similarity to other alpha i-like cDNAs and the presence of a predicted site for ADP ribosylation by pertussis toxin. We have determined the expression of mRNA for this and two other subtypes of human alpha i (alpha i-1 and alpha i-2) in a variety of human fetal tissues and in human cell lines. All three alpha i subtypes were present in the tissues tested. However, analysis of individual cell types reveals specificity of alpha i-1 expression. mRNA for alpha i-1 is absent in T cells, B cells, and monocytes but is present in other cell lines. The finding of differential expression of alpha i-1 genes may permit characterization of distinct physiological roles for this alpha i subunit. mRNA for alpha i-2 and alpha i-3 was found in all the primary and transformed cell lines tested. Thus, some cells contain all three alpha i subtypes. This observation raises the question of how cells prevent cross talk among receptors that are coupled to effectors through such similar alpha proteins.

Indexed as

Amino Acid SequenceBase SequenceCell LineCloning, MolecularDNAGenesGTP-Binding ProteinsHumansMacromolecular SubstancesMolecular Sequence DataDNAGTP-Binding ProteinsMacromolecular Substances

Identifiers

PMID3132707
PMCPMC280384
OpenAlexW2043868434

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.