Evidence map›Paper›PMID 7504272›Full record

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

A conserved helix motif complements the protein kinase core.

M Veron, E Radzio-Andzelm, I Tsigelny, L F Ten Eyck, S S Taylor

Abstract readComparative Study
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 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
–field-weighted citation impact
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

21 citing papers in PubMed.

  1. Article
  2. Article
  3. The Tails of Protein Kinase A.Molecular pharmacology · 2022
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Conserved water molecules contribute to the extensive network of interactions at the active site of protein kinase A.Proceedings of the National Academy of Sciences of the United States of America · 1998
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Molecular cloning and characterization of a conserved nuclear serine(threonine) protein kinase.Proceedings of the National Academy of Sciences of the United States of America · 1995
    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

5 authors.

M VeronUnité de Biochimie Cellulaire, Centre National de la Recherche Scientifique: URA1129, Institut Pasteur, France.
E Radzio-Andzelm
I Tsigelny
L F Ten Eyck
S S Taylor

Funding

HEMOGLOBIN AND BLOOD PROTEIN CHEMISTRYT32DK007233 · NIDDK · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI KOMIVES, ELIZABETH A. · 1986 to 2012
$4.6M
NIDDK NIH HHS 5T32 DK07233
6 · The paper itself

Abstract

Residues 40-300 of the mammalian catalytic (C) subunit of cAMP-dependent protein kinase define a conserved bilobal catalytic core shared by all eukaryotic protein kinases. Contiguous to the core is an extended amphipathic alpha-helix (A helix). Trp30, a prominent feature of this helix, fills a deep hydrophobic pocket between the two lobes on the surface opposite to the active site. The C subunit in Dictyostelium discoideum shows sequence conservation of residues 40-350 with the mouse enzyme but contains an N-terminal extension of 332 residues. A sequence corresponding to the A helix contiguous to the core is absent. However, we have now identified a remote A-helix motif (residues 77-98). When the core of the Dictyostelium C subunit was modeled, based on the mouse C subunit, complementarity between this putative A helix and the surface of the core was found to be conserved. Analysis of other protein kinases reveals that the A-helix motif is not restricted to cAMP-dependent protein kinase. In the Src-related family of protein kinases, for example, an A helix is very likely contiguous to the core, thus serving as a linker between the conserved catalytic core and the Src homology 2 domain. We predict that an A-helix motif complementary to the core will be a conserved feature of most eukaryotic protein kinases.

Indexed as

Amino Acid SequenceAnimalsCasein KinasesCyclic AMP-Dependent Protein KinasesDictyosteliumMiceModels, MolecularMolecular Sequence DataProtein KinasesProtein Structure, SecondaryProtein Structure, TertiaryProtein-Tyrosine KinasesProto-Oncogene Proteins pp60(c-src)Sequence AlignmentSequence Homology, Amino AcidCasein KinasesCyclic AMP-Dependent Protein KinasesProtein KinasesProtein-Tyrosine KinasesProto-Oncogene Proteins pp60(c-src)

Identifiers

PMID7504272
PMCPMC47828

What OpenQuestion holds

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Registered trials

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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.