Evidence map›Paper›PMID 11029057›Full record

ArticleMolecular biology of the cell2000

Rotational coupling of the transmembrane and kinase domains of the Neu receptor tyrosine kinase.

C A Bell, J A Tynan, K C Hart, A N Meyer, S C Robertson, D J Donoghue

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

69 citing papers in PubMed, 136 citations in OpenAlex.

  1. Article
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  8. Review
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  12. Article
  13. Elucidation and refinement of synthetic receptor mechanisms.Synthetic biology (Oxford, England) · 2020
    Article
  14. Article
  15. Review
  16. Review
  17. Context-dependent regulation of receptor tyrosine kinases: Insights from systems biology approaches.Wiley interdisciplinary reviews. Systems biology and medicine · 2019
    Review
  18. Article
  19. Article
  20. Review

9 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.

C A BellDepartment of Chemistry and Biochemistry, University of California, San Diego, La Jolla, California 92093-0367, USA.
J A Tynan
K C Hart
A N Meyer
S C Robertson
D J Donoghue
University of California San Diego · US

Funding

MOLECULAR STUDIES OF TRANSFORMING GROWTH FACTORSR01DE012581 · NIDCR · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI DONOGHUE, DANIEL J · 1997 to 2001
$581k
NIDCR NIH HHS R01 DE12581
6 · The paper itself

Abstract

Ligand binding to receptor tyrosine kinases (RTKs) regulates receptor dimerization and activation of the kinase domain. To examine the role of the transmembrane domain in regulation of RTK activation, we have exploited a simplified transmembrane motif, [VVVEVVV](n), previously shown to activate the Neu receptor. Here we demonstrate rotational linkage of the transmembrane domain with the kinase domain, as evidenced by a periodic activation of Neu as the dimerization motif is shifted across the transmembrane domain. These results indicate that activation requires a specific orientation of the kinase domains with respect to each other. Results obtained with platelet-derived growth factor receptor-beta suggest that this rotational linkage of the transmembrane domain to the kinase domain may be a general feature of RTKs. These observations suggest that activating mutations in RTK transmembrane and juxtamembrane domains will be limited to those residues that position the kinase domains in an allowed rotational conformation.

Indexed as

3T3 CellsAmino Acid SequenceAnimalsBase SequenceChlorocebus aethiopsCOS CellsDimerizationErb-b2 Receptor Tyrosine KinasesLigandsMiceModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedOligodeoxyribonucleotidesProtein ConformationReceptor, Platelet-Derived Growth Factor betaErb-b2 Receptor Tyrosine KinasesLigandsOligodeoxyribonucleotidesReceptor, Platelet-Derived Growth Factor betaReceptor Protein-Tyrosine Kinases

Identifiers

PMID11029057
PMCPMC15017
OpenAlexW2164646304

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.