Evidence map›Paper›PMID 1979168›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1990

Tissue-specific transformation by epidermal growth factor receptor: a single point mutation within the ATP-binding pocket of the erbB product increases its intrinsic kinase activity and activates its sarcomagenic potential.

H K Shu, R J Pelley, H J Kung

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. (124)I-iodopyridopyrimidinone for PET of Abl kinase-expressing tumors in vivo.Journal of nuclear medicine : official publication, Society of Nuclear Medicine · 2010
    Article
  3. Wa5 is a novel ENU-induced antimorphic allele of the epidermal growth factor receptor.Mammalian genome : official journal of the International Mammalian Genome Society · 2004
    Article
  4. Article
  5. Article
  6. Review
  7. Article
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  9. Article
  10. Disease specificity of kinase domains: the src-encoded catalytic domain converts erbB into a sarcoma oncogene.Proceedings of the National Academy of Sciences of the United States of America · 1995
    Article
  11. Article
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  19. Review
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

3 authors at 1 institution in 1 country.

H K ShuDepartment of Molecular Biology and Microbiology, Case Western Reserve University, Cleveland, OH 44106.
R J Pelley
H J Kung
Case Western Reserve University · US

Funding

TUMOR METABOLISM PROGRAMP30CA043703 · NCI · CASE WESTERN RESERVE UNIVERSITY · PI MARK R CHANCE · 1987 to 2026
$142.3M
ERBB KINASE ACTIVATION AND TRANSFORMATIONR01CA039207 · NCI · UNIVERSITY OF CALIFORNIA DAVIS · PI KUNG, HSING-JIEN · 1986 to 2004
$1.5M
ERB-B ACTIVATION: FROM EGF-RECEPTOR TO LEUKEMIA ONCOGENEK08CA001199 · NCI · CASE WESTERN RESERVE UNIVERSITY · PI PELLEY, ROBERT J · 1987 to 1991
–
ERBB KINASE ACTIVATION AND TRANSFORMATIONR37CA039207 · NCI · UNIVERSITY OF CALIFORNIA DAVIS · PI KUNG, HSING-JIEN · 1991 to 1999
–
NCI NIH HHS CA39207NCI NIH HHS K08-CA01199NCI NIH HHS P-30 CA43703
6 · The paper itself

Abstract

Avian c-erbB is activated to a leukemia oncogene following truncation of its amino-terminal, ligand-binding domain by retroviral insertion. The insertionally activated transcripts encode protein products that have constitutive tyrosine kinase activity and that can induce erythro-leukemia but not sarcomas. We have found that a single point mutation within the ATP-binding pocket of the tyrosine kinase domain in this truncated molecule can increase the ability of this oncogene to induce anchorage-independent growth of fibroblasts in vitro and fibrosarcoma formation in vivo. Associated with this increased transforming potential is a corresponding increase in the kinase activity of the mutant erbB protein product. The mutation, which converts a valine to isoleucine at position 157 of the insertionally activated c-erbB product, is at a residue that is highly conserved within the protein kinase family. To our knowledge, this is the first demonstration of a point mutation in the ATP-binding pocket that activates a tyrosine kinase.

Indexed as

Cell Transformation, NeoplasticMutagenesis, Site-DirectedProto-OncogenesAdenosine TriphosphateAlpharetrovirusAmino Acid SequenceAnimalsBase SequenceBinding SitesChick EmbryoCodonErb-b2 Receptor Tyrosine KinasesErbB ReceptorsFibrosarcomaGene ExpressionMolecular Sequence DataAdenosine TriphosphateCodonErb-b2 Receptor Tyrosine KinasesErbB ReceptorsOligonucleotide ProbesProtein-Tyrosine KinasesProto-Oncogene Proteins

Identifiers

PMID1979168
PMCPMC55112
OpenAlexW2057099744

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.