Evidence map›Paper›PMID 7907978›Full record

ArticleThe EMBO journal1994

The SH2 domain protein GRB-7 is co-amplified, overexpressed and in a tight complex with HER2 in breast cancer.

D Stein, J Wu, S A Fuqua, C Roonprapunt, V Yajnik, P D'Eustachio, J J Moskow, A M Buchberg, C K Osborne, B Margolis

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed
11.0field-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

81 citing papers in PubMed, 251 citations in OpenAlex.

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  8. Review
  9. Phosphotyrosine isosteres: past, present and future.Organic & biomolecular chemistry · 2020
    Review
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  11. Article
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  13. Article
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  19. Article
  20. Grb7 gene amplification and protein expression by FISH and IHC in ovarian cancer.International journal of clinical and experimental pathology · 2015
    Article

21 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

10 authors at 1 institution in 1 country.

D SteinNew York University Medical Center, Department of Pharmacology, Kaplan Cancer Center, NY 10016.
J Wu
S A Fuqua
C Roonprapunt
V Yajnik
P D'Eustachio
J J Moskow
A M Buchberg
C K Osborne
B Margolis
Columbia University Irving Medical Center · US

Funding

TISSUE CULTURE---COREP30CA054174 · NCI · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI Lei Zheng · 1991 to 2026
$59.1M
TRANSFORMING GROWTH FACTOR ALPHA IN PATHOGENESIS OF BREAST CANCERP01CA030195 · NCI · UNIVERSITY OF TEXAS HLTH SCI CTR SAN ANT · PI OESTERREICH, STEFFI · 1985 to 2009
$16.8M
INVOLVEMENT OF THE EVI-2 LOCUS IN MYELOID LEUKEMIAR01CA058586 · NCI · THOMAS JEFFERSON UNIVERSITY · PI BUCHBERG, ARTHUR M. · 1993 to 1995
–
NCI NIH HHS CA58586NCI NIH HHS P01 CA30195NCI NIH HHS P30 CA54174
6 · The paper itself

Abstract

SH2 domain proteins are important components of the signal transduction pathways activated by growth factor receptor tyrosine kinases. We have been cloning SH2 domain proteins by bacterial expression cloning using the tyrosine phosphorylated C-terminus of the epidermal growth factor receptor as a probe. One of these newly cloned SH2 domain proteins, GRB-7, was mapped on mouse chromosome 11 to a region which also contains the tyrosine kinase receptor, HER2/erbB-2. The analogous chromosomal locus in man is often amplified in human breast cancer leading to overexpression of HER2. We find that GRB-7 is amplified in concert with HER2 in several breast cancer cell lines and that GRB-7 is overexpressed in both cell lines and breast tumors. GRB-7, through its SH2 domain, binds tightly to HER2 such that a large fraction of the tyrosine phosphorylated HER2 in SKBR-3 cells is bound to GRB-7. GRB-7 can also bind tyrosine phosphorylated SHC, albeit at a lower affinity than GRB2 binds SHC. We also find that GRB-7 has a strong similarity over > 300 amino acids to a newly identified gene in Caenorhabditis elegans. This region of similarity, which lies outside the SH2 domain, also contains a pleckstrin homology domain. The presence of evolutionarily conserved domains indicates that GRB-7 is likely to perform a basic signaling function. The fact that GRB-7 and HER2 are both overexpressed and bound tightly together suggests that this basic signaling pathway is greatly amplified in certain breast cancers.

Indexed as

Gene Amplification3T3 CellsAmino Acid SequenceAnimalsBreast NeoplasmsCaenorhabditis elegansChromosome MappingErb-b2 Receptor Tyrosine KinasesErbB ReceptorsGRB7 Adaptor ProteinHumansMiceMolecular Sequence DataPhosphorylationProtein BindingProteinsErb-b2 Receptor Tyrosine KinasesErbB ReceptorsGRB7 Adaptor ProteinGRB7 protein, humanGrb7 protein, mouseProteinsProto-Oncogene Proteins

Identifiers

PMID7907978
PMCPMC394949
OpenAlexW2249984074

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.