Evidence map›Paper›PMID 7809090›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1994

Binding of Vav to Grb2 through dimerization of Src homology 3 domains.

Z S Ye, D Baltimore

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

32 citing papers in PubMed, 110 citations in OpenAlex.

  1. Article
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  3. Review
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  6. Studies of novel interactions between Nck and VAV SH3 domains.Communicative & integrative biology · 2011
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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

2 authors at 2 institutions in 1 country.

Z S YeRockefeller University, New York, NY 10021.
D Baltimore
Massachusetts Institute of Technology · USRockefeller University · US

Funding

MALIGNANCY AND NORMAL DEVELOPMENT IN PREB LYMPHOCYTESR01CA051462 · NCI · WHITEHEAD INSTITUTE FOR BIOMEDICAL RES · PI BALTIMORE, DAVID · 1990 to 2004
$1.9M
NCI NIH HHS CA51462
6 · The paper itself

Abstract

The protooncogenic protein Vav has the structure of an intracellular signal transducer. It is exclusively expressed in cells of hematopoietic lineage and plays a crucial role in hematopoietic cell differentiation. Here we report that both in cell extracts and within intact mammalian cells Vav binds to Grb2 (Sem-5/ASH/Drk), an adaptor molecule which plays a key role in Ras activation. The interaction became evident from a yeast two-hybrid screen and its specificity was demonstrated by in vitro binding assays. It is mediated by an unusual protein-protein binding reaction: dimerization of specific intact Src homology 3 domains of each of the partners. Signaling during hematopoietic lineage differentiation may therefore involve the tissue-specific signal transducer Vav linking into the ubiquitous pathway involving Grb2 and ultimately Ras.

Indexed as

Adaptor Proteins, Signal TransducingCell Cycle ProteinsAmino Acid SequenceAnimalsDNA Mutational AnalysisGRB2 Adaptor ProteinHumansMiceMolecular Sequence DataPeptidesProtein BindingProteinsProto-Oncogene ProteinsProto-Oncogene Proteins c-vavSignal TransductionStructure-Activity RelationshipAdaptor Proteins, Signal TransducingCell Cycle ProteinsGRB2 Adaptor ProteinGRB2 protein, humanGrb2 protein, mousePeptidesProteinsProto-Oncogene ProteinsProto-Oncogene Proteins c-vavVAV1 protein, humanVav1 protein, mouse

Identifiers

PMID7809090
PMCPMC45492
OpenAlexW2079138949

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.