Evidence map›Paper›PMID 10980601›Full record

ArticleOncogene2000

A novel adaptor-like protein which is a substrate for the non-receptor tyrosine kinase, BRK.

P J Mitchell, E A Sara, M R Crompton

Abstract readComparative Study
PubMed Publisher
In one paragraph

Article in Oncogene, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

36 citing papers in PubMed, 82 citations in OpenAlex.

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  7. Targeting protein tyrosine kinase 6 in cancer.Biochimica et biophysica acta. Reviews on cancer · 2020
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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

3 authors at 2 institutions in 1 country.

P J MitchellSection of Cell Biology and Experimental Pathology, The Breakthrough Toby Robinson Cancer Research Centre, Institute of Cancer Research, 237 Fulham Road, London SW3 6JB, UK.
E A Sara
M R Crompton
Institute of Cancer Research · GBRoyal Holloway University of London · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The brk gene encodes a non-receptor tyrosine kinase that has been found to be overexpressed in approximately two thirds of breast tumours. Using a yeast two-hybrid based screen, we have cloned cDNAs encoding a novel protein, BKS, that is a substrate for the kinase activity of BRK and has the characteristics of an adaptor protein. BKS possesses an N-terminal PH-like domain followed by an SH2-like domain. In co-transfection experiments, high levels of phosphotyrosine were observed on BKS and BRK was found to be associated with BKS, both of which were dependent on the catalytic activity of BRK. The phosphorylation of and association with BKS by BRK was also dependent on the SH2-like domain present within BKS. In addition, BKS recruited an unidentified 100 kDa protein that was also phosphorylated on tyrosine residues in the presence of BRK. We have determined that the BKS protein is expressed in most adult human tissues. Oncogene (2000) 19, 4273 - 4282

Indexed as

Adaptor Proteins, Signal TransducingProtein Processing, Post-TranslationalAdultAmino Acid SequenceBase SequenceBreastDNA, ComplementaryFemaleHumansMolecular Sequence DataNeoplasm ProteinsPhosphoproteinsPhosphorylationProtein Structure, TertiaryProtein-Tyrosine KinasesRecombinant Fusion ProteinsAdaptor Proteins, Signal TransducingDNA, ComplementaryNeoplasm ProteinsPhosphoproteinsProtein-Tyrosine KinasesPTK6 protein, humanRecombinant Fusion ProteinsSTAP2 protein, human

Identifiers

PMID10980601
OpenAlexW2118895328

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.