Evidence map›Paper›PMID 12456653›Full record

ArticleThe EMBO journal2002

BLNK: molecular scaffolding through 'cis'-mediated organization of signaling proteins.

Christopher W Chiu, Mark Dalton, Masamichi Ishiai, Tomohiro Kurosaki, Andrew C Chan

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

45 citing papers in PubMed, 120 citations in OpenAlex.

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  10. Noncatalytic Bruton's tyrosine kinase activates PLCγThe Journal of biological chemistry · 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

5 authors at 1 institution in 1 country.

Christopher W ChiuCenter for Immunology, Washington University School of Medicine, St Louis, MO 63110, USA.
Mark Dalton
Masamichi Ishiai
Tomohiro Kurosaki
Andrew C Chan
Washington University in St. Louis · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Assembly of intracellular macromolecular complexes is thought to provide an important mechanism to coordinate the generation of second messengers upon receptor activation. We have previously identified a B cell linker protein, termed BLNK, which serves such a scaffolding function in B cells. We demonstrate here that phosphorylation of five tyrosine residues within human BLNK nucleates distinct signaling effectors following B cell antigen receptor activation. The phosphorylation of multiple tyrosine residues not only amplifies PLCgamma-mediated signaling but also supports 'cis'-mediated interaction between distinct signaling effectors within a large molecular complex. These data demonstrate the importance of coordinate phosphorylation of molecular scaffolds, and provide insights into how assembly of macromolecular complexes is required for normal receptor function.

Indexed as

Adaptor Proteins, Signal TransducingAgammaglobulinaemia Tyrosine KinaseAnimalsBinding SitesB-LymphocytesCalciumCarrier ProteinsHumansIsoenzymesMiceMitogen-Activated Protein KinasesPhospholipase C gammaPhosphoproteinsPhosphorylationProtein-Tyrosine KinasesReceptors, Antigen, B-CellAdaptor Proteins, Signal TransducingAgammaglobulinaemia Tyrosine KinaseB cell linker proteinCalciumCarrier ProteinsIsoenzymesMitogen-Activated Protein KinasesPhospholipase C gammaPhosphoproteinsProtein-Tyrosine KinasesReceptors, Antigen, B-CellType C PhospholipasesTyrosine

Identifiers

PMID12456653
PMCPMC136961
OpenAlexW2158843076

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.