Evidence map›Paper›PMID 10900006›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2000

The serine and threonine residues in the Ig-alpha cytoplasmic tail negatively regulate immunoreceptor tyrosine-based activation motif-mediated signal transduction.

R Müller, J Wienands, M Reth

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.0field-weighted citation impact, top 26% 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

15 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
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  7. Syk is a dual-specificity kinase that self-regulates the signal output from the B-cell antigen receptor.Proceedings of the National Academy of Sciences of the United States of America · 2010
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  10. Review
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  12. Somatic hypermutation of the B cell receptor genes B29 (Igbeta, CD79b) and mb1 (Igalpha, CD79a).Proceedings of the National Academy of Sciences of the United States of America · 2003
    Article
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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.

R MüllerDepartment of Molecular Immunology, Biology III, University of Freiburg and Max-Planck-Institute for Immunobiology, Stübeweg 51, 79108 Freiburg, Germany.
J Wienands
M Reth
University of Freiburg · DEMax Planck Institute of Immunobiology and Epigenetics · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The B cell antigen receptor (BCR) is a multiprotein complex consisting of the membrane-bound Ig molecule and the Ig-alpha/Ig-beta heterodimer. On BCR engagement, Ig-alpha and Ig-beta become phosphorylated not only on tyrosine residues of the immunoreceptor tyrosine-based activation motif but also on serine and threonine residues. We have mutated all serine and threonine residues in the Ig-alpha tail to alanine and valine, respectively. The mutated Ig-alpha sequence was expressed either as a single-chain Fv/Ig-alpha molecule or in the context of the complete BCR. In both cases, the mutated Ig-alpha showed a stronger tyrosine phosphorylation than the wild-type Ig-alpha and initiated increased signaling on stimulation. These findings suggest that serine/threonine kinases can negatively regulate signal transduction from the BCR.

Indexed as

Signal TransductionAdaptor Proteins, Signal TransducingAmino Acid SequenceAntigens, CDCarrier ProteinsCD79 AntigensCytoplasmEnzyme InhibitorsHumansImmunoglobulin FragmentsImmunoglobulin Variable RegionMolecular Sequence DataPhosphoproteinsProtein Serine-Threonine KinasesProtein Tyrosine PhosphatasesReceptors, Antigen, B-CellAdaptor Proteins, Signal TransducingAntigens, CDB cell linker proteinCarrier ProteinsCD79 AntigensCD79A protein, humanEnzyme InhibitorsImmunoglobulin Fragmentsimmunoglobulin FvImmunoglobulin Variable RegionpervanadatePhosphoproteinsProtein Serine-Threonine KinasesProtein Tyrosine PhosphatasesReceptors, Antigen, B-CellRecombinant Fusion ProteinsSerineThreonineTyrosineVanadates

Identifiers

PMID10900006
PMCPMC26968
OpenAlexW2005898236

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.