Evidence map›Paper›PMID 10688914›Full record

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

Posttranscriptional regulation of Bruton's tyrosine kinase expression in antigen receptor-stimulated splenic B cells.

S Nisitani, A B Satterthwaite, K Akashi, I L Weissman, O N Witte, M I Wahl

Erratum issuedOpen 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. An erratum has been issued. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

20 citing papers in PubMed, 48 citations in OpenAlex.

  1. Trial
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Comparison of Acalabrutinib, A Selective Bruton Tyrosine Kinase Inhibitor, with Ibrutinib in Chronic Lymphocytic Leukemia Cells.Clinical cancer research : an official journal of the American Association for Cancer Research · 2017
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Ibrutinib for B cell malignancies.Experimental hematology & oncology · 2014
    Article
  17. Article
  18. Article
  19. Tyrosine kinase Btk is required for NK cell activation.The Journal of biological chemistry · 2012
    Article
  20. Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

6 authors at 3 institutions in 1 country.

S NisitaniDepartment of Microbiology, Immunology, and Molecular Genetics, and Howard Hughes Medical Institute, University of California at Los Angeles, Los Angeles, CA 90095, USA.
A B Satterthwaite
K Akashi
I L Weissman
O N Witte
M I Wahl
University of California, Los Angeles · USHoward Hughes Medical Institute · USStanford University · US

Funding

NORMAL AND NEOPLASTIC LYMPHOCYTE MATURATIONR35CA042551 · NCI · STANFORD UNIVERSITY · PI WEISSMAN, IRVING LERNER · 1986 to 1999
–
NCI NIH HHS CA42551
6 · The paper itself

Abstract

Mutation of Bruton's tyrosine kinase (Btk) causes human X-linked agammaglobulinemia and murine X-linked immunodeficiency syndrome (xid). Quantitative aspects of B lymphocyte development and function have been demonstrated to depend on Btk level in vivo by using a murine transgenic model system. A sensitive intracellular immunofluorescent assay was developed to measure Btk protein on a per cell basis to test the hypothesis that its dosage is dynamically regulated during B cell development or functional responses. Marrow-derived hematopoietic stem cells, common lymphoid progenitor cells, and developing B and myeloid lineages expressed Btk protein at comparable levels. Resting peripheral B lineage cells had a significantly lower amount of Btk than marrow-derived cells in both wild-type and xid mice. Activation of the B cell antigen receptor up-regulated Btk protein level 10-fold within several hours by a phosphatidylinositol 3-kinase-dependent, posttranscriptional mechanism. In contrast, the protein level of Btk R28C in activated B lymphocytes from xid mice remained low. Bypass of the antigen receptor signaling pathways by treatment of cells with phorbol myristic acid and ionomycin rescued up-regulation of Btk protein in xid splenic B cells. These combined results suggest that certain receptor signals mediated by Btk regulate the level of expression of Btk protein in responding B lymphocytes to potentiate signal transduction. Dynamic regulation of Btk protein dosage is an additional mechanism to modulate B lymphocyte immune functions.

Indexed as

RNA Processing, Post-TranscriptionalAgammaglobulinaemia Tyrosine KinaseAnimalsB-LymphocytesBone MarrowCell DivisionDNA-Binding ProteinsDNA NucleotidylexotransferaseFlow CytometryHematopoietic Stem CellsHumansImmunoglobulin MMiceMice, Inbred BALB CMice, KnockoutMutationAgammaglobulinaemia Tyrosine KinaseBTK protein, humanBtk protein, mouseDNA-Binding ProteinsDNA NucleotidylexotransferaseImmunoglobulin MNuclear ProteinsPhosphatidylinositol 3-KinasesProtein-Tyrosine KinasesProto-Oncogene Proteins c-bcl-2RAG2 protein, humanRag2 protein, mouseReceptors, AntigenV(D)J recombination activating protein 2

Identifiers

PMID10688914
PMCPMC15999
OpenAlexW2098631564

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.