Evidence map›Paper›PMID 8627155›Full record

ArticleThe Journal of experimental medicine1996

Fate of surrogate light chains in B lineage cells.

K Lassoued, H Illges, K Benlagha, M D Cooper

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Journal of experimental medicine, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.9field-weighted citation impact, top 8% 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

12 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Mutations of the Igbeta gene cause agammaglobulinemia in man.The Journal of experimental medicine · 2007
    Article
  5. Article
  6. Article
  7. Aberrant B cell receptor signaling from B29 (Igbeta, CD79b) gene mutations of chronic lymphocytic leukemia B cells.Proceedings of the National Academy of Sciences of the United States of America · 2000
    Article
  8. Article
  9. Novel mechanisms control the folding and assembly of lambda5/14.1 and VpreB to produce an intact surrogate light chain.Proceedings of the National Academy of Sciences of the United States of America · 1999
    Article
  10. Article
  11. Article
  12. Article
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

4 authors at 1 institution in 1 country.

K LassouedDepartment of Medicine, University of Alabama at Birmingham, 35294, USA.
H Illges
K Benlagha
M D Cooper
University of Alabama at Birmingham · US

Funding

XRAY CRYSTALLOGRAPHYP30CA013148 · NCI · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI Robert S Welner · 1985 to 2026
$165.9M
NORMAL AND ABNORMAL LYMPHOID DIFFERENTIATION IN HUMANSP01AI030879 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI KEARNEY, JOHN F · 1990 to 1994
–
NCI NIH HHS CA13148NIAID NIH HHS AI30879
6 · The paper itself

Abstract

Biosynthesis of the immunoglobulin (Ig) receptor components and their assembly were examined in cell lines representative of early stages in human B lineage development. In pro-B cells, the nascent surrogate light chain proteins form a complex that transiently associates in the endoplasmic reticulum with a spectrum of unidentified proteins (40, 60, and 98 kD) and Bip, a heat shock protein family member. Lacking companion heavy chains, the surrogate light chains in pro-B cells do not associate with either the Ig(alpha) or Ig(beta) signal transduction units, undergo rapid degradation, and fail to reach the pro-B cell surface. In pre-B cells, by contrast, a significant portion of the surrogate light chain proteins associate with mu heavy chains, Ig(alpha), and Ig(beta) to form a stable receptor complex with a relatively long half-life. Early in this assembly process, Bip/GRP78, calnexin, GRP94, and a protein of approximately 17 kD differentially bind to the nascent mu heavy chains. The 17-kD intermediate is gradually replaced by the surrogate light chain protein complex, and the Ig(alpha) and Ig(beta) chains bind progressively to the mu heavy chains during the complex and relatively inefficient process of pre-B receptor assembly. The results suggest that, in humans, heavy chain association is essential for surrogate light chain survival and transport to the cell surface as an integral receptor component.

Indexed as

Heat-Shock ProteinsAntigens, CDB-LymphocytesCalcium-Binding ProteinsCalnexinCarrier ProteinsCD79 AntigensCell CompartmentationCell LineCell MembraneEndoplasmic Reticulum Chaperone BiPHematopoietic Stem CellsHSP70 Heat-Shock ProteinsHumansImmunoglobulin Light ChainsImmunoglobulin Light Chains, SurrogateAntigens, CDCalcium-Binding ProteinsCalnexinCarrier ProteinsCD79 AntigensCD79A protein, humanCD79B protein, humanEndoplasmic Reticulum Chaperone BiPglucose-regulated proteinsHeat-Shock ProteinsHSP70 Heat-Shock ProteinsHSPA5 protein, humanImmunoglobulin Light ChainsImmunoglobulin Light Chains, SurrogateMembrane GlycoproteinsMembrane ProteinsMolecular ChaperonesReceptors, Antigen, B-Cell

Identifiers

PMID8627155
PMCPMC2192437
OpenAlexW2134067907

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.