Evidence map›Paper›PMID 12454284›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2002

Disulfide bond-mediated dimerization of HLA-G on the cell surface.

Jonathan E Boyson, Robert Erskine, Mary C Whitman, Michael Chiu, Julie M Lau, Louise A Koopman, Markus M Valter, Pavla Angelisova, Vaclav Horejsi, Jack L Strominger

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
80citing papers in PubMed, 1 pooled it
3.2field-weighted citation impact, top 7% 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

80 citing papers in PubMed, 1 synthesis or guideline pooled it, 206 citations in OpenAlex.

  1. Pooled it
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  18. Homotypic and heterotypicCurrent research in immunology · 2022
    Review
  19. Article
  20. Open MHC Class I Conformers: A Look through the Looking Glass.International journal of molecular sciences · 2021
    Review

20 more citing papers are in PubMed but not listed here.

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

10 authors at 2 institutions in 2 countries.

Jonathan E BoysonDepartment of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138; and Institute of Molecular Genetics, 142 20 Prague, Czech Republic.
Robert Erskine
Mary C Whitman
Michael Chiu
Julie M Lau
Louise A Koopman
Markus M Valter
Pavla Angelisova
Vaclav Horejsi
Jack L Strominger
Harvard University · USCzech Academy of Sciences, Institute of Molecular Genetics · CZ

Funding

CHEMISTRY AND BIOLOGY OF LYMPHOCYTESR35CA047554 · NCI · HARVARD UNIVERSITY · PI STROMINGER, JACK L · 1988 to 2001
$4.7M
Human Natural Killer Cells: Formation and Structure of Activating SynapsesR01AI050207 · NIAID · HARVARD UNIVERSITY · PI STROMINGER, JACK L · 2001 to 2011
$4.3M
HLA-G AND NK RECEPTOR INTERACTIONS IN TROPHOBLASTF32HD008515 · NICHD · HARVARD UNIVERSITY · PI BOYSON, JONATHAN E · 1999 to 2001
$76k
NCI NIH HHS CA-47554NIAID NIH HHS AI-50207-02NIAID NIH HHS R01 AI050207NICHD NIH HHS F32 HD008515
6 · The paper itself

Abstract

HLA-G is a nonclassical class I MHC molecule with an unknown function and with unusual characteristics that distinguish it from other class I MHC molecules. Here, we demonstrate that HLA-G forms disulfide-linked dimers that are present on the cell surface. Immunoprecipitation of HLA-G from surface biotinylated transfectants using the anti-beta2-microglobulin mAb BBM.1 revealed the presence of an approximately equal 78-kDa form of HLA-G heavy chain that was reduced by using DTT to a 39-kDa form. Mutation of Cys-42 to a serine completely abrogated dimerization of HLA-G, suggesting that the disulfide linkage formed exclusively through this residue. A possible interaction between the HLA-G monomer or dimer and the KIR2DL4 receptor was also investigated, but no interaction between these molecules could be detected through several approaches. The cell-surface expression of dimerized HLA-G molecules may have implications for HLA-Greceptor interactions and for the search for specific receptors that bind HLA-G.

Indexed as

Amino Acid SubstitutionAntigens, SurfaceChoriocarcinomaCysteineCystineDimerizationDithiothreitolFemaleGenes, MHC Class IIHistocompatibility Antigens Class IHLA AntigensHLA-G AntigensHumansMolecular WeightOxidation-ReductionPregnancyAntigens, SurfaceCysteineCystineDithiothreitolHistocompatibility Antigens Class IHLA AntigensHLA-G AntigensKIR2DL4 protein, humanReceptors, ImmunologicReceptors, KIRReceptors, KIR2DL4Recombinant Fusion Proteins

Identifiers

PMID12454284
PMCPMC138585
OpenAlexW2137015486

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.