Evidence map›Paper›PMID 27601175›Full record

ArticleThe protein journal2016

Multi-modal Binding of a 'Self' Peptide by HLA-B*27:04 and B*27:05 Allelic Variants, but not B*27:09 or B*27:06 Variants: Fresh Support for Some Theories Explaining Differential Disease Association.

Manish Kumar Rana, Manni Luthra-Guptasarma

Abstract read
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In one paragraph

Article in The protein journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0cells of the map it votes in
0citing papers in PubMed
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1 · What the graph read from it

What it found

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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

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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

2 authors.

Manish Kumar RanaDepartment of Immunopathology, Research Block A, Postgraduate Institute of Medical Education and Research (PGIMER), Sector-12, Chandigarh, 160012, India.
Manni Luthra-GuptasarmaDepartment of Immunopathology, Research Block A, Postgraduate Institute of Medical Education and Research (PGIMER), Sector-12, Chandigarh, 160012, India. mguptasarma@yahoo.com.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A self-derived-peptide with the same amino acid sequence (N-RRYLENGKETLQR-C) as residues 169-181 of the human leukocyte antigen (HLA) B27 heavy chain is known to bind to MHC Class I complexes containing the HLA-B27 heavy chain. This observation has been invoked previously in at least two different (but related) molecular explanations for the disease-association of the HLA-B27 allele. Here, we use a combination of fluorescence polarization, competitive inhibition and gel filtration chromatographic studies to show that a fluorescently-labeled peptide of the above sequence binds to two disease-associated subtypes of HLA-B27 (namely HLA-B*27:04 and HLA-B*27:05) but not to non-disease-associated subtypes (HLA-B*27:06 or HLA-B*27:09). This differential binding behavior is seen both in (a) peptide binding to complexes of heavy chain (HLA-B27) and light chain (β

Indexed as

Models, ImmunologicalAllelesAmino Acid SequenceAutoimmunityFluorescamineFluorescent DyesGene ExpressionHLA-B27 AntigenHumansModels, MolecularPeptidesProtein BindingRecombinant ProteinsStaining and LabelingFluorescamineFluorescent DyesHLA-B*27:04 antigenHLA-B*27:05 antigenHLA-B*27:06 antigenHLA-B*27:09 antigenHLA-B27 AntigenPeptidesRecombinant ProteinsDisease associationFluorescence polarizationGel filtrationHuman leukocyte antigenPeptide binding

Identifiers

PMID27601175

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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.