Evidence map›Paper›PMID 31201791›Full record

ArticleAnalytical biochemistry2019

MHC-I peptide binding activity assessed by exchange after cleavage of peptide covalently linked to β2-microglobulin.

Mollie M Jurewicz, Richard A Willis, Vasanthi Ramachandiran, John D Altman, Lawrence J Stern

Open access · greenAbstract read
In one paragraph

Article in Analytical biochemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.4field-weighted citation impact, top 38% 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

6 citing papers in PubMed, 7 citations in OpenAlex.

  1. Review
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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

5 authors at 3 institutions in 1 country.

Mollie M JurewiczProgram in Immunology and Microbiology, University of Massachusetts Medical School, Worcester, MA, 01605, United States; Department of Pathology, University of Massachusetts Medical School, Worcester, MA, 01605, United States.
Richard A WillisEmory Vaccine Center, Yerkes National Primate Research Center, Atlanta, GA, 30329, United States.
Vasanthi RamachandiranEmory Vaccine Center, Yerkes National Primate Research Center, Atlanta, GA, 30329, United States.
John D AltmanEmory Vaccine Center, Yerkes National Primate Research Center, Atlanta, GA, 30329, United States; Department of Microbiology and Immunology, Emory Vaccine Center at Yerkes, Emory University School of Medicine, Atlanta, GA, 30329, United States.
Lawrence J SternProgram in Immunology and Microbiology, University of Massachusetts Medical School, Worcester, MA, 01605, United States; Department of Pathology, University of Massachusetts Medical School, Worcester, MA, 01605, United States; Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA, 01605, United States. Electronic address: lawrence.stern@umassmed.edu.
Emory National Primate Research CenterUniversity of Massachusetts Chan Medical School · USEmory University · US

Funding

TRAINING IN IMMUNOLOGY (COMPETITIVE RENEWAL OF AI07439)T32AI007349 · NIAID · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI STERN, LAWRENCE J. · 1989 to 2024
$4.5M
Structure and Function of Class II MHC ProteinsR01AI038996 · NIAID · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI STERN, LAWRENCE J · 1996 to 2006
$1.6M
NIAID NIH HHS HHSN272201300006CNIAID NIH HHS R01 AI038996NIAID NIH HHS T32 AI007349
6 · The paper itself

Abstract

A common approach to measuring binding constants involves combining receptor and ligand and measuring the distribution of bound and free states after equilibration. For class I major histocompatibility (MHC-I) proteins, which bind short peptides for presentation to T cells, this approach is precluded by instability of peptide-free protein. Here we develop a method wherein a weakly-binding peptide covalently attached to the N-terminus of the MHC-I β2m subunit is released from the peptide binding site after proteolytic cleavage of the linker. The resultant protein is able to bind added peptide. A direct binding assay and method for estimation of peptide binding constant (K

Indexed as

ProteolysisAmino Acid Sequencebeta 2-MicroglobulinHistocompatibility Antigens Class IPeptidesProtein Bindingbeta 2-MicroglobulinHistocompatibility Antigens Class IPeptidesCompetition assayEquilibrium binding constantFluorescence polarizationIC(50)Major histocompatibility proteinPeptide exchange

Identifiers

PMID31201791
PMCPMC6760266
OpenAlexW2950797298

What OpenQuestion holds

Textmetadata
LicenceTDM
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.