Evidence map›Paper›PMID 10595544›Full record

ArticleProtein science : a publication of the Protein Society1999

Production of soluble alphabeta T-cell receptor heterodimers suitable for biophysical analysis of ligand binding.

B E Willcox, G F Gao, J R Wyer, C A O'Callaghan, J M Boulter, E Y Jones, P A van der Merwe, J I Bell, B K Jakobsen

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
0.5field-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

31 citing papers in PubMed, 54 citations in OpenAlex.

  1. Discovery of TCR-like antibodies to the KRAS G12D neoantigen via in silico-in vitro workflow.Molecular therapy : the journal of the American Society of Gene Therapy · 2026
    Article
  2. ImmTAC: A Novel Platform of T-Cell Receptor-Based Soluble Bispecifics.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
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  8. Design of a native-like secreted form of the hepatitis C virus E1E2 heterodimer.Proceedings of the National Academy of Sciences of the United States of America · 2021
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  17. Structural and energetic evidence for highly peptide-specific tumor antigen targeting via allo-MHC restriction.Proceedings of the National Academy of Sciences of the United States of America · 2011
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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

9 authors at 3 institutions in 1 country.

B E WillcoxMRC Human Immunology Unit, Institute of Molecular Medicine, John Radcliffe Hospital, Oxford, United Kingdom.
G F Gao
J R Wyer
C A O'Callaghan
J M Boulter
E Y Jones
P A van der Merwe
J I Bell
B K Jakobsen
John Radcliffe Hospital · GBMRC Human Immunology Unit · GBUniversity of Oxford · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A method to produce alphabeta T-cell receptors (TCRs) in a soluble form suitable for biophysical analysis was devised involving in vitro refolding of a TCR fusion protein. Polypeptides corresponding to the variable and constant domains of each chain of a human and a murine receptor, fused to a coiled coil heterodimerization motif from either c-Jun (alpha) or v-Fos (beta), were overexpressed separately in Escherichia coli. Following recovery from inclusion bodies, the two chains of each receptor were denatured, and then refolded together in the presence of denaturants. For the human receptor, which is specific for the immunodominant influenza A HLA-A2-restricted matrix epitope (M58-66), a heterodimeric protein was purified in milligram yields and found to be homogeneous, monomeric, antibody-reactive, and stable at concentrations lower than 1 microM. Using similar procedures, analogous results were obtained with a murine receptor specific for an influenza nucleoprotein epitope (366-374) restricted by H2-Db. Production of these receptors has facilitated a detailed analysis of viral peptide-Major Histocompatibility Complex (peptide-MHC) engagement by the TCR using both surface plasmon resonance (SPR) and, in the case of the human TCR, isothermal titration calorimetry (ITC) (Willcox et al., 1999). The recombinant methods described should enable a wide range of TCR-peptide-MHC interactions to be studied and may also have implications for the production of other heterodimeric receptor molecules.

Indexed as

Amino Acid SequenceBinding SitesBiophysicsDimerizationHLA-A2 AntigenHumansLeucine ZippersLigandsMajor Histocompatibility ComplexModels, MolecularMolecular Sequence DataOncogene Proteins v-fosProtein ConformationProtein DenaturationProtein FoldingProto-Oncogene Proteins c-junHLA-A2 AntigenLigandsOncogene Proteins v-fosProto-Oncogene Proteins c-junReceptors, Antigen, T-Cell, alpha-beta

Identifiers

PMID10595544
PMCPMC2144200
OpenAlexW2124170576

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.