ReviewImmunologic research2002
The interface between tapasin and MHC class I: identification of amino acid residues in both proteins that influence their interaction.
Review in Immunologic research, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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.
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.
Who cites it
11 citing papers in PubMed, 27 citations in OpenAlex.
- Chaperones and Catalysts: How Antigen Presentation Pathways Cope With Biological Necessity.Frontiers in immunology · 2022Review
- Crystal structure of a TAPBPR-MHC I complex reveals the mechanism of peptide editing in antigen presentation.Science (New York, N.Y.) · 2017Article
- Partial Dissociation of Truncated Peptides Influences the Structural Dynamics of the MHCI Binding Groove.Frontiers in immunology · 2017Article
- Proofreading of Peptide-MHC Complexes through Dynamic Multivalent Interactions.Frontiers in immunology · 2017Review
- Understanding the obstacle of incompatibility at residue 156 within HLA-B*35 subtypes.Immunogenetics · 2016Article
- Molecular mechanism of peptide editing in the tapasin-MHC I complex.Scientific reports · 2016Article
- Productive association between MHC class I and tapasin requires the tapasin transmembrane/cytosolic region and the tapasin C-terminal Ig-like domain.Molecular immunology · 2012Article
- What is the role of alternate splicing in antigen presentation by major histocompatibility complex class I molecules?Immunologic research · 2010Review
- A transmembrane tail: interaction of tapasin with TAP and the MHC class I molecule.Molecular immunology · 2009Article
- Specificity of amyloid precursor-like protein 2 interactions with MHC class I molecules.Immunogenetics · 2008Article
- Crystal structure of the murine cytomegalovirus MHC-I homolog m144.Journal of molecular biology · 2006Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Prior to the binding of antigenic peptide, a complex of chaperone proteins associates with the Major Histocompatibility Complex (MHC) class I heavy chain/beta2m heterodimer. Although each domain of the MHC class I heavy chain contains amino acid residues that influence chaperone binding, there are several pieces of evidence that point to an interaction between the MHC class I alpha/2/alpha3 domains and tapasin. In regard to the site on tapasin involved in the tapasin/MHC interface, we have found that a particular region of tapasin (containing amino acid residues 334-342) is necessary for the binding of tapasin to the MHC class I heavy chain. Our results also indicate that amino acids in this region of tapasin also affect the proportion of MHC class I open forms expressed at the cell surface and MHC class I egress from the endoplasmic reticulum. Based on these results and those obtained by other laboratories, a model for MHC class I/tapasin interaction is proposed.
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Registered trials
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.