ArticleMolecular immunology2009
A transmembrane tail: interaction of tapasin with TAP and the MHC class I molecule.
Article in Molecular immunology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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.
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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.
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Who cites it
3 citing papers in PubMed, 6 citations in OpenAlex.
- Newly discovered viral E3 ligase pK3 induces endoplasmic reticulum-associated degradation of class I major histocompatibility proteins and their membrane-bound chaperones.The Journal of biological chemistry · 2012Article
- 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
- Downregulation of tapasin expression in primary human oral squamous cell carcinoma: association with clinical outcome.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2010Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The transmembrane protein tapasin has an essential role in the assembly of stable major histocompatibility (MHC) class I/peptide complexes. Within the endoplasmic reticulum, tapasin associates with both the transporter associated with antigen processing (TAP) and the MHC class I molecule. The tapasin/TAP association has been clearly shown to involve the transmembrane domains (TMDs) of both molecules and to result in the stable expression of TAP. Although the influence of tapasin on MHC class I molecule folding and surface expression has been extensively studied, relatively little is known at the structural level regarding the interaction between tapasin and the MHC class I molecule. Here we summarize our current understanding of functions involving the tapasin TMD and propose that, beyond stabilizing TAP, the tapasin TMD may also interact with the MHC class I heavy chain.
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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.