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1997•The Journal of ImmunologyRequires access

Are transporter associated with antigen processing (TAP) and tapasin class I MHC chaperones?

Joyce C. Solheim, Beatriz M. Carreno, Ted H. Hansen

Open publisher page 41 citations

Abstract

Class I MHC heavy chains associate with many proteins in the endoplasmic reticulum, including TAP, calnexin, calreticulin, and the newly defined tapasin molecule. Recent studies have begun to resolve the nature of how these proteins interact with class I as well as the functional significance of each of these interactions. We propose here that TAP and tapasin are leading candidates to be highly specific chaperones for the class I molecule.

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What this paper is about

Class I MHC heavy chains associate with many proteins in the endoplasmic reticulum, including TAP, calnexin, calreticulin, and the newly defined tapasin molecule. Recent studies have begun to resolve the nature of how these proteins interact with class I as well as the functional significance of each of these interactions. We propose here that TAP and tapasin are leading candidates to be highly specific chaperones for the class I molecule.

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OpenAlex reports 41 citations for this work. Citation counts describe recorded attention and do not establish research quality.

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Available abstract

Class I MHC heavy chains associate with many proteins in the endoplasmic reticulum, including TAP, calnexin, calreticulin, and the newly defined tapasin molecule. Recent studies have begun to resolve the nature of how these proteins interact with class I as well as the functional significance of each of these interactions. We propose here that TAP and tapasin are leading candidates to be highly specific chaperones for the class I molecule.

Key concepts: Transporter associated with antigen processing, Calnexin, Calreticulin, MHC class I, Endoplasmic reticulum, Antigen processing, Cell biology, Chaperone (clinical)

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Are transporter associated with antigen processing (TAP) and tapasin class I MHC chaperones? — Research Paper | ScholarLens