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An unstable beta 2-microglobulin: major histocompatibility complex class I heavy chain intermediate dissociates from calnexin and then is stabilized by binding peptide.

Data up to Jan 2025

Published1994
Citations93
References43

Total Citations Per Year

Abstract

References (43)

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1992 • 259 citations

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1994 • 243 citations

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1991 • 221 citations

Interaction with newly synthesized and retained proteins in the endoplasmic reticulum suggests a chaperone function for human integral membrane protein IP90 (calnexin)

1993 • 203 citations

Efficient dissociation of the p88 chaperone from major histocompatibility complex class I molecules requires both beta 2-microglobulin and peptide.

1992 • 184 citations

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1989 • 153 citations

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1991 • 129 citations

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1992 • 125 citations

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1993 • 116 citations

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1992 • 91 citations

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The major histocompatibility complex class I antigen-binding protein p88 is the product of the calnexin gene.

1992 • 74 citations

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Peptide binding to HLA-A2 and HLA-B27 isolated from Escherichia coli. Reconstitution of HLA-A2 and HLA-B27 heavy chain/beta 2-microglobulin complexes requires specific peptides.

1992 • 46 citations

Class I molecules retained in the endoplasmic reticulum bind antigenic peptides.

1993 • 31 citations

Short peptides assist the folding of free class I heavy chains in solution

1992 • 19 citations

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An unstable beta 2-microglobulin: major histocompatibility complex class I heavy chain… (1994) – The Journal of Experimental Medicine | Metascience Observatory Explorer