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Cited by 355

The DOI matches its Crossref record; 27 of the 27 references it cites were found in a registry or an index.

Regulation of MHC Class I Transport by the Molecular Chaperone, Calnexin (p88, IP90)

Jackson, Michael R., Cohen-Doyle, Myrna F., Peterson, Per A., Williams, David B.·1994·Science

Abstract

Assembled class I histocompatibility molecules, consisting of heavy chain, β 2 -microglobulin, and peptide ligand, are transported rapidly to the cell surface. In contrast, the intracellular transport of free heavy chains or peptide-deficient heavy chain-β 2 -microglobulin heterodimers is impaired. A 90-kilodalton membrane-bound chaperone of the endoplasmic reticulum (ER), termed calnexin, associates quantitatively with newly synthesized class I heavy chains, but the functions of calnexin in this interaction are unknown. Class I subunits were expressed alone or in combination with calnexin in Drosophila melanogaster cells. Calnexin retarded the intracellular transport of both peptide-deficient heavy chain-β 2 -microglobulin heterodimers and free heavy chains. Calnexin also impeded the rapid intracellular degradation of free heavy chains. The ability of calnexin to protect and retain class I assembly intermediates is likely to contribute to the efficient intracellular formation of class I-peptide complexes.

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Crossref · 10.1126/science.8278813

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Metadata

Authors
Jackson, M. R., Cohen-Doyle, M. F., Peterson, P. A., & Williams, D. B.
Venue
Science
Published
1994-01-21
Volume
263
Issue
5145
Pages
384-387
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2091797397
Cited by
355
References
27
FWCI
18.35
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Regulation of MHC Class I Transport by the Molecular Chaperone, Calnexin (p88, IP90). https://app.cochat.ai/papers/10.1126/science.8278813
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Jackson, M. R., Cohen-Doyle, M. F., Peterson, P. A., & Williams, D. B. (1994). Regulation of MHC Class I Transport by the Molecular Chaperone, Calnexin (p88, IP90). Science. https://doi.org/10.1126/science.8278813

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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