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Biochemical, cell biological and immunological issues surrounding the endoplasmic reticulum chaperone GRP94/gp96.

Publication ,  Journal Article
Nicchitta, CV
Published in: Curr Opin Immunol
February 1998

The past year has born witness to compelling demonstrations of the utility of peptide complexes with glucose regulated protein 94 (GRP94, also known as gp96) in cancer immunotherapy. Insights into the structural basis of peptide binding to GRP94 have been obtained and the role of the transporter for antigen presentation in defining the GRP94-bound peptide composition has been determined.

Duke Scholars

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Published In

Curr Opin Immunol

DOI

ISSN

0952-7915

Publication Date

February 1998

Volume

10

Issue

1

Start / End Page

103 / 109

Location

England

Related Subject Headings

  • Subcellular Fractions
  • Phylogeny
  • Peptides
  • Molecular Chaperones
  • Membrane Proteins
  • Immunology
  • Humans
  • HSP70 Heat-Shock Proteins
  • Endoplasmic Reticulum
  • Antigens, Neoplasm
 

Citation

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Chicago
ICMJE
MLA
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Nicchitta, C. V. (1998). Biochemical, cell biological and immunological issues surrounding the endoplasmic reticulum chaperone GRP94/gp96. Curr Opin Immunol, 10(1), 103–109. https://doi.org/10.1016/s0952-7915(98)80039-3
Nicchitta, C. V. “Biochemical, cell biological and immunological issues surrounding the endoplasmic reticulum chaperone GRP94/gp96.Curr Opin Immunol 10, no. 1 (February 1998): 103–9. https://doi.org/10.1016/s0952-7915(98)80039-3.
Nicchitta, C. V. “Biochemical, cell biological and immunological issues surrounding the endoplasmic reticulum chaperone GRP94/gp96.Curr Opin Immunol, vol. 10, no. 1, Feb. 1998, pp. 103–09. Pubmed, doi:10.1016/s0952-7915(98)80039-3.
Journal cover image

Published In

Curr Opin Immunol

DOI

ISSN

0952-7915

Publication Date

February 1998

Volume

10

Issue

1

Start / End Page

103 / 109

Location

England

Related Subject Headings

  • Subcellular Fractions
  • Phylogeny
  • Peptides
  • Molecular Chaperones
  • Membrane Proteins
  • Immunology
  • Humans
  • HSP70 Heat-Shock Proteins
  • Endoplasmic Reticulum
  • Antigens, Neoplasm