D
Daniel C. Chapman
Researcher at University of Toronto
Publications - 6
Citations - 819
Daniel C. Chapman is an academic researcher from University of Toronto. The author has contributed to research in topics: Endoplasmic reticulum & MHC class I. The author has an hindex of 6, co-authored 6 publications receiving 690 citations.
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Journal ArticleDOI
Mechanisms of pre-apoptotic calreticulin exposure in immunogenic cell death
Theocharis Panaretakis,Theocharis Panaretakis,Theocharis Panaretakis,Oliver Kepp,Oliver Kepp,Oliver Kepp,Ulf Brockmeier,Antoine Tesniere,Antoine Tesniere,Antoine Tesniere,Ann Charlotte Björklund,Daniel C. Chapman,Michael Durchschlag,Nicholas Joza,Nicholas Joza,Nicholas Joza,Gérard Pierron,Peter van Endert,Peter van Endert,Junying Yuan,Laurence Zitvogel,Laurence Zitvogel,Frank Madeo,David B. Williams,Guido Kroemer,Guido Kroemer,Guido Kroemer +26 more
TL;DR: Depletion of PERK, caspase‐8 or SNAREs had no effect on cell death induced by anthracyclines, yet abolished the immunogenicity of cell death, which could be restored by absorbing recombinant CRT to the cell surface.
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ER quality control in the biogenesis of MHC class I molecules.
TL;DR: This review discusses the folding and assembly of class I molecules as well as a number of strategies that viruses have evolved to subvert normal class I assembly within the ER and thereby evade immune recognition by cytotoxic T cells.
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Depletion of Cyclophilins B and C Leads to Dysregulation of Endoplasmic Reticulum Redox Homeostasis
TL;DR: The novel involvement of cyclophilins B and C in ER redox homeostasis is demonstrated, and the existence of an additional ER oxidative pathway that is modulated by ER cyclophILins is suggested.
Journal ArticleDOI
Inhibition of the FKBP family of peptidyl prolyl isomerases induces abortive translocation and degradation of the cellular prion protein
Pawel Stocki,Maxime Sawicki,Charles E. Mays,Seo Jung Hong,Daniel C. Chapman,David Westaway,David B. Williams +6 more
TL;DR: The FKBP inhibitor FK506 profoundly reduces expression of the cellular prion protein by causing its abortive translocation into the ER and degradation by the proteasome.
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Contributions of the Lectin and Polypeptide Binding Sites of Calreticulin to Its Chaperone Functions in Vitro and in Cells.
TL;DR: Findings indicate that the lectin-based mode of client interaction is the predominant contributor to the chaperone functions of calreticulin within the endoplasmic reticulum.