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Michael R. Harris

Researcher at Boston Children's Hospital

Publications -  25
Citations -  1835

Michael R. Harris is an academic researcher from Boston Children's Hospital. The author has contributed to research in topics: Tapasin & MHC class I. The author has an hindex of 15, co-authored 23 publications receiving 1678 citations. Previous affiliations of Michael R. Harris include Washington University in St. Louis & National Museum of American History.

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British Thoracic Society guidelines for the management of community acquired pneumonia in children: update 2011

TL;DR: These updated guidelines represent a review of new evidence since then and consensus clinical opinion where evidence was not found and supersedes the previous guideline document.
Journal Article

Prominence of beta 2-microglobulin, class I heavy chain conformation, and tapasin in the interactions of class I heavy chain with calreticulin and the transporter associated with antigen processing.

TL;DR: Beta 2m appears to bind TAP in the absence of H chain, providing an elegant mechanism to retain beta 2m in the endoplasmic reticulum at the site of peptide loading.
Journal ArticleDOI

Virus Subversion of the MHC Class I Peptide-Loading Complex

TL;DR: This work identifies cellular components of the MHC class I assembly machinery, TAP and tapasin, that are required for mK3 function and subverts TAP/tapasin to specifically target class I molecules for destruction.
Journal Article

Calreticulin and calnexin interact with different protein and glycan determinants during the assembly of MHC class I.

TL;DR: Evidence is presented that calreticulin clearly differs from calnexin in how it associates with class I and the structural basis of the association, the oligosaccharide moiety in the alpha1 domain and the amino acid residue at position 227 in thealpha3 domain were both found to be critical for the interaction of class I with cal reticulin.
Journal Article

TAP associates with a unique class I conformation, whereas calnexin associates with multiple class I forms in mouse and man

TL;DR: Open forms of Ld are uniquely and specifically associated with TAP and that the conformational change in the class I H chain coincident with peptide binding induces TAP release, and a model for the sequential assembly of class I heterotrimers and their respective interactions with T AP and calnexin is proposed.