P
Per A. Peterson
Researcher at Scripps Research Institute
Publications - 356
Citations - 36377
Per A. Peterson is an academic researcher from Scripps Research Institute. The author has contributed to research in topics: Antigen & Major histocompatibility complex. The author has an hindex of 102, co-authored 356 publications receiving 35788 citations. Previous affiliations of Per A. Peterson include General Atomics & University of Dundee.
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Journal ArticleDOI
An αβ T cell receptor structure at 2.5 Å and its orientation in the TCR-MHC complex
K. Christopher Garcia,Massimo Degano,Robyn L. Stanfield,Anders Brunmark,Michael R. Jackson,Per A. Peterson,Luc Teyton,Ian A. Wilson +7 more
TL;DR: In this article, the x-ray structure of the complete extracellular fragment of a glycosylated αβ T cell receptor (TCR) was determined at 2.5 angstroms, and its orientation bound to a class I MHC-peptide (pMHC) complex was elucidated from crystals of the TCR- pMHC complex.
Journal ArticleDOI
Identification of a consensus motif for retention of transmembrane proteins in the endoplasmic reticulum.
TL;DR: In this paper, the retention motifs of transmembrane endoplasmic reticulum (ER) proteins were identified as a retrieval signal that brought proteins back from a sorting compartment adjacent to the ER.
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Crystal structures of two viral peptides in complex with murine MHC class I H-2Kb.
TL;DR: Small but significant conformational changes in H-2Kb are associated with peptide binding, and these synergistic movements may be an integral part of the T cell receptor recognition process.
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β-Amyloid1–42 Binds to α7 Nicotinic Acetylcholine Receptor with High Affinity IMPLICATIONS FOR ALZHEIMER'S DISEASE PATHOLOGY
Hoau-Yan Wang,Daniel H. S. Lee,Michael R. D'Andrea,Per A. Peterson,Richard P. Shank,Allen B. Reitz +5 more
TL;DR: It is proposed that interaction of the α7nAChR and Aβ1–42 is a pivotal mechanism involved in the pathophysiology of Alzheimer's disease.
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Emerging principles for the recognition of peptide antigens by MHC class I molecules
TL;DR: The structures of the peptide-binding specificity pockets in the groove of murine H-2Kb as well as human histocompatibility antigen class I molecules have been analyzed and usage of a limited number of both deep and shallow pockets in multiple combinations appears to allow the binding of a broad range of peptides.