scispace - formally typeset
J

James A. Mastrianni

Researcher at University of Chicago

Publications -  67
Citations -  10524

James A. Mastrianni is an academic researcher from University of Chicago. The author has contributed to research in topics: PRNP & Gene. The author has an hindex of 30, co-authored 64 publications receiving 9850 citations. Previous affiliations of James A. Mastrianni include National Institutes of Health & Hospital of the University of Pennsylvania.

Papers
More filters
Journal ArticleDOI

Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)

Daniel J. Klionsky, +2522 more
- 21 Jan 2016 - 
TL;DR: In this paper, the authors present a set of guidelines for the selection and interpretation of methods for use by investigators who aim to examine macro-autophagy and related processes, as well as for reviewers who need to provide realistic and reasonable critiques of papers that are focused on these processes.
Journal ArticleDOI

Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein

Glenn C. Telling, +7 more
- 06 Oct 1995 - 
TL;DR: The results demonstrate that PrPSc binds to PrPC in a region delimited by codons 96 to 167, and suggest that PrPC binds protein X through residues near the C-terminus, and argue that a species-specific macromolecule, provisionally designated protein X, participates in prion formation.
Journal ArticleDOI

Evidence for the Conformation of the Pathologic Isoform of the Prion Protein Enciphering and Propagating Prion Diversity

Glenn C. Telling, +9 more
- 20 Dec 1996 - 
TL;DR: The results presented indicate that the conformation of PrP sc functions as a template in directing the formation of nascent PrPSc and suggest a mechanism to explain strains of prions where diversity is encrypted in the conformed PrP Sc.
Journal ArticleDOI

A transmembrane form of the prion protein in neurodegenerative disease.

Ramanujan S. Hegde, +8 more
- 06 Feb 1998 - 
TL;DR: Aberrant regulation of protein biogenesis and topology at the endoplasmic reticulum can result in neurodegeneration.
Journal ArticleDOI

A novel human disease with abnormal prion protein sensitive to protease

Pierluigi Gambetti, +22 more
- 01 Jun 2008 - 
TL;DR: In this paper, the authors report a human disease characterized by the presence of detergent insoluble PrP that is predominantly sensitive to protease digestion and forms unusual immunohistochemical patterns.