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Troy T. Rohn

Researcher at Boise State University

Publications -  64
Citations -  8961

Troy T. Rohn is an academic researcher from Boise State University. The author has contributed to research in topics: Caspase & Apolipoprotein E. The author has an hindex of 30, co-authored 61 publications receiving 8153 citations.

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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.
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Caspase-cleavage of tau is an early event in Alzheimer disease tangle pathology

TL;DR: It is demonstrated that tau is cleaved at D421 (DeltaTau) by executioner caspases, and therapeutics aimed at inhibiting tau caspase-cleavage may prove beneficial not only in preventing NFT formation, but also in slowing cognitive decline.
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Passive Immunization Reduces Behavioral and Neuropathological Deficits in an Alpha-Synuclein Transgenic Model of Lewy Body Disease

TL;DR: 9E4 was effective at reducing behavioral deficits in the water maze and immunization with 9E4 reduced the accumulation of calpain-cleaved α-syn in axons and synapses and the associated neurodegenerative deficits, suggesting that passive immunizations with monoclonal antibodies may be of therapeutic relevance in patients with PD and DLB.
Journal ArticleDOI

Caspase-9 activation and caspase cleavage of tau in the Alzheimer's disease brain

TL;DR: A quantitative analysis indicates that as the number of neurons containing neurofibrillary tangles (NFTs) increases, the extent of caspase-9 activation decreases, supporting the idea that caspases and cleavage of tau may precede NFT formation.
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Calpain-Cleavage of α-Synuclein : Connecting Proteolytic Processing to Disease-Linked Aggregation

TL;DR: It is demonstrated that proteolytic processing of α-Syn by the protease calpain I leads to the formation of aggregated high-molecular weight species and adoption of a β-sheet structure, which suggests that cal pain I may participate in the disease-linked aggregation ofα-Syn in various α-synucleinopathies.