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Gregory J. Raymond
National Institutes of Health
54Publications
30H-index
6,257Citations
Publications 55
Newest
#1Eric MinikelH-Index: 12
#2Eric KuhnH-Index: 16
Last.Steven A. CarrH-Index: 18
view all 16 authors...
2 CitationsSource
#1Zerui Wang (Case Western Reserve University)H-Index: 2
#2Matteo Manca (NIH: National Institutes of Health)H-Index: 6
Last.Wen-Quan ZouH-Index: 29
view all 25 authors...
The original version of this Article contained errors in the author affiliations. Affiliation 2 incorrectly read ‘Department of Neurology, The First Hospital of Jilin University, Changchun 130021 Jilin Province, China.’Affiliation 5 incorrectly read ‘Department of Otolaryngology, The First Affiliated Hospital of Xi’an Jiaotong University, Xi’an 710061 Shanxi Province, China’Affiliation 9 incorrectly read ‘State Key Laboratory for Infectious Disease Prevention and Control, National Institute for ...
Source
#1Zerui Wang (Case Western Reserve University)H-Index: 2
#2Matteo Manca (NIH: National Institutes of Health)H-Index: 6
Last.Wen-Quan ZouH-Index: 29
view all 25 authors...
A definitive pre-mortem diagnosis of prion disease depends on brain biopsy for prion detection currently and no validated alternative preclinical diagnostic tests have been reported to date. To determine the feasibility of using skin for preclinical diagnosis, here we report ultrasensitive serial protein misfolding cyclic amplification (sPMCA) and real-time quaking-induced conversion (RT-QuIC) assays of skin samples from hamsters and humanized transgenic mice (Tg40h) at different time points aft...
2 CitationsSource
#1Gregory J. RaymondH-Index: 30
#2Hien ZhaoH-Index: 4
Last.Sonia M. VallabhH-Index: 4
view all 22 authors...
Prion disease is a fatal, incurable neurodegenerative disease of humans and other mammals caused by conversion of cellular prion protein (PrPC) into a self-propagating neurotoxic conformer (prions; PrPSc). Strong genetic proofs of concept support lowering PrP expression as a therapeutic strategy. Antisense oligonucleotides (ASOs) can provide a practical route to lowering 1 target mRNA in the brain, but their development for prion disease has been hindered by 3 unresolved issues from prior work: ...
4 CitationsSource
#1Eric Minikel (Broad Institute)H-Index: 12
#2Eric Kuhn (Broad Institute)H-Index: 16
Last.Steven A. Carr (Broad Institute)H-Index: 18
view all 16 authors...
Therapies currently in preclinical development for prion disease seek to lower prion protein (PrP) expression in the brain. Trials of such therapies are likely to rely on quantification of PrP in cerebrospinal fluid (CSF) as a pharmacodynamic biomarker and possibly as a trial endpoint. Studies using PrP ELISA kits have reproducibly shown that CSF PrP is lowered in the symptomatic phase of disease, a potential confounder for reading out the effect of PrP-lowering drugs in symptomatic patients. To...
1 CitationsSource
#1Allison KrausH-Index: 10
#2Gregory J. RaymondH-Index: 30
Last.Byron CaugheyH-Index: 67
view all 8 authors...
ABSTRACT Accumulation of fibrillar protein aggregates is a hallmark of many diseases. While numerous proteins form fibrils by prion-like seeded polymerization in vitro , only some are transmissible and pathogenic in vivo . To probe the structural features that confer transmissibility to prion protein (PrP) fibrils, we have analyzed synthetic PrP amyloids with or without the human prion disease-associated P102L mutation. The formation of infectious prions from PrP molecules in vitro has required ...
2 CitationsSource
#1Bradley R. Groveman (NIH: National Institutes of Health)H-Index: 17
#2Gregory J. Raymond (NIH: National Institutes of Health)H-Index: 30
Last.Byron Caughey (NIH: National Institutes of Health)H-Index: 67
view all 10 authors...
Mammalian prion structures and replication mechanisms are poorly understood. Most synthetic recombinant prion protein (rPrP) amyloids prepared without cofactors are non-infectious or much less infectious than bona fide tissue-derived PrPSc. This effect has been associated with differences in folding of the aggregates, manifested in part by reduced solvent exclusion and protease-resistance in rPrP amyloids, especially within residues ~90–160. Substitution of 4 lysines within residues 101–110 of r...
9 CitationsSource
#1Byron Caughey (NIH: National Institutes of Health)H-Index: 67
#2Christina D. Orrú (NIH: National Institutes of Health)H-Index: 20
Last.Gianluigi Zanusso (University of Verona)H-Index: 32
view all 12 authors...
1 CitationsSource
#1Christina D. Orrú (NIH: National Institutes of Health)H-Index: 20
#2Bradley R. Groveman (NIH: National Institutes of Health)H-Index: 17
Last.Byron Caughey (NIH: National Institutes of Health)H-Index: 67
view all 10 authors...
11 CitationsSource
#1Gerald S. Baron (NIH: National Institutes of Health)H-Index: 21
#2Gregory J. Raymond (NIH: National Institutes of Health)H-Index: 30
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