نتایج جستجو برای: prion disease

تعداد نتایج: 1496086  

2013
Teresa M Gunn George A Carlson

While the conversion of the normal form of prion protein to a conformationally distinct pathogenic form is recognized to be the primary cause of prion disease, it is not clear how this leads to spongiform change, neuronal dysfunction and death. Mahogunin ring finger-1 (Mgrn1) and Attractin (Atrn) null mutant mice accumulate vacuoles throughout the brain that appear very similar to those associa...

Journal: :Genome Biology 2001

Journal: :European Journal of Human Genetics 2006

Journal: :Brain : a journal of neurology 2010
Ichiro Nozaki Tsuyoshi Hamaguchi Nobuo Sanjo Moeko Noguchi-Shinohara Kenji Sakai Yosikazu Nakamura Takeshi Sato Tetsuyuki Kitamoto Hidehiro Mizusawa Fumio Moriwaka Yusei Shiga Yoshiyuki Kuroiwa Masatoyo Nishizawa Shigeki Kuzuhara Takashi Inuzuka Masatoshi Takeda Shigetoshi Kuroda Koji Abe Hiroyuki Murai Shigeo Murayama Jun Tateishi Ichiro Takumi Susumu Shirabe Masafumi Harada Atsuko Sadakane Masahito Yamada

We analysed the epidemiological data and clinical features of patients with prion diseases that had been registered by the Creutzfeldt-Jakob Disease Surveillance Committee, Japan, over the past 10 years, since 1999. We obtained information on 1685 Japanese patients suspected as having prion diseases and judged that 1222 patients had prion diseases, consisting of definite (n=180, 14.7%) and prob...

2015
Kevin C. Gough Helen C. Rees Sarah E. Ives Ben C. Maddison Christian D. Doerig

Prions are an enigma amongst infectious disease agents as they lack a genome yet confer specific pathologies thought to be dictated mainly, if not solely, by the conformation of the disease form of the prion protein (PrP(Sc)). Prion diseases affect humans and animals, the latter including the food-producing ruminant species cattle, sheep, goats and deer. Importantly, it has been shown that the ...

Journal: :Communications biology 2021

Abstract Prion diseases are distinguished by long pre-clinical incubation periods during which prions actively propagate in the brain and cause neurodegeneration. In stage, we hypothesize that upon prion infection, transcriptional changes occur can lead to early A longitudinal analysis of miRNAs clinical forms murine disease demonstrated dynamic expression progression affected thalamus region s...

Journal: :Folia neuropathologica 2012
James Hope Louise Kirby

Prion-like transmission of protein aggregates or amyloid in several neurodegenerative diseases, such as Parkinson's disease, Huntington's disease and Alzheimer's disease, in addition to the transmissible spongiform encephalopathies (or prion diseases), has been proposed recently. This is a controversial idea and, in this paper, we consider what we mean by a "prion", and by "amyloid", and presen...

Journal: :Journal of virology 2011
Mikael Klingeborn Brent Race Kimberly D Meade-White Rebecca Rosenke James F Striebel Bruce Chesebro

In nature prion diseases are usually transmitted by extracerebral prion infection, but clinical disease results only after invasion of the central nervous system (CNS). Prion protein (PrP), a host-encoded glycosylphosphatidylinositol (GPI)-anchored membrane glycoprotein, is necessary for prion infection and disease. Here, we investigated the role of the anchoring of PrP on prion neuroinvasion b...

2010
Laura D'Castro Adam Wenborn Nathalie Gros Susan Joiner Sabrina Cronier John Collinge Jonathan D. F. Wadsworth

Disease-related prion protein, PrP(Sc), is classically distinguished from its normal cellular precursor, PrP(C), by its detergent insolubility and partial resistance to proteolysis. Molecular diagnosis of prion disease typically relies upon detection of protease-resistant fragments of PrP(Sc) using proteinase K, however it is now apparent that the majority of disease-related PrP and indeed prio...

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