Non-human primates in prion research.

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Non-human primates in prion research. / Krasemann, Susanne; Sikorska, Beata; Liberski, Paweł P; Glatzel, Markus.

In: FOLIA NEUROPATHOL, Vol. 50, No. 1, 1, 2012, p. 57-67.

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@article{ad7183fcfd06426387861f44b458b406,
title = "Non-human primates in prion research.",
abstract = "Prion diseases or transmissible spongiform encephalopathies are neurodegenerative disorders affecting a broad range of mammals including humans. Initially thought to be of viral origin, it became apparent that prion diseases are unique transmissible entities where a misfolded, highly stable conformer (PrPSc) of the host encoded prion protein (PrPC) represents an essential component of infectious {"}prions{"}. Prion diseases are mainly studied in rodents, yet several scientific breakthroughs in prion research can be attributed to prion research in primates. In this review we summarize and discuss how studies in non-human primates have advanced our knowledge on transmissibility, pathophysiology and tissue tropism of prions. We discuss assets of non-human primate and rodent models of prion disease pointing out alternatives to experiments in primates.",
keywords = "Animals, Humans, Prion Diseases/*etiology/*transmission, Animals, Humans, Prion Diseases/*etiology/*transmission",
author = "Susanne Krasemann and Beata Sikorska and Liberski, {Pawe{\l} P} and Markus Glatzel",
year = "2012",
language = "English",
volume = "50",
pages = "57--67",
journal = "FOLIA NEUROPATHOL",
issn = "1641-4640",
publisher = "Termedia Publishing House Ltd.",
number = "1",

}

RIS

TY - JOUR

T1 - Non-human primates in prion research.

AU - Krasemann, Susanne

AU - Sikorska, Beata

AU - Liberski, Paweł P

AU - Glatzel, Markus

PY - 2012

Y1 - 2012

N2 - Prion diseases or transmissible spongiform encephalopathies are neurodegenerative disorders affecting a broad range of mammals including humans. Initially thought to be of viral origin, it became apparent that prion diseases are unique transmissible entities where a misfolded, highly stable conformer (PrPSc) of the host encoded prion protein (PrPC) represents an essential component of infectious "prions". Prion diseases are mainly studied in rodents, yet several scientific breakthroughs in prion research can be attributed to prion research in primates. In this review we summarize and discuss how studies in non-human primates have advanced our knowledge on transmissibility, pathophysiology and tissue tropism of prions. We discuss assets of non-human primate and rodent models of prion disease pointing out alternatives to experiments in primates.

AB - Prion diseases or transmissible spongiform encephalopathies are neurodegenerative disorders affecting a broad range of mammals including humans. Initially thought to be of viral origin, it became apparent that prion diseases are unique transmissible entities where a misfolded, highly stable conformer (PrPSc) of the host encoded prion protein (PrPC) represents an essential component of infectious "prions". Prion diseases are mainly studied in rodents, yet several scientific breakthroughs in prion research can be attributed to prion research in primates. In this review we summarize and discuss how studies in non-human primates have advanced our knowledge on transmissibility, pathophysiology and tissue tropism of prions. We discuss assets of non-human primate and rodent models of prion disease pointing out alternatives to experiments in primates.

KW - Animals

KW - Humans

KW - Prion Diseases/etiology/transmission

KW - Animals

KW - Humans

KW - Prion Diseases/etiology/transmission

M3 - SCORING: Journal article

VL - 50

SP - 57

EP - 67

JO - FOLIA NEUROPATHOL

JF - FOLIA NEUROPATHOL

SN - 1641-4640

IS - 1

M1 - 1

ER -