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Cellular and Molecular Mechanisms of Prion Disease

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Cellular and Molecular Mechanisms of Prion Disease. / Sigurdson, Christina J; Bartz, Jason C; Glatzel, Markus.

in: ANNU REV PATHOL-MECH, Jahrgang 14, 24.01.2019, S. 497-516.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Review › Forschung

Harvard

Sigurdson, CJ, Bartz, JC & Glatzel, M 2019, 'Cellular and Molecular Mechanisms of Prion Disease', ANNU REV PATHOL-MECH, Jg. 14, S. 497-516. https://doi.org/10.1146/annurev-pathmechdis-012418-013109

APA

Sigurdson, C. J., Bartz, J. C., & Glatzel, M. (2019). Cellular and Molecular Mechanisms of Prion Disease. ANNU REV PATHOL-MECH, 14, 497-516. https://doi.org/10.1146/annurev-pathmechdis-012418-013109

Vancouver

Sigurdson CJ, Bartz JC, Glatzel M. Cellular and Molecular Mechanisms of Prion Disease. ANNU REV PATHOL-MECH. 2019 Jan 24;14:497-516. https://doi.org/10.1146/annurev-pathmechdis-012418-013109

Bibtex

@article{eab87c385e034dcd9945bd7662ffb12f,
title = "Cellular and Molecular Mechanisms of Prion Disease",
abstract = "Prion diseases are rapidly progressive, incurable neurodegenerative disorders caused by misfolded, aggregated proteins known as prions, which are uniquely infectious. Remarkably, these infectious proteins have been responsible for widespread disease epidemics, including kuru in humans, bovine spongiform encephalopathy in cattle, and chronic wasting disease in cervids, the latter of which has spread across North America and recently appeared in Norway and Finland. The hallmark histopathological features include widespread spongiform encephalopathy, neuronal loss, gliosis, and deposits of variably sized aggregated prion protein, ranging from small, soluble oligomers to long, thin, unbranched fibrils, depending on the disease. Here, we explore recent advances in prion disease research, from the function of the cellular prion protein to the dysfunction triggering neurotoxicity, as well as mechanisms underlying prion spread between cells. We also highlight key findings that have revealed new therapeutic targets and consider unanswered questions for future research.",
keywords = "Journal Article, Neurodegenerative Diseases, Animals, Prion Diseases/etiology, Cattle, Humans, Prion Proteins/metabolism, Amyloid, Deer",
author = "Sigurdson, {Christina J} and Bartz, {Jason C} and Markus Glatzel",
year = "2019",
month = jan,
day = "24",
doi = "10.1146/annurev-pathmechdis-012418-013109",
language = "English",
volume = "14",
pages = "497--516",
journal = "ANNU REV PATHOL-MECH",
issn = "1553-4006",
publisher = "Annual Reviews Inc.",

}

RIS

TY - JOUR

T1 - Cellular and Molecular Mechanisms of Prion Disease

AU - Sigurdson, Christina J

AU - Bartz, Jason C

AU - Glatzel, Markus

PY - 2019/1/24

Y1 - 2019/1/24

N2 - Prion diseases are rapidly progressive, incurable neurodegenerative disorders caused by misfolded, aggregated proteins known as prions, which are uniquely infectious. Remarkably, these infectious proteins have been responsible for widespread disease epidemics, including kuru in humans, bovine spongiform encephalopathy in cattle, and chronic wasting disease in cervids, the latter of which has spread across North America and recently appeared in Norway and Finland. The hallmark histopathological features include widespread spongiform encephalopathy, neuronal loss, gliosis, and deposits of variably sized aggregated prion protein, ranging from small, soluble oligomers to long, thin, unbranched fibrils, depending on the disease. Here, we explore recent advances in prion disease research, from the function of the cellular prion protein to the dysfunction triggering neurotoxicity, as well as mechanisms underlying prion spread between cells. We also highlight key findings that have revealed new therapeutic targets and consider unanswered questions for future research.

AB - Prion diseases are rapidly progressive, incurable neurodegenerative disorders caused by misfolded, aggregated proteins known as prions, which are uniquely infectious. Remarkably, these infectious proteins have been responsible for widespread disease epidemics, including kuru in humans, bovine spongiform encephalopathy in cattle, and chronic wasting disease in cervids, the latter of which has spread across North America and recently appeared in Norway and Finland. The hallmark histopathological features include widespread spongiform encephalopathy, neuronal loss, gliosis, and deposits of variably sized aggregated prion protein, ranging from small, soluble oligomers to long, thin, unbranched fibrils, depending on the disease. Here, we explore recent advances in prion disease research, from the function of the cellular prion protein to the dysfunction triggering neurotoxicity, as well as mechanisms underlying prion spread between cells. We also highlight key findings that have revealed new therapeutic targets and consider unanswered questions for future research.

KW - Journal Article

KW - Neurodegenerative Diseases

KW - Animals

KW - Prion Diseases/etiology

KW - Cattle

KW - Humans

KW - Prion Proteins/metabolism

KW - Amyloid

KW - Deer

U2 - 10.1146/annurev-pathmechdis-012418-013109

DO - 10.1146/annurev-pathmechdis-012418-013109

M3 - SCORING: Review article

C2 - 30355150

VL - 14

SP - 497

EP - 516

JO - ANNU REV PATHOL-MECH

JF - ANNU REV PATHOL-MECH

SN - 1553-4006

ER -