PortalPublikationenUnderstanding the natural variability of prion diseases.

Understanding the natural variability of prion diseases.

Standard

Understanding the natural variability of prion diseases. / Geissen, Markus; Krasemann, Susanne; Matschke, Jakob; Glatzel, Markus.

in: VACCINE, Jahrgang 25, Nr. 30, 30, 2007, S. 5631-5636.

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

Harvard

Geissen, M, Krasemann, S, Matschke, J & Glatzel, M 2007, 'Understanding the natural variability of prion diseases.', VACCINE, Jg. 25, Nr. 30, 30, S. 5631-5636. https://doi.org/10.1016/j.vaccine.2007.02.041

APA

Geissen, M., Krasemann, S., Matschke, J., & Glatzel, M. (2007). Understanding the natural variability of prion diseases. VACCINE, 25(30), 5631-5636. [30]. https://doi.org/10.1016/j.vaccine.2007.02.041

Vancouver

Geissen M, Krasemann S, Matschke J, Glatzel M. Understanding the natural variability of prion diseases. VACCINE. 2007;25(30):5631-5636. 30. https://doi.org/10.1016/j.vaccine.2007.02.041

Bibtex

@article{cc14e40968cd49158e1cd184b220640b,
title = "Understanding the natural variability of prion diseases.",
abstract = "Prion diseases are a heterogeneous group of disorders with an invariably fatal disease course. Although various etiologies have been proposed it is apparent that at least a subset of these diseases are of infectious nature. An essential part of the infectious agent, termed the prion, is mainly composed of an abnormal isoform (PrP(Sc)) of a host-encoded normal cellular protein (PrP(C)). The molecular details of the pathophysiology of this group of diseases are unclear but the conversion of PrP(C) to PrP(Sc) plays a fundamental role. In all human prion diseases, PrP(Sc) is deposited in the central nervous system. These disorders include sporadic, genetic and acquired Creutzfeldt-Jakob disease. The molecular classification of human prion diseases is important in order to understand underlying disease mechanisms and for the development of novel therapy protocols. Current classification systems are based on the assessment of clinical presentation, genetic investigations, neuropathological findings and biochemical analysis of PrP(Sc).",
author = "Markus Geissen and Susanne Krasemann and Jakob Matschke and Markus Glatzel",
year = "2007",
doi = "10.1016/j.vaccine.2007.02.041",
language = "Deutsch",
volume = "25",
pages = "5631--5636",
journal = "VACCINE",
issn = "0264-410X",
publisher = "Elsevier BV",
number = "30",

}

RIS

TY - JOUR

T1 - Understanding the natural variability of prion diseases.

AU - Geissen, Markus

AU - Krasemann, Susanne

AU - Matschke, Jakob

AU - Glatzel, Markus

PY - 2007

Y1 - 2007

N2 - Prion diseases are a heterogeneous group of disorders with an invariably fatal disease course. Although various etiologies have been proposed it is apparent that at least a subset of these diseases are of infectious nature. An essential part of the infectious agent, termed the prion, is mainly composed of an abnormal isoform (PrP(Sc)) of a host-encoded normal cellular protein (PrP(C)). The molecular details of the pathophysiology of this group of diseases are unclear but the conversion of PrP(C) to PrP(Sc) plays a fundamental role. In all human prion diseases, PrP(Sc) is deposited in the central nervous system. These disorders include sporadic, genetic and acquired Creutzfeldt-Jakob disease. The molecular classification of human prion diseases is important in order to understand underlying disease mechanisms and for the development of novel therapy protocols. Current classification systems are based on the assessment of clinical presentation, genetic investigations, neuropathological findings and biochemical analysis of PrP(Sc).

AB - Prion diseases are a heterogeneous group of disorders with an invariably fatal disease course. Although various etiologies have been proposed it is apparent that at least a subset of these diseases are of infectious nature. An essential part of the infectious agent, termed the prion, is mainly composed of an abnormal isoform (PrP(Sc)) of a host-encoded normal cellular protein (PrP(C)). The molecular details of the pathophysiology of this group of diseases are unclear but the conversion of PrP(C) to PrP(Sc) plays a fundamental role. In all human prion diseases, PrP(Sc) is deposited in the central nervous system. These disorders include sporadic, genetic and acquired Creutzfeldt-Jakob disease. The molecular classification of human prion diseases is important in order to understand underlying disease mechanisms and for the development of novel therapy protocols. Current classification systems are based on the assessment of clinical presentation, genetic investigations, neuropathological findings and biochemical analysis of PrP(Sc).

U2 - 10.1016/j.vaccine.2007.02.041

DO - 10.1016/j.vaccine.2007.02.041

M3 - SCORING: Review

VL - 25

SP - 5631

EP - 5636

JO - VACCINE

JF - VACCINE

SN - 0264-410X

IS - 30

M1 - 30

ER -