Understanding the natural variability of prion diseases.
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Understanding the natural variability of prion diseases. / Geissen, Markus; Krasemann, Susanne; Matschke, Jakob; Glatzel, Markus.
In: VACCINE, Vol. 25, No. 30, 30, 2007, p. 5631-5636.Research output: SCORING: Contribution to journal › SCORING: Review article › Research
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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 -