Human prion diseases: molecular and clinical aspects.
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Human prion diseases: molecular and clinical aspects. / Glatzel, Markus; Stoeck, Katharina; Seeger, Harald; Lührs, Thorsten; Aguzzi, Adriano.
In: ARCH NEUROL-CHICAGO, Vol. 62, No. 4, 4, 2005, p. 545-552.Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review
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TY - JOUR
T1 - Human prion diseases: molecular and clinical aspects.
AU - Glatzel, Markus
AU - Stoeck, Katharina
AU - Seeger, Harald
AU - Lührs, Thorsten
AU - Aguzzi, Adriano
PY - 2005
Y1 - 2005
N2 - Compared with that of other human pathogens, the proposed replicative cycle of prions is disarmingly simple. It encompasses misfolding of a single protein, the cellular prion protein (PrPC), into a disease-associated form called PrPSc. This is followed by PrPSc aggregation and possibly fragmentation of aggregates, which may augment the number of replicative units. Although there is no formal proof of the correctness of this model, a wealth of evidence indicates that pathogen-encoded informational nucleic acids are dispensable for prion replication. Despite the simplicity of the replicative process, the human phenotypic range of prion diseases is extremely variable and includes the sporadic, inherited, and acquired forms of Creutzfeldt-Jakob disease. In addition, prion diseases occur in a wide range of animals and can be propagated within and between animal species. The present review article discusses current concepts and controversies surrounding the basic biological features of prions.
AB - Compared with that of other human pathogens, the proposed replicative cycle of prions is disarmingly simple. It encompasses misfolding of a single protein, the cellular prion protein (PrPC), into a disease-associated form called PrPSc. This is followed by PrPSc aggregation and possibly fragmentation of aggregates, which may augment the number of replicative units. Although there is no formal proof of the correctness of this model, a wealth of evidence indicates that pathogen-encoded informational nucleic acids are dispensable for prion replication. Despite the simplicity of the replicative process, the human phenotypic range of prion diseases is extremely variable and includes the sporadic, inherited, and acquired forms of Creutzfeldt-Jakob disease. In addition, prion diseases occur in a wide range of animals and can be propagated within and between animal species. The present review article discusses current concepts and controversies surrounding the basic biological features of prions.
M3 - SCORING: Zeitschriftenaufsatz
VL - 62
SP - 545
EP - 552
IS - 4
M1 - 4
ER -
