In vitro amplification of prions from milk in the detection of subclinical infections [0.03%]
体外法从乳汁中扩增致病蛋白以检测亚临床期感染
Kevin C Gough,Claire A Baker,Maged Taema et al.
Kevin C Gough et al.
Prions can be amplified by serial protein misfolding cyclic amplification (sPMCA) from the milk of a high proportion of apparently healthy, scrapie exposed sheep with PRNP genotypes not previously associated with high disease penetrance. Th...
Amyloid fibrils of human prion protein are spun and woven from morphologically disordered aggregates [0.03%]
人朊蛋白淀粉样原纤维由形态无序聚集体纺纱编织而成
Karin Almstedt,Sofie Nyström,K Peter R Nilsson et al.
Karin Almstedt et al.
Propagation and infectivity of prions in human prionopathies are likely associated with conversion of the mainly alpha-helical human prion protein, HuPrP, into an aggregated form with amyloid-like properties. Previous reports on efficient c...
Context dependent neuroprotective properties of prion protein (PrP) [0.03%]
朊病毒蛋白（PrP）的神经保护特性取决于情境因素的影响
Andrew D Steele,Zhipeng Zhou,Walker S Jackson et al.
Andrew D Steele et al.
Although it has been known for more than twenty years that an aberrant conformation of the prion protein (PrP) is the causative agent in prion diseases, the role of PrP in normal biology is undetermined. Numerous studies have suggested a pr...
Prion-like propagation of cytosolic protein aggregates: insights from cell culture models [0.03%]
胞质内蛋白质聚集体朊病毒样的传播：来自细胞培养模型的启示
Carmen Krammer,Hermann M Schätzl,Ina Vorberg
Carmen Krammer
Amyloid formation is a hallmark of several systemic and neurodegenerative diseases. Extracellular amyloid deposits or intracellular inclusions arise from the conformational transition of normally soluble proteins into highly ordered fibrill...
Is, indeed, the prion protein a Harlequin servant of "many" masters? [0.03%]
确然，朊病毒蛋白是一个服务于“许多”主人的哈勒昆仆人吗？
M Catia Sorgato,Caterina Peggion,Alessandro Bertoli
M Catia Sorgato
Tens of putative interacting partners of the cellular prion protein (PrP(C)) have been identified, yet the physiologic role of PrP(C) remains unclear. For the first time, however, a recent paper has demonstrated that the absence of PrP(C) p...
Giovanna R Mallucci
Giovanna R Mallucci
Synaptic dysfunction is a key process in the evolution of many neurodegenerative diseases, with synaptic loss preceding that of neuronal cell bodies. In Alzheimer, Huntington, and prion diseases early synaptic changes correlate with cogniti...
Katherine A B Kellett,Nigel M Hooper
Katherine A B Kellett
Alzheimer and prion diseases are neurodegenerative disorders characterised by the abnormal processing of amyloid-beta (Abeta) peptide and prion protein (PrP(C)), respectively. Recent evidence indicates that PrP(C) may play a critical role i...
Federico Benetti,Giuseppe Legname
Federico Benetti
Prions are responsible for a heterogeneous group of fatal neurodegenerative diseases. They can be sporadic, genetic, or infectious disorders involving post-translational modifications of the cellular prion protein (PrP(C)). Prions (PrP(Sc))...
Detection of protease-resistant cervid prion protein in water from a CWD-endemic area [0.03%]
在CWD流行区的水中检测蛋白酶抗性鹿PrP蛋白质
T A Nichols,Bruce Pulford,A Christy Wyckoff et al.
T A Nichols et al.
Chronic wasting disease (CWD) is the only known transmissible spongiform encephalopathy affecting free-ranging wildlife. Although the exact mode of natural transmission remains unknown, substantial evidence suggests that prions can persist ...
Lei Wang
Lei Wang
Protein aggregation is a widely observed phenomenon in human diseases, biopharmaceutical production, and biological research. Protein aggregates are generally classified as highly ordered, such as amyloid fibrils, or amorphous, such as bact...