Modulation and elimination of yeast prions by protein chaperones and co-chaperones [0.03%]
蛋白质分子伴侣和辅助因子对酵母朊病毒的调控作用
Michael Reidy,Daniel C Masison
Michael Reidy
The yeast system has provided considerable insight into the biology of amyloid and prions. Here we focus on how alterations in abundance or function of protein chaperones and co-chaperones affect propagation of yeast prions. In spite of a c...
Kyle S MacLea,Eric D Ross
Kyle S MacLea
The unexpected discovery of two prions, [URE3] and [PSI+], in Saccharomyces cerevisiae led to questions about how many other proteins could undergo similar prion-based structural conversions. However, [URE3] and [PSI+] were discovered by se...
Modeling Huntington disease in yeast: perspectives and future directions [0.03%]
酵母中的亨廷顿舞蹈病建模：前景与未来方向
Robert P Mason,Flaviano Giorgini
Robert P Mason
Yeast have been extensively used to model aspects of protein folding diseases, yielding novel mechanistic insights and identifying promising candidate therapeutic targets. In particular, the neurodegenerative disorder Huntington disease (HD...
Yeast prions assembly and propagation: contributions of the prion and non-prion moieties and the nature of assemblies [0.03%]
芽殖酵母prion蛋白的聚集及传播：prion和非prion结构域的作用以及聚合体的性质
Mehdi Kabani,Ronald Melki
Mehdi Kabani
Yeast prions are self-perpetuating protein aggregates that are at the origin of heritable and transmissible non-Mendelian phenotypic traits. Among these, [PSI+], [URE3] and [PIN+] are the most well documented prions and arise from the assem...
Martin L Duennwald
Martin L Duennwald
Protein misfolding is associated with many human diseases, including neurodegenerative diseases, such as Alzheimer disease, Parkinson disease and Huntington disease. Protein misfolding often results in the formation of intracellular or extr...
The [RNQ+] prion: a model of both functional and pathological amyloid [0.03%]
[RNQ+]毒蛋白：功能性和病理性淀粉样纤维模型的例子
Kevin C Stein,Heather L True
Kevin C Stein
The formation of fibrillar amyloid is most often associated with protein conformational disorders such as prion diseases, Alzheimer disease and Huntington disease. Interestingly, however, an increasing number of studies suggest that amyloid...
Agnès Baudin-Baillieu,Céline Fabret,Olivier Namy
Agnès Baudin-Baillieu
The [PSI+] determinant in Saccharomyces cerevisiae is the prion protein corresponding to the eRF3 translation termination factor. Numerous infectious proteins have been described in yeast, in comparison of the unique PrP protein in higher e...
Site-specific structural analysis of a yeast prion strain with species-specific seeding activity [0.03%]
具有物种特异性种子活性的酵母芽殖菌株的位点特异性结构分析
Anna Marie Marcelino-Cruz,Moumita Bhattacharya,Aaron C Anselmo et al.
Anna Marie Marcelino-Cruz et al.
Prion proteins misfold and aggregate into multiple infectious strain variants that possess unique abilities to overcome prion species barriers, yet the structural basis for the species-specific infectivities of prion strains is poorly under...
Can prion disease suspicion be supported earlier? Clinical, radiological and laboratory findings in a series of cases [0.03%]
朊毒病临床、影像及实验室指标的早期征兆：一系列病例报道
Alejandra González-Duarte,Zaira Medina,Rainier Rodriguez Balaguer et al.
Alejandra González-Duarte et al.
The subacute spongiform encephalopathies are prion diseases characterized by acute and rapid neurodegeneration that lead to the death of the patient within months to a few years. The epidemiology of CJD is complicated and the frequency in M...
Case Reports
Prion. 2011 Jul-Sep;5(3):201-7. DOI:10.4161/pri.5.3.16187 2011
Comparative analysis of essential collective dynamics and NMR-derived flexibility profiles in evolutionarily diverse prion proteins [0.03%]
来自进化上具有多样性的朊病毒蛋白的本质集体动力学和核磁共振解析的柔韧性谱系的比较分析
Kolattukudy P Santo,Mark Berjanskii,David S Wishart et al.
Kolattukudy P Santo et al.
Collective motions on ns-μs time scales are known to have a major impact on protein folding, stability, binding and enzymatic efficiency. It is also believed that these motions may have an important role in the early stages of prion protei...
Comparative Study
Prion. 2011 Jul-Sep;5(3):188-200. DOI:10.4161/pri.5.3.16097 2011