Fibril fragmentation in amyloid assembly and cytotoxicity: when size matters [0.03%]
淀粉样蛋白聚集及细胞毒性的纤维断裂：大小的影响
Wei-Feng Xue,Andrew L Hellewell,Eric W Hewitt et al.
Wei-Feng Xue et al.
Amyloid assemblies are associated with several debilitating human disorders. Understanding the intra- and extracellular assembly of normally soluble proteins and peptides into amyloid aggregates and how they disrupt normal cellular function...
Mouse neuronal cells expressing exogenous bovine PRNP and simultaneous downregulation of endogenous mouse PRNP using siRNAs [0.03%]
表达外源牛PRNP并利用siRNAs同时下调内源小鼠PRNP的神经细胞系
Sang-Gyun Kang,Yu Mi Roh,Mi Lan Kang et al.
Sang-Gyun Kang et al.
Prion diseases, which are called transmissible spongiform encephalopathies (TSEs), comprise a group of fatal infectious neurodegenerative disorders. Investigation of prion strains and generation of species dependent TSE model are necessary ...
Fragment molecular orbital calculations reveal that the E200K mutation markedly alters local structural stability in the human prion protein [0.03%]
片段分子轨道计算显示E200K变异显著改变人朊病毒蛋白局部结构稳定性
Koji Hasegawa,Shirou Mohri,Takashi Yokoyama
Koji Hasegawa
The E200K mutation of the human prion protein (PrP) is known to cause familial Creutzfeldt-Jakob disease. In order to elucidate the effects of the mutation on the local structural stability of PrP, we performed ab initio fragment molecular ...
Interdependence of amyloid formation in yeast: implications for polyglutamine disorders and biological functions [0.03%]
酵母中淀粉样蛋白形成的互依性：对聚谷氨酰胺障碍及生物功能的启示
Valery N Urakov,Aleksandra B Vishnevskaya,Ilya M Alexandrov et al.
Valery N Urakov et al.
In eukaryotic cells amyloid aggregates may incorporate various functionally unrelated proteins. In mammalian diseases this may cause amyloid toxicity, while in yeast this could contribute to prion phenotypes. Insolubility of amyloids in the...
Miroslav Hodak,Jerzy Bernholc
Miroslav Hodak
Computer simulations are a powerful tool for studies of biological systems. They have often been used to study prion protein (PrP), a protein responsible for neurodegenerative diseases, which include "mad cow disease" in cattle and Creutzfe...
Diego E Rincon-Limas,Sergio Casas-Tinto,Pedro Fernandez-Funez
Diego E Rincon-Limas
The fruit fly Drosophila melanogaster has been a favored tool for genetic studies for over 100 years and has become an excellent model system to study development, signal transduction, cell biology, immunity and behavior. The relevance of D...
Pyrroloquinoline quinone inhibits the fibrillation of amyloid proteins [0.03%]
吡咯喹啉醌抑制淀粉样蛋白的聚集成熟转动免疫荧光酶免疫吸附症褪黑素抗氧化活性微管相关蛋白tauß-片层结构乙醇提取物海马神经元非诺贝特氧化应激原纤维多巴胺皮质宁甘油磷酯脑心清注射液细胞活力PC12细胞线粒体动力学BQ10抑制剂分子伴侣前驱蛋白C端片段突变型毒性果 fly 果 fly 神经毒性果 flyTauP301L过表达模型N-末端结构域内质网应激自噬活化聚集毒性的双相调控亚micromolar浓度下保护神经元免疫共沉淀实验pull down实验原纤维的形成寡聚态可溶性毒性中间体多聚态不溶性毒性团块
Jihoon Kim,Masaki Kobayashi,Makoto Fukuda et al.
Jihoon Kim et al.
Several neurodegenerative diseases involve the selective damage of neuron cells resulting from the accumulation of amyloid fibril formation. Considering that the formation of amyloid fibrils as well as their precursor oligomers is cytotoxic...
New insights into the molecular mechanism of amyloid formation from cysteine scanning [0.03%]
基于半胱氨酸扫描的蛋白质分子开关新机制及其调控的淀粉样纤维化作用研究
Li Fei,Sarah Perrett
Li Fei
Our laboratory recently reported the identification of a peptide region, QVNI, within the prion domain of the yeast protein Ure2 that may act as an initiation point for fibril formation.(1) This potential amyloid-forming region, which corre...
Localization of prion-destabilizing mutations in the N-terminal non-prion domain of Rnq1 in Saccharomyces cerevisiae [0.03%]
酿酒酵母RNQ1的N端非朊毒结构域中朊病毒去稳定的变异定位
Shoichiro Shibata,Hiroshi Kurahashi,Yoshikazu Nakamura
Shoichiro Shibata
[PIN(+)] is the prion form of Rnq1 in Saccharomyces cerevisiae and is necessary for the de novo induction of a second prion, [PSI(+)]. The function of Rnq1, however, is little understood. The limited availability of defective rnq1 alleles i...
Natalia Fernández-Borges,Jorge de Castro,Joaquín Castilla
Natalia Fernández-Borges
Protein Misfolding Cyclic Amplification (PMCA) has proved to be an efficient method mimicking in vitro some of the fundamental steps involved in prion replication in vivo. Thus, it can be used to efficiently replicate a variety of prion str...