The environmental dependency of protein folding best explains prion and amyloid diseases.
作者信息
Kelly J W
机构信息
The Skaggs Institute of Chemical Biology and The Department of Chemistry, The Scripps Research Institute, 10550 North Torrey Pines Road MB 12, La Jolla, CA 92037, USA.
出版信息
Proc Natl Acad Sci U S A. 1998 Feb 3;95(3):930-2. doi: 10.1073/pnas.95.3.930.
Abstract
摘要
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本文引用的文献
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Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible.重组全长仓鼠朊病毒蛋白PrP(29 - 231)的结构：N端具有高度灵活性。
Proc Natl Acad Sci U S A. 1997 Dec 9;94(25):13452-7. doi: 10.1073/pnas.94.25.13452.
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The chemistry of scrapie infection: implications of the 'ice 9' metaphor.羊瘙痒病感染的化学原理：“冰九”隐喻的启示
Chem Biol. 1995 Jan;2(1):1-5. doi: 10.1016/1074-5521(95)90074-8.
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Prion diseases and the BSE crisis.朊病毒疾病与疯牛病危机。
Science. 1997 Oct 10;278(5336):245-51. doi: 10.1126/science.278.5336.245.
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Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform.与羊瘙痒病同种型感染性片段相对应的142个残基重组朊病毒蛋白的溶液结构。
Proc Natl Acad Sci U S A. 1997 Sep 16;94(19):10086-91. doi: 10.1073/pnas.94.19.10086.
5
NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231).全长重组小鼠朊病毒蛋白mPrP(23 - 231)的核磁共振表征
FEBS Lett. 1997 Aug 18;413(2):282-8. doi: 10.1016/s0014-5793(97)00920-4.
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Engineering peptides and proteins that undergo alpha-to-beta transitions.设计经历从α结构向β结构转变的肽和蛋白质。
Curr Opin Struct Biol. 1997 Aug;7(4):501-8. doi: 10.1016/s0959-440x(97)80113-3.
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Amyloid fibril formation and protein misassembly: a structural quest for insights into amyloid and prion diseases.淀粉样纤维形成与蛋白质错误组装：对淀粉样蛋白和朊病毒疾病认识的结构探索
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Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis.淀粉样纤维形成背后的人溶菌酶变体的不稳定性、解折叠和聚集。
Nature. 1997 Feb 27;385(6619):787-93. doi: 10.1038/385787a0.
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Alzheimer's disease: genotypes, phenotypes, and treatments.阿尔茨海默病：基因型、表型与治疗方法
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10
Molecular biology and pathogenesis of prion diseases.朊病毒疾病的分子生物学与发病机制。
Trends Biochem Sci. 1996 Dec;21(12):482-7. doi: 10.1016/s0968-0004(96)10063-3.
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