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Updated: Feb 22, 2026

Generation of Native, Untagged Huntingtin Exon1 Monomer and Fibrils Using a SUMO Fusion Strategy
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Generation of Native, Untagged Huntingtin Exon1 Monomer and Fibrils Using a SUMO Fusion Strategy

Published on: June 27, 2018

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单体亨廷丁外子1具有与野生类型和病态多重胺长度相似的整体结构特征

John B Warner1, Kiersten M Ruff2, Piau Siong Tan3

  • 1Laboratory of Molecular and Chemical Biology of Neurodegeneration, Brain Mind Institute, Station 19, School of Life Sciences, Ecole Polytechnique Fédérale de Lausanne (EPFL) , CH-1015 Lausanne, Switzerland.

Journal of the American Chemical Society
|September 23, 2017
PubMed
概括

亨廷顿病的研究显示单体亨廷丁蛋白质不会急剧改变形状. 相反,较长的多重胺 (polyQ) 链导致持续的紧缩,这表明细胞相互作用推动了疾病的进展.

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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
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