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Wencheng Xia
Researcher at Chinese Academy of Sciences
Publications - 19
Citations - 219
Wencheng Xia is an academic researcher from Chinese Academy of Sciences. The author has contributed to research in topics: Fibril & Medicine. The author has an hindex of 3, co-authored 7 publications receiving 22 citations.
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Journal ArticleDOI
Hsp40 proteins phase separate to chaperone the assembly and maintenance of membraneless organelles.
Jinge Gu,Zhenying Liu,Shengnan Zhang,Yang Li,Wencheng Xia,Chen Wang,Huaijiang Xiang,Zhijun Liu,Li Tan,Yanshan Fang,Cong Liu,Dan Li +11 more
TL;DR: It is suggested that phase separation is an intrinsic property of Hsp40 proteins, which enables efficient incorporation and function of HSp40 in membraneless organelles and may further mediate the buildup of chaperone network in membrAneless organlles.
Journal ArticleDOI
Liquid-liquid phase separation of RBGD2/4 is required for heat stress resistance in Arabidopsis.
Shaobo Zhu,Jinge Gu,Juanjuan Yao,Yichen Li,Zheting Zhang,Wencheng Xia,Zhen Wang,Xinrui Gui,Lei Li,Dan Li,Heng Zhang,Cong Liu +11 more
TL;DR: In this article , two RNA-binding proteins, RBGD2 and RBGD4, function redundantly to improve heat resistance in Arabidopsis and showed that modifying these proteins by mutating TRA abolishes their condensation in SGs and impairs their protective function against heat stress.
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The nuclear localization sequence mediates hnRNPA1 amyloid fibril formation revealed by cryoEM structure.
Yunpeng Sun,Kun Zhao,Wencheng Xia,Guoqin Feng,Jinge Gu,Yeyang Ma,Xinrui Gui,Xia Zhang,Yanshan Fang,Bo Sun,Renxiao Wang,Renxiao Wang,Cong Liu,Dan Li +13 more
TL;DR: Cryo-electron microscopy is used to determine the amyloid fibril structure formed by hnRNPA1 LC domain and reveals that the nuclear localization sequence of hn RNPA1 (termed PY-NLS), which is initially known to mediate the nucleo-cytoplamic transport of hsRNA A1 through binding with karyopherin-β2 (Kapβ2), represents the major component of the fibrils core.
Journal ArticleDOI
The hereditary mutation G51D unlocks a distinct fibril strain transmissible to wild-type α-synuclein.
Yunpeng Sun,Houfang Long,Wencheng Xia,Kun Wang,Xia Zhang,Bo Sun,Qin Cao,Yaoyang Zhang,Bin Dai,Dan Li,Cong Liu +10 more
TL;DR: In this paper, the structure of the G51D alpha-synuclein fibril was determined using a 2.96 angstrom resolution, which is a relatively small and extended serpentine fold.
Journal ArticleDOI
Wild-type α-synuclein inherits the structure and exacerbated neuropathology of E46K mutant fibril strain by cross-seeding
Houfang Long,Weitong Zheng,Yang Liu,Yunpeng Sun,Kun Zhao,Zhenying Liu,Wencheng Xia,Shiran Lv,Zhengtao Liu,Dan Li,Kaiwen He,Cong Liu +11 more
TL;DR: In this paper, the interplay between hereditary mutant and wild-type α-syn and its role in the exacerbated pathology of αsyn in fPD progression is poorly understood, and the authors find that WT mice inoculated with the human E46K mutant αsyn fibril (hE46K) strain develop early onset and rapid progression of familial Parkinson's diseases (fPD).