H
Huayi Wang
Researcher at University of Texas Southwestern Medical Center
Publications - 14
Citations - 4056
Huayi Wang is an academic researcher from University of Texas Southwestern Medical Center. The author has contributed to research in topics: Necroptosis & Phosphorylation. The author has an hindex of 11, co-authored 13 publications receiving 3255 citations. Previous affiliations of Huayi Wang include Peking Union Medical College.
Papers
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Journal ArticleDOI
Mixed Lineage Kinase Domain-like Protein Mediates Necrosis Signaling Downstream of RIP3 Kinase
Liming Sun,Huayi Wang,Zhigao Wang,Sudan He,She Chen,Daohong Liao,Lai Wang,Jiacong Yan,Weilong Liu,Xiaoguang Lei,Xiaodong Wang +10 more
TL;DR: The identification of a small molecule called necrosulfonamide that specifically blocks necrosis downstream of RIP3 activation is reported, which implicate MLKL as a key mediator of necrosis signaling downstream of the kinase RIP3.
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Mixed Lineage Kinase Domain-like Protein MLKL Causes Necrotic Membrane Disruption upon Phosphorylation by RIP3
TL;DR: The development of a monoclonal antibody that specifically recognizes phosphorylated MLKL in cells dying of this pathway and in human liver biopsy samples from patients suffering from drug-induced liver injury is reported.
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A plug release mechanism for membrane permeation by MLKL.
TL;DR: The results suggest that the four-helix bundle mediates membrane breakdown during necroptosis and that the sixth helix acts as a plug that prevents opening of the bundle and is released upon RIP3 phosphorylation.
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Structural basis for the specific recognition of methylated histone H3 lysine 4 by the WD-40 protein WDR5.
TL;DR: The structure of WDR5 in complex with a dimethylated H3-K4 peptide and structural and biochemical studies presented here suggest another mode of recognition for the methylated histone tail.
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Structural basis for modulation of Kv4 K+ channels by auxiliary KChIP subunits.
Huayi Wang,Yan Yan,Qun Liu,Yanhua H. Huang,Yue Shen,Linjie Chen,Yi Chen,Qiuyue Yang,Quan Hao,KeWei Wang,Jijie Chai +10 more
TL;DR: The structure reveals a unique clamping action of the complex, in which a single KChIP1 molecule, as a monomer, laterally clamps two neighboring Kv4.3 N-termini in a 4:4 manner, forming an octamer.