L
Lei Wei
Researcher at Wuhan University
Publications - 320
Citations - 13830
Lei Wei is an academic researcher from Wuhan University. The author has contributed to research in topics: Cartilage & Osteoarthritis. The author has an hindex of 57, co-authored 304 publications receiving 11840 citations. Previous affiliations of Lei Wei include Rhode Island Hospital & Brown University.
Papers
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Journal ArticleDOI
Rho kinase in the regulation of cell death and survival.
Jianjian Shi,Lei Wei +1 more
TL;DR: This review, based on recent molecular, cellular, and animal studies, focuses on the current understanding of ROCK signaling in the regulation of apoptosis and highlights new findings from recently generated ROCK-deficient mice.
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Activation of Rho-associated coiled-coil protein kinase 1 (ROCK-1) by caspase-3 cleavage plays an essential role in cardiac myocyte apoptosis
Jiang Chang,Min Xie,Viraj R. Shah,Michael D. Schneider,Mark L. Entman,Lei Wei,Robert J. Schwartz +6 more
TL;DR: Data suggest an obligatory role for ROCK-1 cleavage in promoting apoptotic signals in myocardial hypertrophy and/or failure in human heart failure.
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Rho kinases play an obligatory role in vertebrate embryonic organogenesis
Lei Wei,Wilmer B. Roberts,Lu Wang,Miho Yamada,Shuxing Zhang,Zhiyong Zhao,Scott A. Rivkees,Robert J. Schwartz,Kyoko Imanaka-Yoshida +8 more
TL;DR: New biological functions for Rho kinases are revealed in regulating major morphogenetic events during early chick and mouse development.
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Targeted deletion of ROCK1 protects the heart against pressure overload by inhibiting reactive fibrosis
Ying Min Zhang,Jacqueline Bo,George E. Taffet,Jiang Chang,Jianjian Shi,Anilkumar K. Reddy,Lloyd H. Michael,Michael D. Schneider,Mark L. Entman,Robert J. Schwartz,Lei Wei +10 more
TL;DR: Results indicate that ROCK1 contributes to the development of cardiac fibrosis and induction of fibrogenic cytokines in cardiomyocytes in response to pathological stimuli.
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Expression and characterization of recombinant human angiotensin I-converting enzyme. Evidence for a C-terminal transmembrane anchor and for a proteolytic processing of the secreted recombinant and plasma enzymes
TL;DR: Results indicate that ACE is anchored to the plasma membrane by the predicted C-terminal transmembrane domain, and the secreted form is derived from the membrane-bound form by a post-translational proteolytic cleavage of the C- terminus of ACE.