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Cong Yu
Researcher at Southern University of Science and Technology
Publications - 25
Citations - 982
Cong Yu is an academic researcher from Southern University of Science and Technology. The author has contributed to research in topics: Ankyrin & Scaffold protein. The author has an hindex of 12, co-authored 25 publications receiving 764 citations. Previous affiliations of Cong Yu include Hong Kong University of Science and Technology & South University of Science and Technology of China.
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Journal ArticleDOI
Structural basis of kindlin-mediated integrin recognition and activation
Huadong Li,Yi Deng,Kang Sun,Haibin Yang,Haibin Yang,Jie Liu,Meiling Wang,Zhang Zhang,Jirong Lin,Chuanyue Wu,Chuanyue Wu,Zhiyi Wei,Zhiyi Wei,Cong Yu +13 more
TL;DR: The structural, biochemical, and cellular results provide mechanistic explanations that account for the effects of kindlins on integrin activation as well as for how kindlin mutations found in patients with Kindler syndrome and leukocyte-adhesion deficiency may impact integrin-mediated processes.
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DISC1 Regulates Neurogenesis via Modulating Kinetochore Attachment of Ndel1/Nde1 during Mitosis
Fei Ye,Eunchai Kang,Eunchai Kang,Chuan Yu,Xuyu Qian,Xuyu Qian,Fadi Jacob,Fadi Jacob,Cong Yu,Mao Mao,Randy Yat Choi Poon,Jieun Kim,Hongjun Song,Guo Li Ming,Mingjie Zhang +14 more
TL;DR: This study solves the high-resolution structure of DISC1 C-terminal tail in complex with its binding domain of Ndel1 and uncovers a new mechanism of action based on its structure, and it has implications for how genetic insults may contribute to psychiatric disorders.
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Myosin VI Undergoes Cargo-Mediated Dimerization
TL;DR: The high-resolution NMR structure of the cargo-free myosin VI cargo-binding domain (CBD) is reported and it is shown that it is a stable monomer in solution and may represent a general paradigm for the regulation of processivity for myOSin VI as well as other myosins, including myosIn VII and myos in X.
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Autoinhibition of UNC5b Revealed by the Cytoplasmic Domain Structure of the Receptor
TL;DR: The crystal structure of the cytoplasmic portion of UNC5b is determined, finding that it contains three distinctly folded domains, namely ZU5, UPA, and death domain (DD), which form a structural supramodule that leads to the activation of the receptor in the promotion of apoptosis and blood vessel patterning.
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Liprin-mediated large signaling complex organization revealed by the liprin-α/CASK and liprin-α/liprin-β complex structures.
Zhiyi Wei,Suilan Zheng,Samantha A. Spangler,Cong Yu,Casper C. Hoogenraad,Casper C. Hoogenraad,Mingjie Zhang +6 more
TL;DR: It is demonstrated that three recently identified X-linked mental retardation mutants of CASK are defective in binding to liprin-α, suggesting that liprins can mediate assembly of target proteins into large protein complexes capable of regulating numerous cellular activities.