25 Papers
86 Citations
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. 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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Papers
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.
161
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.
156
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.
131
Structural basis of diverse membrane target recognitions by ankyrins
Chao Wang,Zhiyi Wei,Zhiyi Wei,Keyu Chen,Fei Ye,Cong Yu,Cong Yu,Vann Bennett,Vann Bennett,Mingjie Zhang +9 more
TL;DR: The structures of ANK repeats in complex with an inhibitory segment from the C-terminal regulatory domain and with a sodium channel Nav1.2 peptide are reported, showing that the extended, extremely conserved inner groove spanning the entire ANK repeat solenoid contains multiple target binding sites capable of accommodating target proteins with very diverse sequences via combinatorial usage of these sites.
76
Structural Basis of Cargo Recognitions for Class V Myosins
TL;DR: The apo-MyoVa-GTD structure indicates that most mutations found in patients with Griscelli syndrome, microvillus inclusion disease, or cancers or in “dilute” rodents likely impair the folding of GTD, and provides a framework for future functional studies of vertebrate class V myosins.