Y
Young In Chi
Researcher at University of Minnesota
Publications - 52
Citations - 4723
Young In Chi is an academic researcher from University of Minnesota. The author has contributed to research in topics: Hepatocyte nuclear factors & Protein structure. The author has an hindex of 27, co-authored 49 publications receiving 4362 citations. Previous affiliations of Young In Chi include University of California, Berkeley & Purdue University.
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Journal ArticleDOI
Electron transfer by domain movement in cytochrome bc1.
Zhaolei Zhang,Li-Shar Huang,Li-Shar Huang,Vladimir M. Shulmeister,Young In Chi,Kyeong Kyu Kim,Li-Wei Hung,Antony R. Crofts,Edward A. Berry,Sung-Hou Kim,Sung-Hou Kim +10 more
TL;DR: X-ray crystal structures of the cytochrome bc1 complex from chicken, cow and rabbit in both the presence and absence of inhibitors of quinone oxidation, reveal two different locations for the extrinsic domain of one component of the enzyme, an iron–sulphur protein.
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Three-dimensional structure of a human class II histocompatibility molecule complexed with superantigen.
Theodore S. Jardetzky,Jerry H. Brown,Jerry H. Brown,Joan C. Gorga,Lawrence J. Stern,Robert G. Urban,Young In Chi,Cynthia V. Stauffacher,Jack L. Strominger,Don C. Wiley +9 more
TL;DR: The structure of a bacterial superantigen bound to a human class II histocompatibility complex molecule (HLA-DR1) has been determined by X-ray crystallography and suggests a model for ternary complex formation with the T-cell antigen receptor (TCR), in which unconventional TCR-MHC contacts are possible.
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The G0/G1 Switch Gene 2 Regulates Adipose Lipolysis through Association with Adipose Triglyceride Lipase
Xingyuan Yang,Xin Lu,Marc Lombès,Geun Bae Rha,Young In Chi,Theresa Guerin,Eric J. Smart,Jun Liu +7 more
TL;DR: G0S2 functions to attenuate ATGL action both in vitro and in vivo and by this mechanism regulates TAG hydrolysis.
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The SNAG domain of Snail1 functions as a molecular hook for recruiting lysine‐specific demethylase 1
Yiwei Lin,Yadi Wu,Junlin Li,Chenfang Dong,Xiaofeng Ye,Young In Chi,B. Mark Evers,Binhua P. Zhou +7 more
TL;DR: The study suggests that the SNAG domain of Snail1 resembles a histone H3‐like structure and functions as a molecular hook for recruiting LSD1 to repress gene expression in metastasis.
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Crystal structure of the HNF4α ligand binding domain in complex with endogenous fatty acid ligand
TL;DR: It is suggested that fatty acids are endogenous ligands for HNF4α and establish a framework for understanding how H NF4α activity is enhanced by ligand binding and diminished by MODY1 mutations.