C
Cong Han
Researcher at Chinese Academy of Sciences
Publications - 14
Citations - 644
Cong Han is an academic researcher from Chinese Academy of Sciences. The author has contributed to research in topics: Nitrite & Peptide deformylase. The author has an hindex of 11, co-authored 14 publications receiving 554 citations. Previous affiliations of Cong Han include Fudan University Shanghai Medical College & University of Liverpool.
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d-Alanine:d-alanine ligase as a new target for the flavonoids quercetin and apigenin
TL;DR: It is determined that d-alanine:d-alanin ligase (Ddl) is another new target for quercetin and apigenin, and this work is expected to help shed more light on the potential antibacterial mechanism of flavonoids.
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Biochemical characterization and inhibitor discovery of shikimate dehydrogenase from Helicobacter pylori.
Cong Han,Lirui Wang,Kunqian Yu,Lili Chen,Lihong Hu,Kaixian Chen,Hualiang Jiang,Hualiang Jiang,Xu Shen,Xu Shen +9 more
TL;DR: A new aroE gene encoding SDH from Helicobacter’s strain SS1 is identified and expected to favor better understanding the features of SDH and provide useful information for the development of novel antibiotics to treat H.’pylori‐associated infection.
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Peptide deformylase is a potential target for anti-Helicobacter pylori drugs: reverse docking, enzymatic assay, and X-ray crystallography validation
Jianhua Cai,Cong Han,Tiancen Hu,Jian Zhang,Dalei Wu,Fangdao Wang,Yunqing Liu,Jianping Ding,Kaixian Chen,Jianmin Yue,Xu Shen,Xu Shen,Hualiang Jiang,Hualiang Jiang +13 more
TL;DR: The results demonstrated that the strategy, reverse docking in conjunction with bioassay and structural biology, is effective and can be used as a complementary approach of functional genomics and chemical biology in target identification.
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Structures of Protein-Protein Complexes involved in electron transfer
TL;DR: Very high resolution provides the first view of the atomic detail of the interface between the core trimeric cupredoxin structure of CuNiR and the tethered cytochrome c domain that allows the enzyme to function as an effective self-electron transfer system where the donor and acceptor proteins are fused together by genomic acquisition for functional advantage.
Journal ArticleDOI
Proton-Coupled Electron Transfer in the Catalytic Cycle of Alcaligenes Xylosoxidans Copper-Dependent Nitrite Reductase.
Nicole G. H. Leferink,Cong Han,Svetlana V. Antonyuk,Derren J. Heyes,Stephen E. J. Rigby,Michael A. Hough,Robert R. Eady,Nigel S. Scrutton,S. Samar Hasnain +8 more
TL;DR: Crystallographic structures provide a clear structural rationale for these observations, including restoration of the proton delivery via a significant movement of the loop connecting the T1Cu ligands Cys130 and His139 that occurs on binding of nitrite.