W
Wei Yang
Researcher at National Institutes of Health
Publications - 193
Citations - 21732
Wei Yang is an academic researcher from National Institutes of Health. The author has contributed to research in topics: DNA polymerase & DNA. The author has an hindex of 60, co-authored 160 publications receiving 19325 citations. Previous affiliations of Wei Yang include Harvard University & Brandeis University.
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Journal ArticleDOI
CHARMM: the biomolecular simulation program.
Bernard R. Brooks,Charles L. Brooks,Alexander D. MacKerell,Lennart Nilsson,Robert J. Petrella,Benoît Roux,Youngdo Won,Georgios Archontis,Christian Bartels,Stefan Boresch,Amedeo Caflisch,Leo S. D. Caves,Qiang Cui,Aaron R. Dinner,Michael Feig,Stefan Fischer,Jiali Gao,Milan Hodošček,Wonpil Im,K. Kuczera,Themis Lazaridis,Jianpeng Ma,V. Ovchinnikov,Emanuele Paci,Richard W. Pastor,Carol Beth Post,Jingzhi Pu,M. Schaefer,Bruce Tidor,Richard M. Venable,H. L. Woodcock,Xiongwu Wu,Wei Yang,Darrin M. York,Martin Karplus,Martin Karplus +35 more
TL;DR: An overview of the CHARMM program as it exists today is provided with an emphasis on developments since the publication of the original CHARMM article in 1983.
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Crystal structures of mismatch repair protein MutS and its complex with a substrate DNA
TL;DR: The crystal structures reveal the general architecture of members of the MutS family, an induced-fit mechanism of recognition between four domains of a MutS dimer and a heteroduplex kinked at the mismatch, a composite ATPase active site composed of residues from both MutS subunits, and a transmitter region connecting the mismatch-binding and ATPase domains.
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Crystal structure of a Y-family DNA polymerase in action: a mechanism for error-prone and lesion-bypass replication.
TL;DR: Crystal structures of Dpo4 in ternary complexes with DNA and an incoming nucleotide, either correct or incorrect, have been solved at 1.7 A and 2.1 A resolution, respectively, suggesting a possible mechanism for bypassing thymine dimers.
Journal ArticleDOI
Crystal Structures of RNase H Bound to an RNA/DNA Hybrid: Substrate Specificity and Metal-Dependent Catalysis
TL;DR: The crystal structures of RNase H are reported and it is concluded that two-metal-ion catalysis is a general feature of the superfamily and the catalytic residues of Argonaute are predicted.
Journal ArticleDOI
Making and Breaking Nucleic Acids: Two-Mg2+-Ion Catalysis and Substrate Specificity
TL;DR: It is proposed that two-metal-ion catalysis greatly enhances substrate recognition and catalytic specificity in DNA and RNA polymerases.