Wei Yang

Publications295
h-index60
Citations13,511
Highly Influential Citations969
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Crystal structures of mismatch repair protein MutS and its complex with a substrate DNA
TLDR
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
View on Elsevier
Transformation of MutL by ATP Binding and Hydrolysis A Switch in DNA Mismatch Repair
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UvrD Helicase Unwinds DNA One Base Pair at a Time by a Two-Part Power Stroke
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Crystal Structure and ATPase Activity of MutL Implications for DNA Repair and Mutagenesis
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RAG2 PHD finger couples histone H3 lysine 4 trimethylation with V(D)J recombination
TLDR
The results provide the first evidence indicating that disrupting the read-out of histone modifications can cause an inherited human disease and identify a new function for histone methylation in mammalian DNA recombination.
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Crystal Structures of RNase H Bound to an RNA/DNA Hybrid: Substrate Specificity and Metal-Dependent Catalysis
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Structure of a two‐domain fragment of HIV‐1 integrase: implications for domain organization in the intact protein
TLDR
An integrase tetramer formed by crystal lattice contacts bears structural resemblance to a related bacterial transposase, Tn5, and exhibits positively charged channels suitable for DNA binding.
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The Histone Mark H3K36me3 Regulates Human DNA Mismatch Repair through Its Interaction with MutSα
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Making and breaking nucleic acids: two-Mg2+-ion catalysis and substrate specificity.
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