Matthew Bennett

Exploring the active site of herpes simplex virus type-1 thymidine kinase by X-ray crystallography of complexes with aciclovir and other ligands

J.N. Champness, Matthew Bennett, Frank Wien et al. · Proteins Structure Function and Bioinformatics · 1998 · 139 citations

Life Sciences, Molecular Biology, Pharmacology +17

<i>Bacillus subtilis</i> arsenate reductase is structurally and functionally similar to low molecular weight protein tyrosine phosphatases

Matthew Bennett, Zhi Guan, Martin Laurberg et al. · Proceedings of the National Academy of Sciences · 2001 · 94 citations · Full text

Life Sciences, Biochemistry, Microbiology +12

The crystal structure of human adenylate kinase 6: An adenylate kinase localized to the cell nucleus

Hui Ren, Li‐Ya Wang, Matthew Bennett et al. · Proceedings of the National Academy of Sciences · 2005 · 88 citations · Full text

Life Sciences, Biochemistry, Molecular Biology +13

A DNA–porphyrin minor-groove complex at atomic resolution: The structural consequences of porphyrin ruffling

Matthew Bennett, Alexander Krah, Frank Wien et al. · Proceedings of the National Academy of Sciences · 2000 · 68 citations

Natural Sciences, Biophysics, Molecular Biology +17

Structure to 1.9 Å resolution of a complex with herpes simplex virus type‐1 thymidine kinase of a novel, non‐substrate inhibitor: X‐ray crystallographic comparison with binding of aciclovir

Matthew Bennett, Frank Wien, J.N. Champness et al. · FEBS Letters · 1999 · 65 citations

Medicine, Medicinal Chemistry, Pharmacology +17