R A Williamson
Affiliation: University of Kent
- Mapping the binding site for matrix metalloproteinase on the N-terminal domain of the tissue inhibitor of metalloproteinases-2 by NMR chemical shift perturbationR A Williamson
Research School of Biosciences, University of Kent, Canterbury, U K
Biochemistry 36:13882-9. 1997..Sequence conservation data and recent site-directed mutagenesis studies are discussed in relation to the MMP binding site identified in this work...
- High resolution structure of the N-terminal domain of tissue inhibitor of metalloproteinases-2 and characterization of its interaction site with matrix metalloproteinase-3F W Muskett
Department of Biosciences, University of Kent, Canterbury, Kent, CT2 7NJ, United Kingdom
J Biol Chem 273:21736-43. 1998....
- Solution structure of the active domain of tissue inhibitor of metalloproteinases-2. A new member of the OB fold protein familyR A Williamson
Research School of Biosciences, Biological Laboratory, University of Kent, Canterbury, U K
Biochemistry 33:11745-59. 1994..Furthermore, the structure has revealed conserved surface regions of potential functional importance...
- Disulphide bond assignment in human tissue inhibitor of metalloproteinases (TIMP)R A Williamson
Biological Laboratory, University of Kent, Canterbury, U K
Biochem J 268:267-74. 1990..s. analysis permitted the assignments Cys-1-Cys-70, Cys-3-Cys-99, Cys-13-Cys-124 and Cys-127-Cys-174 from these peptides. The sixth bond Cys-132-Cys-137 was assigned by inference, as the native protein has no detectable free thiol groups...
- In vivo evaluation of 111In-DTPA-N-TIMP-2 in Kaposi sarcoma associated with HIV infectionR Kulasegaram
Biosciences Department, University of Kent, Canterbury, UK
Eur J Nucl Med 28:756-61. 2001..It is unlikely to be of use for imaging KS, but may have a role in other tumours that produce matrix metalloproteinases...