AAAAAA

   
Results: 1-14 |
Results: 14
Linear dichroism for the detection of single base pair mutations
Authors: Halsall, DJ Rodger, A Dafforn, TR
Citation: Dj. Halsall et al., Linear dichroism for the detection of single base pair mutations, CHEM COMMUN, (23), 2001, pp. 2410-2411
Protochlorophyllide oxidoreductase: A homology model examined by site-directed mutagenesis
Authors: Townley, HE Sessions, RB Clarke, AR Dafforn, TR Griffiths, WT
Citation: He. Townley et al., Protochlorophyllide oxidoreductase: A homology model examined by site-directed mutagenesis, PROTEINS, 44(3), 2001, pp. 329-335
Different structural requirements for plasminogen activator inhibitor 1 (PAI-1) during latency transition and proteinase inhibition as evidenced by phage-displayed hypermutated PAI-1 libraries
Authors: Stoop, AA Eldering, E Dafforn, TR Read, RJ Pannekoek, H
Citation: Aa. Stoop et al., Different structural requirements for plasminogen activator inhibitor 1 (PAI-1) during latency transition and proteinase inhibition as evidenced by phage-displayed hypermutated PAI-1 libraries, J MOL BIOL, 305(4), 2001, pp. 773-783
Polymerization of plasminogen activator inhibitor-1
Authors: Zhou, A Faint, R Charlton, P Dafforn, TR Carrell, RW Lomas, DA
Citation: A. Zhou et al., Polymerization of plasminogen activator inhibitor-1, J BIOL CHEM, 276(12), 2001, pp. 9115-9122
Topography of a 2.0 angstrom structure of alpha(1)-antitrypsin reveals targets for rational drug design to prevent conformational disease
Authors: Elliott, PR Pei, XY Dafforn, TR Lomas, DA
Citation: Pr. Elliott et al., Topography of a 2.0 angstrom structure of alpha(1)-antitrypsin reveals targets for rational drug design to prevent conformational disease, PROTEIN SCI, 9(7), 2000, pp. 1274-1281
Inactive conformation of the serpin alpha(1)-antichymotrypsin indicates two-stage insertion of the reactive loop: Implications for inhibitory function and conformational disease
Authors: Gooptu, B Hazes, B Chang, WSW Dafforn, TR Carrell, RW Read, RJ Lomas, DA
Citation: B. Gooptu et al., Inactive conformation of the serpin alpha(1)-antichymotrypsin indicates two-stage insertion of the reactive loop: Implications for inhibitory function and conformational disease, P NAS US, 97(1), 2000, pp. 67-72
Nick recognition by DNA ligases
Authors: Doherty, AJ Dafforn, TR
Citation: Aj. Doherty et Tr. Dafforn, Nick recognition by DNA ligases, J MOL BIOL, 296(1), 2000, pp. 43-56
Pathogenic alpha(1)-antitrypsin polymers are formed by reactive loop-beta-sheet A linkage
Authors: Sivasothy, P Dafforn, TR Gettins, PGW Lomas, DA
Citation: P. Sivasothy et al., Pathogenic alpha(1)-antitrypsin polymers are formed by reactive loop-beta-sheet A linkage, J BIOL CHEM, 275(43), 2000, pp. 33663-33668
The effect of a reducing-end extension on pentasaccharide binding by antithrombin
Authors: Belzar, KJ Dafforn, TR Petitou, M Carrell, RW Huntington, JA
Citation: Kj. Belzar et al., The effect of a reducing-end extension on pentasaccharide binding by antithrombin, J BIOL CHEM, 275(12), 2000, pp. 8733-8741
A general method for relieving substrate inhibition in lactate dehydrogenases
Authors: Hewitt, CO Eszes, CM Sessions, RB Moreton, KM Dafforn, TR Takei, J Dempsey, CE Clarke, AR Holbrook, JJ
Citation: Co. Hewitt et al., A general method for relieving substrate inhibition in lactate dehydrogenases, PROTEIN ENG, 12(6), 1999, pp. 491-496
A structural explanation for the binding of multiple ligands by the alpha-adaptin appendage domain
Authors: Owen, DJ Vallis, Y Noble, MEM Hunter, JB Dafforn, TR Evans, PR McMahon, HT
Citation: Dj. Owen et al., A structural explanation for the binding of multiple ligands by the alpha-adaptin appendage domain, CELL, 97(6), 1999, pp. 805-815
Structural basis of substrate specificity in malate dehydrogenases: Crystal structure of a ternary complex of porcine cytoplasmic malate dehydrogenase, alpha-ketomalonate and tetrahydoNAD
Authors: Chapman, ADM Cortes, A Dafforn, TR Clarke, AR Brady, RL
Citation: Adm. Chapman et al., Structural basis of substrate specificity in malate dehydrogenases: Crystal structure of a ternary complex of porcine cytoplasmic malate dehydrogenase, alpha-ketomalonate and tetrahydoNAD, J MOL BIOL, 285(2), 1999, pp. 703-712
Heteropolymerization of S, I, and Z alpha(1)-antitrypsin and liver cirrhosis
Authors: Mahadeva, R Chang, WSW Dafforn, TR Oakley, DJ Foreman, RC Calvin, J Wight, DGD Lomas, DA
Citation: R. Mahadeva et al., Heteropolymerization of S, I, and Z alpha(1)-antitrypsin and liver cirrhosis, J CLIN INV, 103(7), 1999, pp. 999-1006
A kinetic mechanism for the polymerization of alpha(1)-antitrypsin
Authors: Dafforn, TR Mahadeva, R Elliott, PR Sivasothy, P Lomas, DA
Citation: Tr. Dafforn et al., A kinetic mechanism for the polymerization of alpha(1)-antitrypsin, J BIOL CHEM, 274(14), 1999, pp. 9548-9555
Risultati: 1-14 |