AAAAAA

   
Results: 1-10 |
Results: 10
Identification of many crystal forms of Aspergillus nidulans dehydroquinate synthase
Authors: Nichols, CE Ren, J Lamb, H Haldane, F Hawkins, AR Stammers, DK
Citation: Ce. Nichols et al., Identification of many crystal forms of Aspergillus nidulans dehydroquinate synthase, ACT CRYST D, 57, 2001, pp. 306-309
Expression, purification and crystallization of Aspergillus nidulans NmrA,a negative regulatory protein involved in nitrogen-metabolite repression
Authors: Nichols, CE Cocklin, S Dodds, A Ren, J Lamb, H Hawkins, AR Stammers, DK
Citation: Ce. Nichols et al., Expression, purification and crystallization of Aspergillus nidulans NmrA,a negative regulatory protein involved in nitrogen-metabolite repression, ACT CRYST D, 57, 2001, pp. 1722-1725
The structure of the negative transcriptional regulator NmrA reveals a structural superfamily which includes the short-chain dehydrogenase/reductases
Authors: Stammers, DK Ren, J Leslie, K Nichols, CE Lamb, HK Cocklin, S Dodds, A Hawkins, AR
Citation: Dk. Stammers et al., The structure of the negative transcriptional regulator NmrA reveals a structural superfamily which includes the short-chain dehydrogenase/reductases, EMBO J, 20(23), 2001, pp. 6619-6626
Mechanistic studies on type I and type II dehydroquinase with (6R)- and (6S)-6-fluoro-3-dehydroquinic acids
Authors: Parker, EJ Bello, CG Coggins, JR Hawkins, AR Abell, C
Citation: Ej. Parker et al., Mechanistic studies on type I and type II dehydroquinase with (6R)- and (6S)-6-fluoro-3-dehydroquinic acids, BIOORG MED, 10(3), 2000, pp. 231-234
Identification of domains responsible for signal recognition and transduction within the QUTR transcription repressor protein
Authors: Levett, LJ Si-Hoe, SM Liddle, S Wheeler, K Smith, D Lamb, HK Newton, GH Coggins, JR Hawkins, AR
Citation: Lj. Levett et al., Identification of domains responsible for signal recognition and transduction within the QUTR transcription repressor protein, BIOCHEM J, 350, 2000, pp. 189-197
The two types of 3-dehydroquinase have distinct structures but catalyze the same overall reaction
Authors: Gourley, DG Shrive, AK Polikarpov, I Krell, T Coggins, JR Hawkins, AR Isaacs, NW Sawyer, L
Citation: Dg. Gourley et al., The two types of 3-dehydroquinase have distinct structures but catalyze the same overall reaction, NAT ST BIOL, 6(6), 1999, pp. 521-525
Synthesis of 4-deoxyquinic, 4-deoxyshikimic and 4-deoxy-3-dehydroshikimic acids
Authors: Gonzalez-Bello, C Coggins, JR Hawkins, AR Abell, C
Citation: C. Gonzalez-bello et al., Synthesis of 4-deoxyquinic, 4-deoxyshikimic and 4-deoxy-3-dehydroshikimic acids, J CHEM S P1, (8), 1999, pp. 849-854
The folding and assembly of the dodecameric type II dehydroquinases
Authors: Price, NC Boam, DJ Kelly, SM Duncan, D Krell, T Gourley, DG Coggins, JR Virden, R Hawkins, AR
Citation: Nc. Price et al., The folding and assembly of the dodecameric type II dehydroquinases, BIOCHEM J, 338, 1999, pp. 195-202
Selective inhibition of type II dehydroquinases
Authors: Frederickson, M Parker, EJ Hawkins, AR Coggins, JR Abell, C
Citation: M. Frederickson et al., Selective inhibition of type II dehydroquinases, J ORG CHEM, 64(8), 1999, pp. 2612-2613
The slow step of folding of Staphylococcus aureus PC1 beta-lactamase involves the collapse of a surface loop rate limited by the trans to cis isomerization of a non-proline peptide bond
Authors: Wheeler, KA Hawkins, AR Pain, R Virden, R
Citation: Ka. Wheeler et al., The slow step of folding of Staphylococcus aureus PC1 beta-lactamase involves the collapse of a surface loop rate limited by the trans to cis isomerization of a non-proline peptide bond, PROTEINS, 33(4), 1998, pp. 550-557
Risultati: 1-10 |