Virden R - Search Results

1

Mannanase A from Pseudomonas fluorescens ssp. cellulosa is a retaining glycosyl hydrolase in which E212 and E320 are the putative catalytic residues.

Bolam DN, Hughes N, Virden R, Lakey JH, Hazlewood GP, Henrissat B, Braithwaite KL, Gilbert HJ. Bolam DN, et al. Among authors: virden r. Biochemistry. 1996 Dec 17;35(50):16195-204. doi: 10.1021/bi961866d. Biochemistry. 1996. PMID: 8973192

2

Key residues in subsite F play a critical role in the activity of Pseudomonas fluorescens subspecies cellulosa xylanase A against xylooligosaccharides but not against highly polymeric substrates such as xylan.

Charnock SJ, Lakey JH, Virden R, Hughes N, Sinnott ML, Hazlewood GP, Pickersgill R, Gilbert HJ. Charnock SJ, et al. Among authors: virden r. J Biol Chem. 1997 Jan 31;272(5):2942-51. doi: 10.1074/jbc.272.5.2942. J Biol Chem. 1997. PMID: 9006940 Free article.

3

Evidence that galactanase A from Pseudomonas fluorescens subspecies cellulosa is a retaining family 53 glycosyl hydrolase in which E161 and E270 are the catalytic residues.

Braithwaite KL, Barna T, Spurway TD, Charnock SJ, Black GW, Hughes N, Lakey JH, Virden R, Hazlewood GP, Henrissat B, Gilbert HJ. Braithwaite KL, et al. Among authors: virden r. Biochemistry. 1997 Dec 9;36(49):15489-500. doi: 10.1021/bi9712394. Biochemistry. 1997. PMID: 9398278

4

The topology of the substrate binding clefts of glycosyl hydrolase family 10 xylanases are not conserved.

Charnock SJ, Spurway TD, Xie H, Beylot MH, Virden R, Warren RA, Hazlewood GP, Gilbert HJ. Charnock SJ, et al. Among authors: virden r. J Biol Chem. 1998 Nov 27;273(48):32187-99. doi: 10.1074/jbc.273.48.32187. J Biol Chem. 1998. PMID: 9822697 Free article.

These data, in conjunction with a previous study (Charnock, S. J., Lakey, J. H., Virden, R., Hughes, N., Sinnott, M. L., Hazlewood, G. P., Pickersgill, R., and Gilbert, H. ...

These data, in conjunction with a previous study (Charnock, S. J., Lakey, J. H., Virden, R., Hughes, N., Sinnott, M. L., Hazle …

5

The role of conserved tryptophan residues in the interaction of a bacterial cellulose binding domain with its ligand.

Poole DM, Hazlewood GP, Huskisson NS, Virden R, Gilbert HJ. Poole DM, et al. Among authors: virden r. FEMS Microbiol Lett. 1993 Jan 1;106(1):77-83. doi: 10.1111/j.1574-6968.1993.tb05938.x. FEMS Microbiol Lett. 1993. PMID: 8440467

6

Characterization of the Elk-1 ETS DNA-binding domain.

Shore P, Bisset L, Lakey J, Waltho JP, Virden R, Sharrocks AD. Shore P, et al. Among authors: virden r. J Biol Chem. 1995 Mar 17;270(11):5805-11. doi: 10.1074/jbc.270.11.5805. J Biol Chem. 1995. PMID: 7890710 Free article.

7

The TolA-recognition site of colicin N. ITC, SPR and stopped-flow fluorescence define a crucial 27-residue segment.

Gokce I, Raggett EM, Hong Q, Virden R, Cooper A, Lakey JH. Gokce I, et al. Among authors: virden r. J Mol Biol. 2000 Dec 8;304(4):621-32. doi: 10.1006/jmbi.2000.4232. J Mol Biol. 2000. PMID: 11099384

8

Site-directed chemical conversion of serine to cysteine in penicillin acylase from Escherichia coli ATCC 11105. Effect on conformation and catalytic activity.

Slade A, Horrocks AJ, Lindsay CD, Dunbar B, Virden R. Slade A, et al. Among authors: virden r. Eur J Biochem. 1991 Apr 10;197(1):75-80. doi: 10.1111/j.1432-1033.1991.tb15884.x. Eur J Biochem. 1991. PMID: 1849824 Free article.

9

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.

Wheeler KA, Hawkins AR, Pain R, Virden R. Wheeler KA, et al. Among authors: virden r. Proteins. 1998 Dec 1;33(4):550-7. Proteins. 1998. PMID: 9849938

10

Mutations of penicillin acylase residue B71 extend substrate specificity by decreasing steric constraints for substrate binding.

Morillas M, McVey CE, Brannigan JA, Ladurner AG, Forney LJ, Virden R. Morillas M, et al. Among authors: virden r. Biochem J. 2003 Apr 1;371(Pt 1):143-50. doi: 10.1042/BJ20021383. Biochem J. 2003. PMID: 12511194 Free PMC article.

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