Katherine A. Brown

Publication List Details

Period

2003 - 2007

Number

18

Co-Authors

ATP-binding cassette systems in Burkholderia pseudomalleiand Burkholderia mallei (2007)

Harland, David N, Dassa, Elie, Titball, Richard W, Brown, Katherine A, Atkins, Helen S

Abstract Background ATP binding cassette (ABC) systems are responsible for the import and export of a wide variety of molecules across cell membranes and comprise one of largest protein superfamilies...

Genomic plasticity of the causative agent of melioidosis, Burkholderia pseudomallei (2004)

Holden, Matthew T. G., Titball, Richard W., Peacock, Sharon J., Cerdeno-Tarraga, Ana M., Atkins, Timothy, Crossman, Lisa C., ...

Burkholderia pseudomallei is a recognized biothreat agent and the causative agent of melioidosis. This Gram-negative bacterium exists as a soil saprophyte in melioidosis-endemic areas of the world...

Genomic plasticity of the causative agent of melioidosis, Burkholderia pseudomallei (2004)

Holden, Matthew T. G., Titball, Richard W., Peacock, Sharon J., Cerdeno-Tarraga, Ana M., Atkins, Timothy, Crossman, Lisa C., ...

Burkholderia pseudomallei is a recognized biothreat agent and the causative agent of melioidosis. This Gram-negative bacterium exists as a soil saprophyte in melioidosis-endemic areas of the world...

DNA vaccines: improving expression of antigens (2003)

Garmory, Helen S, Brown, Katherine A, Titball, Richard W

Abstract DNA vaccination is a relatively recent development in vaccine methodology. It is now possible to undertake a rational step-by-step approach to DNA vaccine design. Strategies may include the...

DNA vaccines: improving expression of antigens

Garmory, Helen S, Brown, Katherine A, Titball, Richard W

DNA vaccination is a relatively recent development in vaccine methodology. It is now possible to undertake a rational step-by-step approach to DNA vaccine design. Strategies may include the...

Genomic plasticity of the causative agent of melioidosis, Burkholderia pseudomallei

Holden, Matthew T. G., Titball, Richard W., Peacock, Sharon J., Cerdeño-Tárraga, Ana M., Atkins, Timothy, Crossman, Lisa C., ...

Burkholderia pseudomallei is a recognized biothreat agent and the causative agent of melioidosis. This Gram-negative bacterium exists as a soil saprophyte in melioidosis-endemic areas of the world...

Functional Characterization of OXA-57, a Class D β-Lactamase from Burkholderia pseudomallei

Keith, Karen E., Oyston, Petra C., Crossett, Ben, Fairweather, Neil F., Titball, Richard W., Walsh, Timothy R., ...

Class D β-lactamase OXA-57 was identified in a range of isolates of Burkholderia pseudomallei and Burkholderia thailandensis. Comparative kinetic analyses of wild-type and mutant forms of B....

Addition of missing loops and domains to protein models by x-ray solution scattering.

Petoukhov, Maxim V, Eady, Nigel A J, Brown, Katherine A, Svergun, Dmitri I

Inherent flexibility and conformational heterogeneity in proteins can often result in the absence of loops and even entire domains in structures determined by x-ray crystallographic or NMR methods....

The ABC Transporter Protein OppA Provides Protection against Experimental Yersinia pestis Infection

Tanabe, Mikio, Atkins, Helen S., Harland, David N., Elvin, Stephen J., Stagg, Anthony J., Mirza, Osman, ...

The identification of Yersinia pestis as a potential bioterrorism agent and the emergence of antibiotic-resistant strains have highlighted the need for improved vaccines and treatments for plague....

DNA vaccines: improving expression of antigens

Garmory, Helen S, Brown, Katherine A, Titball, Richard W

DNA vaccination is a relatively recent development in vaccine methodology. It is now possible to undertake a rational step-by-step approach to DNA vaccine design. Strategies may include the...

Genomic plasticity of the causative agent of melioidosis, Burkholderia pseudomallei

Holden, Matthew T. G., Titball, Richard W., Peacock, Sharon J., Cerdeño-Tárraga, Ana M., Atkins, Timothy, Crossman, Lisa C., ...

Burkholderia pseudomallei is a recognized biothreat agent and the causative agent of melioidosis. This Gram-negative bacterium exists as a soil saprophyte in melioidosis-endemic areas of the world...

Functional Characterization of OXA-57, a Class D β-Lactamase from Burkholderia pseudomallei

Keith, Karen E., Oyston, Petra C., Crossett, Ben, Fairweather, Neil F., Titball, Richard W., Walsh, Timothy R., ...

Class D β-lactamase OXA-57 was identified in a range of isolates of Burkholderia pseudomallei and Burkholderia thailandensis. Comparative kinetic analyses of wild-type and mutant forms of B....

Addition of missing loops and domains to protein models by x-ray solution scattering.

Petoukhov, Maxim V, Eady, Nigel A J, Brown, Katherine A, Svergun, Dmitri I

Inherent flexibility and conformational heterogeneity in proteins can often result in the absence of loops and even entire domains in structures determined by x-ray crystallographic or NMR methods....

The ABC Transporter Protein OppA Provides Protection against Experimental Yersinia pestis Infection

Tanabe, Mikio, Atkins, Helen S., Harland, David N., Elvin, Stephen J., Stagg, Anthony J., Mirza, Osman, ...

The identification of Yersinia pestis as a potential bioterrorism agent and the emergence of antibiotic-resistant strains have highlighted the need for improved vaccines and treatments for plague....

Identification of a LolC Homologue in Burkholderia pseudomallei, a Novel Protective Antigen for Melioidosis▿

Harland, David N., Chu, Karen, Haque, Ashraful, Nelson, Michelle, Walker, Nicola J., Sarkar-Tyson, Mitali, ...

Melioidosis is an emerging disease of humans in Southeast Asia and tropical Australia. The bacterium causing this disease, Burkholderia pseudomallei, is also considered a bioterrorism agent, and as...

Biophysical and kinetic analysis of wild-type and site-directed mutants of the isolated and native dehydroquinate synthase domain of the AROM protein

Park, Alison, Lamb, Heather K., Nichols, Charlie, Moore, Jonathan D., Brown, Katherine A., Cooper, Alan, ...

Dehydroquinate synthase (DHQS) is the N-terminal domain of the pentafunctional AROM protein that catalyses steps 2 to 7 in the shikimate pathway in microbial eukaryotes. DHQS converts...