P. Dodds

Crystal structures of flax rust avirulence proteins AvrL567-A and -D reveal details of the structural basis for flax disease resistance specificity (2007)

Wang, C., Guncar, G., Forwood, J., Teh, T., Catanzariti, A., Lawrence, G., ...

The gene-for-gene mechanism of plant disease resistance involves direct or indirect recognition of pathogen avirulence (Avr) proteins by plant resistance ( R) proteins. Flax rust (Melampsora lini)...

Purification of the M flax-rust resistance protein expressed in Pichia pastoris (2007)

Schmidt, S., Williams, S., Wang, C., Sornaraj, P., James, B., Kobe, B., ...

The M flax-rust resistance (R) gene is predicted to encode a 150-kDa protein of the Toll-interleukin-like receptor-nucleotide binding site-leucine rich repeat (TIR-NBS-LRR) class of plant disease...

The use of Co2+ for crystallization and structure determination, using a conventional monochromatic X-ray source, of flax rust avirulence protein (2007)

Guncar, G., Wang, C., Forwood, J., Teh, T., Catanzariti, A., Ellis, J., ...

Metal-binding sites are ubiquitous in proteins and can be readily utilized for phasing. It is shown that a protein crystal structure can be solved using single-wavelength anomalous diffraction based...

Crystal structures of flax rust avirulence proteins AvrL567-A and -D reveal details of the structural basis for flax disease resistance specificity (2007)

Wang, C., Guncar, G., Forwood, J., Teh, T., Catanzariti, A., Lawrence, G., ...

The gene-for-gene mechanism of plant disease resistance involves direct or indirect recognition of pathogen avirulence (Avr) proteins by plant resistance ( R) proteins. Flax rust (Melampsora lini)...

The use of Co2+ for crystallization and structure determination, using a conventional monochromatic X-ray source, of flax rust avirulence protein (2007)

Guncar, G., Wang, C., Forwood, J., Teh, T., Catanzariti, A., Ellis, J., ...

Metal-binding sites are ubiquitous in proteins and can be readily utilized for phasing. It is shown that a protein crystal structure can be solved using single-wavelength anomalous diffraction based...

Purification of the M flax-rust resistance protein expressed in Pichia pastoris (2007)

Schmidt, S., Williams, S., Wang, C., Sornaraj, P., James, B., Kobe, B., ...

The M flax-rust resistance (R) gene is predicted to encode a 150-kDa protein of the Toll-interleukin-like receptor-nucleotide binding site-leucine rich repeat (TIR-NBS-LRR) class of plant disease...

Tailoring tissue inhibitor of metalloproteinases-3 to overcome the weakening effects of the cysteine-rich domains of tumour necrosis factor-alpha converting enzyme (2003)

Lee,M. H., Dodds,P., Verma,V., Maskos,K., Knauper,V., Murphy,G.

Better enterprise systems implementation (2003)

Fan, I., Wognum, P.M., Dodds, P.

Tailoring tissue inhibitor of metalloproteinases-3 to overcome the weakening effects of the cysteine-rich domains of tumour necrosis factor-alpha converting enzyme (2003)

Lee, M. H., Dodds, P., Verma, V., Maskos, K., Knauper, V., Murphy, G.

Mapping and characterization of the functional epitopes of tissue inhibitor of metalloproteinases (TIMP)-3 using TIMP-1 as the scaffold: A new frontier in TIMP engineering (2002)

Lee,M. H., Maskos,K., Knäuper,V., Dodds,P., Murphy,G.

Tumor necrosis factor-alpha (TNF-alpha) converting enzyme (TACE/ADAM-17) is responsible for the release of TNF-u, a potent proinflammatory cytokine associated with many chronic debilitating diseases...

The C-terminal domains of TACE weaken the inhibitory action of N-TIMP-3 (2002)

Lee,M. H., Verma,V., Maskos,K., Becherer,J. D., Knäuper,V., Dodds,P., ...

Tumor necrosis factor-alpha converting enzyme (TACE) is an ADAM (a disintegrin and metalloproteinases) that comprises an active catalytic domain and several C-terminal domains. We compare the binding...

Engineering N-terminal domain of tissue inhibitor of metalloproteinase (TIMP)-3 to be a better inhibitor against tumour necrosis factor-alpha-converting enzyme (2002)

Lee,M. H., Verma,V., Maskos,K., Nath,D., Knäuper,V., Dodds,P., ...

We previously reported that full-length tissue inhibitor of metallo-proteinase-3 (TIMP-3) and its N-terminal domain form (N-TIMP-3) displayed equal binding affinity for tissue necrosis factor-alpha...

The C-terminal domains of TACE weaken the inhibitory action of N-TIMP-3 (2002)

Lee, M. H., Verma, V., Maskos, K., Becherer, J. D., Knäuper, V., Dodds, P., ...

Tumor necrosis factor-alpha converting enzyme (TACE) is an ADAM (a disintegrin and metalloproteinases) that comprises an active catalytic domain and several C-terminal domains. We compare the binding...

Engineering N-terminal domain of tissue inhibitor of metalloproteinase (TIMP)-3 to be a better inhibitor against tumour necrosis factor-alpha-converting enzyme (2002)

Lee, M. H., Verma, V., Maskos, K., Nath, D., Knäuper, V., Dodds, P., ...

We previously reported that full-length tissue inhibitor of metallo-proteinase-3 (TIMP-3) and its N-terminal domain form (N-TIMP-3) displayed equal binding affinity for tissue necrosis factor-alpha...

Mapping and characterization of the functional epitopes of tissue inhibitor of metalloproteinases (TIMP)-3 using TIMP-1 as the scaffold: A new frontier in TIMP engineering (2002)

Lee, M. H., Maskos, K., Knäuper, V., Dodds, P., Murphy, G.

Tumor necrosis factor-alpha (TNF-alpha) converting enzyme (TACE/ADAM-17) is responsible for the release of TNF-u, a potent proinflammatory cytokine associated with many chronic debilitating diseases...

Cloning and nucleotide sequence of the S7-RNase from Nicotiana alata Link and Otto.

Vissers, A, Dodds, P, Golz, J F, Clarke, A E

Cloning and nucleotide sequence of the S7-RNase from Nicotiana alata Link and Otto.

Vissers, A, Dodds, P, Golz, J F, Clarke, A E