B. M. Dunn

Publication List Details

Period

1993 - 2002

Number

28

Co-Authors

The 1.4 angstrom crystal structure of kumamolysin: A thermostable serine-carboxyl-type proteinase (2002)

Comellas-Bigler,M., Fuentes-Prior,P., Maskos,K., Huber,R., Oyama,H., Uchida,K., ...

Kumamolysin is a thermostable endopeptidase from Bacillus novosp. MN-32, exhibiting maximal proteolytic activity around pH 3. It belongs to the newly identified family of serine- carboxyl...

The 1.4 angstrom crystal structure of kumamolysin: A thermostable serine-carboxyl-type proteinase (2002)

Comellas-Bigler, M., Fuentes-Prior, P., Maskos, K., Huber, R., Oyama, H., Uchida, K., ...

Kumamolysin is a thermostable endopeptidase from Bacillus novosp. MN-32, exhibiting maximal proteolytic activity around pH 3. It belongs to the newly identified family of serine- carboxyl...

Anti-VPg antibody precipitation of product RNA synthesized in vitro by the poliovirus polymerase and host factor is mediated by VPg on the poliovirion RNA template.

Young, D C, Dunn, B M, Tobin, G J, Flanegan, J B

Antibody to the poliovirus genome-linked protein, VPg, specifically immunoprecipitated the product RNA synthesized in vitro by the poliovirus RNA polymerase and HeLa cell host factor when VPg-linked...

Use of synthetic peptides to identify an N-terminal epitope on mouse gamma interferon that may be involved in function.

Magazine, H I, Carter, J M, Russell, J K, Torres, B A, Dunn, B M, Johnson, H M

We previously have assigned N-terminal specificity to three hamster monoclonal antibodies (mAbs I, II, and III) produced to mouse recombinant gamma interferon (IFN-gamma), based on the ability of the...

The selectivity of statine-based inhibitors against various human aspartic proteinases.

Jupp, R A, Dunn, B M, Jacobs, J W, Vlasuk, G, Arcuri, K E, Veber, D F, ...

The interactions of five human enzymes (renin, pepsin, gastricsin, cathepsin D and cathepsin E) and the aspartic proteinase from Endothia parasitica with several series of synthetic inhibitors were...

Identification of the aspartic proteinases from human erythrocyte membranes and gastric mucosa (slow-moving proteinase) as catalytically equivalent to cathepsin E.

Jupp, R A, Richards, A D, Kay, J, Dunn, B M, Wyckoff, J B, Samloff, I M, ...

Three aspartic proteinases with similar Mr values (approx. 80,000) but from distinct sources (human gastric mucosa, human erythrocyte membranes and rat spleen) were shown to have immunological...

A systematic series of synthetic chromophoric substrates for aspartic proteinases.

Dunn, B M, Jimenez, M, Parten, B F, Valler, M J, Rolph, C E, Kay, J

The hydrolysis of the chromogenic peptide Pro-Thr-Glu-Phe-Phe(4-NO2)-Arg-Leu at the Phe-Phe(4-NO2) bond by nine aspartic proteinases of animal origin and seven enzymes from micro-organisms is...

The selectivity of action of the aspartic-proteinase inhibitor IA3 from yeast (Saccharomyces cerevisiae).

Dreyer, T, Valler, M J, Kay, J, Charlton, P, Dunn, B M

The ability of the aspartic-proteinase inhibitor IA3 from yeast (Saccharomyces cerevisiae) to affect the activities of a range of mammalian and microbial aspartic proteinases was examined. The...

Inhibition of pepsin by analogues of pepsinogen-(1-12)-peptide with substitutions in the 4-7 sequence region.

Dunn, B M, Lewitt, M, Pham, C

Derivatives of the 1-12 sequence of pig pepsinogen were prepared by solid-phase peptide synthesis. The three derivatives contain substitutions in the 4-7 region of the 1-12 sequence. Glycine was used...

The effects of lactoyl-pepstatin and the pepsin inhibitor peptide on pig cathepsin D.

Kay, J, Afting, E G, Aoyagi, T, Dunn, B M

Lactoyl-pepstatin (an acylated tetrapeptide) is much more readily soluble in aqueous media than the more common isovaleryl- and acetyl-pepstatins (acylated pentapeptides). However, the K1 value for...

Anti-VPg antibody precipitation of product RNA synthesized in vitro by the poliovirus polymerase and host factor is mediated by VPg on the poliovirion RNA template.

Young, D C, Dunn, B M, Tobin, G J, Flanegan, J B

Antibody to the poliovirus genome-linked protein, VPg, specifically immunoprecipitated the product RNA synthesized in vitro by the poliovirus RNA polymerase and HeLa cell host factor when VPg-linked...

Use of synthetic peptides to identify an N-terminal epitope on mouse gamma interferon that may be involved in function.

Magazine, H I, Carter, J M, Russell, J K, Torres, B A, Dunn, B M, Johnson, H M

We previously have assigned N-terminal specificity to three hamster monoclonal antibodies (mAbs I, II, and III) produced to mouse recombinant gamma interferon (IFN-gamma), based on the ability of the...

The selectivity of statine-based inhibitors against various human aspartic proteinases.

Jupp, R A, Dunn, B M, Jacobs, J W, Vlasuk, G, Arcuri, K E, Veber, D F, ...

The interactions of five human enzymes (renin, pepsin, gastricsin, cathepsin D and cathepsin E) and the aspartic proteinase from Endothia parasitica with several series of synthetic inhibitors were...

Identification of the aspartic proteinases from human erythrocyte membranes and gastric mucosa (slow-moving proteinase) as catalytically equivalent to cathepsin E.

Jupp, R A, Richards, A D, Kay, J, Dunn, B M, Wyckoff, J B, Samloff, I M, ...

Three aspartic proteinases with similar Mr values (approx. 80,000) but from distinct sources (human gastric mucosa, human erythrocyte membranes and rat spleen) were shown to have immunological...

A systematic series of synthetic chromophoric substrates for aspartic proteinases.

Dunn, B M, Jimenez, M, Parten, B F, Valler, M J, Rolph, C E, Kay, J

The hydrolysis of the chromogenic peptide Pro-Thr-Glu-Phe-Phe(4-NO2)-Arg-Leu at the Phe-Phe(4-NO2) bond by nine aspartic proteinases of animal origin and seven enzymes from micro-organisms is...

The selectivity of action of the aspartic-proteinase inhibitor IA3 from yeast (Saccharomyces cerevisiae).

Dreyer, T, Valler, M J, Kay, J, Charlton, P, Dunn, B M

The ability of the aspartic-proteinase inhibitor IA3 from yeast (Saccharomyces cerevisiae) to affect the activities of a range of mammalian and microbial aspartic proteinases was examined. The...

Inhibition of pepsin by analogues of pepsinogen-(1-12)-peptide with substitutions in the 4-7 sequence region.

Dunn, B M, Lewitt, M, Pham, C

Derivatives of the 1-12 sequence of pig pepsinogen were prepared by solid-phase peptide synthesis. The three derivatives contain substitutions in the 4-7 region of the 1-12 sequence. Glycine was used...

The effects of lactoyl-pepstatin and the pepsin inhibitor peptide on pig cathepsin D.

Kay, J, Afting, E G, Aoyagi, T, Dunn, B M

Lactoyl-pepstatin (an acylated tetrapeptide) is much more readily soluble in aqueous media than the more common isovaleryl- and acetyl-pepstatins (acylated pentapeptides). However, the K1 value for...

Exploration of subsite binding specificity of human cathepsin D through kinetics and rule-based molecular modeling.

Scarborough, P. E., Guruprasad, K., Topham, C., Richo, G. R., Conner, G. E., Blundell, T. L., ...

The family of aspartic proteinases includes several human enzymes that may play roles in both physiological and pathophysiological processes. The human lysosomal aspartic proteinase cathepsin D is...

Engineering the substrate specificity of rhizopuspepsin: the role of Asp 77 of fungal aspartic proteinases in facilitating the cleavage of oligopeptide substrates with lysine in P1.

Lowther, W. T., Majer, P., Dunn, B. M.

Rhizopuspepsin and other fungal aspartic proteinases are distinct from the mammalian enzymes in that they are able to cleave substrates with lysine in the P1 position. Sequence and structural...

Prime region subsite specificity characterization of human cathepsin D: the dominant role of position 128.

Beyer, B. M., Dunn, B. M.

In order to contribute to our understanding of cathepsin D (CatD) active site specificity, two series of chromogenic octapeptides with systematic substitutions in positions P2' and P3' were...

Toward a universal inhibitor of retroviral proteases: comparative analysis of the interactions of LP-130 complexed with proteases from HIV-1, FIV, and EIAV.

Kervinen, J., Lubkowski, J., Zdanov, A., Bhatt, D., Dunn, B. M., Hui, K. Y., ...

One of the major problems encountered in antiviral therapy against AIDS is the emergence of viral variants that exhibit drug resistance. The sequences of proteases (PRs) from related retroviruses...

Active site specificity of plasmepsin II.

Westling, J., Cipullo, P., Hung, S. H., Saft, H., Dame, J. B., Dunn, B. M.

Members of the aspartic proteinase family of enzymes have very similar three-dimensional structures and catalytic mechanisms. Each, however, has unique substrate specificity. These distinctions arise...