Zobrazeno 1 - 10 of 55 pro vyhledávání: '"B M Dunn"'
1
Interactions of substrates and inhibitors with a family of tethered HIV-1 and HIV-2 homo- and heterodimeric proteinases
Autor: N D Cook, J S Mills, L A Tomchak, M C Graves, J T Griffiths, John Kay, B M Dunn
Publikováno v: Journal of Biological Chemistry. 269:4787-4793
Genes were constructed to encode single-chain tethered human immunodeficiency virus HIV-1/HIV-1 and HIV-2/HIV-2 homodimeric proteinases and two HIV-1/HIV-2 heterodimers which differed in the nature of the interface strands. All four constructs under
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::6764c2541d5280d26d2439d516976771
https://doi.org/10.1016/s0021-9258(17)37613-5
Zobrazit plný text záznamu
3
Substrate specificity and inhibitors of aspartic proteinases
Autor: B. M. Dunn, J. Kay
Publikováno v: Scandinavian Journal of Clinical and Laboratory Investigation. 52:23-30
Aspartic proteinases of vertebrate, fungal and retroviral origin have been characterised by utilisation of chromogenic peptide substrates and synthetic inhibitors as probes. By this means, the molecular topography of sub-sites within the active site
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1e05d5b9336d268649cd09deaacb4f0e
https://doi.org/10.3109/00365519209104651
Zobrazit plný text záznamu
4
The Sequencing, Synthesis, and Biological Actions of an ANP-Like Peptide Isolated from the Brain of the Killifish Fundulus heteroclitus
Autor: B. M. Dunn, Terry D. Lee, S. M. Galli, B. Parten, D. A. Price, D. H. Evans, K. E. Doble
Publikováno v: The Biological Bulletin. 178:279-285
We have extracted, purified, and sequenced an ANP-like peptide from the killifish. The peptide was extracted from whole brains with acidic acetone, and the aqueous phase remaining after evaporation of the ace- tone was subjected directly to HPLC. A p
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5191f54f4bbfb0b070171ddc8ad775e1
https://doi.org/10.2307/1541829
Zobrazit plný text záznamu
5
Sensitive, soluble chromogenic substrates for HIV-1 proteinase
Autor: William G. Farmerie, B M Dunn, P E Scarborough, Jan Konvalinka, A Alvarez, P Strop, Lowri H. Phylip, P H Hirel, Anthony D. Richards, L Pavlickova
Publikováno v: Journal of Biological Chemistry. 265:7733-7736
By replacement of the P1' residue in a capsid/nucleocapsid cleavage site mimic with 4-NO2-phenylalanine (Nph), an excellent chromogenic substrate, Lys-Ala-Arg-Val-Leu*Nph-Glu-Ala-Met, for HIV-1 proteinase (kappa cat = 20 s-1, Km = 22 microM) has been
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::d6b351cd0464c37e5ffb2e3b9477a07a
https://doi.org/10.1016/s0021-9258(19)38989-6
Zobrazit plný text záznamu
6
The selectivity of statine-based inhibitors against various human aspartic proteinases
Autor: R A Jupp, B M Dunn, J W Jacobs, G Vlasuk, K E Arcuri, D F Veber, D S Perlow, L S Payne, J Boger, S de Laszlo, P K Chakravarty, J T Broeke, D G Hangauer, D Ondeyka, W J Greenlee, J Kay
Publikováno v: Biochemical Journal. 265:871-878
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 examined. All of the inhibitors contained the dipept
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::62a4f9d0bd5c538f6a6fe0780add6d9d
https://doi.org/10.1042/bj2650871
Zobrazit plný text záznamu
7
MiniReview: Antiviral Targets Series, Number 1
Autor: B. M. Dunn, J. Kay
Publikováno v: Antiviral Chemistry and Chemotherapy. 1:3-8
The impetus to generate effective but safe compounds to combat the acquired immune deficiency syndrome (AIDS) has been hastened by the increasing incidence of human immunodeficiency virus (HIV) infection. With the toxicities associated with zidovudin
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::6fb437dd2d6cb69f11620cdc71e8e1e6
https://doi.org/10.1177/095632029000100102
Zobrazit plný text záznamu
9
Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes
Autor: A, Wlodawer, M, Li, Z, Dauter, A, Gustchina, K, Uchida, H, Oyama, B M, Dunn, K, Oda
Publikováno v: Nature structural biology. 8(5)
The crystal structure of a pepstatin-insensitive carboxyl proteinase from Pseudomonas sp. 101 (PSCP) has been solved by single-wavelength anomalous diffraction using the absorption peak of bromide anions. Structures of the uninhibited enzyme and of c
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::eedb8bb27de31654467fe31ea9be83ab
https://pubmed.ncbi.nlm.nih.gov/11323721
Zobrazit plný text záznamu
10
Structural basis for the inhibition of porcine pepsin by Ascaris pepsin inhibitor-3
Autor: K K, Ng, J F, Petersen, M M, Cherney, C, Garen, J J, Zalatoris, C, Rao-Naik, B M, Dunn, M R, Martzen, R J, Peanasky, M N, James
Publikováno v: Nature structural biology. 7(8)
The three-dimensional structures of pepsin inhibitor-3 (PI-3) from Ascaris suum and of the complex between PI-3 and porcine pepsin at 1. 75 A and 2.45 A resolution, respectively, have revealed the mechanism of aspartic protease inhibition by this uni
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::53e8479304e858ecc5bcb9412eb995ec
https://pubmed.ncbi.nlm.nih.gov/10932249
Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání

Omezení vyhledávání
Plný text Recenzováno Digitální knihovna AV ČR
Zdroje