Zobrazeno 1 - 5
of 5
pro vyhledávání: '"David P. Acland"'
Publikováno v:
Molecular Plant-Microbe Interactions, Vol 13, Iss 1, Pp 54-61 (2000)
Dm-AMP1, an antifungal plant defensin from seeds of dahlia (Dahlia merckii), was radioactively labeled with t-butoxycarbonyl-[35S]-L-methionine N-hydroxy-succinimi-dylester. This procedure yielded a 35S-labeled peptide with unaltered antifungal activ
Externí odkaz:
https://doaj.org/article/72a75a67ff8647acb992ec0aa432c990
Autor:
Bruno P. A. Cammue, Ian Jeffrey Evans, Ravi Tailor, David P. Acland, Rupert W. Osborn, Willem F. Broekaert, John Anthony Ray, Sheila Attenborough, Sarah Bronwen Rees
Publikováno v:
Journal of Biological Chemistry. 272:24480-24487
Four closely related peptides were isolated from seed of Impatiens balsamina and were shown to be inhibitory to the growth of a range of fungi and bacteria, while not being cytotoxic to cultured human cells. The peptides, designated Ib-AMP1, Ib-AMP2,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2d10c7672c5349c6e6ac4ea49a6dd53b
https://doi.org/10.1074/jbc.272.39.24480
https://doi.org/10.1074/jbc.272.39.24480
Publikováno v:
Molecular plant-microbe interactions : MPMI. 13(1)
Dm-AMP1, an antifungal plant defensin from seeds of dahlia (Dahlia merckii), was radioactively labeled with t-butoxycarbonyl-[35S]-L-methionine N-hydroxy-succinimi-dylester. This procedure yielded a 35S-labeled peptide with unaltered antifungal activ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::743e600bc3727b2f6f004f5e64242d52
https://pubmed.ncbi.nlm.nih.gov/10656585
https://pubmed.ncbi.nlm.nih.gov/10656585
Autor:
Severine Tassin, Didier Marion, Willem F. Broekaert, Patrick Sodano, Marius Ptak, David P. Acland, Françoise Vovelle
Publikováno v:
Biochemistry. 37(11)
The three-dimensional solution structure of Ace-AMP1, an antifungal protein extracted from onion seeds, was determined using 1H NMR spectroscopy and molecular modeling. This cationic protein contains 93 amino acid residues and four disulfide bridges.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::83b86382cce692a2debd7375de92a7d7
https://pubmed.ncbi.nlm.nih.gov/9521681
https://pubmed.ncbi.nlm.nih.gov/9521681
Autor:
Romaan Raemaekers, Genoveva W. De Samblanx, David P. Acland, Inge J.W.M. Goderis, S. V. Patel, Frans Borremans, Rupert W. Osborn, Franky Fant, Karin Thevissen, Willem F. Broekaert
Publikováno v:
The Journal of biological chemistry. 272(2)
Mutational analysis of Rs-AFP2, a radish antifungal peptide belonging to a family of peptides referred to as plant defensins, was performed using polymerase chain reaction-based site-directed mutagenesis and yeast as a system for heterologous express
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c07525b8de8dd53a157a0bbb2fc9d88a
https://pubmed.ncbi.nlm.nih.gov/8995418
https://pubmed.ncbi.nlm.nih.gov/8995418