Ecomycins, unique antimycotics from Pseudomonas viridiflava

Autor: D B Teplow, D Garton-Kenny, Margaret M. Condron, J Sears, C M Miller, B Redgrave, Gary A. Strobel, R V Miller

Publikováno v: Miller, CM; Miller, RV; Garton-Kenny, D; Redgrave, B; Sears, J; Condron, MM; et al.(1998). Ecomycins, unique antimycotics from Pseudomonas viridiflava. Journal of Applied Microbiology, 84(6), 937-944. doi: 10.1046/j.1365-2672.1998.00415.x. UCLA: Retrieved from: http://www.escholarship.org/uc/item/7k1710mw
Journal of applied microbiology, vol 84, iss 6

A novel family of peptide antimycotics, termed ecomycins, is described from Pseudomonas viridiflava, a plant-associated bacterium. Ecomycins B and C have molecular masses of 1153 and 1181. They contain equimolar amounts of a beta hydroxyaspartic acid

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6a7f422b4c2cdcaa07147805f083f584
https://doi.org/10.1046/j.1365-2672.1998.00415.x

Identification and characterization of key kinetic intermediates in amyloid beta-protein fibrillogenesis

Autor: M D, Kirkitadze, M M, Condron, D B, Teplow

Publikováno v: Journal of molecular biology. 312(5)

Amyloid beta-protein (Abeta) assembly into toxic oligomeric and fibrillar structures is a seminal event in Alzheimer's disease, therefore blocking this process could have significant therapeutic benefit. A rigorous mechanistic understanding of Abeta

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e72e3bcd4d017ecb8d5e66286e8a4518
https://pubmed.ncbi.nlm.nih.gov/11580253

A de novo designed helix-turn-helix peptide forms nontoxic amyloid fibrils

Autor: Y, Fezoui, D M, Hartley, D M, Walsh, D J, Selkoe, J J, Osterhout, D B, Teplow

Publikováno v: Nature structural biology. 7(12)

We report here that a monomeric de novo designed alpha-helix-turn-alpha-helix peptide, alpha t alpha, when incubated at 37 degrees C in an aqueous buffer at neutral pH, forms nonbranching, protease resistant fibrils that are 6-10 nm in diameter. Thes

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::7bb268337cb58fcb7f11f3decdd75edf
https://pubmed.ncbi.nlm.nih.gov/11101888

Amyloid beta-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates

Autor: D M, Walsh, D M, Hartley, Y, Kusumoto, Y, Fezoui, M M, Condron, A, Lomakin, G B, Benedek, D J, Selkoe, D B, Teplow

Publikováno v: The Journal of biological chemistry. 274(36)

Alzheimer's disease is characterized by extensive cerebral amyloid deposition. Amyloid deposits associated with damaged neuropil and blood vessels contain abundant fibrils formed by the amyloid beta-protein (Abeta). Fibrils, both in vitro and in vivo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::335b2e9e7bc9b07bcdbd6ef6a51c4a5b
https://pubmed.ncbi.nlm.nih.gov/10464339

Amyloid beta-protein fibrillogenesis. Detection of a protofibrillar intermediate

Autor: D M, Walsh, A, Lomakin, G B, Benedek, M M, Condron, D B, Teplow

Publikováno v: The Journal of biological chemistry. 272(35)

Fibrillogenesis of the amyloid beta-protein (Abeta) is a seminal pathogenetic event in Alzheimer's disease. Inhibiting fibrillogenesis is thus one approach toward disease therapy. Rational design of fibrillogenesis inhibitors requires elucidation of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::aae78f7005f155653095b87caa4e4685
https://pubmed.ncbi.nlm.nih.gov/9268388