Michelle Maranta
Novozymes
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Publication
Featured researches published by Michelle Maranta.
Fems Microbiology Letters | 2003
Uvidelio Castillo; Gary A. Strobel; Joseph Sears; Kara Alesi; Eugene J. Ford; Janine Lin; Michelle Hunter; Michelle Maranta; Haiyan Ge; Debbie Yaver; James B. Jensen; Heidi Porter; Richard A. Robison; D Millar; W. M. Hess; Margret Condron; David B. Teplow
An endophytic streptomycete (NRRL 30566) is described and partially characterized from a fern-leaved grevillea (Grevillea pteridifolia) tree growing in the Northern Territory of Australia. This endophytic streptomycete produces, in culture, novel antibiotics - the kakadumycins. Methods are outlined for the production and chemical characterization of kakadumycin A and related compounds. This antibiotic is structurally related to a quinoxaline antibiotic, echinomycin. Each contains, by virtue of their amino acid compositions, alanine, serine and an unknown amino acid. Other biological, spectral and chromatographic differences between these two compounds occur and are given. Kakadumycin A has wide spectrum antibiotic activity, especially against Gram-positive bacteria, and it generally displays better bioactivity than echinomycin. For instance, against Bacillus anthracis strains, kakadumycin A has minimum inhibitory concentrations of 0.2-0.3 microg x ml(-1) in contrast to echinomycin at 1.0-1.2 microg x ml(-1). Both echinomycin and kakadumycin A have impressive activity against the malarial parasite Plasmodium falciparum with LD(50)s in the range of 7-10 ng x ml(-1). In macromolecular synthesis assays both kakadumycin A and echinomycin have similar effects on the inhibition of RNA synthesis. It appears that the endophytic Streptomyces sp. offer some promise for the discovery of novel antibiotics with pharmacological potential.
Acta Crystallographica Section F-structural Biology and Crystallization Communications | 2015
Olga V. Moroz; Michelle Maranta; Tarana Shaghasi; Paul Harris; Keith S. Wilson; Gideon J. Davies
The enzymatic degradation of plant cell-wall cellulose is central to many industrial processes, including second-generation biofuel production. Key players in this deconstruction are the fungal cellobiohydrolases (CBHs), notably those from family GH7 of the carbohydrate-active enzymes (CAZY) database, which are generally known as CBHI enzymes. Here, three-dimensional structures are reported of the Aspergillus fumigatus CBHI Cel7A solved in uncomplexed and disaccharide-bound forms at resolutions of 1.8 and 1.5 Å, respectively. The product complex with a disaccharide in the +1 and +2 subsites adds to the growing three-dimensional insight into this family of industrially relevant biocatalysts.
Microbiology | 2004
David Ezra; Uvidelio Castillo; Gary A. Strobel; W. M. Hess; Heidi Porter; James B. Jensen; Margaret M. Condron; David B. Teplow; Joseph Sears; Michelle Maranta; Michelle Hunter; Barbara Weber; Debbie Yaver
Archive | 2010
Kimberly Brown; Michelle Maranta; Eric Abbate
Archive | 2009
Michelle Maranta; Kimberly Brown
Archive | 2008
Michelle Maranta; Kimberly Brown; James Langston
Archive | 2009
Michelle Maranta; Kimberly Brown
Archive | 2012
Janine Lin; Doreen Bohan; Michelle Maranta; Leslie Beresford; Michael Lamsa; Matt Sweeney; Mark Wogulis; Elizabeth Znameroski; Frank Winther Rasmussen
Archive | 2007
Randy M. Berka; Michelle Maranta; Maria Tang; Barbara Cherry
Fems Microbiology Letters | 2003
Uvidelio Castillo; James K. Harper; Gary A. Strobel; Joseph Sears; Kara Alesi; Eugene J. Ford; Janine Lin; Michelle Hunter; Michelle Maranta; Haiyan Ge; Debbie Yaver; James B. Jensen; Heidi Porter; Richard A. Robison; D Millar; W. M. Hess; Margret Condron; David B. Teplow