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Marcos A. Oliveira

Researcher at University of the Incarnate Word

Publications -  20
Citations -  863

Marcos A. Oliveira is an academic researcher from University of the Incarnate Word. The author has contributed to research in topics: Arginine decarboxylase & Ligand (biochemistry). The author has an hindex of 10, co-authored 19 publications receiving 810 citations. Previous affiliations of Marcos A. Oliveira include Markey Cancer Center & University of Kentucky.

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Journal ArticleDOI

Polyamines Are Essential for the Formation of Plague Biofilm

TL;DR: The first evidence for a link between polyamines and biofilm levels in Yersinia pestis is provided, as measured by high-performance liquid chromatography-mass spectrometry and as observed in a chemical complementation curve.
Book ChapterDOI

Polyamines in bacteria: pleiotropic effects yet specific mechanisms.

TL;DR: Key developments in the investigation of the function of polyamines in bacteria that have revealed new roles for polyamines distinct from growth are described.
Journal ArticleDOI

Mithramycin SK, a novel antitumor drug with improved therapeutic index, mithramycin SA, and demycarosyl-mithramycin SK: three new products generated in the mithramycin producer Streptomyces argillaceus through combinatorial biosynthesis.

TL;DR: The structures of these three compounds confirmed indirectly the proposed role of MtmW in MTM biosynthesis, and the new mithramycin derivatives bear unexpectedly shorter 3-side chains than MTM, presumably caused by nonenzymatic rearrangement or cleavage reactions of the initially formed pentyl side chain with a reactive beta-dicarbonyl functional group.
Journal ArticleDOI

Characterization of kinetics and products of the Baeyer-Villiger oxygenase MtmOIV, the key enzyme of the biosynthetic pathway toward the natural product anticancer drug mithramycin from Streptomyces argillaceus.

TL;DR: MtmOIV, the key oxygenase of the mithramycin biosynthetic pathway in Streptomyces argillaceus, was proven to act initially as Baeyer-Villiger monooxygenase, but may also catalyze various follow-up reaction steps.
Journal ArticleDOI

Identification of three critical acidic residues of poly(ADP-ribose) glycohydrolase involved in catalysis: determining the PARG catalytic domain

TL;DR: A PARG 'signature sequence' was defined, which was used to identify putative PARG sequences across a range of organisms and suggest the presence of a conserved catalytic domain of approx.