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Roberto Antolović

Researcher at GlaxoSmithKline

Publications -  33
Citations -  917

Roberto Antolović is an academic researcher from GlaxoSmithKline. The author has contributed to research in topics: Ouabain & Na+/K+-ATPase. The author has an hindex of 16, co-authored 32 publications receiving 823 citations. Previous affiliations of Roberto Antolović include University of Giessen & University of Rijeka.

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Bovine Adrenals Contain, in Addition to Ouabain, a Second Inhibitor of the Sodium Pump

TL;DR: Sodium pump inhibitor B from bovine adrenals is the cardenolide ouabain, which shows properties similar to the proscillaridin A immunoreactivity that increased in humans with systolic blood pressure and pulse pressure.
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Structural aspects of flavonoids as inhibitors of human butyrylcholinesterase

TL;DR: Docking study showed that flavonoids bind to the BChE active site by forming multiple hydrogen bonds and pi-pi interactions, and UV-VIS absorption spectra of the flavonoid phosphate buffer solution revealed time dependant changes indicating precipitation of Flavonoids or in the case of myricetin, a change in the chemical structure resulting in a BChChE non-inhibiting specie.
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From Erythromycin to Azithromycin and New Potential Ribosome-Binding Antimicrobials.

TL;DR: A novel class of antibiotic compounds—macrolones, which are derived from macrolides and comprise macrocyclic moiety, linker, and either free or esterified quinolone 3-carboxylic group, show excellent antibacterial potency towards key erythromycin-resistant Gram-positive and Gram-negative bacterial strains, with possibly decreased potential of bacterial resistance to macrolide antibiotics.
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Epitope mapping by amino‐acid‐sequence‐specific antibodies reveals that both ends of the α subunit of Na+/K+‐ATPase are located on the cytoplasmic side of the membrane

TL;DR: Right-side-out vesicles of pig kidney microsomes and amino-acid-sequence-specific antibodies were used to probe the sidedness of the C- terminus and the N-terminus of the catalytic alpha subunit of Na+/K(+)-ATPase.
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Homology modeling of human Fyn kinase structure: discovery of rosmarinic acid as a new Fyn kinase inhibitor and in silico study of its possible binding modes.

TL;DR: The three-dimensional structure of Fyn tyrosine kinase, a Src-family enzyme involved in T-cell receptor signal transduction, is presented and it is revealed that Fyn is inhibited by a linear-mixed noncompetitive mechanism of inhibition by rosmarinic acid.