P
Pavel Martásek
Researcher at First Faculty of Medicine, Charles University in Prague
Publications - 288
Citations - 12880
Pavel Martásek is an academic researcher from First Faculty of Medicine, Charles University in Prague. The author has contributed to research in topics: Nitric oxide synthase & Heme. The author has an hindex of 53, co-authored 282 publications receiving 12245 citations. Previous affiliations of Pavel Martásek include French Institute of Health and Medical Research & Northwest University (United States).
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Journal ArticleDOI
Superoxide generation by endothelial nitric oxide synthase: The influence of cofactors
Jeannette Vasquez-Vivar,Balaraman Kalyanaraman,Pavel Martásek,Neil Hogg,Bettie Sue Siler Masters,Hakim Karoui,Paul Tordo,Kirkwood A. Pritchard +7 more
TL;DR: The mechanism of superoxide generation by endothelial nitric oxide synthase (eNOS) was investigated by the electron spin resonance spin-trapping technique using 5-diethoxyphosphoryl-5-methyl-1-pyrroline N-oxide as discussed by the authors.
Journal ArticleDOI
Dissecting the interaction between nitric oxide synthase (NOS) and caveolin. Functional significance of the nos caveolin binding domain in vivo
Guillermo García-Cardeña,Pavel Martásek,Bettie Sue Siler Masters,Phillip M. Skidd,Jacques Couet,Shengwen Li,Michael P. Lisanti,William C. Sessa +7 more
TL;DR: The data demonstrate a novel functional role for Caveolin-1 in mammalian cells as a potential molecular chaperone that directly inactivates NOS and the inactivation of eNOS and nNOS by the scaffolding domain of caveolin-3 suggests that eN OS in cardiac myocytes and n NOS in skeletal muscle are likely subject to negative regulation by this muscle-specific caveolin isoform.
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Crystal structure of constitutive endothelial nitric oxide synthase: a paradigm for pterin function involving a novel metal center.
Chander Raman,Huiying Li,Pavel Martásek,Vladimír Král,Bettie Sue Siler Masters,Thomas L. Poulos +5 more
TL;DR: The unexpected recognition of the substrate, L-arginine, at the H4B site indicates that this site is poised to stabilize a positively charged pterin ring and suggests a model involving a cationic pterIn radical in the catalytic cycle.
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Endothelial nitric oxide synthase-dependent superoxide generation from adriamycin
Jeannette Vasquez-Vivar,Pavel Martásek,Neil Hogg,Bettie Sue Siler Masters,Kirkwood A. Pritchard,Balaraman Kalyanaraman +5 more
TL;DR: It is demonstrated here that the endothelial isoform of nitric oxide synthase (eNOS) reduces adriamycin to the semiquinone radical, which enhances superoxide formation and Nitric oxide production and leads eNOS to generate peroxynitrite and hydrogen peroxide, potent oxidants implicated in several vascular pathologies.
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Plant nitric oxide synthase: a never-ending story?
Tomasz Zemojtel,Andreas Fröhlich,M. Cristina Palmieri,Mateusz Kolanczyk,Ivan Mikula,Lucjan S. Wyrwicz,Erich E. Wanker,Stefan Mundlos,Martin Vingron,Pavel Martásek,Jörg Durner +10 more
TL;DR: Although the AtNOS1 sequence has no similarities to any mammalian NOS isoform, the cloned and purified AtNos1 protein was demonstrated to use the substrates arginine and nicotinamide adenine dinucleotide phosphate to produce NO.