Search

Your search keyword '"Petrova, Olga N."' showing total 12 results
Start Over Author "Petrova, Olga N."
12 results on '"Petrova, Olga N."'

1. Some uncertainties of neutrino oscillation effect in the NO$\nu$A experiment

Author

Kolupaeva, Lyudmila D., Kuzmin, Konstantin S., Petrova, Olga N., and Shandrov, Igor M.

Subjects
High Energy Physics - Phenomenology
Abstract

Uncertainties related to the effect of neutrino coherent forward scattering in Earth's matter (MSW mechanism) and with the cross sections of quasi-elastic neutrino scattering on nuclear targets of the NO$\nu$A detectors are studied. The NO$\nu$A sensitivity to the neutrino mass hierarchy and the CP violating phase is discussed., Comment: 15 pages, 7 figures. Accepted for publication in Modern Physics Letters A

Published
2016
Full Text
View/download PDF

3. Dystrophin myonuclear domain restoration governs treatment efficacy in dystrophic muscle

Author

Morin, Adrien, primary, Stantzou, Amalia, additional, Petrova, Olga N., additional, Hildyard, John, additional, Tensorer, Thomas, additional, Matouk, Meriem, additional, Petkova, Mina V., additional, Richard, Isabelle, additional, Manoliu, Tudor, additional, Goyenvalle, Aurélie, additional, Falcone, Sestina, additional, Schuelke, Markus, additional, Laplace-Builhé, Corinne, additional, Piercy, Richard J., additional, Garcia, Luis, additional, and Amthor, Helge, additional

Published
2023
Full Text
View/download PDF

6. Dystrophin myonuclear domain restoration governs treatment efficacy in dystrophic muscle.

Author

Morina, Adrien, Stantzou, Amalia, Petrova, Olga N., Hildyard, John, Tensorer, Thomas, Matouk, Meriem, Petkova, Mina V., Richard, Isabelle, Manoliu, Tudor, Goyenvallea, Aurélie, Falcone, Sestina, Schuelke, Markus, Laplace-Builhé, Corinne, Piercy, Richard J., Garcia, Luis, and Amthor, Helge

Subjects
DYSTROPHIN, TREATMENT effectiveness, DUCHENNE muscular dystrophy, MUSCULAR dystrophy, GENOME editing
Abstract

Dystrophin is essential for muscle health: its sarcolemmal absence causes the fatal, X-linked condition, Duchenne muscular dystrophy (DMD). However, its normal, spatial organization remains poorly understood, which hinders the interpretation of efficacy of its therapeutic restoration. Using female reporter mice heterozygous for fluorescently tagged dystrophin (DmdEGFP), we here reveal that dystrophin distribution is unexpectedly compartmentalized, being restricted to myonuclear-defined sarcolemmal territories extending ~80 µm, which we called “basal sarcolemmal dystrophin units (BSDUs).” These territories were further specialized at myotendinous junctions, where both Dmd transcripts and dystrophin protein were enriched. Genome-level correction in X-linked muscular dystrophy mice via CRISPR/Cas9 gene editing restored a mosaic of separated dystrophin domains, whereas transcript-level Dmd correction, following treatment with tricyclo-DNA antisense oligonucleotides, restored dystrophin initially at junctions before extending along the entire fiber—with levels ~2% sufficient to moderate the dystrophic process. We conclude that widespread restoration of fiber dystrophin is likely critical for therapeutic success in DMD, perhaps most importantly, at muscle–tendon junctions. [ABSTRACT FROM AUTHOR]

Published
2023
Full Text
View/download PDF

11. The Dynamics Behind the Affinity: Controlling Heme-Gas Affinity viaGeminate Recombination and Heme Propionate Conformation in the NO Carrier Cytochrome c′

Author

Andrew, Colin R., Petrova, Olga N., Lamarre, Isabelle, Lambry, Jean-Christophe, Rappaport, Fabrice, and Negrerie, Michel

Abstract

Nitric oxide (NO) sensors are heme proteins which may also bind CO and O2. Control of heme-gas affinity and their discrimination are achieved by the structural properties and reactivity of the heme and its distal and proximal environments, leading to several energy barriers. In the bacterial NO sensor cytochrome c′ from Alcaligenes xylosoxidans(AXCP), the single Leu16Ala distal mutation boosts the affinity for gas ligands by a remarkable 106–108-fold, transforming AXCP from one of the lowest affinity gas binding proteins to one of the highest. Here, we report the dynamics of diatomics after photodissociation from wild type and L16A-AXCP over 12 orders of magnitude in time. For the L16A variant, the picosecond geminate rebinding of both CO and NO appears with an unprecedented 100% yield, and no exit of these ligands from protein to solvent could be observed. Molecular dynamic simulations saliently demonstrate that dissociated CO stays within 4 Å from Fe2+, in contrast to wild-type AXCP. The L16A mutation confers a heme propionate conformation and docking site which traps the diatomics, maximizing the probability of recombination and directly explaining the ultrahigh affinities for CO, NO, and O2. Overall, our results point to a novel mechanism for modulating heme-gas affinities in proteins.

Published
2016
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results