about
Two-color fluorescent l-amino acid mimic of tryptophan for probing peptide-nucleic acid complexes.Identification by high throughput screening of small compounds inhibiting the nucleic acid destabilization activity of the HIV-1 nucleocapsid protein.Monitoring penetratin interactions with lipid membranes and cell internalization using a new hydration-sensitive fluorescent probe.Targeting the viral nucleocapsid protein in anti-HIV-1 therapy.Sensing peptide-oligonucleotide interactions by a two-color fluorescence label: application to the HIV-1 nucleocapsid protein.Non-uniform self-assembly: On the anisotropic architecture of α-synuclein supra-fibrillar aggregates.Specificity and kinetics of alpha-synuclein binding to model membranes determined with fluorescent excited state intramolecular proton transfer (ESIPT) probeProbing dynamics of HIV-1 nucleocapsid protein/target hexanucleotide complexes by 2-aminopurineEnvironment-sensitive quinolone demonstrating long-lived fluorescence and unusually slow excited-state intramolecular proton transfer kinetics.Fibril breaking accelerates α-synuclein fibrillization.Membrane insertion of-and membrane potential sensing by-semiconductor voltage nanosensors: Feasibility demonstration.Fluorescent dyes undergoing intramolecular proton transfer with improved sensitivity to surface charge in lipid bilayers.Environmentally sensitive probes for monitoring protein-membrane interactions at nanomolar concentrations.Modulation of dual fluorescence in a 3-hydroxyquinolone dye by perturbation of its intramolecular proton transfer with solvent polarity and basicity.Steric control of the excited-state intramolecular proton transfer in 3-hydroxyquinolones: steady-state and time-resolved fluorescence study.Dual-fluorescence L-amino acid reports insertion and orientation of melittin peptide in cell membranes.Monitoring membrane binding and insertion of peptides by two-color fluorescent labelModulation of excited-state intramolecular proton transfer by viscosity in protic mediaThe mode of α-synuclein binding to membranes depends on lipid composition and lipid to protein ratioHighly Solvatochromic 7-Aryl-3-hydroxychromonesA four-amino acid linker between repeats in the α-synuclein sequence is important for fibril formationInhibition of α-Synuclein Amyloid Fibril Elongation by Blocking Fibril Endsα-Synuclein Dimers as Potent Inhibitors of Fibrillization
P50
Q30577544-D07D8D6E-4CF0-4189-9453-2C38C6E14058Q33436104-83FC23C1-663A-4140-83A3-B96C8FDE2C23Q35215082-39BE629F-A7AE-4A9C-9709-AF222BDEA5C9Q37066805-96582E32-3A56-44B6-A5B0-888AC84D58BDQ38357351-E1D18CE2-7519-44D9-BB08-8BDA9C140FC3Q41331992-E2348767-B55B-42AB-BE2B-F716B2920271Q41922349-2944F05C-54DC-453C-A5BA-00B8C6F481F4Q42077951-AF2CA266-A7D8-4BA2-B898-F9D8786DA0CBQ46394537-ED89BFE3-F156-453A-998B-95368655615EQ47831625-E883AF02-C319-4946-B2B9-8E2AB09BB8BFQ48213489-37C1607E-B47D-4888-9A87-6519EEEA8C26Q50709834-BF4BEC08-FA0F-4AD1-8D61-E9560A1D285EQ51170978-4A22A131-01C2-4F5E-A0D8-D81D5411CE6EQ52574708-B917E9DA-6F10-4A9B-8590-1EEFF8835C91Q52581457-32450673-1118-4A2A-BCAA-3B1A27051AB8Q54550160-08239492-8D4F-479F-BB83-62C2C7D23E17Q57185375-8D781FF0-13B3-4E94-96DB-6C08661AAF89Q81384171-58CB2A71-A897-44AA-99A6-EE2AAEE6FA25Q82058446-4A0A5C6E-E01A-4C1F-A6C4-F866B6C8E357Q85928099-1D5181DF-08DB-4546-A5CD-1CCCEC3948F1Q87046842-69C17FBC-362C-4F40-BC65-91191D0FF277Q88163678-A58456DE-9E4E-42CB-8F36-7AB6EF054134Q90790455-DB11516A-0773-4B3A-AA64-543D9DABD489
P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Volodymyr V Shvadchak
@nl
Volodymyr V Shvadchak
@sl
Volodymyr V. Shvadchak
@en
Volodymyr V. Shvadchak
@es
type
label
Volodymyr V Shvadchak
@nl
Volodymyr V Shvadchak
@sl
Volodymyr V. Shvadchak
@en
Volodymyr V. Shvadchak
@es
prefLabel
Volodymyr V Shvadchak
@nl
Volodymyr V Shvadchak
@sl
Volodymyr V. Shvadchak
@en
Volodymyr V. Shvadchak
@es
P106
P1153
13411269400
P31
P496
0000-0001-8302-8073