about
Effect of poly(phosphate) anions on glyceraldehyde-3-phosphate dehydrogenase structure and thermal aggregation: comparison with influence of poly(sulfoanions).Hydrophobic plant antioxidants. Preparation of nanoparticles and their application for prevention of neurodegenerative diseases. Review and experimental data.Properties of substances inhibiting aggregation of oxidized GAPDH: Data on the interaction with the enzyme and the impact on its intracellular content.Orthologues of a plant-specific At-4/1 gene in the genus Nicotiana and the structural properties of bacterially expressed 4/1 protein.Structural lability of Barley stripe mosaic virus virionsCreation of catalytically active particles from enzymes crosslinked with a natural bifunctional agent--homocysteine thiolactone.Small molecules preventing GAPDH aggregation are therapeutically applicable in cell and rat models of oxidative stress.Expression and functional characterization of the first bacteriophage-encoded chaperonin.Glyceraldehyde-3-phosphate dehydrogenase: Aggregation mechanisms and impact on amyloid neurodegenerative diseases.Effect of disulfide crosslinking on thermal transitions and chaperone-like activity of human small heat shock protein HspB1.Structural Properties of Potexvirus Coat Proteins Detected by Optical Methods.Affinity of the heparin binding motif of Noggin1 to heparan sulfate and its visualization in the embryonic tissues.New GroEL-like chaperonin of bacteriophage OBP Pseudomonas fluorescens suppresses thermal protein aggregation in an ATP-dependent manner.Structural basis for regulation of stability and activity in glyceraldehyde-3-phosphate dehydrogenases. Differential scanning calorimetry and molecular dynamics.Effect of chaperonin encoded by gene 146 on thermal aggregation of lytic proteins of bacteriophage EL Pseudomonas aeruginosa.Partially disordered structure in intravirus coat protein of potyvirus potato virus A.Effect of 2-hydroxypropyl-beta-cyclodextrin on thermal inactivation, denaturation and aggregation of glyceraldehyde-3-phosphate dehydrogenase from rabbit skeletal muscle.GAPDH binders as potential drugs for the therapy of polyglutamine diseases: design of a new screening assay.The unique two-component tail sheath of giant Pseudomonas phage PaBG.Sensitizing tumor cells to conventional drugs: HSP70 chaperone inhibitors, their selection and application in cancer models.Peptide fragments of Hsp70 modulate its chaperone activity and sensitize tumor cells to anti-cancer drugs.Binding of alpha-synuclein to partially oxidized glyceraldehyde-3-phosphate dehydrogenase induces subsequent inactivation of the enzyme.Chaperone-like activity of synthetic polyanions can be higher than the activity of natural chaperones at elevated temperature.Brønsted acids bounded to the mitochondrial membranes as a substrate for ATP synthase.Artificial chaperones based on thermoresponsive polymers recognize the unfolded state of the proteinProtein Interaction with Charged Macromolecules: From Model Polymers to Unfolded Proteins and Post-Translational ModificationsSulfated and sulfonated polymers are able to solubilize efficiently the protein aggregates of different natureComplexes between anionic liposomes and spherical polycationic brushes. An assembly of assembliesSperm-specific glyceraldehyde-3-phosphate dehydrogenase is stabilized by additional proline residues and an interdomain salt bridgeTightly bound polyelectrolytes enhance enzyme proteolysis and destroy amyloid aggregatesGlycation of α-synuclein amplifies the binding with glyceraldehyde-3-phosphate dehydrogenase
P50
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P50
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researcher ORCID ID = 0000-0001-7759-6445
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wetenschapper
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Pavel I Semenyuk
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Pavel I Semenyuk
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Pavel I Semenyuk
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Pavel Semenyuk
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Pawel Igorewitsch Semenjuk
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Павел Игоревич Семенюк
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Pavel I Semenyuk
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Pavel I Semenyuk
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Pavel I Semenyuk
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Pavel Semenyuk
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Pawel Igorewitsch Semenjuk
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Павел Игоревич Семенюк
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Pavel I Semenyuk
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Pavel Igorevich Semenyuk
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Pawel Semenjuk
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Pavel I Semenyuk
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Pavel I Semenyuk
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Pavel I Semenyuk
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Pavel Semenyuk
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Pawel Igorewitsch Semenjuk
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Павел Игоревич Семенюк
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P1153
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0000-0001-7759-6445