about
Complete switch from α-2,3- to α-2,6-regioselectivity in Pasteurella dagmatis β-D-galactoside sialyltransferase by active-site redesignMechanistic study of CMP-Neu5Ac hydrolysis by α2,3-sialyltransferase from Pasteurella dagmatis.Microhomology-mediated DNA strand annealing and elongation by human DNA polymerases λ and β on normal and repetitive DNA sequences.Kinetic Analysis and Probing with Substrate Analogues of the Reaction Pathway of the Nitrile Reductase QueF from Escherichia coli.Oleate inhibits steryl ester synthesis and causes liposensitivity in yeast.Effect of lipid particle biogenesis on the subcellular distribution of squalene in the yeast Saccharomyces cerevisiaeHigh-quality production of human α-2,6-sialyltransferase in Pichia pastoris requires control over N-terminal truncations by host-inherent protease activities.Phosphatidylethanolamine synthesized by four different pathways is supplied to the plasma membrane of the yeast Saccharomyces cerevisiae.Characterization of a multifunctional α2,3-sialyltransferase from Pasteurella dagmatis.Comparison of broad-scope assays of nucleotide sugar-dependent glycosyltransferases.All-in-one assay for β-d-galactoside sialyltransferases: Quantification of productive turnover, error hydrolysis, and site selectivity.Structural and biochemical properties of lipid particles from the yeast Saccharomyces cerevisiae
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description
onderzoeker
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researcher
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հետազոտող
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name
Tibor Czabany
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Tibor Czabany
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Tibor Czabany
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Tibor Czabany
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Tibor Czabany
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Tibor Czabany
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Tibor Czabany
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Tibor Czabany
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Tibor Czabany
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Tibor Czabany
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Tibor Czabany
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Tibor Czabany
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P106
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P1153
24075130000
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P496
0000-0003-1754-6723