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Byung-Gee Kim

Researcher at Seoul National University

Publications -  410
Citations -  10826

Byung-Gee Kim is an academic researcher from Seoul National University. The author has contributed to research in topics: Streptomyces coelicolor & Gene. The author has an hindex of 52, co-authored 382 publications receiving 9479 citations. Previous affiliations of Byung-Gee Kim include New Generation University College & Chungnam National University.

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Characterization of a Tryptophan 6‐Halogenase from Streptomyces albus and Its Regioselectivity Determinants

TL;DR: Through structure‐based protein mutagenesis, it has been revealed that two consecutive residues, A78/V79 in SatH and G77/I78 in PyrH, are key determinants in the regioselectivity difference between tryptophan 6‐ and 5‐halogenases.
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Preclinical studies for pharmacokinetics and biodistribution of Ad-stTRAIL, an adenovirus delivering secretable trimeric TRAIL for gene therapy

TL;DR: Ad-stTRAIL, an adenovirus delivering secretable trimeric TRAIL for gene therapy and demonstrated the potential to treat malignant gliomas is reported, demonstrating the potential as a novel therapy for treating glioma.
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Crystallization and preliminary X-ray crystallographic studies of omega-transaminase from Vibrio fluvialis JS17

TL;DR: π-TA from Vibrio fluvialis JS17 (ω-TAVf) is a novel amine:pyruvate transaminase that is capable of stereoselective transamination of aryl chiral amines and was overexpressed in Escherichia coli with engineered C-terminal His tags.
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Rapid Functional Screening of Streptomyces coelicolor Regulators by Use of a pH Indicator and Application to the MarR-Like Regulator AbsC

TL;DR: A member of the MarR-like regulator family, SCO5405 (AbsC), was newly characterized to control pyruvate dehydrogenase in Streptomyces coelicolor and could be a high-throughput method for the characterization of unknown regulators.
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trans-Sialidase catalyzed sialylation of β-galactosyldisaccharide with an introduction of β-galactosidase

TL;DR: Introduction of β-galactosidase into a trans-sialidase reaction, i.e. sialic acid transfer reaction from a donor substrate to an acceptor substrate, could improve the yield of desired sialylated trisaccharide by hydrolyzing lactose, a byproduct from the donor.