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Jun-Pil Jang

Researcher at Korea Research Institute of Bioscience and Biotechnology

Publications -  35
Citations -  548

Jun-Pil Jang is an academic researcher from Korea Research Institute of Bioscience and Biotechnology. The author has contributed to research in topics: Streptomyces & Medicine. The author has an hindex of 11, co-authored 29 publications receiving 437 citations. Previous affiliations of Jun-Pil Jang include Chosun University.

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Fusarisetin A, an Acinar Morphogenesis Inhibitor from a Soil Fungus, Fusarium sp. FN080326

TL;DR: An acinar morphogenesis inhibitor named fusarisetin A (1) that possesses both an unprecedented carbon skeleton and a new pentacyclic ring system has been identified from an in-house fractionated fungal library using a three-dimensional matrigel-induced acinar Morphogenesis assay system.
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Protein tyrosine phosphatase-1B inhibitory activity of isoprenylated flavonoids isolated from Erythrina mildbraedii.

TL;DR: Bioassay-guided fractionation of an EtOAc-soluble extract of the root bark of Erythrina mildbraedii, using an in vitro PTP1B inhibitory assay, resulted in the isolation of three new isoprenylated flavonoids, abyssinone-IV-4'-O-methyl ether, which may be considered as a new class of P TP1B inhibitors.
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Fatty acid synthase inhibitory activity of acylphloroglucinols isolated from Dryopteris crassirhizoma.

TL;DR: Bioassay-guided fractionation of a MeOH extract of the rhizomes of Dryopteris crassirhizoma resulted in the isolation of a series of acylphloroglucinol derivatives, which could be considered to be a promising class of FAS inhibitors.
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PTP1B inhibitory activity of kaurane diterpenes isolated from Siegesbeckia glabrescens

TL;DR: Kinetic studies suggest that both 1 and 2 are non-competitive inhibitors of PTP1B, however, compound 3 substituted with a hydroxyl group at C-17 in kaurane-type showed no inhibitory effects towards P TP1B.
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Prenylated flavonoids with PTP1B inhibitory activity from the root bark of Erythrina mildbraedii

TL;DR: The isolates, except for compound 4, inhibited PTP1B activity in vitro with IC(50) values ranging from 5.3 to 42.6 microM, suggests that the prenyl group on the B ring of flavonoids plays an important role in suppressing the enzyme PTP 1B.