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Your search keyword '"de Voogd, Nicole J."' showing total 11 results
Start Over Author "de Voogd, Nicole J." Journal bioorganic & medicinal chemistry letters
11 results on '"de Voogd, Nicole J."'

1. Tetradehydrohalicyclamine B, a new proteasome inhibitor from the marine sponge Acanthostrongylophora ingens

Author

El-Desoky, Ahmed H., Nehira, Tatsuo, Angkouw, Esther D., Mangindaan, Remy E.P., de Voogd, Nicole J., Hikaru, Kato, Ahmed H. , El-Desoky, Yuya, Takeishi, Tesuo, Nehira, Esther D. , Angkouw, Remy E.P. , Mangindaan, Nicole J. , de Voogd, and Sachiko, Tsukamoto

Subjects
Models, Molecular, Constitutive proteasome, Proteasome Endopeptidase Complex, Stereochemistry, Clinical Biochemistry, Pharmaceutical Science, Acanthostrongylophora ingens, Crystallography, X-Ray, Ring (chemistry), Immunoproteasome, 01 natural sciences, Biochemistry, Structure-Activity Relationship, chemistry.chemical_compound, 499.3, Depsipeptides, Drug Discovery, medicine, Animals, Proteasome inhibitor, Molecular Biology, Dose-Response Relationship, Drug, Molecular Structure, biology, 010405 organic chemistry, Organic Chemistry, Absolute configuration, biology.organism_classification, 483.2, Porifera, 0104 chemical sciences, Halicyclamine, 010404 medicinal & biomolecular chemistry, Sponge, chemistry, Proteasome, Molecular Medicine, Pyridinium, Proteasome Inhibitors, Derivative (chemistry), medicine.drug
Abstract

A new halicyclamine derivative, tetradehydrohalicyclamine B (1), was isolated from the marine sponge Acanthostrongylophora ingens, along with halicyclamine B (2) as proteasome inhibitors. Compound 1 is the second example found to have a pyridinium ring in the halicyclamine family. Although the relative configuration of 2 was previously determined by X-ray crystallographic analysis, here we determined the absolute configuration of 2 by ECD experiment. Compounds 1 and 2 inhibited the constitutive proteasome as well as the immunoproteasome. The inhibitory activities of 2 were 4- to 10-fold more potent than those of 1.

Published
2019

3. Strongylophorines, meroditerpenoids from the marine sponge Petrosia corticata, function as proteasome inhibitors

Author

Losung, Fitje, Mangindaan, Remy E.P., de Voogd, Nicole J., Yokosawa, Hideyoshi, Ai, Noda, Eriko, Sakai, Hikaru, Katou, Fitje , Losung, Remy E.P. , Mangindaan, Nicole J. , de Voogd, Hideyoshi , Yokosawa, and Sachiko, Tsukamoto

Subjects
Magnetic Resonance Spectroscopy, Clinical Biochemistry, Drug Evaluation, Preclinical, Pharmaceutical Science, Antineoplastic Agents, Petrosia, Meroditerpenoid, Corticata, Spectrometry, Mass, Fast Atom Bombardment, Biochemistry, chemistry.chemical_compound, Structure-Activity Relationship, 499.3, Drug Discovery, medicine, Animals, Humans, Proteasome inhibitor, Petrosia corticata, Strongylophorine, Molecular Biology, biology, Chemistry, Organic Chemistry, biology.organism_classification, 483.2, Sponge, Proteasome, Molecular Medicine, Hemiacetal, Diterpenes, Proteasome Inhibitors, Function (biology), medicine.drug
Abstract

Two new strongylophorine derivatives, along with six known strongylophorines, were isolated from the marine sponge Petrosia corticata as proteasome inhibitors. Of these, a hemiacetal mixture of strongylophorines-13/-14 was the strongest inhibitor of the proteasome with an IC 50 of 2.1 μM.

Published
2015

4. Halenaquinone inhibits RANKL-induced osteoclastogenesis

Author

Takeushi, Tomoharu, El-Desoky, Ahmed H., Losung, Fitje, Mangindaan, Remy E.P., de Voogd, Nicole J., Arata, Yoichiro, Yokosawa, Hideyoshi, Sachiko, Tsukamoto, Tomoharu, Takeuchi, Tetsuro, Kawabata, Hikaru, Katou, Michiko, Yamakuma, Kanae, Matsuo, Ahmed H. , El-Desoky, Fitje , Losung, Remy E.P. , Mangindaan, Nicole J. , de Voogd, Yoichiro, Arata, and Hideyoshi, Yokosawa

Subjects
musculoskeletal diseases, Osteoclastogenesis, Clinical Biochemistry, Petrosia alfiani, Osteoclasts, Pharmaceutical Science, Petrosia, Biochemistry, Cell Line, Mice, Downregulation and upregulation, Osteogenesis, 499.3, Drug Discovery, Animals, Phosphorylation, Receptor, Molecular Biology, Protein kinase B, Marine sponge, biology, Chemistry, Activator (genetics), RANK Ligand, Organic Chemistry, Quinones, Acid phosphatase, Cell Differentiation, Cell biology, 483.2, RANKL, Halenaquinone, biology.protein, Molecular Medicine, I-kappa B Proteins, Signal transduction, Proto-Oncogene Proteins c-akt, Signal Transduction
Abstract

Halenaquinone was isolated from the marine sponge Petrosia alfiani as an inhibitor of osteoclastogenic differentiation of murine RAW264 cells. It inhibited the RANKL (receptor activator of nuclear factor-κB ligand)-induced upregulation of TRAP (tartrate-resistant acid phosphatase) activity as well as the formation of multinuclear osteoclasts. In addition, halenaquinone substantially suppressed RANKL-induced IκB degradation and Akt phosphorylation. Thus, these results suggest that halenaquinone inhibits RANKL-induced osteoclastogenesis at least by suppressing the NF-κB and Akt signaling pathways.

Published
2014

8. Spongiacidin C, a pyrrole alkaloid from the marine sponge Stylissa massa, functions as a USP7 inhibitor

Author

Miyazaki, Mitsue, Kodrasov, Matthew P., Rotinsulu, Henki, Losung, Fitje, Mangindaan, Remy E.P., de Voogd, Nicole J., Yokosawa, Hideyoshi, Nicholson, Benjamin, Michitaka, Yamaguchi, Mitsue, Miyazaki, Matthew P., Kodrasov, Henki , Rotinsulu, Fitje, Losung, Remy E.P., Mangindaan, Nicole J., de Voogd, Benjamin, Nicholson, and Sachiko, Tsukamoto

Subjects
Stereochemistry, Clinical Biochemistry, Pharmaceutical Science, Biochemistry, Ubiquitin-Specific Peptidase 7, Structure-Activity Relationship, chemistry.chemical_compound, Ubiquitin, Pyrrole alkaloid, 499.3, Drug Discovery, Animals, Humans, Structure–activity relationship, Protease Inhibitors, Pyrroles, USP7 inhibitor, Molecular Biology, Pyrrole, chemistry.chemical_classification, Isopeptide bond, Dose-Response Relationship, Drug, Molecular Structure, biology, Alkaloid, Organic Chemistry, biology.organism_classification, Spongiacidin C, Porifera, 483.2, Sponge, chemistry, Stylissa massa, biology.protein, Molecular Medicine, Ubiquitin Thiolesterase
Abstract

USP7, a deubiquitylating enzyme hydrolyzing the isopeptide bond at the C-terminus of ubiquitin, is an emerging cancer target. We isolated spongiacidin C from the marine sponge Stylissa massa as the first USP7 inhibitor from a natural source. This compound inhibited USP7 most strongly with an IC50 of 3.8 μM among several USP family members tested.

Published
2013

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