ChemInform Abstract: New Cdc25B Tyrosine Phosphatase Inhibitors, Nocardiones A and B, Produced by Nocardia sp. TP-A0248: Taxonomy, Fermentation, Isolation, Structural Elucidation and Biological Properties.

ChemInform ◽  
2000 ◽  
Vol 31 (39) ◽  
pp. no-no
Author(s):  
Toshio Otani ◽  
Yoshikazu Sugimoto ◽  
Yoshimi Aoyagi ◽  
Yasuhiro Igarashi ◽  
Tamotsu Furumai ◽  
...  
Keyword(s):  
Tyrosine Phosphatase ◽  
Biological Properties ◽  
Structural Elucidation ◽  
Phosphatase Inhibitors ◽  
Nocardia Sp

scholarly journals New Cdc25B Tyrrosine Phosphatase Inhibitors, Nocardiones A and B, Produced by Nocardia sp. TP-A0248. Taxonomy, Fermentation, Isolation, Structural Elucidation and Biological Prbperties.

2000 ◽  
Vol 53 (4) ◽  
pp. 337-344 ◽  
Author(s):  
TOSHIO OTANI ◽  
YOSHIKAZU SUGIMOTO ◽  
YOSHIMI AOYAGI ◽  
YASUHIRO IGARASHI ◽  
TAMOTSU FURUMAI ◽  
...  
Keyword(s):  
Structural Elucidation ◽  
Phosphatase Inhibitors ◽  
Nocardia Sp

Design and Biological Evaluation of Novel Imidazolyl Flavonoids as Potent and Selective Protein Tyrosine Phosphatase Inhibitors

2020 ◽  
Vol 16 (4) ◽  
pp. 563-574 ◽  
Author(s):  
Rong Y. Han ◽  
Yu Ge ◽  
Ling Zhang ◽  
Qing M. Wang
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Protein Tyrosine Phosphatases ◽  
Structural Features ◽  
Biological Evaluation ◽  
Cell Protein ◽  
Phosphatase Inhibitors ◽  
Protein Tyrosine ◽  
Therapeutic Development ◽  
Chemical Studies

Background: Protein tyrosine phosphatases 1B are considered to be a desirable validated target for therapeutic development of type II diabetes and obesity. Methods: A new series of imidazolyl flavonoids as potential protein tyrosine phosphatase inhibitors were synthesized and evaluated. Results: Bioactive results indicated that some synthesized compounds exhibited potent protein phosphatase 1B (PTP1B) inhibitory activities at the micromolar range. Especially, compound 8b showed the best inhibitory activity (IC50=1.0 µM) with 15-fold selectivity for PTP1B over the closely related T-cell protein tyrosine phosphatase (TCPTP). Cell viability assays indicated that 8b is cell permeable with lower cytotoxicity. Molecular modeling and dynamics studies revealed the reason for selectivity of PTP1B over TCPTP. Quantum chemical studies were carried out on these compounds to understand the structural features essential for activity. Conclusion: Compound 8b should be a potential selective PTP1B inhibitor.

scholarly journals Exploration of marine natural resources in Indonesia and development of efficient strategies for the production of microbial halogenated metabolites

2021 ◽  
Author(s):  
Hiroyuki Yamazaki
Keyword(s):  
Natural Product ◽  
Protein Tyrosine Phosphatase ◽  
Biological Activities ◽  
Tyrosine Phosphatase ◽  
Osteoblastic Differentiation ◽  
Biological Properties ◽  
Protein Tyrosine Phosphatase 1B ◽  
Productive Performance ◽  
Halogenated Metabolites ◽  
Morphogenetic Protein

AbstractNature is a prolific source of organic products with diverse scaffolds and biological activities. The process of natural product discovery has gradually become more challenging, and advances in novel strategic approaches are essential to evolve natural product chemistry. Our focus has been on surveying untouched marine resources and fermentation to enhance microbial productive performance. The first topic is the screening of marine natural products isolated from Indonesian marine organisms for new types of bioactive compounds, such as antineoplastics, antimycobacterium substances, and inhibitors of protein tyrosine phosphatase 1B, sterol O-acyl-transferase, and bone morphogenetic protein-induced osteoblastic differentiation. The unique biological properties of marine organohalides are discussed herein and attempts to efficiently produce fungal halogenated metabolites are documented. This review presents an overview of our recent work accomplishments based on the MONOTORI study. Graphic abstract

Structure-Based Design and Discovery of Protein Tyrosine Phosphatase Inhibitors Incorporating Novel Isothiazolidinone Heterocyclic Phosphotyrosine Mimetics

2005 ◽  
Vol 48 (21) ◽  
pp. 6544-6548 ◽  
Author(s):  
Andrew P. Combs ◽  
Eddy W. Yue ◽  
Michael Bower ◽  
Paul J. Ala ◽  
Brian Wayland ◽  
...  
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Phosphatase Inhibitors ◽  
Protein Tyrosine

scholarly journals Protein phosphatase PP2C in the flagellum of Leishmania major: cloning and characterization

2017 ◽  
Vol 3 ◽  
Author(s):  
A. R. Escalona-Montaño ◽  
R. Pérez-Montfort ◽  
N. Cabrera ◽  
R. Mondragón-Flores ◽  
D. E. Vélez-Ramírez ◽  
...  
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Protein Phosphatase ◽  
Protein Concentration ◽  
Leishmania Major ◽  
Polyclonal Antibodies ◽  
Divalent Cations ◽  
Tyrosine Phosphatase ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Phosphatase Inhibitors

AbstractThe main goal of this work consisted in cloning, purifying and characterizing a protein phosphatase 2C (PP2C) from promastigotes ofLeishmania major. The gene was cloned and amplified by PCR using specific oligonucleotides and the recombinant protein was purified by affinity chromatography. The peak with maximal protein concentration was analysed by sodium dodecyl sulphate-polyacrylamide gel electrophoresis and revealed a protein of 44·9 kDa with PP2C activity. This activity was dependent on divalent cations (Mg+2and Mn+2) and was optimal at pH of 8·5, using phosphothreonine as the substrate. Sanguinarine inhibited the activity of the recombinantLmPP2C, while protein tyrosine phosphatase inhibitors had no effect. The recombinantLmPP2C was used to generate polyclonal antibodies. These antibodies recognized a protein of 44·9 kDa in differentLeishmaniaspecies; theLmPP2C was localized in the flagellar pocket and the flagellum of promastigotes.

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