Compounds > 1-Anilino-9-10-dioxo-2-anthroic-acid

1-Anilino-9-10-dioxo-2-anthroic-acid and Neoplasms

1-Anilino-9-10-dioxo-2-anthroic-acid has been researched along with Neoplasms* in 1 studies

*Neoplasms: New abnormal growth of tissue. Malignant neoplasms show a greater degree of anaplasia and have the properties of invasion and metastasis, compared to benign neoplasms. [MeSH]

Other Studies

1 other study(ies) available for 1-Anilino-9-10-dioxo-2-anthroic-acid and Neoplasms

Article	Year
Identification of new inhibitors for low molecular weight protein tyrosine phosphatase isoform B. Bioorganic & medicinal chemistry letters, 2013, Nov-01, Volume: 23, Issue:21 The National Cancer Institute Diversity Set II (1356 compounds) and Diversity Set III (1597 compounds) were screened via in silico methods as potential inhibitors of low molecular weight protein tyrosine phosphatase (LWM-PTP) isoform B (EC 3.1.3.48). Those candidates that demonstrated comparable or better docking scores than that of pyridoxal 5'-phosphate (PLP), one of the most potent known inhibitors of LMW-PTP with a competitive inhibitor dissociation constant (Kis) of 7.6μM (pH 5.0), were analyzed via in vitro kinetic assays against LMW-PTP isoform B. While none of the compounds tested in vitro was significantly better that PLP, five compounds showed comparable inhibition. These five compounds are very diverse in structure and represent new therapeutic leads for inhibition of this isozyme. Topics: Enzyme Inhibitors; Humans; Molecular Docking Simulation; Neoplasms; Protein Conformation; Protein Isoforms; Protein Tyrosine Phosphatase, Non-Receptor Type 1	2013

Article

Year

Identification of new inhibitors for low molecular weight protein tyrosine phosphatase isoform B.

Bioorganic & medicinal chemistry letters, 2013, Nov-01, Volume: 23, Issue:21

The National Cancer Institute Diversity Set II (1356 compounds) and Diversity Set III (1597 compounds) were screened via in silico methods as potential inhibitors of low molecular weight protein tyrosine phosphatase (LWM-PTP) isoform B (EC 3.1.3.48). Those candidates that demonstrated comparable or better docking scores than that of pyridoxal 5'-phosphate (PLP), one of the most potent known inhibitors of LMW-PTP with a competitive inhibitor dissociation constant (Kis) of 7.6μM (pH 5.0), were analyzed via in vitro kinetic assays against LMW-PTP isoform B. While none of the compounds tested in vitro was significantly better that PLP, five compounds showed comparable inhibition. These five compounds are very diverse in structure and represent new therapeutic leads for inhibition of this isozyme.

Topics: Enzyme Inhibitors; Humans; Molecular Docking Simulation; Neoplasms; Protein Conformation; Protein Isoforms; Protein Tyrosine Phosphatase, Non-Receptor Type 1

2013