aristolactam-aiiia and thymoquinone

aristolactam-aiiia has been researched along with thymoquinone* in 1 studies

*thymoquinone: constituent of cedarwood; can cause dermatitis; structure [MeSH]

Reviews

1 review(s) available for aristolactam-aiiia and thymoquinone

Article	Year
[Targeting the substrate binding domain of polo-like kinase 1: advances in the study of PBD1 inhibitors]. Yao xue xue bao = Acta pharmaceutica Sinica, 2013, Volume: 48, Issue:3 Polo-box domain 1 (PBD1) is a characteristic domain of polo-like kinase 1 (PLK1), which locates in C-terminal and can influence the catalytic activity and specific subcellular locations of PLK1. At present, most PLK1 inhibitors are developed to occupy the ATP pocket or its close sites. However, this kind of PLK1 inhibitors is difficult to pursue target selectivity and may encounter cross drug resistance with other kinase inhibitors due to the conserved sequence of ATP pocket. Recently, PBD1, with aberrant specificity in sequence and structure, has attracted enormous interests as the alternative target to the discovery of corresponding inhibitors for anti-tumor drugs. The structure and function of PBD1 as well as the advances of its inhibitors are reviewed in this paper. Topics: Benzocycloheptenes; Benzoquinones; Cell Cycle Proteins; Cell Line, Tumor; Cell Proliferation; Humans; Indole Alkaloids; Lactams; Peptides, Cyclic; Phosphopeptides; Polo-Like Kinase 1; Protein Serine-Threonine Kinases; Proto-Oncogene Proteins	2013

Article

Year

[Targeting the substrate binding domain of polo-like kinase 1: advances in the study of PBD1 inhibitors].

Yao xue xue bao = Acta pharmaceutica Sinica, 2013, Volume: 48, Issue:3

Polo-box domain 1 (PBD1) is a characteristic domain of polo-like kinase 1 (PLK1), which locates in C-terminal and can influence the catalytic activity and specific subcellular locations of PLK1. At present, most PLK1 inhibitors are developed to occupy the ATP pocket or its close sites. However, this kind of PLK1 inhibitors is difficult to pursue target selectivity and may encounter cross drug resistance with other kinase inhibitors due to the conserved sequence of ATP pocket. Recently, PBD1, with aberrant specificity in sequence and structure, has attracted enormous interests as the alternative target to the discovery of corresponding inhibitors for anti-tumor drugs. The structure and function of PBD1 as well as the advances of its inhibitors are reviewed in this paper.

Topics: Benzocycloheptenes; Benzoquinones; Cell Cycle Proteins; Cell Line, Tumor; Cell Proliferation; Humans; Indole Alkaloids; Lactams; Peptides, Cyclic; Phosphopeptides; Polo-Like Kinase 1; Protein Serine-Threonine Kinases; Proto-Oncogene Proteins

2013