scholarly journals Increased Protein Stability Causes DNA Methyltransferase 1 Dysregulation in Breast Cancer

2005 ◽  
Vol 280 (18) ◽  
pp. 18302-18310 ◽  
Author(s):  
Agoston T. Agoston ◽  
Pedram Argani ◽  
Srinivasan Yegnasubramanian ◽  
Angelo M. De Marzo ◽  
Mohammad Ali Ansari-Lari ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Protein Stability ◽  
Dna Methyltransferase ◽  
Dna Methyltransferase 1 ◽  
Methyltransferase 1

scholarly journals Increased protein stability causes DNA methyltransferase 1 dysregulation in breast cancer. Vol. 280 (2005) 18302-18310

2005 ◽  
Vol 280 (31) ◽  
pp. 28828
Author(s):  
Agoston T. Agoston ◽  
Pedram Argani ◽  
Srinivasan Yegnasubramanian ◽  
Angelo M. De Marzo ◽  
Mohammad Ali Ansari-Lari ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Protein Stability ◽  
Dna Methyltransferase ◽  
Dna Methyltransferase 1 ◽  
Methyltransferase 1

scholarly journals Virtual screening of natural products as an inhibitor of DNA methyltransferase 1 enzyme for breast cancer disease

2019 ◽  
Vol 509 ◽  
pp. 012052
Author(s):  
Ina Nur Istiqomah ◽  
Ahmad Husein Alkaff ◽  
Mutiara Saragih ◽  
Ade Hanna Natalia ◽  
Usman Sumo Friend Tambunan
Keyword(s):  
Breast Cancer ◽  
Natural Products ◽  
Virtual Screening ◽  
Dna Methyltransferase ◽  
Dna Methyltransferase 1 ◽  
Cancer Disease ◽  
Methyltransferase 1

scholarly journals Identification of DNA Methyltransferase-1 Inhibitor for Breast Cancer Therapy through Computational Fragment-Based Drug Design

Molecules ◽  
2021 ◽  
Vol 26 (2) ◽  
pp. 375
Author(s):  
Ahmad Husein Alkaff ◽  
Mutiara Saragih ◽  
Shabrina Noor Imana ◽  
Mochammad Arfin Fardiansyah Nasution ◽  
Usman Sumo Friend Tambunan
Keyword(s):  
Breast Cancer ◽  
Natural Products ◽  
Molecular Docking ◽  
Dna Methyltransferase ◽  
Docking Simulation ◽  
Binding Activity ◽  
Dna Methyltransferase 1 ◽  
Docking Simulations ◽  
Pubchem Database ◽  
Methyltransferase 1

Epimutation by DNA Methyltransferase 1 (DNMT1), an epigenetic regulator enzyme, may lead to the proliferation of breast cancer. In this report, 168,686 natural products from the PubChem database were screened and modified by in silico method to acquire the potential inhibitor of DNMT1. The initial screening of PubChem natural products using Lipinski’s and Veber’s rules of three and toxic properties have resulted in 2601 fragment candidates. Four fragments from pharmacophore-based molecular docking simulation were modified by utilizing FragFP and the Lipinski’s and Veber’s rules of five, and resulted in 51,200 ligands. The toxicological screening collected 13,563 ligands for a series of pharmacophore-based molecular docking simulations to sort out the modified ligands, which had the better binding activity and interactions to DNMT1 compared to the standards, SAH, SAM, and SFG. This step resulted in five ligand candidates, namely C-7756, C-5769, C-1723, C-2129, and C-2140. The ADME-Tox properties prediction showed that the selected ligands are generally better than standards in terms of druglikeness, GI absorption, and oral bioavailability. C-7756 exhibited a stronger affinity to DNMT1 as well as better ADME-Tox properties compared to the other ligands.

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