![](/images/graphics-bg.png)
In silico analysis of glycinamide ribonucleotide transformylase inhibition by PY873, PY899 and DIA
Joint Authors
Batul, Sidra
Nawaz, Muhammad Sulaman
Mushtaq, Jawhar
Parvaiz, Fahd
Kamal, Muhammad A.
Source
Saudi Journal of Biological Sciences
Issue
Vol. 24, Issue 6 (30 Sep. 2017), pp.1155-1161, 7 p.
Publisher
Publication Date
2017-09-30
Country of Publication
Saudi Arabia
No. of Pages
7
Main Subjects
Abstract EN
In humans, purine de novo synthesis pathway consists of multi-functional enzymes.
Nucleotide metabolism enzymes are potential drug targets for treating cancer and autoimmune diseases.
Glycinamide ribonucleotide transformylase (GART) is one of the most important trifunctional enzymes involved in purine synthesis.
Previous studies have demonstrated the role of folate inhibitors against tumor activity.
In this present study, three components of GART enzyme were targeted as receptor dataset and in silico analysis was carried out with folate ligand dataset.
To accomplish the task, Autodock 4.2 was used for determining the docking compatibilities of ligand and receptor dataset.
Taken together, it has been suggested that folate ligands could be potentially used as inhibitors of GART.
American Psychological Association (APA)
Batul, Sidra& Nawaz, Muhammad Sulaman& Mushtaq, Jawhar& Parvaiz, Fahd& Kamal, Muhammad A.. 2017. In silico analysis of glycinamide ribonucleotide transformylase inhibition by PY873, PY899 and DIA. Saudi Journal of Biological Sciences،Vol. 24, no. 6, pp.1155-1161.
https://search.emarefa.net/detail/BIM-776425
Modern Language Association (MLA)
Batul, Sidra…[et al.]. In silico analysis of glycinamide ribonucleotide transformylase inhibition by PY873, PY899 and DIA. Saudi Journal of Biological Sciences Vol. 24, no. 6 (Sep. 2017), pp.1155-1161.
https://search.emarefa.net/detail/BIM-776425
American Medical Association (AMA)
Batul, Sidra& Nawaz, Muhammad Sulaman& Mushtaq, Jawhar& Parvaiz, Fahd& Kamal, Muhammad A.. In silico analysis of glycinamide ribonucleotide transformylase inhibition by PY873, PY899 and DIA. Saudi Journal of Biological Sciences. 2017. Vol. 24, no. 6, pp.1155-1161.
https://search.emarefa.net/detail/BIM-776425
Data Type
Journal Articles
Language
English
Notes
Includes bibliographical references : p. 1160-1161
Record ID
BIM-776425