Z
Zahra Ouaray
Researcher at Agency for Science, Technology and Research
Publications - 3
Citations - 59
Zahra Ouaray is an academic researcher from Agency for Science, Technology and Research. The author has contributed to research in topics: Binding site & Protein Data Bank. The author has an hindex of 3, co-authored 3 publications receiving 41 citations. Previous affiliations of Zahra Ouaray include University of Southampton.
Papers
More filters
Journal ArticleDOI
Simulations of mutant p53 DNA binding domains reveal a novel druggable pocket
Mohan R. Pradhan,Jia Wei Siau,Srinivasaraghavan Kannan,Matthew Nguyen,Zahra Ouaray,Zahra Ouaray,Chee Keong Kwoh,David P. Lane,Farid J. Ghadessy,Chandra S. Verma,Chandra S. Verma,Chandra S. Verma +11 more
TL;DR: This work investigates the dynamics of the wild type (WT) and some aggregating mutants through extensive all atom explicit solvent MD simulations and speculate that changes that take place in this network as a result of the mutational stress result in the events that destabilize the DBD and initiate unfolding.
Journal ArticleDOI
The Multifaceted Roles of Molecular Dynamics Simulations in Drug Discovery.
Stephen J. Fox,Jianguo Li,Yaw Sing Tan,Matthew Nguyen,Arumay Pal,Zahra Ouaray,Shilpa Yadahalli,Srinivasaraghavan Kannan +7 more
TL;DR: The use of computational approaches, particularly molecular dynamics, in drug design is rapidly gaining momentum and acceptance as an essential part of the toolkit for modern drug discovery as mentioned in this paper, with the number of approved drugs declining steadily, combined with increasing costs, a rational approach is needed to facilitate, expedite and streamline the drug discovery process.
Journal ArticleDOI
Reactivation of mutant p53: Constraints on mechanism highlighted by principal component analysis of the DNA binding domain.
Zahra Ouaray,Zahra Ouaray,Karim M. ElSawy,Karim M. ElSawy,David P. Lane,Jonathan W. Essex,Chandra S. Verma,Chandra S. Verma,Chandra S. Verma +8 more
TL;DR: A need to retain the flexibility of the p53 DNA binding surface (DBS) is highlighted because it is the adaptability of this region that enables p53 to engage in the diverse interactions responsible for its functionality.