Browse

Author Profile

Browsing by Subject silico

Jump to: 0-9 A B C D E F G H I J K L M N O P Q R S T U V W X Y Z
or enter first few letters:  
Showing results 1 to 3 of 3
  • OER000002364.pdf.jpg
  • Journal Article

  • Drug repurposing approach for potential Pfmrk inhibitors as antimalarial agents: an In-silico analysis

    • Authors : McBride, John M. (2023)

  • Alteration of one or few amino acid residues can affect structure [1–3] and function [4] of a protein and, in extreme cases, be the difference between health and disease [5, 6]. Understanding structural consequences of point mutations is important for drug design [7, 8] and could also accelerate optimization of enzymatic function via directed evolution [9, 10]. In these and other applications, theoretical models [11] could...
  • OER000002291.pdf.jpg
  • Journal Article

  • Identification of putative druggable pockets in PRL3, a significant oncology target, using in silico analysis

    • Authors : Bennett, Grace M. (2023)

  • Aberrant cellular phosphorylation is a hallmark of several diseases including inflammation and cancers (1–3). Protein phosphorylation is a post-translational modification that can act as a switch to regulate biochemical pathways and is regulated by the concerted action of two classes of enzymes: kinases and phosphatases. As such, kinases and phosphatases present as significant potential clinical molecular targets. To date, several kinase inhibitors have&#...
  • OER000002731.pdf.jpg
  • Journal article

  • In-silico identification of Tyr232 in AMPKα2 as a dephosphorylation site for the protein tyrosine phosphatase PTP-PEST

    • Authors : Manikandan, Amrutha (2023)

  • The AMP-activated protein kinase (AMPK) is known to be activated by the protein tyrosine phosphatase non-receptor type 12 (PTP-PEST) under hypoxic conditions. This activation is mediated by tyrosine dephosphorylation of the AMPKα subunit. However, the identity of the phosphotyrosine residues remains unknown. In this study we first predicted the structure of the complex of the AMPKα2 subunit and PTP-PEST catalytic domain using bioinformatics too...