Explore the Potential with AI-Driven Innovation
Our detailed focused library is generated on demand with advanced virtual screening and parameter assessment technology powered by the Receptor.AI drug discovery platform. This method surpasses traditional approaches, delivering compounds of better quality with enhanced activity, selectivity, and safety.
We carefully select specific compounds from a vast collection of over 60 billion molecules in virtual chemical space. Our partner Reaxense helps in synthesizing and delivering these compounds.
The library includes a list of the most effective modulators, each annotated with 38 ADME-Tox and 32 physicochemical and drug-likeness parameters. Furthermore, each compound is shown with its optimal docking poses, affinity scores, and activity scores, offering a detailed summary.
Our top-notch dedicated system is used to design specialised libraries.
Fig. 1. The sreening workflow of Receptor.AI
Our strategy employs molecular simulations to explore an extensive range of proteins, capturing their dynamics both individually and within complexes with other proteins. Through ensemble virtual screening, we address proteins' conformational mobility, uncovering key binding sites at both functional regions and remote allosteric locations. This comprehensive investigation ensures a thorough assessment of all potential mechanisms of action, with the goal of discovering innovative therapeutic targets and lead molecules across across diverse biological functions.
Our library distinguishes itself through several key aspects:
partner
Reaxense
upacc
P61326
UPID:
MGN_HUMAN
Alternative names:
-
Alternative UPACC:
P61326; B1ARP8; B2R5A2; O35169; P50606; Q5SW69
Background:
Protein mago nashi homolog is essential for pre-mRNA splicing as part of the spliceosome, influencing mRNA metabolism. It functions with MAGOHB in the exon junction complex (EJC) and nonsense-mediated decay (NMD) pathway, marking exon-exon junctions in mRNA. This protein plays a key role in mRNA export, localization, translation efficiency, and NMD, by forming a heterodimer with RBM8A that regulates EIF4A3 ATPase activity and interacts with PYM1 for EJC disassembly and translation enhancement.
Therapeutic significance:
Understanding the role of Protein mago nashi homolog could open doors to potential therapeutic strategies.