Explore the Potential with AI-Driven Innovation
The specialised, focused library is developed on demand with the most recent virtual screening and parameter assessment technology, guided by the Receptor.AI drug discovery platform. This approach exceeds the capabilities of traditional methods and offers compounds with higher activity, selectivity, and safety.
We pick out particular compounds from an extensive virtual database of more than 60 billion molecules. The preparation and shipment of these compounds are facilitated by our associate Reaxense.
Contained in the library are leading modulators, each labelled with 38 ADME-Tox and 32 physicochemical and drug-likeness qualities. In addition, each compound is illustrated with its optimal docking poses, affinity scores, and activity scores, giving a complete picture.
We employ our advanced, specialised process to create targeted libraries for enzymes.
Fig. 1. The sreening workflow of Receptor.AI
The procedure entails thorough molecular simulations of the catalytic and allosteric binding pockets, accompanied by ensemble virtual screening that factors in their conformational flexibility. When developing modulators, the structural modifications brought about by reaction intermediates are factored in to optimize activity and selectivity.
Our library is unique due to several crucial aspects:
partner
Reaxense
upacc
P19971
UPID:
TYPH_HUMAN
Alternative names:
Gliostatin; Platelet-derived endothelial cell growth factor; TdRPase
Alternative UPACC:
P19971; A8MW15; H9KVA0; Q13390; Q8WVB7
Background:
Thymidine phosphorylase, also known as Gliostatin or Platelet-derived endothelial cell growth factor, plays a pivotal role in maintaining blood vessel integrity, promoting endothelial cell growth, and exhibiting angiogenic and chemotactic activities. It catalyzes the reversible phosphorolysis of thymidine, facilitating the utilization of produced molecules for energy or nucleotide synthesis.
Therapeutic significance:
Linked to Mitochondrial DNA depletion syndrome 1, MNGIE type, Thymidine phosphorylase's dysfunction underscores its critical biological role. Targeting its pathway offers a promising avenue for therapeutic intervention in mitochondrial-related diseases.