Predicting druggable binding sites at the protein-protein interface.
By Jonathan C. Fuller, N. Burgoyne, R. Jackson. 2009
292 citations recorded by the source corpus.
Subfields: Computational Biology & Bioinformatics, Computational Chemistry & Drug Discovery
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Computational Biology & Bioinformatics
- Carlos J. Camacho
- Glaucius Oliva
- Lidio M. C. Meireles
- John Karanicolas
- Adriano Defini Andricopulo
- L. Ferreira
- Alexander S. Dömling
- Ricardo N Dos Santos
In Computational Chemistry & Drug Discovery
- Lidio M. C. Meireles
- Alexander S. Dömling
- L. Ferreira
- Glaucius Oliva
- Ricardo N Dos Santos
- Adriano Defini Andricopulo
- John Karanicolas
- Carlos J. Camacho
Citations in the corpus
- Molecular Docking and Structure-Based Drug Design Strategies (2015, background): “The major challenge faced by SBDD and molecular docking in the field of PPIs is the identification and characterization of binding sites, as well as the assessment of their potential for interacting with small-molecule compounds [119].”
- SWISS-MODEL: homology modelling of protein structures and complexes (2018, neutral): “A detailed description of their interactions and the overall quaternary structure is essential for a comprehensive understanding of biological systems, how protein complexes and networks operate and how we can modulate them (1,2).”
- Fast Docking on Graphics Processing Units via Ray-Casting (2013, background): “DARC was designed for docking at shallow pockets characteristic of those used by small-molecule inhibitors of proteinprotein interfaces [30,31].”
- PROteolysis TArgeting Chimeras (PROTACs) - Past, Present and Future (2019, background): “Although successful, this MOA cannot be applied to all biological targets, especially those which lack enzymatic activity such as scaffolding proteins or proteins that function via protein-protein interaction (PPIs) [4].”
- Small-molecule inhibitors of protein-protein interactions: progressing toward the reality. (2014, background): “High-resolution structures in the 1980s to 1990s showed that PPI interfaces are generally flat and large (roughly 1,000–2,000 A2 per side) (Hwang et al., 2010), in stark contrast to the deep cavities that typically bind small molecules ( 300–500 A2) (Fuller et al., 2009).”
- ANCHOR: a web server and database for analysis of protein–protein interaction binding pockets for drug discovery (2010, background): “Out of these 15 entries, 14 entries are anti-cancer PPI targets, namely: eight related structures of MDM2 and MDMX bound to p53 and short peptides; five related structures of CDK4 bound to cyclin D1 and cyclin D3; and one structure of Smad4 bound to Ski.”