Protein-Protein Interactions: Coupling of Structurally Conserved Residues and of Hot Spots across Interfaces. Implications for Docking

By Inbal Halperin, Haim J. Wolfson, Ruth Nussinov. 2004

142 citations recorded by the source corpus.

Subfields: Materials Chemistry, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/59666e0359d31a79ec97e532d5fb49b2de34b08c

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Materials Chemistry

1. Ranjit Prasad Bahadur
2. Pinak Chakrabarti
3. D. Ritchie
4. Joël Janin
5. Alexandre M. J. J. Bonvin
6. Martin Zacharias
7. Burkhard Rost
8. Yanay Ofran

In Molecular Biology

1. Ranjit Prasad Bahadur
2. D. Ritchie
3. Pinak Chakrabarti
4. Joël Janin
5. Martin Zacharias
6. Alexandre M. J. J. Bonvin
7. Zhiping Weng
8. M. V. van Dijk

Citations in the corpus

• Protein–protein interaction and quaternary structure (2008, background): “In general, hotspot residues tend to cluster and be sheltered from the solvent (Bogan & Thorn, 1998 ; Halperin et al. 2004).”
• Recent progress and future directions in protein-protein docking. (2008, background): “…main challenges in protein docking today are to be able to generate reliably trial conformations which closely resemble those of the native complex, and to devise improved scoring functions which can correctly distinguish near-native docking orientations from a list of highly complementary decoys.”