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Morcos, F., Pagnani, A., Lunt, B., Bertolino, A., Marks, D.S., Sander, C., Zecchina, R., Onuchic, J.N., Hwa, T. and Weigt, M. (2011) Direct-coupling analysis of residue coevolution captures native contacts across many protein families. Proceedings of the National Academy of Sciences of the United States of America, 108, E1293-E1301. http://dx.doi.org/10.1073/pnas.1111471108

has been cited by the following article:

• TITLE: Predicting residue contacts for protein-protein interactions by integration of multiple information

  AUTHORS: Tu Kien T. Le, Osamu Hirose, Vu Anh Tran, Thammakorn Saethang, Lan Anh T. Nguyen, Xuan Tho Dang, Duc Luu Ngo, Mamoru Kubo, Yoichi Yamada, Kenji Satou

  KEYWORDS: Residue-Residue Contacts;Domain-Domain Interactions; Protein-Protein Interactions; Domain Interfaces; Residue Co-Evolution; Contact Potentials

  JOURNAL NAME: Journal of Biomedical Science and Engineering, Vol.7 No.1, January 24, 2014

  ABSTRACT: Detailed knowledge of interfacial region between interacting proteins is not only helpful in annotating function for proteins, but also very important for structure-based drug design and disease treatment. However, this is one of the most difficult tasks and current methods are constrained by some factors. In this study, we developed a new method to predict residue-residue contacts of two interacting protein domains by integrating information about evolutionary couplings andamino acid pairwise contact potentials, as well as domain-domain interaction interfaces. The experimental results showed that our proposed method outperformed the previous method with the same datasets. Moreover, the method promises an improvement in the source of template-based protein docking.