Protein–protein interactions: Structurally conserved residues distinguish between binding sites and exposed protein surfaces

By Buyong Ma, T. Elkayam, Haim J. Wolfson, Ruth Nussinov. Proceedings of the National Academy of Sciences of the United States of America, 2003

604 citations recorded by the source corpus.

Subfields: Materials Chemistry, Molecular Biology, Radiology, Nuclear Medicine and Imaging

View Paper: https://www.semanticscholar.org/paper/ff52378ac996019d57ea33255fe510225495ce03

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. Alexandre M. J. J. Bonvin
2. Ruth Nussinov
3. Aleksey A. Porollo
4. Jaroslaw Meller
5. Anna R. Panchenko
6. Benjamin A. Shoemaker
7. Morten Nielsen
8. M. V. van Dijk

In Molecular Biology

1. Morten Nielsen
2. Alexandre M. J. J. Bonvin
3. Ole Lund
4. Jens Vindahl Kringelum
5. Ruth Nussinov
6. Aleksey A. Porollo
7. Jaroslaw Meller
8. Anna R. Panchenko

In Radiology, Nuclear Medicine and Imaging

1. Morten Nielsen
2. Alexandre M. J. J. Bonvin
3. Jens Vindahl Kringelum
4. Ole Lund
5. Ruth Nussinov
6. Bjoern Peters
7. Massimo Andreatta
8. Alessandro Sette

Citations in the corpus

• Residue centrality, functionally important residues, and active site shape: Analysis of enzyme and non‐enzyme families (2006, background): “Usually, the antibody presents a large cleft for antigen binding, while homodimers tend to have planar interfaces (Laskowski et al. 1996; Valdar and Thornton 2001; Ma et al. 2003).”
• Protein–protein interaction and quaternary structure (2008, neutral): “GIOT, L., BADER, J. S., BROUWER, C., CHAUDHURI, A., KUANG, B. et al. (2003).”
• Structural analysis of B-cell epitopes in antibody:protein complexes (2012, background): “The concept of amino acid cooperatively has been adopted from studies on protein:protein interfaces, where pairs of hydrophobic and polar amino acids have been argued to play an important role in the binding formation (Lijnzaad and Argos, 1997; Ma et al., 2003; Neuvirth et al., 2004).”
• Flexible protein-protein docking. (2006, positive): “This resulted in an increased hit rate and prediction accuracy for one of the recent CAPRI targets [16].”
• Deciphering Protein–Protein Interactions. Part I. Experimental Techniques and Databases (2007, background): “were found to be structurally conserved [14], and the”
• Flexible nets: disorder and induced fit in the associations of p53 and 14-3-3 with their partners (2008, neutral): “[158].”
• Exploiting sequence and structure homologs to identify protein–protein binding sites (2005, neutral): “14 Integrated structure-based approaches will likely become more important as more protein structures are determined by structural genomics.”
• Prediction‐based fingerprints of protein–protein interactions (2006, background): “27,34 In this work, we describe a novel approach to the recognition of protein–protein interaction sites in the case when the structure of an isolated protein chain (i.e., unbound structure) is known.”