Ligand-dependent dynamics and intramolecular signaling in a PDZ domain.

By E. Fuentes, C. Der, Andrew L. Lee. 2004

239 citations recorded by the source corpus.

Subfields: Computational Theory and Mathematics, Materials Chemistry, Molecular Biology

How researchers see this paper

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

In Computational Theory and Mathematics

1. Jaime G. Carbonell
2. Olivier Michielin
3. Rama Ranganathan
4. Olivier Rivoire
5. Su-In Lee
6. Lucy J. Colwell
7. Hetunandan Kamisetty
8. Sivaraman Balakrishnan

In Materials Chemistry

1. Rama Ranganathan
2. Lucy J. Colwell
3. Olivier Rivoire
4. Jaime G. Carbonell
5. Olivier Michielin
6. Christopher James Langmead
7. Hetunandan Kamisetty
8. Sivaraman Balakrishnan

In Molecular Biology

1. Rama Ranganathan
2. Lucy J. Colwell
3. Hetunandan Kamisetty
4. Sivaraman Balakrishnan
5. Stanislas Leibler
6. Tiberiu Teşileanu
7. Olivier Rivoire
8. Sergey Ovchinnikov

Citations in the corpus

• Learning generative models for protein fold families (2011, background): “This position is connected to ALA-88 and VAL-60 in our model, and does not appear in the network suggested by [8], but has been implicated by NMR experiments [26] as being dynamically linked to the active site.”
• Protein sectors: evolutionary units of three-dimensional structure (2009, background): “Indeed, a large body of experimental work now argues that amino acids contribute cooperatively but unequally in specifying protein structure and function (Agarwal et al., 2002; Benkovic and Hammes-Schiffer, 2003; Clackson and Wells, 1995; Datta et al., 2008; Eisenmesser et al., 2002; Fuentes et al.,”
• Finding and Leveraging Structure in Learning Problems (2012, methodology): “, 2008], to NMR based experimental studies ([Fuentes et al., 2004]).”
• Dynamically driven protein allostery (2006, background): “Although there is increasing evidence suggesting a role of conformational dynamics in cooperative ligand-binding processe”
• Functional dynamics of PDZ binding domains: a normal-mode analysis. (2005, background): “(8) have argued, on the basis of NMR data, that the dynamics of PDZ domains upon ligand binding should show correlations over the entire protein structure.”
• Protein Sectors: Statistical Coupling Analysis versus Conservation (2014, background): “An experimental test for such inhomogeneities inside proteins could employ NMR spectroscopy to follow the dynamics of specific atoms while the protein is undergoing conformational change [14, 26].”