Structure-based mechanism of ligand binding for periplasmic solute-binding protein of the Bug family.
By J. Herrou, C. Bompard, R. Antoine, Arnaud Leroy, P. Rucktooa, D. Hot, I. Huvent, C. Locht, V. Villeret, F. Jacob-Dubuisson. 2007
21 citations recorded by the source corpus.
Subfields: Cell Biology, Materials Chemistry, Molecular Biology
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In Cell Biology
In Materials Chemistry
- Martin Weigt
- Faruck Morcos
- José N. Onuchic
- Terence Hwa
- Christopher Sander
- Riccardo Zecchina
- Andrea Pagnani
- Debora Marks
In Molecular Biology
- Martin Weigt
- Debora Marks
- Christopher Sander
- Faruck Morcos
- José N. Onuchic
- Anne-Florence Bitbol
- Sergey Ovchinnikov
- David T. Jones
Citations in the corpus
- Direct-coupling analysis of residue coevolution captures native contacts across many protein families (2011, background): “mily of bacterial tripartite tricarboxylate receptors (PF03401), NAP 70 was 600, i.e., 70% of the top 600 DI pairs correspond to true contacts when mapped to the best-predicted structure (PDB ID 2qpq (38)), see Fig. S9A. This domain has a length of L=274 and has ~2300 contacts. In another example, t”