Quantitative use of chemical shifts for the modeling of protein complexes
暂无分享,去创建一个
[1] Holger Gohlke,et al. Steering Protein-Ligand Docking with Quantitative NMR Chemical Shift Perturbations , 2009, J. Chem. Inf. Model..
[2] Michele Vendruscolo,et al. Protein structure determination from NMR chemical shifts , 2007, Proceedings of the National Academy of Sciences.
[3] David S. Wishart,et al. CS23D: a web server for rapid protein structure generation using NMR chemical shifts and sequence data , 2008, Nucleic Acids Res..
[4] Jaime L. Stark,et al. Rapid protein-ligand costructures using chemical shift perturbations. , 2008, Journal of the American Chemical Society.
[5] C. Dominguez,et al. HADDOCK: a protein-protein docking approach based on biochemical or biophysical information. , 2003, Journal of the American Chemical Society.
[6] D. Wyss,et al. Structures of protein-protein complexes are docked using only NMR restraints from residual dipolar coupling and chemical shift perturbations. , 2002, Journal of the American Chemical Society.
[7] M. Williamson,et al. C alpha and C beta carbon-13 chemical shifts in proteins from an empirical database. , 1999, Journal of biomolecular NMR.
[8] Simon W. Ginzinger,et al. CheckShift improved: fast chemical shift reference correction with high accuracy , 2009, Journal of biomolecular NMR.
[9] Mitsuo Iwadate,et al. Cα and Cβ Carbon-13 Chemical Shifts in Proteins From an Empirical Database , 1999 .
[10] A. Bonvin,et al. The HADDOCK web server for data-driven biomolecular docking , 2010, Nature Protocols.
[11] D. Wyss,et al. Alignment of weakly interacting molecules to protein surfaces using simulations of chemical shift perturbations , 2000, Journal of biomolecular NMR.
[12] D. Wishart,et al. Rapid and accurate calculation of protein 1H, 13C and 15N chemical shifts , 2003, Journal of Biomolecular NMR.
[13] D. Case,et al. A new analysis of proton chemical shifts in proteins , 1991 .
[14] Jakob Dogan,et al. Thermodynamics of folding and binding in an affibody:affibody complex. , 2006, Journal of molecular biology.
[15] Alexandre M J J Bonvin,et al. HADDOCK versus HADDOCK: New features and performance of HADDOCK2.0 on the CAPRI targets , 2007, Proteins.
[16] A. Bax,et al. Protein backbone chemical shifts predicted from searching a database for torsion angle and sequence homology , 2007, Journal of biomolecular NMR.
[17] Miron Livny,et al. BioMagResBank , 2007, Nucleic Acids Res..
[18] David S Wishart,et al. A simple method to adjust inconsistently referenced 13C and 15N chemical shift assignments of proteins , 2005, Journal of biomolecular NMR.
[19] E. Zuiderweg,et al. Mapping protein-protein interactions in solution by NMR spectroscopy. , 2002, Biochemistry.
[20] L. Waskell,et al. Characterization and calculation of a cytochrome c-cytochrome b5 complex using NMR data. , 2005, Biochemistry.
[21] Kai J. Kohlhoff,et al. Fast and accurate predictions of protein NMR chemical shifts from interatomic distances. , 2009, Journal of the American Chemical Society.
[22] Oliver F. Lange,et al. Consistent blind protein structure generation from NMR chemical shift data , 2008, Proceedings of the National Academy of Sciences.
[23] N. Tjandra,et al. Structural Basis of Focal Adhesion Localization of LIM-only Adaptor PINCH by Integrin-linked Kinase* , 2009, Journal of Biological Chemistry.
[24] M. McCoy,et al. Spatial localization of ligand binding sites from electron current density surfaces calculated from NMR chemical shift perturbations. , 2002, Journal of the American Chemical Society.
[25] Martin J Packer,et al. Determination of protein-ligand binding modes using complexation-induced changes in (1)h NMR chemical shift. , 2008, Journal of medicinal chemistry.
[26] Wolfram Gronwald,et al. Combined chemical shift changes and amino acid specific chemical shift mapping of protein–protein interactions , 2007, Journal of biomolecular NMR.
[27] C. Hunter,et al. Use of quantitative 1H NMR chemical shift changes for ligand docking into barnase , 2009, Journal of biomolecular NMR.
[28] Michele Vendruscolo,et al. Structure determination of protein-protein complexes using NMR chemical shifts: case of an endonuclease colicin-immunity protein complex. , 2008, Journal of the American Chemical Society.
[29] S. Wodak,et al. Assessment of CAPRI predictions in rounds 3–5 shows progress in docking procedures , 2005, Proteins.
[30] Marc F Lensink,et al. Docking and scoring protein interactions: CAPRI 2009 , 2010, Proteins.
[31] Alexandre M. J. J. Bonvin,et al. SAMPLEX: Automatic mapping of perturbed and unperturbed regions of proteins and complexes , 2010, BMC Bioinformatics.
[32] Zhiping Weng,et al. Docking unbound proteins using shape complementarity, desolvation, and electrostatics , 2002, Proteins.
[33] Maxim Totrov,et al. Improving CAPRI predictions: Optimized desolvation for rigid‐body docking , 2005, Proteins.
[34] K. Merz,et al. Fast semiempirical calculations for nuclear magnetic resonance chemical shifts: a divide-and-conquer approach. , 2004, The Journal of chemical physics.
[35] Reino Laatikainen,et al. 4D prediction of protein 1H chemical shifts , 2009, Journal of biomolecular NMR.
[36] D. S. Garrett,et al. Identification by NMR of the binding surface for the histidine-containing phosphocarrier protein HPr on the N-terminal domain of enzyme I of the Escherichia coli phosphotransferase system. , 1997, Biochemistry.
[37] G. Moore,et al. Protein-protein interactions in colicin E9 DNase-immunity protein complexes. 1. Diffusion-controlled association and femtomolar binding for the cognate complex. , 1995, Biochemistry.
[38] J. Markley,et al. Empirical correlation between protein backbone 15N and 13C secondary chemical shifts and its application to nitrogen chemical shift re-referencing , 2009, Journal of biomolecular NMR.
[39] David S Wishart,et al. RefDB: A database of uniformly referenced protein chemical shifts , 2003, Journal of biomolecular NMR.