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Dawson, J. E. & Nicholson, L. K. Folding kinetics and thermodynamics of Pseudomonas syringae effector protein AvrPto provide insight into translocation via the type III secretion system. Protein Sci. 17, 1109-1119 (2008). Pubmed Xiao, F. et al. The N-terminal region of Pseudomonas type III effector AvrPtoB elicits Pto-dependent immunity and has two distinct virulence determinants. Plant J. 52, 595-614 (2007). Pubmed Jayaraman, B. & Nicholson, L. K. Thermodynamic dissection of the Ezrin FERM/CERMAD interface. Biochemistry 46, 12174-12189 (2007). Pubmed Lu, K. P., Finn, G., Lee, T. H. & Nicholson, L. K. Prolyl cis-trans isomerization as a molecular timer. Nat. Chem. Biol. 3, 619-629 (2007). Pubmed Nicholson, L. K. & Lu, K. P. Prolyl cis-trans Isomerization as a molecular timer in Crk signaling. Mol. Cell 25, 483-485 (2007). Pubmed Pastorino, L. et al. The prolyl isomerase Pin1 regulates amyloid precursor protein processing and amyloid-beta production. Nature 440, 528-534 (2006). Pubmed Jayaraman, B. & Nicholson, L. K. Backbone resonance assignments of Ezrin C ERMAD in a non-covalent complex with Ezrin N FERM. J. Biomol. NMR 36 Suppl 1, 63 (2006). Pubmed Wulf, J., Pascuzzi, P. E., Fahmy, A., Martin, G. B. & Nicholson, L. K. The solution structure of type III effector protein AvrPto reveals conformational and dynamic features important for plant pathogenesis. Structure 12, 1257-1268 (2004). Pubmed Pawley, N. H., Koide, S. & Nicholson, L. K. Backbone dynamics and thermodynamics of Borrelia outer surface protein A. J. Mol. Biol. 324, 991-1002 (2002). Pubmed Pawley, N. H., Gans, J. D. & Nicholson, L. K. Factors determining the reliable description of global tumbling parameters in solution NMR. J. Biomol. NMR 24, 215-229 (2002). Pubmed Wulf, J., Pascuzzi, P. E., Martin, G. B. & Nicholson, L. K. 1H, 15N and 13C chemical shift assignments of the structured core of the pseudomonas effector protein AvrPto. J. Biomol. NMR 23, 247-248 (2002). Pubmed Wang, C., Pawley, N. H. & Nicholson, L. K. The role of backbone motions in ligand binding to the c-Src SH3 domain. J. Mol. Biol. 313, 873-887 (2001). Pubmed Pawley, N. H., Wang, C., Koide, S. & Nicholson, L. K. An improved method for distinguishing between anisotropic tumbling and chemical exchange in analysis of 15N relaxation parameters. J. Biomol. NMR 20, 149-165 (2001). Pubmed Schatz, G. W., Reinking, J., Zippin, J., Nicholson, L. K. & Vogt, V. M. Importance of the N terminus of rous sarcoma virus protease for structure and enzymatic function. J. Virol. 75, 4761-4770 (2001). Pubmed Loh, A. P., Pawley, N., Nicholson, L. K. & Oswald, R. E. An increase in side chain entropy facilitates effector binding: NMR characterization of the side chain methyl group dynamics in Cdc42Hs. Biochemistry 40, 4590-4600 (2001). Pubmed Ramelot, T. A. & Nicholson, L. K. Phosphorylation-induced structural changes in the amyloid precursor protein cytoplasmic tail detected by NMR. J. Mol. Biol. 307, 871-884 (2001). Pubmed Reinking, J. L., Schatz, G. W., Vogt, V. M. & Nicholson, L. K. 1H, 15N and 13C assignments of a monomeric N-terminal deletion mutant of the Rous sarcoma virus protease. J. Biomol. NMR 19, 279-280 (2001). Pubmed Wang, C., Xi, J., Begley, T. P. & Nicholson, L. K. Solution structure of ThiS and implications for the evolutionary roots of ubiquitin. Nat. Struct. Biol. 8, 47-51 (2001). Pubmed Cordier, F., Wang, C., Grzesiek, S. & Nicholson, L. K. Ligand-induced strain in hydrogen bonds of the c-Src SH3 domain detected by NMR. J. Mol. Biol. 304, 497-505 (2000). Pubmed Zhu, G., Xia, Y., Nicholson, L. K. & Sze, K. H. Protein dynamics measurements by TROSY-based NMR experiments. J. Magn. Reson. 143, 423-426 (2000). Pubmed Ramelot, T. A., Gentile, L. N. & Nicholson, L. K. Transient structure of the amyloid precursor protein cytoplasmic tail indicates preordering of structure for binding to cytosolic factors. Biochemistry 39, 2714-2725 (2000). Pubmed Loh, A. P., Guo, W., Nicholson, L. K. & Oswald, R. E. Backbone dynamics of inactive, active, and effector-bound Cdc42Hs from measurements of (15)N relaxation parameters at multiple field strengths. Biochemistry 38, 12547-12557 (1999). Pubmed Cross, T. A. et al. Gramicidin channel controversy--revisited. Nat. Struct. Biol. 6, 610-1; discussion 611-2 (1999). Pubmed Tessari, M. et al. Heteronuclear NMR studies of the combined Src homology domains 2 and 3 of pp60 c-Src: effects of phosphopeptide binding. Biochemistry 36, 14561-14571 (1997). Pubmed Yamazaki, T. et al. Three-dimensional solution structure of the HIV-1 protease complexed with DMP323, a novel cyclic urea-type inhibitor, determined by nuclear magnetic resonance spectroscopy. Protein Sci. 5, 495-506 (1996). Pubmed Nicholson, L. K. et al. Flexibility and function in HIV-1 protease. Nat. Struct. Biol. 2, 274-280 (1995). Pubmed Yeo, J. H. et al. Structural analysis of highly oriented poly(p-phenylene-terephthalamide) by 15N solid-state nuclear magnetic resonance. Solid State Nucl. Magn. Reson. 3, 209-218 (1994). Pubmed Yamazaki, T. et al. Secondary structure and signal assignments of human-immunodeficiency-virus-1 protease complexed to a novel, structure-based inhibitor. Eur. J. Biochem. 219, 707-712 (1994). Pubmed Nicholson, L. K., Asakura, T., Demura, M. & Cross, T. A. A method for studying the structure of uniaxially aligned biopolymers using solid state 15N-nmr: application to Bombyx mori silk fibroin fibers. Biopolymers 33, 847-861 (1993). Pubmed Nicholson, L. K. et al. Dynamics of methyl groups in proteins as studied by proton-detected 13C NMR spectroscopy. Application to the leucine residues of staphylococcal nuclease. Biochemistry 31, 5253-5263 (1992). Pubmed Chiu, S. W. et al. Molecular dynamics computations and solid state nuclear magnetic resonance of the gramicidin cation channel. Biophys. J. 60, 974-978 (1991). Pubmed Nicholson, L. K., Teng, Q. & Cross, T. A. Solid-state nuclear magnetic resonance derived model for dynamics in the polypeptide backbone of the gramicidin A channel. J. Mol. Biol. 218, 621-637 (1991). Pubmed Teng, Q., Nicholson, L. K. & Cross, T. A. Experimental determination of torsion angles in the polypeptide backbone of the gramicidin A channel by solid state nuclear magnetic resonance. J. Mol. Biol. 218, 607-619 (1991). Pubmed Nicholson, L. K. & Cross, T. A. Gramicidin cation channel: an experimental determination of the right-handed helix sense and verification of beta-type hydrogen bonding. Biochemistry 28, 9379-9385 (1989). Pubmed Killian, J. A., Nicholson, L. K. & Cross, T. A. Solid-state 15N-NMR evidence that gramicidin A can adopt two different backbone conformations in dimyristoylphosphatidylcholine model membrane preparations. Biochim. Biophys. Acta 943, 535-540 (1988). Pubmed Nicholson, L. K. et al. Solid-state 15N NMR of oriented lipid bilayer bound gramicidin A'. Biochemistry 26, 6621-6626 (1987). Pubmed |