Nicholson Lab Papers


  • Mechanism of midline defect-causing mutation P151L in MID1 revealed, FEBS J. in press, (invited commentary) DOI 10.111/febs.14149. Nicholson, L. K.

  • Cyclic cis-Locked Phospho-Dipeptides Reduce Entry of AβPP into Amyloidogenic Processing Pathway, J Alzheimers Dis. 55, 391-410. PMCID: PMC5096988. Fisher, C. L., Resnick, R. J., De, S., Acevedo, L. A., Lu, K. P., Schroeder, F. C. & Nicholson, L. K.2016


  • Neighboring phosphoSer-Pro motifs in the undefined domain of IRAK1 impart bivalent advantage for Pin1 binding, FEBS J. 283, 4528-4548.  PMCID: PMC5298935.Rogals, M. J., Greenwood, A. I., Kwon, J., Lu, K. P. & Nicholson, L. K.



  • Complete thermodynamic and kinetic characterization of the isomer-specific interaction between Pin1-WW domain and the amyloid precursor protein cytoplasmic tail phosphorylated at Thr668.
    De, S., Greenwood, A. I., Rogals, M. J., Kovrigin, E., Lu, K. P. & Nicholson, L. K.
    Biochem (2012). 
  • Proline Isomer-Specific Antibodies Reveal the Early Pathogenic Tau Conformation in Alzheimer's Disease
    Nakamura, K., Greenwood, A., Denial, S. J., Binder, L., Bigio, E. H., Nicholson, L. K., Zhou, X. Z. & Lu, K. P.
    Cell 149, 232-244 (2012).
  • Alzheimer’s disease-related loss of Pin1 function influences the intracellular localization and processing of AβPP
    Pastorino, L., Ma, S.L., Balastic, M., Huang, P., Nicholson, L. K. & Lu, K. P.
    J. Alzheimer's Disease 30, 277-297 (2012).


  • Complete determination of the Pin1 catalytic domain thermodynamic cycle by NMR lineshape analysis.
    Greenwood, A. I., Rogals, M. J., De, S., Lu, K. P., Kovrigin, E. L. & Nicholson, L. K.
    J Biomol NMR 51, 21-34 (2011).
  • Essential role for the prolyl isomerase Pin1 in Toll-like receptor signaling and type I interferon-mediated immunity.
    Tun-Kyi, A., Finn, G., Greenwoord A., Nowak, M., Lee, T. H., Asara, J.M., Tsokos, G. C., Fitzgerald, K., Israel, E., Li, X., Exley, M., Nicholson, L. K. & Lu, K. P.
    Nat. Immun. 12, 733-741 (2011).
  • Structural biology: The twist in Crk signaling revealed.
    Nicholson, L. K. & De, S.
    Nat. Chem. Bio. 7, 5-6 (2011).


  • Determining the Charge State of Histidine Side Chains in Antimicrobial Piscidin By Nuclear Magnetic Resonance
    McGavin, J., Sudheendra, U. S., Baxter, M., Seckute, J., Nicholson, L. K. & Cotten, M.
    Biophys. J. 98, 3, Sup. 1 (2010).
  • The single kinin receptor signals to separate and independent physiological pathways in Malpighian tubules of the yellow fever mosquito
    Schepel, S. A., Fox, A. J., Miyauchi, J. T., Sou, T., Yang, J. D., Lau, K., Blum, A. W., Nicholson, L. K., Tiburcy, F., Nachman, R. J., Piermarini, P. M. & Beyenbach, K. W.
    Am. J. Physiol. Regul. Integr. Comp. Physiol. 299(2):R612-22


  • A novel fibronectin type III module binding motif identified on C-terminus of Leptospira immunoglobulin-like protein, LigB.
    Lin, Y. P., Greenwood, A., Yan, W., Nicholson, L. K., Sharma, Y., McDonough, S. P. & Chang, Y. F.
    Biochem. and Biophys. Res. Comm. 1, 57-62 (2009).
  • Fibronectin binds to and induces conformational change in a disordered region of leptospiral immunoglobulin-like protein B.
    Lin, Y. P., Greenwood, A., Nicholson, L. K., Sharma, Y. & Chang, Y. F.
    J. Biol. Chem. 284, 23547-23557 (2009).
  • Elucidation of a pH-folding switch in the Pseudomonas syringae effector protein AvrPto.
    Dawson, J. E., Seckute, J., De, S., Schueler, S. A., Oswald, A. B. & Nicholson, L. K.
    PNAS 106, 21 8543-8548 (2009).
  • Repeated Domains of Leptospira Immunoglobulin-like Proteins Interact with Elastin and Tropoelastin
    Lin, Y. P., Lee, D. W., McDonough, S. P., Nicholson, L. K., Sharma, Y. & Chang, Y. F.
    J. Biol. Chem. 284, 19380-19391.


  • Folding kinetics and thermodynamics of Pseudomonas syringae effector protein AvrPto provide insight into translocation via the type III secretion system
    Dawson, J. E. & Nicholson, L. K.
    Protein Sci. 17, 1109-1119 (2008).


  • The N-terminal region of Pseudomonas type III effector AvrPtoB elicits Pto-dependent immunity and has two distinct virulence determinants
    Xiao, F., He, P., Abramovitch, R. B., Dawson, J. E., Nicholson, L. K., Sheen, J., & Martin, G. B.
    Plant J. 52, 595-614 (2007).
  • Thermodynamic dissection of the Ezrin FERM/CERMAD interface.
    Jayaraman, B. & Nicholson, L. K.
    Biochemistry 46, 12174-12189 (2007).
  • Prolyl cis-trans isomerization as a molecular timer.
    Lu, K. P., Finn, G., Lee, T. H. & Nicholson, L. K.
    Nat. Chem. Biol. 3, 619-629 (2007).
  • Prolyl cis-trans Isomerization as a molecular timer in Crk signaling.
    Nicholson, L. K. & Lu, K. P.
    Mol. Cell 25, 483-485 (2007).


  • The prolyl isomerase Pin1 regulates amyloid precursor protein processing and amyloid-beta production.
    Pastorino, L., Sun, A., Lu, P., Zhou, X. Z., Balastik, M., Finn, G., Wulf, G., Lim, J., Li, S., Li, X., Xia, W., Nicholson, L. K., & Lu, K. P.
    Nature 440, 528-534 (2006).
  • Backbone resonance assignments of Ezrin C ERMAD in a non-covalent complex with Ezrin N FERM.
    Jayaraman, B. & Nicholson, L. K.
    J. Biomol. NMR 36 Suppl 1, 63 (2006).


  • The solution structure of type III effector protein AvrPto reveals conformational and dynamic features important for plant pathogenesis.
    Wulf, J., Pascuzzi, P.E., Fahmy, A., Martin, G. B. & Nicholson, L. K.
    Structure 12, 1257-1268 (2004).


  • Backbone dynamics and thermodynamics of Borrelia outer surface protein A.
    Pawley, N. H., Koide, S. & Nicholson, L. K.
    J. Mol. Biol. 324, 991-1002 (2002).
  • Factors determining the reliable description of global tumbling parameters in solution NMR.
    Pawley, N. H., Gans, J. D. & Nicholson, L. K.
    J. Biomol. NMR 24, 215-229 (2002).
  • 1H, 15N and 13C chemical shift assignments of the structured core of the pseudomonas effector protein AvrPto.
    Wulf, J., Pascuzzi, P. E., Martin, G. B. & Nicholson, L. K.
    J. Biomol. NMR 23, 247-248 (2002).


  • The role of backbone motions in ligand binding to the c-Src SH3 domain.
    Wang, C., Pawley, N. H. & Nicholson, L. K.
    J. Mol. Biol. 313, 873-887 (2001).
  • An improved method for distinguishing between anisotropic tumbling and chemical exchange in analysis of 15N relaxation parameters.
    Pawley, N. H., Wang, C., Koide, S. & Nicholson, L. K.
    J. Biomol. NMR 20, 149-165 (2001).
  • Importance of the N terminus of rous sarcoma virus protease for structure and enzymatic function.
    Schatz, G. W., Reinking, J., Zippin, J., Nicholson, L. K. & Vogt, V. M.
    J. Virol. 75, 4761-4770 (2001).
  • An increase in side chain entropy facilitates effector binding: NMR characterization of the side chain methyl group dynamics in Cdc42Hs.
    Loh, A. P., Pawley, N., Nicholson, L. K. & Oswald, R. E.
    Biochemistry 40, 4590-4600 (2001).
  • Phosphorylation-induced structural changes in the amyloid precursor protein cytoplasmic tail detected by NMR.
    Ramelot, T. A. & Nicholson, L. K.
    J. Mol. Biol. 307, 871-884 (2001).
  • 1H, 15N and 13C assignments of a monomeric N-terminal deletion mutant of the Rous sarcoma virus protease.
    Reinking, J. L., Schatz, G. W., Vogt, V. M. & Nicholson, L. K.
    J. Biomol. NMR 19, 279-280 (2001).
  • Solution structure of ThiS and implications for the evolutionary roots of ubiquitin.
    Wang, C., Xi, J., Begley, T. P. & Nicholson, L. K.
    Nat. Struct. Biol. 8, 47-51 (2001).


  • Ligand-induced strain in hydrogen bonds of the c-Src SH3 domain detected by NMR.
    Cordier, F., Wang, C., Grzesiek, S. & Nicholson, L. K.
    J. Mol. Biol. 304, 497-505 (2000).
  • Protein dynamics measurements by TROSY-based NMR experiments.
    Zhu, G., Xia, Y., Nicholson, L. K. & Sze, K. H.
    J. Magn. Reson. 143, 423-426 (2000).
  • Transient structure of the amyloid precursor protein cytoplasmic tail indicates preordering of structure for binding to cytosolic factors.
    Ramelot, T. A., Gentile, L. N. & Nicholson, L. K.
    Biochemistry 39, 2714-2725 (2000).


  • Backbone dynamics of inactive, active, and effector-bound Cdc42Hs from measurements of (15)N relaxation parameters at multiple field strengths.
    Loh, A. P., Guo, W., Nicholson, L. K. & Oswald, R. E.
    Biochemistry 38, 12547-12557 (1999).
  • Gramicidin channel controversy--revisited.
    Cross, T. A., Arseniev, A., Cornell, B. A., Davis, J. H., Killian, J. A., Koeppe II, R. E., Nicholson, L. K., Separovic, F. & Wallace, B. A.
    Nat. Struct. Biol. 6, 610-1; discussion 611-2 (1999).


  • Heteronuclear NMR studies of the combined Src homology domains 2 and 3 of pp60 c-Src: effects of phosphopeptide binding.
    Tessari, M., Gentile, L. N., Taylor, S. J., Shalloway, D. I., Nicholson, L. K. & Vuister, G. W.
    Biochemistry 36, 14561-14571 (1997).


  • Three-dimensional solution structure of the HIV-1 protease complexed with DMP323, a novel cyclic urea-type inhibitor, determined by nuclear magnetic resonance spectroscopy.
    Yamazaki, T., Hinck, A. P., Wang, Y. X., Nicholson, L. K., Torchia, D. A., Wingfield, P., Stahl, S. J., Kaufman, J. D., Chang, C. H., Domaille, P. J. & Lam, P. Y.
    Protein Sci. 5, 495-506 (1996).


  • Flexibility and function in HIV-1 protease.
    Nicholson, L. K., Yamazaki, T., Torchia, D. A., Grzesiek, S., Bax, A., Stalh, S. J., Kaufman, J. D., Wingfield, P. T., Lam, P. Y. S., Jadhav, P. K., Hodge, C. N., Domaille, P. J. & Chang, C. H.
    Nat. Struct. Biol. 2, 274-280 (1995).


  • Structural analysis of highly oriented poly(p-phenylene-terephthalamide) by 15N solid-state nuclear magnetic resonance.
    Yeo, J. H., Demura, M., Asakura, T., Fujito, T., Imanari, M., Nicholson, L. K. & Cross, T. A.
    Solid State Nucl. Magn. Reson. 3, 209-218 (1994).
  • Yamazaki, T. et al. Secondary structure and signal assignments of human-immunodeficiency-virus-1 protease complexed to a novel, structure-based inhibitor.
    Yamazaki, T., Nicholson, L. K., Torchia, D. A., Stahl, S. J., Kaufman, J. D., Wingfield, P. T., Domaille, P. J. & Campbell-Burk, S.
    Eur. J. Biochem. 219, 707-712 (1994).


  • A method for studying the structure of uniaxially aligned biopolymers using solid state 15N-nmr: application to Bombyx mori silk fibroin fibers.
    Nicholson, L. K., Asakura, T., Demura, M. & Cross, T.A.
    Biopolymers 33, 847-861 (1993).


  • Dynamics of methyl groups in proteins as studied by proton-detected 13C NMR spectroscopy. Application to the leucine residues of staphylococcal nuclease.
    Nicholson, L. K. et al.
    Biochemistry 31, 5253-5263 (1992).


  • Molecular dynamics computations and solid state nuclear magnetic resonance of the gramicidin cation channel.
    Chiu, S. W., Nicholson, L. K., Brenneman, M. T., Subramaniam, S., Teng, Q., McCammon, J. A., Cross, T. A., & Jakobsson, E.
    Biophys. J. 60, 974-978 (1991).
  • Solid-state nuclear magnetic resonance derived model for dynamics in the polypeptide backbone of the gramicidin A channel.
    Nicholson, L. K., Teng, Q. & Cross, T. A.
    J. Mol. Biol. 218, 621-637 (1991).
  • Experimental determination of torsion angles in the polypeptide backbone of the gramicidin A channel by solid state nuclear magnetic resonance.
    Teng, Q., Nicholson, L. K. & Cross, T. A.
    J. Mol. Biol. 218, 607-619 (1991).


  • Gramicidin cation channel: an experimental determination of the right-handed helix sense and verification of beta-type hydrogen bonding.
    Nicholson, L. K. & Cross, T. A.
    Biochemistry 28, 9379-9385 (1989).


  • Solid-state 15N-NMR evidence that gramicidin A can adopt two different backbone conformations in dimyristoylphosphatidylcholine model membrane preparations.
    Killian, J. A., Nicholson, L. K. & Cross, T. A.
    Biochim. Biophys. Acta 943, 535-540 (1988).