Pubmed list of publications.

  1. Thiagarajan-Rosenkranz P, Draney AW, Lorieau JL. (2017) Hybrid NMR: A Union of Solution- and Solid-State NMR. J. Am. Chem. Soc. 139(13): 4715-4723. doi: 10.1021/jacs.6b11402.
  2. Smrt ST, Lorieau JL. (2016) Membrane Fusion and Infection of the Influenza Hemagglutinin (Chapter). Adv. Exp. Med. Biol. (Springer): 1-18. doi: 10.1007/5584_2016_174.
  3. Sheng R, Jung DJ, Silkov A, Kim H, Singaram I, Wang ZG, Xin Y, Kim E, Park MJ, Thiagarajan-Rosenkranz P, Smrt S, Honig B, Beak K, Ryu S, Lorieau JL, Kim YM, Cho W. (2016) Lipids regulate Lck activity through their interactions with the Lck SH2 domain. J. Biol. Chem,. 291: 17639-17650. doi: 10.1074/jbc.M116.720284.
  4. Park MJ, Sheng R, Silkov A, Jung DJ, Wang ZG, Xin Y, Kim H, Thiagarajan-Rosenkranz P, Song S, Yoon Y, Nam W, Kim I, Kim E, Lee DG, Chen Y, Singaram I, Wang L, Jang MH, Hwang CS, Honig B, Ryu S, Lorieau JL, Kim YM, Cho W. (2016) SH2 Domains Serve as Lipid-Binding Modules for pTyr-Signaling Proteins. Mol. Cell. 62(1): 7-20. doi: 10.1016/j.molcel.2016.01.027.
  5. Thiagarajan-Rosenkranz P, Draney AW, Smrt ST, Lorieau JL. (2015) A Positively Charged Liquid Crystalline Medium for Measuring Residual Dipolar Couplings in Membrane Proteins by NMR. J. Am. Chem. Soc. 137(37): 11932-11934. doi: 10.1021/jacs.5b07515.
  6. Smrt ST, Draney AW, Lorieau JL. (2015) The Influenza Hemagglutinin Fusion Domain is an Amphipathic Helical-Hairpin that Functions by Inducing Membrane Curvature. J. Biol. Chem. 290: 228-238. doi: 10.1074/jbc.M114.611657.
  7. Eichmann C, Orts J, Tzitzilonis C, Vögeli BR, Smrt ST, Lorieau JL, Riek R. (2014) Intermolecular Detergent – Membrane Protein NOEs for the Characterization of Dynamics of Membrane Protein-Detergent Complexes. J. Chem. Phys. B. 118: 14288-14301. doi: 10.1021/jp509137q.
  8. Draney AW, Smrt ST, Lorieau JL. (2014) Use of Isotropically Tumbling Bicelles to Measure Curvature Induced by Membrane Components. Langmuir. 30: 11723-11733. doi: 10.1021/la5030668.

  1. Lorieau JL, Maltsev AS, Louis JM, Bax A. (2013) Modulating alignment of membrane proteins in liquid-crystalline and oriented gel media by changing the size and charge of phospholipid bicelles. J. Biomol. NMR. 55: 369-377. doi: 10.1007/s10858-013-9720-3.
  2. Lorieau JL, Louis JM, Schwieters CD, Bax A. (2012) pH-triggered, activated-state conformations of the influenza hemagglutinin fusion peptide revealed by NMR. Proc. Nat'l. Acad. Sci. USA. 109: 19994-19999. doi: 10.1073/pnas.1213801109.
  3. Lorieau JL, Louis JM, Bax A. (2012) The impact of influenza hemagglutinin fusion peptide length and viral subtype on its structure and dynamics. Biopolymers. 99(3): 189-195. doi: 10.1002/bip.22102.
  4. Lorieau JL, Louis JM, Bax A. (2011) Whole-Body Rocking Motion of a Fusion Peptide in Lipid Bilayers from Size-Dispersed 15N NMR Relaxation. J. Am. Chem. Soc. 133: 14184-14187. doi: 10.1021/ja2045309.
  5. Lorieau JL, Louis JM, Bax A. (2011) Helical Hairpin Structure of Influenza Hemagglutinin Fusion Peptide Stabilized by Charge−Dipole Interactions between the N-Terminal Amino Group and the Second Helix. J. Am. Chem. Soc. 133: 2824-2827. doi: 10.1021/ja1099775.
  6. Lorieau JL, Louis JM, Bax A. (2010) The complete influenza hemagglutinin fusion domain adopts a tight helical hairpin arrangement at the lipid:water interface. Proc. Nat'l. Acad. Sci. USA. 107: 11341-11346. doi: 10.1073/pnas.1006142107.
  7. Xu YM, Lorieau JL, McDermott, AE. (2010) Triosephosphate Isomerase: N-15 and C-13 Chemical Shift Assignments and Conformational Change upon Ligand Binding by Magic-Angle Spinning Solid-State NMR Spectroscopy. J. Mol. Biol. 397: 233-248. doi: 10.1016/j.jmb.2009.10.043.
  8. Lorieau JL, Yao L, Bax A. (2008) Liquid crystalline phase of G-tetrad DNA for NMR study of detergent-solubilized proteins. J. Am. Chem. Soc. 130: 7536-7537. doi: 10.1021/ja801729f.
  9. Lorieau JL, Day LA, McDermott AE. (2008) Conformational dynamics of an intact virus: Order parameters for the coat protein of Pf1 bacteriophage. Proc. Nat'l. Acad. Sci. USA. 105: 10366-10371. doi: 10.1073/pnas.0800405105.
  10. Lorieau JL, McDermott AE. (2006) Conformational Flexibility of a Microcrystalline Globular Protein: Order Parameters by Solid-State NMR. J. Am. Chem. Soc. 128: 11505-11512. doi: 10.1021/ja062443u.
  11. Lorieau JL, McDermott AE. (2006) Order Parameters Based on 13C1H, 13C1H2 and 13C1H3 Heteronuclear Dipolar Powder Patterns: A Comparison of MAS-Based Solid-State NMR Sequences. Magn. Reson. Chem. 44: 334-347. doi: 10.1002/mrc.1773.
  12. Shoemaker GK, Lorieau JL, Lau LH, Gillmore CS, Palcic MM. (2006) Multiple Sampling in Single-Cell Enzyme Assays Using CE-Laser-Induced Fluorescence to Monitor Reaction Progress. Anal. Chem. 77: 3132-3137. doi: 10.1021/ac0481304.
  13. Lorieau JL, Shoemaker GK, Palcic MM. (2003) Quantitative Nanopipettor for Miniaturized Chemical and Biochemical Reaction Sampling. Anal. Chem. 75: 6351-6354. doi: 10.1021/ac0302410.
  14. Gillmor CS, Poindexter P, Lorieau JL, Palcic MM, Somerville C. (2002) Alpha-Glucosidase I is Required for Cellulose Biosynthesis and Morphogenesis in Arabidopsis. J. Cell. Biol. 156: 1003-1013. doi: 10.1083/jcb.200111093.