- T. Doherty and M. Hong, “2D 1H-31P Solid-State NMR Studies of the Dependence of Inter-Bilayer Water Dynamics on Lipid Headgroup Structure and Membrane Peptides”, J. Magn. Reson., 196, 39-47 (2009). PMID: 18938095.
- M. Tang, A.J. Waring and M. Hong, “Effects of Arginine Density on the Membrane-Bound Structure of a Cationic Antimicrobial Peptide from Solid-State NMR”, Biochim. Biophys. Acta Biomembranes, 1788, 514-521 (2009). PMID: 19059201.
- S.D. Cady, T.V. Mishanina and M. Hong, “Structure of Amantadine-Bound M2 Transmembrane Peptide of Influenza A in Lipid Bilayers from Magic-Angle-Spinning Solid-State NMR: the Role of Ser31 in Amantadine Binding”, J. Mol. Biol. 385, 1127-1141 (2009). PMID: 19061899.
- M. Tang and M. Hong. “Structure and Mechanism of Beta-Hairpin Antimicrobial Peptides in Lipid Bilayers from Solid-State NMR Spectroscopy”, review, Mol. Biosys, 5, 317-322 (2009). PMID: 19396367.
- W. Luo, S.D. Cady, and M. Hong, “Immobilization of the Influenza A M2 Transmembrane Peptide in Viral-Envelope Mimetic Lipid Membranes Detected by Solid-State NMR Spectroscopy”, Biochemistry, 48, 6361-6368 (2009). PMID: 19489611.
- J. Wang, S.D. Cady, V. Balannik, L.H. Pinto, W.F. DeGrado, and M. Hong, “Discovery of Spiro-piperidine inhibitors and their modulation of the dynamics of the M2 proton channel from influenza A Virus”, J. Am. Chem. Soc. 131, 8066-8076 (2009). PMID: 19469531.
- Y. Su and M. Hong, “Roles of arginine and lysine residues in the translocation of a cell-penetrating peptide from (13)C, (31)P, and (19)F solid-state NMR”, Biochemistry, 48, 4587-4595 (2009). PMID: 19364134.
- M. Hong, T.V. Mishanina and S.D. Cady, “Accurate Measurement of Methyl 13C Chemical Shifts by Solid-State NMR for the Determination of Protein Sidechain Conformation: the Influenza A M2 Transmembrane Peptide as an Example”, J. Am. Chem. Soc. 131, 7806-7816 (2009). PMID: 19441789.
- T. Doherty and M. Hong, “High-Resolution Solid-State NMR of Anisotropically Mobile Molecules Under Very Low Power 1H Decoupling and Moderate Magic-Angle Spinning”, J. Magn. Reson. 199, 225-232 (2009). PMID:19501003.
- S. D. Cady and M. Hong, “Effects of Amantadine Binding on the Dynamics of Bilayer-Bound Influenza A M2 Transmembrane Peptide Studied by NMR Relaxation”, J. Biomol. NMR, 45, 185-196 (2009). PMID: 19633911.
- .S.D. Cady, W. Luo, F. Hu, and M. Hong, “Structure and function of the influenza M2 proton channel”, Current Topic, Biochemistry, 48, 7356-7364 (2009). PMID: 19601584.
- Y. Zhang, T. Doherty, J. Li, W. Lu, C. Barinka, J. Lubkowski and M. Hong, “Resonance Assignment and Three-Dimensional Structure Determination of a Human Alpha-Defensin, HNP-1, by Solid-State NMR”, J. Mol. Biol., 397, 408-422 (2010). PMID: 20097206.
- S. Li, Y. Zhang, and M. Hong, “3D 13C-13C-13C Correlation NMR for De Novo Distance Determination of Solid Proteins and Application to a Human Alpha Defensin”, J. Magn. Reson. 202, 203-210 (2010). PMID: 19963419.
- S. D. Cady, K. Schmidt-Rohr, J. Wang, C.S. Soto, W. F. DeGrado, and M. Hong, “Structure of the Amantadine Binding Site of Influenza M2 Proton Channels In Lipid Bilayers”, Nature, 463, 689 (2010). PMID: 20130653.
- W. Luo and M. Hong, “Conformational Changes of an Ion Channel Detected Through Water-Protein Interactions Using Solid-State NMR”, J. Am. Chem. Soc. 132, 2378-2384 (2010). PMID: 20112896.
- S. Li, Y. Su, W. Luo, and M. Hong., “Water-protein interactions of an arginine-rich membrane peptide in lipid bilayers investigated by solid-state nuclear magnetic resonance spectroscopy”. J. Phys. Chem. B, 114, 4063-4069 (2010). PMID: 20199036.
- T. Doherty, Y. Su and M. Hong, “High-Resolution Orientation and Depth of Insertion of the Voltage-Sensing S4 Helix of a Potassium Channel in Lipid Bilayers”, J. Mol. Biol. 401, 642-652 (2010). PMID: 20600109.
- Y. Su, W.F. DeGrado and M. Hong, “Orientation, dynamics and lipid interaction of an antimicrobial arylamide in lipid bilayers investigated by 19F and 31P solid-state NMR”, J. Am. Chem. Soc. 132, 9197-9205 (2010). PMID: 20536141.
- Y. Su, A.J. Waring, P. Ruchala, and M. Hong, “Membrane-bound dynamic structure of an Arginine-rich cell-penetrating peptide, the protein transduction domain of HIV TAT, from solid-state NMR”, Biochemistry, 49, 6009-6020 (2010). PMID: 20550193.
- F. Hu, W. Luo, and M. Hong, “Mechanisms of proton conduction and gating by influenza M2 proton channels from solid-state NMR”, Science, 330, 505-508 (2010). PMID: 20966251.
- Y. Zhang and M. Hong, “Membrane-bound structure and topology of a human alpha-defensin indicates dimer pore as the mechanism of antimicrobial activity”, Biochemistry, 49, 9770-9782 (2010). PMID: 20961099.
- F. Hu, W. Luo, S.D. Cady and M. Hong, “Conformational Plasticity of the Influenza A M2 Transmembrane Peptide in Lipid Bilayers Under Varying pH, Drug Binding and Membrane Thickness”, Biochim. Biophys. Acta, 1808, 415-423 (2011). PMID: 20883664.
- S. Li and M. Hong, “Protonation, Tautomerization and Rotameric Structure of Histidine: A Comprehensive Study through High Resolution Solid-state NMR”, J. Am. Chem. Soc. 133, 1534-1544 (2011). PMID: 21207964.
- M. Dick-Perez, Y. Zhang, J. Hayes, A. Salazar, O.A. Zabotina and M. Hong, “Structure and Interactions of Plant Cell-Wall Polysaccharides by 2D and 3D Magic-Angle-Spinning Solid-State NMR”, Biochemistry, 50, 989-1000 (2011). PMID: 21204530.
- S.D. Cady, J. Wang, Yibing Wu, W.F. DeGrado, and M. Hong, “Specific binding of adamantane drugs and direction of their polar amines in the pore of the influenza M2 transmembrane domain in lipid bilayers and dodecylphosphocholine micelles determined by NMR spectroscopy”, J. Am. Chem. Soc. 133, 4274-4284 (2011). PMID: 21381693.
- Y. Su, A.J. Waring, P. Ruchala, and M. Hong, “Structure of ?-hairpin Antimicrobial Peptides in Lipopolysaccharide Membranes: Mechanism of Gram Selectivity Obtained from Solid-State Nuclear Magnetic Resonance”, Biochemistry, 50, 2072-2083 (2011). PMID: 21302955.
- M. Hong and Y. Su, “Structure and Dynamics of Cationic Membrane Peptides and Proteins: Insights from Solid-State NMR”, Protein Sci., review, 20, 641-655 (2011). PMID: 21344534.
- S.D. Cady, T. Wang, and M. Hong, “Membrane-Dependent Effects of a Cytoplasmic Helix on the Structure and Drug Binding of the Influenza M2 Protein”, J. Am. Chem. Soc. 133, 11572-11579 (2011). PMID: 21661724.
- J. Wang, C. Ma, G. Fiorin, V. Carnevale, T. Wang, F. Hu, R. A. Lamb, M. L. Klein, L. H. Pinto, M. Hong, and W. F. DeGrado, “Molecular Dynamics Simulation Directed Rational Design of Inhibitors Targeting Drug-Resistant Mutants of Influenza A Virus M2”, J. Am. Chem. Soc. 133, 12834-12841 (2011). PMID: 21744829.
- Y. Su and M. Hong, “Conformational disorder of membrane peptides investigated from solid-state NMR line widths and line shapes”, J. Phys. Chem. 115, 10758-10767 (2011). PMID: 21806038.
- M. Hong, Y. Zhang and F. Hu, “Membrane protein structure and dynamics from NMR spectroscopy”, Review, Annu. Rev. Phys. Chem., 63, 1-24. (2012). PMID: 22136620.
- F. Hu, K. Schmidt-Rohr and M. Hong, “NMR Detection of pH-Dependent Histidine-Water Proton Exchange Reveals the Conduction Mechanism of a Transmembrane Proton Channel”, J. Am. Chem. Soc. 134, 3703-3713 (2012). PMID: 21974716. Cover of JACS volume 134, issue 8.
- T. Wang, S.D. Cady, and M. Hong, “NMR Determination of Protein Partitioning into Membrane Domains with Different Curvatures and Application to the Influenza M2 Protein”, Biophys. J. 102, 787-794 (2012). PMID: 22385849.
- D. M Harris, K. Corbin, T. Wang, R. Gutierrez, A.L. Bertolo, C. Petti, D.M. Smilgies, J. M. Estevez, D. Bonetta, B. Urbanowicz, D. Ehrhardt, C. R. Somerville, J. K.C. Rose, M. Hong, S. DeBolt, “Cellulose microfibril crystallinity is reduced by mutating C-terminal transmembrane region residues CESA1A903V and CESA3T942I of cellulose synthase”, Proc. Natl. Acad. Sci. USA, 109, 4098-4103 (2012). PMID: 22375033.
- M. Dick-Perez, T. Wang, A. Salazar, O. Zabotina, and M. Hong, “Multidimensional Solid-State NMR Studies of the Structure and Dynamics of Pectic Polysaccharides in Uniformly 13C-Labeled Arabidopsis Primary Cell Walls”, Magn. Reson. Chem. 50, 539-550 (2012). PMID: 22777793.
- Y. Su, F. Hu and M. Hong, “Paramagnetic Cu(II) For Probing Membrane Protein Structure and Function: Inhibition Mechanism of the Influenza M2 Proton Channel”, J. Am. Chem. Soc. 134, 8693-8702, 2012. PMID: 22519936.
- M. Hong, K. Fritzsching, and J. K. Williams, “Hydrogen-Bonding Partner of the Proton-Conducting Histidine in the Influenza M2 Proton Channel Revealed From 1H Chemical Shifts”, J. Am. Chem. Soc. 134, 14753-5 (2012).
- S. Li, Y. Su, and M. Hong, “Intramolecular 1H-13C distance measurement in uniformly 13C, 15N labeled peptides by solid-state NMR”, Solid State Nucl. Magn. Reson. 45-46, 51-58 (2012).
- M. Hong and W.F. DeGrado, “Structural Basis For Proton Conduction and Inhibition by the Influenza M2 Protein”, Invited review, Protein Sci, 21, 1620-1633 (2012).
- K. Schmidt-Rohr, K. J. Fritzsching, S. Y. Liao, M. Hong, “Spectral Editing of Two-Dimensional Magic-Angle-Spinning Solid-State NMR Spectra for Protein Resonance Assignment and Structure Determination”, J. Biomol. NMR., 54, 343-353 (2012).
- T. Wang, L. Widanapathirana, Y. Zhao* and M. Hong*, “Aggregation and Dynamics of Oligocholate Transporters in Phospholipid Bilayers Revealed by Solid-State NMR Spectroscopy”, Langmuir, 28, 17071-17078 (2012).
- T. Wang, O. Zabotina, and M. Hong, “Pectin-cellulose and protein-polysaccharide interactions in Arabidopsis primary cell walls by 2D 13C Correlation NMR”, Biochemistry, 51, 9846-9856 (2012).
- H. Yao, and M. Hong, “Membrane-Dependent Conformation, Dynamics, and Lipid Interactions of the Fusion Peptide of the Paramyxovirus PIV5 From Solid-State NMR”, J. Mol. Biol, 425, 563-576 (2013).
- Su Y, Li S, and Hong M. “Cationic membrane peptides: atomic-level insight of structure-activity relationships from solid-state NMR”, Amino Acids, 2013, 44, 821-833 (2013).
- M. Hong and K. Schmidt-Rohr, “Magic-Angle-Spinning NMR Techniques for Measuring Long-Range Distances in Biological Macromolecules”, Acct. Chem. Res, 46, 2154-63 (2013).
- J. Williams, Y. Zhang, K. Schmidt-Rohr, and M. Hong, “Solid-state NMR investigation of the pH-dependent structure and dynamics of the gating residue of the influenza M2 proton channel”, Biophys. J., 104, 1698-1708 (2013). New and Notable commentary on 1639-1640.
- T. Wang, H. Yao and M. Hong, “Determining the Depth of Insertion of Dynamically Invisible Membrane Peptides by Gel-Phase 1H Spin Diffusion Heteronuclear Correlation NMR”, J. Biomol. NMR, 56, 139-148 (2013).
- K. J. Fritzsching, Y. Yang, K. Schmidt-Rohr, and Mei Hong, “Practical Use of Chemical Shift Databases for Protein Solid-State NMR: 2D Chemical Shift Maps and Amino-Acid Assignment with Secondary-Structure Information”, J. Biomol. NMR, 56, 155-167 (2013).
- J.K. Williams, D. Tietze, J. Wang, Y. Wu, W.F. DeGrado and M. Hong, “Structural Basis for Proton Conduction and Inhibition of the S31N Mutant of the Influenza M2 Proton Channel Investigated by Solid-State NMR”, J. Am. Chem. Soc. 135, 9885-9897 (2013).
- R.L. Johnson, J.M. Anderson, B.H. Shanks, X. Fang, M. Hong, K. Schmidt-Rohr, “Spectrally edited 2D 13C-13C NMR spectra without diagonal ridge for characterizing 13C-enriched low-temperature carbon materials”, J. Magn. Reson. 234C, 112-124 (2013).
- B. Kwon, A.J. Waring and M. Hong, “A 2H Solid-State NMR Study of Lipid Clustering by Cationic Antimicrobial and Cell-Penetrating Peptides in Model Bacterial Membranes”, Biophys. J. 105, 2333-42 (2013).
- T. Wang, Y.B. Park, M.A. Caporini, M. Rosay, D.J. Cosgrove and M. Hong, “Sensitivity-Enhanced Solid-State NMR Elucidation of Protein Binding to Cell Walls”, Proc. Natl. Acad. Sci. USA, 110, 16444-9 (2013).
- S. Y. Liao, K. J. Fritzsching, and M. Hong, “Conformational analysis of the full-length M2 protein of the influenza A virus using solid-state NMR”, Protein Sci. 22, 1623-38 (2013).
- Y. Yang, K.J. Fritzsching, and M. Hong, “Resonance Assignment of Disordered Proteins Using a Multi-Objective Non-Dominated Sorting Genetic Algorithm”, J. Biomol. NMR, 57, 281-96 (2013).
- H. Yao and M. Hong, “Conformation and Lipid Interaction of the Fusion Peptide of the Paramyxovirus PIV5 in Anionic and Negative-Curvature Membranes From Solid-State NMR”, J. Am. Chem. Soc., 136, 2611-2624 (2014).
- T. Wang, O. Zabotina, and M. Hong, “Structure and Dynamics of Brachypodium Primary Cell Wall Polysaccharides From Solid-State NMR Spectroscopy”, Biochemistry, 53, 2840-2854 (2014).
- P. B. White, T. Wang, Y.B. Park, D.C. Cosgrove and M. Hong, “Water-Polysaccharide Interactions in the Primary Cell Wall of Arabidopsis Thaliana from Polarization Transfer Solid-State NMR”, J. Am. Chem. Soc. 136, 10399-10409 (2014).
- M. Lee and M. Hong, “Cryoprotection of Lipid Membranes for High-Resolution Solid-State NMR Studies of Membrane Peptides and Proteins at Low Temperature”, J. Biomol. NMR, 59, 263-277 (2014).
- J. K. Williams and M. Hong, “Probing Membrane Protein Structure Using Water Polarization Transfer Solid-State NMR”, perspectives article, J. Magn. Reson. 247, 118-127 (2014).
- N. Joh, T. Wang, M. Bhate, R. Acharya, Y. Wu, M. Grabe*, M. Hong*, G. Grigoryan* and W.F. DeGrado*, De novo design of a transmembrane Zn(II) transporting four-helix bundle, Science, 346, 1520-1524 (2014).
- T. Wang, J. K. Williams, K. Schmidt-Rohr and M. Hong, “Relaxation-Compensated Difference Spin Diffusion NMR for Detecting 13C-13C Long-Range Correlations in Proteins and Polysaccharides”, J. Biomol. NMR, 61, 97-107 (2015).
- T. Wang and M. Hong, “Investigation of the Curvature Generation and Membrane Localization of the Influenza Virus M2 Protein Using Static and Off-Magic-Angle Spinning Solid-State NMR of Oriented Bicelles”, Biochemistry, in press (2015).
- Y. Yang, H.W. Yao and M. Hong, “Differentiating bicontinuous lipid cubic phases from isotropic membrane morphologies using 31P solid-state NMR spectroscopy”, J. Phys. Chem. B, in press (2015).
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