Year |
Citation |
Score |
2023 |
Medeiros-Silva J, Dregni AJ, Hong M. Distinguishing Different Hydrogen-Bonded Helices in Proteins by Efficient H-Detected Three-Dimensional Solid-State NMR. Biochemistry. 63: 181-190. PMID 38127783 DOI: 10.1021/acs.biochem.3c00589 |
0.329 |
|
2023 |
Sučec I, El Mammeri N, Dregni AJ, Hong M. Rapid Determination of the Topology of Oligomeric α-Helical Membrane Proteins by Water- and Lipid-Edited Methyl NMR. The Journal of Physical Chemistry. B. 127: 7518-7530. PMID 37606918 DOI: 10.1021/acs.jpcb.3c05295 |
0.391 |
|
2022 |
Medeiros-Silva J, Somberg NH, Wang HK, McKay MJ, Mandala VS, Dregni AJ, Hong M. pH- and Calcium-Dependent Aromatic Network in the SARS-CoV-2 Envelope Protein. Journal of the American Chemical Society. 144: 6839-6850. PMID 35380805 DOI: 10.1021/jacs.2c00973 |
0.341 |
|
2022 |
Sutherland M, Tran N, Hong M. Clustering of tetrameric influenza M2 peptides in lipid bilayers investigated by F solid-state NMR. Biochimica Et Biophysica Acta. Biomembranes. 1864: 183909. PMID 35276226 DOI: 10.1016/j.bbamem.2022.183909 |
0.319 |
|
2021 |
Shcherbakov AA, Medeiros-Silva J, Tran N, Gelenter MD, Hong M. From Angstroms to Nanometers: Measuring Interatomic Distances by Solid-State NMR. Chemical Reviews. PMID 34694769 DOI: 10.1021/acs.chemrev.1c00662 |
0.319 |
|
2021 |
Reif B, Ashbrook SE, Emsley L, Hong M. Solid-state NMR spectroscopy. Nature Reviews. Methods Primers. 1. PMID 34368784 DOI: 10.1038/s43586-020-00002-1 |
0.529 |
|
2021 |
Sutherland M, Kwon B, Hong M. Interactions of HIV gp41's membrane-proximal external region and transmembrane domain with phospholipid membranes from P NMR. Biochimica Et Biophysica Acta. Biomembranes. 183723. PMID 34352242 DOI: 10.1016/j.bbamem.2021.183723 |
0.341 |
|
2021 |
Elkins MR, Bandara A, Pantelopulos GA, Straub JE, Hong M. Direct Observation of Cholesterol Dimers and Tetramers in Lipid Bilayers. The Journal of Physical Chemistry. B. PMID 33560844 DOI: 10.1021/acs.jpcb.0c10631 |
0.302 |
|
2020 |
Mandala VS, McKay MJ, Shcherbakov AA, Dregni AJ, Kolocouris A, Hong M. Structure and drug binding of the SARS-CoV-2 envelope protein transmembrane domain in lipid bilayers. Nature Structural & Molecular Biology. PMID 33177698 DOI: 10.1038/s41594-020-00536-8 |
0.323 |
|
2020 |
Gelenter MD, Dregni AJ, Hong M. Pulsed Third-Spin-Assisted Recoupling NMR for Obtaining Long-Range C-C and N-C Distance Restraints. The Journal of Physical Chemistry. B. PMID 32700540 DOI: 10.1021/Acs.Jpcb.0C04574 |
0.417 |
|
2020 |
Kwon B, Mandal T, Elkins MR, Oh Y, Cui Q, Hong M. Cholesterol Interaction with the Trimeric HIV Fusion Protein gp41 in Lipid Bilayers Investigated by Solid-State NMR Spectroscopy and Molecular Dynamics Simulations. Journal of Molecular Biology. PMID 32592698 DOI: 10.1016/J.Jmb.2020.06.017 |
0.428 |
|
2020 |
Dregni AJ, Duan P, Hong M. Hydration and Dynamics of Full-Length Tau Amyloid Fibrils Investigated by Solid-State NMR. Biochemistry. PMID 32453948 DOI: 10.1021/Acs.Biochem.0C00342 |
0.354 |
|
2020 |
Shcherbakov AA, Roos M, Kwon B, Hong M. Two-dimensional F-C correlation NMR for F resonance assignment of fluorinated proteins. Journal of Biomolecular Nmr. PMID 32088840 DOI: 10.1007/S10858-020-00306-0 |
0.337 |
|
2020 |
Mandala VS, Loftis AR, Shcherbakov AA, Pentelute BL, Hong M. Atomic structures of closed and open influenza B M2 proton channel reveal the conduction mechanism. Nature Structural & Molecular Biology. PMID 32015551 DOI: 10.1038/S41594-019-0371-2 |
0.376 |
|
2019 |
Phyo P, Hong M. Fast MAS H-C correlation NMR for structural investigations of plant cell walls. Journal of Biomolecular Nmr. PMID 31535304 DOI: 10.1007/S10858-019-00277-X |
0.394 |
|
2019 |
Lee M, Morgan CA, Hong M. Fully Hydrophobic HIV gp41 Adopts a Hemifusion-Like Conformation in Phospholipid Bilayers. The Journal of Biological Chemistry. PMID 31409642 DOI: 10.1074/Jbc.Ra119.009542 |
0.461 |
|
2019 |
Dregni AJ, Mandala VS, Wu H, Elkins MR, Wang HK, Hung I, DeGrado WF, Hong M. In vitro 0N4R tau fibrils contain a monomorphic β-sheet core enclosed by dynamically heterogeneous fuzzy coat segments. Proceedings of the National Academy of Sciences of the United States of America. PMID 31358628 DOI: 10.1073/Pnas.1906839116 |
0.317 |
|
2019 |
Gelenter MD, Smith KJ, Liao SY, Mandala VS, Dregni AJ, Lamm MS, Tian Y, Xu W, Pochan DJ, Tucker TJ, Su Y, Hong M. The peptide hormone glucagon forms amyloid fibrils with two coexisting β-strand conformations. Nature Structural & Molecular Biology. PMID 31235909 DOI: 10.1038/s41594-019-0238-6 |
0.602 |
|
2019 |
Kwon B, Roos M, Mandala VS, Shcherbakov AA, Hong M. Elucidating Relayed Proton Transfer through a his-Trp-his Triad of a Transmembrane Proton Channel by Solid-State NMR. Journal of Molecular Biology. PMID 31082440 DOI: 10.1016/J.Jmb.2019.05.009 |
0.382 |
|
2019 |
Shcherbakov AA, Mandala VS, Hong M. High-Sensitivity Detection of Nanometer H-F Distances for Protein Structure Determination by H-Detected Fast MAS NMR. The Journal of Physical Chemistry. B. PMID 31034230 DOI: 10.1021/Acs.Jpcb.9B03812 |
0.39 |
|
2019 |
Mandala VS, Hong M. High-sensitivity protein solid-state NMR spectroscopy. Current Opinion in Structural Biology. PMID 31031067 DOI: 10.1016/J.Sbi.2019.03.027 |
0.44 |
|
2019 |
Elkins MR, Hong M. Elucidating ligand-bound structures of membrane proteins using solid-state NMR spectroscopy. Current Opinion in Structural Biology. 57: 103-109. PMID 30903830 DOI: 10.1016/J.Sbi.2019.02.002 |
0.476 |
|
2019 |
Mandala VS, Liao SY, Gelenter MD, Hong M. The Transmembrane Conformation of the Influenza B Virus M2 Protein in Lipid Bilayers. Scientific Reports. 9: 3725. PMID 30842530 DOI: 10.1038/S41598-019-40217-1 |
0.508 |
|
2019 |
Hong M, Doherty T. Orientation Determination of Membrane-Disruptive Proteins Using Powder Samples and Rotational Diffusion: A Simple Solid-State NMR Approach. Chemical Physics Letters. 432: 296-300. PMID 17364006 DOI: 10.1016/J.Cplett.2006.10.067 |
0.448 |
|
2019 |
Gelenter MD, Smith KJ, Liao S, Mandala VS, Dregni AJ, Lamm MS, Tian Y, Xu W, Pochan DJ, Tucker TJ, Su Y, Hong M. The peptide hormone glucagon forms amyloid fibrils with two coexisting beta-strand conformations. Nature Structural & Molecular Biology. 26: 592-598. DOI: 10.2210/Pdb6Nzn/Pdb |
0.641 |
|
2018 |
Li FS, Phyo P, Jacobowitz J, Hong M, Weng JK. The molecular structure of plant sporopollenin. Nature Plants. PMID 30559416 DOI: 10.1038/S41477-018-0330-7 |
0.52 |
|
2018 |
Elkins MR, Sergeyev IV, Hong M. Determining Cholesterol Binding to Membrane Proteins by Cholesterol 13C Labeling in Yeast and Dynamic Nuclear Polarization NMR. Journal of the American Chemical Society. PMID 30338997 DOI: 10.1021/Jacs.8B09658 |
0.447 |
|
2018 |
Roos MK, Mandala VS, Hong M. Determination of Long-Range Distances by Fast Magic-Angle-Spinning Radiofrequency-Driven 19F-19F Dipolar Recoupling NMR. The Journal of Physical Chemistry. B. PMID 30211552 DOI: 10.1021/Acs.Jpcb.8B06878 |
0.343 |
|
2018 |
Gelenter MD, Hong M. Efficient N-C Polarization Transfer By Third-Spin Assisted Pulsed Cross Polarization Magic-Angle-Spinning NMR for Protein Structure Determination. The Journal of Physical Chemistry. B. PMID 30106585 DOI: 10.1021/Acs.Jpcb.8B06400 |
0.413 |
|
2018 |
Kwon B, Lee M, Waring AJ, Hong M. Oligomeric Structure and Three-Dimensional Fold of the HIV gp41 MPER and Transmembrane Domain in Phospholipid Bilayers. Journal of the American Chemical Society. PMID 29888593 DOI: 10.1021/Jacs.8B04010 |
0.478 |
|
2018 |
Shcherbakov AA, Hong M. Rapid measurement of long-range distances in proteins by multidimensional C-F REDOR NMR under fast magic-angle spinning. Journal of Biomolecular Nmr. PMID 29785460 DOI: 10.1007/S10858-018-0187-0 |
0.423 |
|
2018 |
Phyo P, Wang T, Yang Y, O'Neill HM, Hong M. Direct Determination of Hydroxymethyl Conformations of Plant Cell Wall Cellulose Using 1H Polarization Transfer Solid-State NMR. Biomacromolecules. PMID 29562125 DOI: 10.1021/Acs.Biomac.8B00039 |
0.403 |
|
2018 |
Liao SY, Lee M, Hong M. Interplay Between Membrane Curvature and Protein Conformational Equilibrium Investigated by Solid-State NMR. Journal of Structural Biology. PMID 29501472 DOI: 10.1016/J.Jsb.2018.02.007 |
0.472 |
|
2018 |
Mandala VS, Williams JK, Hong M. Structure and Dynamics of Membrane Proteins from Solid-State NMR. Annual Review of Biophysics. PMID 29498890 DOI: 10.1146/Annurev-Biophys-070816-033712 |
0.632 |
|
2018 |
Roos M, Wang T, Shcherbakov AA, Hong M. Fast Magic-Angle-Spinning 19F Spin Exchange NMR for Determining Nanometer 19F-19F Distances in Proteins and Pharmaceutical Compounds. The Journal of Physical Chemistry. B. PMID 29486126 DOI: 10.1021/Acs.Jpcb.8B00310 |
0.323 |
|
2018 |
Lee M, Yao H, Kwon B, Waring AJ, Ruchala P, Singh C, Hong M. Conformation and Trimer Association of the Transmembrane Domain of the Parainfluenza Virus Fusion Protein in Lipid Bilayers from Solid-State NMR: Insights into the Sequence Determinants of Trimer Structure and Fusion Activity. Journal of Molecular Biology. PMID 29330069 DOI: 10.1016/J.Jmb.2018.01.002 |
0.478 |
|
2018 |
Mandala V, Gelenter MD, Hong M. Transport-Relevant Protein Conformational Dynamics and Water Dynamics on Multiple Timescales in an Archetypal Proton Channel - Insights from Solid-State NMR. Journal of the American Chemical Society. PMID 29303574 DOI: 10.1021/Jacs.7B12464 |
0.423 |
|
2018 |
Phyo P, Gu Y, Hong M. Impact of acidic pH on plant cell wall polysaccharide structure and dynamics: insights into the mechanism of acid growth in plants from solid-state NMR Cellulose. 26: 291-304. DOI: 10.1007/S10570-018-2094-7 |
0.361 |
|
2017 |
Elkins MR, Williams JK, Gelenter MD, Dai P, Kwon B, Sergeyev IV, Pentelute BL, Hong M. Cholesterol-binding site of the influenza M2 protein in lipid bilayers from solid-state NMR. Proceedings of the National Academy of Sciences of the United States of America. PMID 29158386 DOI: 10.1073/Pnas.1715127114 |
0.6 |
|
2017 |
Phyo P, Wang T, Kiemle SN, O'Neill H, Pingali SV, Hong M, Cosgrove DJ. Gradients in wall mechanics and polysaccharides along growing inflorescence stems. Plant Physiology. PMID 29084904 DOI: 10.1104/Pp.17.01270 |
0.311 |
|
2017 |
Williams JK, Shcherbakov AA, Wang J, Hong M. Protonation equilibria and pore-opening structure of the dual-histidine influenza B virus M2 transmembrane proton channel from solid-state NMR. The Journal of Biological Chemistry. PMID 28893910 DOI: 10.1074/Jbc.M117.813998 |
0.597 |
|
2017 |
Dai P, Williams JK, Zhang C, Welborn M, Shepherd JJ, Zhu T, Van Voorhis T, Hong M, Pentelute BL. A structural and mechanistic study of π-clamp-mediated cysteine perfluoroarylation. Scientific Reports. 7: 7954. PMID 28801573 DOI: 10.1038/S41598-017-08402-2 |
0.589 |
|
2017 |
Phyo P, Wang T, Xiao C, Anderson CT, Hong M. Effects of Pectin Molecular-Weight Changes on the Structure, Dynamics, and Polysaccharide Interactions of Primary Cell Walls of Arabidopsis thaliana: Insights from Solid-State NMR. Biomacromolecules. PMID 28783321 DOI: 10.1021/Acs.Biomac.7B00888 |
0.344 |
|
2017 |
Gelenter MD, Wang T, Liao SY, O'Neill H, Hong M. (2)H-(13)C correlation solid-state NMR for investigating dynamics and water accessibilities of proteins and carbohydrates. Journal of Biomolecular Nmr. PMID 28674916 DOI: 10.1007/S10858-017-0124-7 |
0.407 |
|
2017 |
Lee M, Wang T, Makhlynets OV, Wu Y, Polizzi NF, Wu H, Gosavi PM, Stöhr J, Korendovych IV, DeGrado WF, Hong M. Zinc-binding structure of a catalytic amyloid from solid-state NMR. Proceedings of the National Academy of Sciences of the United States of America. PMID 28566494 DOI: 10.1073/Pnas.1706179114 |
0.36 |
|
2017 |
Mandala VS, Liao SY, Kwon B, Hong M. Structural Basis for Asymmetric Conductance of the Influenza M2 Proton Channel Investigated by Solid-State NMR Spectroscopy. Journal of Molecular Biology. PMID 28535993 DOI: 10.1016/J.Jmb.2017.05.015 |
0.417 |
|
2017 |
Wang T, Jo H, DeGrado WF, Hong M. Water Distribution, Dynamics and Interactions with Alzheimer's β-Amyloid Fibrils Investigated by Solid-State NMR. Journal of the American Chemical Society. PMID 28406028 DOI: 10.1021/Jacs.7B02089 |
0.314 |
|
2017 |
Lee M, Wang T, Makhlynets OV, Wu Y, Polizzi N, Wu H, Gosavi PM, Korendovych IV, DeGrado WF, Hong M. Zinc-Binding Structure of a Catalytic Amyloid from Solid-State NMR Spectroscopy Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr30227 |
0.361 |
|
2017 |
Yang H, Wang T, Oehme D, Petridis L, Hong M, Kubicki JD. Structural factors affecting 13C NMR chemical shifts of cellulose: a computational study Cellulose. 25: 23-36. DOI: 10.1007/S10570-017-1549-6 |
0.4 |
|
2016 |
Liang R, Swanson JM, Madsen JJ, Hong M, DeGrado WF, Voth GA. Acid activation mechanism of the influenza A M2 proton channel. Proceedings of the National Academy of Sciences of the United States of America. PMID 27791184 DOI: 10.1073/Pnas.1615471113 |
0.34 |
|
2016 |
Yao H, Lee M, Liao SY, Hong M. Solid-State NMR Investigation of the Structural Topology and Lipid Interactions of a Viral Fusion Protein Chimera Containing the Fusion Peptide and Transmembrane Domain. Biochemistry. PMID 27766858 DOI: 10.1021/Acs.Biochem.6B00568 |
0.477 |
|
2016 |
Wang T, Chen Y, Tabuchi A, Hong M, Cosgrove DJ. The Target of β-Expansin EXPB1 in Maize Cell Walls from Binding and Solid-State NMR Studies. Plant Physiology. PMID 27729469 DOI: 10.1104/Pp.16.01311 |
0.328 |
|
2016 |
Kwon B, Hong M. The Influenza M2 Ectodomain Regulates the Conformational Equilibria of the Transmembrane Proton Channel: Insights from Solid-State NMR. Biochemistry. PMID 27571210 DOI: 10.1021/Acs.Biochem.6B00727 |
0.447 |
|
2016 |
Elkins MR, Wang T, Nick M, Jo H, Lemmin T, Prusiner SB, DeGrado WF, Stoehr J, Hong M. Structural Polymorphism of Alzheimer's β-Amyloid Fibrils as Controlled by an E22 Switch: A Solid-State NMR Study. Journal of the American Chemical Society. PMID 27414264 DOI: 10.1021/Jacs.6B03715 |
0.374 |
|
2016 |
Williams JK, Tietze D, Lee M, Wang J, Hong M. Solid-State NMR Investigation of the Conformation, Proton Conduction, and Hydration of the Influenza B Virus M2 Transmembrane Proton Channel. Journal of the American Chemical Society. PMID 27286559 DOI: 10.1021/Jacs.6B03142 |
0.623 |
|
2016 |
Wang T, Yang H, Kubicki JD, Hong M. Cellulose Structural Polymorphism in Plant Primary Cell Walls Investigated by High-Field 2D Solid-State NMR Spectroscopy and Density Functional Theory Calculations. Biomacromolecules. PMID 27192562 DOI: 10.1021/Acs.Biomac.6B00441 |
0.431 |
|
2016 |
Liao SY, Lee M, Wang T, Sergeyev IV, Hong M. Efficient DNP NMR of membrane proteins: sample preparation protocols, sensitivity, and radical location. Journal of Biomolecular Nmr. PMID 26873390 DOI: 10.1007/S10858-016-0023-3 |
0.448 |
|
2016 |
Fritzsching KJ, Hong M, Schmidt-Rohr K. Conformationally selective multidimensional chemical shift ranges in proteins from a PACSY database purged using intrinsic quality criteria. Journal of Biomolecular Nmr. PMID 26787537 DOI: 10.1007/S10858-016-0013-5 |
0.805 |
|
2016 |
Hong M. Structure and Mechanisms of Actions of Curvature-Inducing Viral Membrane Proteins from Solid-State NMR Biophysical Journal. 110: 5a. DOI: 10.1016/j.bpj.2015.11.073 |
0.306 |
|
2015 |
Guo SS, Tang LQ, Zhang L, Chen QY, Liu LT, Guo L, Mo HY, Luo DH, Huang PY, Xiang YQ, Sun R, Chen MY, Wang L, Lv X, Zhao C, ... ... Hong MH, et al. The impact of the cumulative dose of cisplatin during concurrent chemoradiotherapy on the clinical outcomes of patients with advanced-stage nasopharyngeal carcinoma in an era of intensity-modulated radiotherapy. Bmc Cancer. 15: 977. PMID 26675209 DOI: 10.1186/s12885-015-1964-8 |
0.445 |
|
2015 |
Jiang R, You R, Pei XQ, Zou X, Zhang MX, Wang TM, Sun R, Luo DH, Huang PY, Chen QY, Hua YJ, Tang LQ, Guo L, Mo HY, Qian CN, ... ... Hong MH, et al. Development of a ten-signature classifier using a support vector machine integrated approach to subdivide the M1 stage into M1a and M1b stages of nasopharyngeal carcinoma with synchronous metastases to better predict patients' survival. Oncotarget. PMID 26636646 DOI: 10.18632/oncotarget.6436 |
0.444 |
|
2015 |
Liu LT, Tang LQ, Chen QY, Zhang L, Guo SS, Guo L, Mo HY, Zhao C, Guo X, Cao KJ, Qian CN, Zeng MS, Bei JX, Hong MH, Shao JY, et al. The Prognostic Value of Plasma Epstein-Barr Viral DNA and Tumor Response to Neoadjuvant Chemotherapy in Advanced-Stage Nasopharyngeal Carcinoma. International Journal of Radiation Oncology, Biology, Physics. 93: 862-9. PMID 26530755 DOI: 10.1016/j.ijrobp.2015.08.003 |
0.431 |
|
2015 |
Kim HS, Hong M, Lee SC, Lee HY, Suh YG, Oh DC, Seo JH, Choi H, Kim JY, Kim KW, Kim JH, Kim J, Kim YM, Park SJ, Park HJ, et al. Ring-truncated deguelin derivatives as potent Hypoxia Inducible Factor-1α (HIF-1α) inhibitors. European Journal of Medicinal Chemistry. 104: 157-164. PMID 26457742 DOI: 10.1016/j.ejmech.2015.09.033 |
0.397 |
|
2015 |
Williams JK, Schmidt-Rohr K, Hong M. Aromatic spectral editing techniques for magic-angle-spinning solid-state NMR spectroscopy of uniformly (13)C-labeled proteins. Solid State Nuclear Magnetic Resonance. PMID 26440131 DOI: 10.1016/J.Ssnmr.2015.09.006 |
0.729 |
|
2015 |
Yang P, Hong MS, Fu C, Schmit BM, Su Y, Berceli SA, Jiang Z. Preexisting smooth muscle cells contribute to neointimal cell repopulation at an incidence varying widely among individual lesions. Surgery. PMID 26387788 DOI: 10.1016/j.surg.2015.08.015 |
0.515 |
|
2015 |
Ye YF, Xiang YQ, Fang F, Gao R, Zhang LF, Xie SH, Liu Z, Du JL, Chen SH, Hong MH, Qian CN, Ye W, Zeng YX, Liu Q, Cao SM. Hepatitis B Virus Infection and Risk of Nasopharyngeal Carcinoma in Southern China. Cancer Epidemiology, Biomarkers & Prevention : a Publication of the American Association For Cancer Research, Cosponsored by the American Society of Preventive Oncology. PMID 26364160 DOI: 10.1158/1055-9965.EPI-15-0344 |
0.436 |
|
2015 |
Wang T, Hong M. Solid-state NMR investigations of cellulose structure and interactions with matrix polysaccharides in plant primary cell walls. Journal of Experimental Botany. PMID 26355148 DOI: 10.1093/Jxb/Erv416 |
0.369 |
|
2015 |
Guo SS, Tang LQ, Chen QY, Zhang L, Liu LT, Huang PY, Cao KJ, Guo L, Mo HY, Guo X, Hong MH, Zeng MS, Qian CN, Mai HQ. Is Hemoglobin Level in Patients with Nasopharyngeal Carcinoma Still a Significant Prognostic Factor in the Era of Intensity-Modulated Radiotherapy Technology? Plos One. 10: e0136033. PMID 26313452 DOI: 10.1371/journal.pone.0136033 |
0.443 |
|
2015 |
Yao H, Lee MW, Waring AJ, Wong GC, Hong M. Viral fusion protein transmembrane domain adopts β-strand structure to facilitate membrane topological changes for virus-cell fusion. Proceedings of the National Academy of Sciences of the United States of America. 112: 10926-31. PMID 26283363 DOI: 10.1073/Pnas.1501430112 |
0.461 |
|
2015 |
White PB, Hong M. (15)N and (1)H Solid-State NMR Investigation of a Canonical Low-Barrier Hydrogen-Bond Compound: 1,8-Bis(dimethylamino)naphthalene. The Journal of Physical Chemistry. B. 119: 11581-9. PMID 26244754 DOI: 10.1021/Acs.Jpcb.5B06171 |
0.356 |
|
2015 |
Huang PY, Zeng Q, Cao KJ, Guo X, Guo L, Mo HY, Wu PH, Qian CN, Mai HQ, Hong MH. Ten-year outcomes of a randomised trial for locoregionally advanced nasopharyngeal carcinoma: A single-institution experience from an endemic area. European Journal of Cancer (Oxford, England : 1990). PMID 26093812 DOI: 10.1016/j.ejca.2015.05.025 |
0.439 |
|
2015 |
You R, Zou X, Wang SL, Jiang R, Tang LQ, Zhang WD, Li L, Zhang MX, Shen GP, Guo L, Qian CN, Mai HQ, Ma J, Hong MH, Chen MY. New surgical staging system for patients with recurrent nasopharyngeal carcinoma based on the AJCC/UICC rTNM classification system. European Journal of Cancer (Oxford, England : 1990). PMID 26055204 DOI: 10.1016/j.ejca.2015.05.014 |
0.427 |
|
2015 |
Wang T, Park YB, Cosgrove DJ, Hong M. Cellulose-Pectin Spatial Contacts Are Inherent to Never-Dried Arabidopsis Primary Cell Walls: Evidence from Solid-State Nuclear Magnetic Resonance. Plant Physiology. 168: 871-84. PMID 26036615 DOI: 10.1104/Pp.15.00665 |
0.344 |
|
2015 |
Kwon B, Tietze D, White PB, Liao SY, Hong M. Chemical ligation of the influenza M2 protein for solid-state NMR characterization of the cytoplasmic domain. Protein Science : a Publication of the Protein Society. 24: 1087-99. PMID 25966817 DOI: 10.1002/Pro.2690 |
0.484 |
|
2015 |
Liao SY, Yang Y, Tietze D, Hong M. The influenza m2 cytoplasmic tail changes the proton-exchange equilibria and the backbone conformation of the transmembrane histidine residue to facilitate proton conduction. Journal of the American Chemical Society. 137: 6067-77. PMID 25892574 DOI: 10.1021/Jacs.5B02510 |
0.456 |
|
2015 |
Yang Y, Yao H, Hong M. Distinguishing bicontinuous lipid cubic phases from isotropic membrane morphologies using (31)P solid-state NMR spectroscopy. The Journal of Physical Chemistry. B. 119: 4993-5001. PMID 25815701 DOI: 10.1021/Acs.Jpcb.5B01001 |
0.405 |
|
2015 |
Wang T, Hong M. Investigation of the curvature induction and membrane localization of the influenza virus M2 protein using static and off-magic-angle spinning solid-state nuclear magnetic resonance of oriented bicelles. Biochemistry. 54: 2214-26. PMID 25774685 DOI: 10.1021/Acs.Biochem.5B00127 |
0.494 |
|
2015 |
Wang T, Williams JK, Schmidt-Rohr K, Hong M. Relaxation-compensated difference spin diffusion NMR for detecting 13C-13C long-range correlations in proteins and polysaccharides. Journal of Biomolecular Nmr. 61: 97-107. PMID 25510834 DOI: 10.1007/S10858-014-9889-0 |
0.71 |
|
2014 |
Joh NH, Wang T, Bhate MP, Acharya R, Wu Y, Grabe M, Hong M, Grigoryan G, DeGrado WF. De novo design of a transmembrane Zn²âº-transporting four-helix bundle. Science (New York, N.Y.). 346: 1520-4. PMID 25525248 DOI: 10.1126/Science.1261172 |
0.379 |
|
2014 |
Williams JK, Hong M. Probing membrane protein structure using water polarization transfer solid-state NMR. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 247: 118-27. PMID 25228502 DOI: 10.1016/J.Jmr.2014.08.007 |
0.599 |
|
2014 |
Lee M, Hong M. Cryoprotection of lipid membranes for high-resolution solid-state NMR studies of membrane peptides and proteins at low temperature. Journal of Biomolecular Nmr. 59: 263-77. PMID 25015530 DOI: 10.1007/S10858-014-9845-Z |
0.471 |
|
2014 |
White PB, Wang T, Park YB, Cosgrove DJ, Hong M. Water-polysaccharide interactions in the primary cell wall of Arabidopsis thaliana from polarization transfer solid-state NMR. Journal of the American Chemical Society. 136: 10399-409. PMID 24984197 DOI: 10.1021/Ja504108H |
0.323 |
|
2014 |
Wang T, Salazar A, Zabotina OA, Hong M. Structure and dynamics of Brachypodium primary cell wall polysaccharides from two-dimensional (13)C solid-state nuclear magnetic resonance spectroscopy. Biochemistry. 53: 2840-54. PMID 24720372 DOI: 10.1021/Bi500231B |
0.426 |
|
2014 |
Yao H, Hong M. Conformation and lipid interaction of the fusion peptide of the paramyxovirus PIV5 in anionic and negative-curvature membranes from solid-state NMR. Journal of the American Chemical Society. 136: 2611-24. PMID 24428385 DOI: 10.1021/Ja4121956 |
0.468 |
|
2014 |
Hong M. Ion Conduction Mechanism of a Viral Proton Channel from Solid-State NMR Biophysical Journal. 106: 11a. DOI: 10.1016/J.Bpj.2013.11.113 |
0.457 |
|
2013 |
Kwon B, Waring AJ, Hong M. A 2H solid-state NMR study of lipid clustering by cationic antimicrobial and cell-penetrating peptides in model bacterial membranes. Biophysical Journal. 105: 2333-42. PMID 24268145 DOI: 10.1016/J.Bpj.2013.08.020 |
0.441 |
|
2013 |
Yang Y, Fritzsching KJ, Hong M. Resonance assignment of the NMR spectra of disordered proteins using a multi-objective non-dominated sorting genetic algorithm. Journal of Biomolecular Nmr. 57: 281-96. PMID 24132778 DOI: 10.1007/S10858-013-9788-9 |
0.741 |
|
2013 |
Wang T, Park YB, Caporini MA, Rosay M, Zhong L, Cosgrove DJ, Hong M. Sensitivity-enhanced solid-state NMR detection of expansin's target in plant cell walls. Proceedings of the National Academy of Sciences of the United States of America. 110: 16444-9. PMID 24065828 DOI: 10.1073/Pnas.1316290110 |
0.437 |
|
2013 |
Liao SY, Fritzsching KJ, Hong M. Conformational analysis of the full-length M2 protein of the influenza A virus using solid-state NMR. Protein Science : a Publication of the Protein Society. 22: 1623-38. PMID 24023039 DOI: 10.1002/Pro.2368 |
0.808 |
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2013 |
Johnson RL, Anderson JM, Shanks BH, Fang X, Hong M, Schmidt-Rohr K. Spectrally edited 2D 13C-13C NMR spectra without diagonal ridge for characterizing 13C-enriched low-temperature carbon materials. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 234: 112-24. PMID 23871898 DOI: 10.1016/J.Jmr.2013.06.006 |
0.594 |
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2013 |
Williams JK, Tietze D, Wang J, Wu Y, DeGrado WF, Hong M. Drug-induced conformational and dynamical changes of the S31N mutant of the influenza M2 proton channel investigated by solid-state NMR. Journal of the American Chemical Society. 135: 9885-97. PMID 23758317 DOI: 10.1021/Ja4041412 |
0.611 |
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2013 |
Fritzsching KJ, Yang Y, Schmidt-Rohr K, Hong M. Practical use of chemical shift databases for protein solid-state NMR: 2D chemical shift maps and amino-acid assignment with secondary-structure information. Journal of Biomolecular Nmr. 56: 155-67. PMID 23625364 DOI: 10.1007/S10858-013-9732-Z |
0.802 |
|
2013 |
Wang T, Yao H, Hong M. Determining the depth of insertion of dynamically invisible membrane peptides by gel-phase ¹H spin diffusion heteronuclear correlation NMR. Journal of Biomolecular Nmr. 56: 139-48. PMID 23606274 DOI: 10.1007/S10858-013-9730-1 |
0.479 |
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2013 |
Williams JK, Zhang Y, Schmidt-Rohr K, Hong M. pH-dependent conformation, dynamics, and aromatic interaction of the gating tryptophan residue of the influenza M2 proton channel from solid-state NMR. Biophysical Journal. 104: 1698-708. PMID 23601317 DOI: 10.1016/J.Bpj.2013.02.054 |
0.695 |
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2013 |
Hong M, Schmidt-Rohr K. Magic-angle-spinning NMR techniques for measuring long-range distances in biological macromolecules. Accounts of Chemical Research. 46: 2154-63. PMID 23387532 DOI: 10.1021/Ar300294X |
0.62 |
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2013 |
Yao H, Hong M. Membrane-dependent conformation, dynamics, and lipid interactions of the fusion peptide of the paramyxovirus PIV5 from solid-state NMR. Journal of Molecular Biology. 425: 563-76. PMID 23183373 DOI: 10.1016/J.Jmb.2012.11.027 |
0.474 |
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2013 |
Su Y, Li S, Hong M. Cationic membrane peptides: atomic-level insight of structure-activity relationships from solid-state NMR. Amino Acids. 44: 821-33. PMID 23108593 DOI: 10.1007/S00726-012-1421-9 |
0.692 |
|
2012 |
Wang T, Zabotina O, Hong M. Pectin-cellulose interactions in the Arabidopsis primary cell wall from two-dimensional magic-angle-spinning solid-state nuclear magnetic resonance. Biochemistry. 51: 9846-56. PMID 23167456 DOI: 10.1021/Bi3015532 |
0.43 |
|
2012 |
Wang T, Widanapathirana L, Zhao Y, Hong M. Aggregation and dynamics of oligocholate transporters in phospholipid bilayers revealed by solid-state NMR spectroscopy. Langmuir : the Acs Journal of Surfaces and Colloids. 28: 17071-8. PMID 23153411 DOI: 10.1021/La303661P |
0.451 |
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2012 |
Schmidt-Rohr K, Fritzsching KJ, Liao SY, Hong M. Spectral editing of two-dimensional magic-angle-spinning solid-state NMR spectra for protein resonance assignment and structure determination. Journal of Biomolecular Nmr. 54: 343-53. PMID 23053913 DOI: 10.1007/S10858-012-9676-8 |
0.801 |
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2012 |
Hong M, DeGrado WF. Structural basis for proton conduction and inhibition by the influenza M2 protein. Protein Science : a Publication of the Protein Society. 21: 1620-33. PMID 23001990 DOI: 10.1002/Pro.2158 |
0.423 |
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2012 |
Hong M, Fritzsching KJ, Williams JK. Hydrogen-bonding partner of the proton-conducting histidine in the influenza M2 proton channel revealed from 1H chemical shifts. Journal of the American Chemical Society. 134: 14753-5. PMID 22931093 DOI: 10.1021/Ja307453V |
0.788 |
|
2012 |
Dick-Perez M, Wang T, Salazar A, Zabotina OA, Hong M. Multidimensional solid-state NMR studies of the structure and dynamics of pectic polysaccharides in uniformly 13C-labeled Arabidopsis primary cell walls. Magnetic Resonance in Chemistry : Mrc. 50: 539-50. PMID 22777793 DOI: 10.1002/Mrc.3836 |
0.802 |
|
2012 |
Li S, Su Y, Hong M. Intramolecular 1H-13C distance measurement in uniformly 13C, 15N labeled peptides by solid-state NMR. Solid State Nuclear Magnetic Resonance. 45: 51-8. PMID 22749432 DOI: 10.1016/J.Ssnmr.2012.06.001 |
0.648 |
|
2012 |
Su Y, Hu F, Hong M. Paramagnetic Cu(II) for probing membrane protein structure and function: inhibition mechanism of the influenza M2 proton channel. Journal of the American Chemical Society. 134: 8693-702. PMID 22519936 DOI: 10.1021/Ja3026328 |
0.632 |
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2012 |
Wang T, Cady SD, Hong M. NMR determination of protein partitioning into membrane domains with different curvatures and application to the influenza M2 peptide. Biophysical Journal. 102: 787-94. PMID 22385849 DOI: 10.1016/J.Bpj.2012.01.010 |
0.784 |
|
2012 |
Harris DM, Corbin K, Wang T, Gutierrez R, Bertolo AL, Petti C, Smilgies DM, Estevez JM, Bonetta D, Urbanowicz BR, Ehrhardt DW, Somerville CR, Rose JK, Hong M, Debolt S. Cellulose microfibril crystallinity is reduced by mutating C-terminal transmembrane region residues CESA1A903V and CESA3T942I of cellulose synthase. Proceedings of the National Academy of Sciences of the United States of America. 109: 4098-103. PMID 22375033 DOI: 10.1073/Pnas.1200352109 |
0.365 |
|
2012 |
Hu F, Schmidt-Rohr K, Hong M. NMR detection of pH-dependent histidine-water proton exchange reveals the conduction mechanism of a transmembrane proton channel. Journal of the American Chemical Society. 134: 3703-13. PMID 21974716 DOI: 10.1021/Ja2081185 |
0.634 |
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2012 |
Fiorin G, Carnevale V, Wang J, Ma C, Wang T, Hu F, Lamb R, Pinto L, Hong M, DeGrado W, Klein M. Mapping Water Density to Design New Blockers Against a Viral Proton Channel Biophysical Journal. 102: 682a. DOI: 10.1016/J.Bpj.2011.11.3708 |
0.333 |
|
2011 |
Hong M, Zhang Y, Hu F. Membrane protein structure and dynamics from NMR spectroscopy. Annual Review of Physical Chemistry. 63: 1-24. PMID 22136620 DOI: 10.1146/Annurev-Physchem-032511-143731 |
0.48 |
|
2011 |
Su Y, Hong M. Conformational disorder of membrane peptides investigated from solid-state NMR line widths and line shapes. The Journal of Physical Chemistry. B. 115: 10758-67. PMID 21806038 DOI: 10.1021/Jp205002N |
0.699 |
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2011 |
Cady S, Wang T, Hong M. Membrane-dependent effects of a cytoplasmic helix on the structure and drug binding of the influenza virus M2 protein. Journal of the American Chemical Society. 133: 11572-9. PMID 21661724 DOI: 10.1021/Ja202051N |
0.783 |
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2011 |
Cady SD, Wang J, Wu Y, DeGrado WF, Hong M. 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. Journal of the American Chemical Society. 133: 4274-84. PMID 21381693 DOI: 10.1021/Ja102581N |
0.781 |
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2011 |
Hong M, Su Y. Structure and dynamics of cationic membrane peptides and proteins: insights from solid-state NMR. Protein Science : a Publication of the Protein Society. 20: 641-55. PMID 21344534 DOI: 10.1002/Pro.600 |
0.71 |
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2011 |
Su Y, Waring AJ, Ruchala P, Hong M. Structures of β-hairpin antimicrobial protegrin peptides in lipopolysaccharide membranes: mechanism of gram selectivity obtained from solid-state nuclear magnetic resonance. Biochemistry. 50: 2072-83. PMID 21302955 DOI: 10.1021/Bi101975V |
0.686 |
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2011 |
Li S, Hong M. Protonation, tautomerization, and rotameric structure of histidine: a comprehensive study by magic-angle-spinning solid-state NMR. Journal of the American Chemical Society. 133: 1534-44. PMID 21207964 DOI: 10.1021/Ja108943N |
0.462 |
|
2011 |
Dick-Pérez M, Zhang Y, Hayes J, Salazar A, Zabotina OA, Hong M. Structure and interactions of plant cell-wall polysaccharides by two- and three-dimensional magic-angle-spinning solid-state NMR. Biochemistry. 50: 989-1000. PMID 21204530 DOI: 10.1021/Bi101795Q |
0.793 |
|
2011 |
Hu F, Luo W, Cady SD, Hong M. Conformational plasticity of the influenza A M2 transmembrane helix in lipid bilayers under varying pH, drug binding, and membrane thickness. Biochimica Et Biophysica Acta. 1808: 415-23. PMID 20883664 DOI: 10.1016/J.Bbamem.2010.09.014 |
0.822 |
|
2011 |
Liu XK, Su Y, Jha N, Hong MH, Mai HQ, Fan W, Zeng ZY, Guo ZM. Submandibular salivary gland transfer for the prevention of radiation-induced xerostomia in patients with nasopharyngeal carcinoma: 5-Year outcomes. Head & Neck. 33: 389-95. PMID 20629074 DOI: 10.1002/Hed.21461 |
0.517 |
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2010 |
Hu F, Luo W, Hong M. Mechanisms of proton conduction and gating in influenza M2 proton channels from solid-state NMR. Science (New York, N.Y.). 330: 505-8. PMID 20966251 DOI: 10.1126/Science.1191714 |
0.612 |
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2010 |
Zhang Y, Lu W, Hong M. The membrane-bound structure and topology of a human α-defensin indicate a dimer pore mechanism for membrane disruption. Biochemistry. 49: 9770-82. PMID 20961099 DOI: 10.1021/Bi101512J |
0.49 |
|
2010 |
Doherty T, Su Y, Hong M. High-resolution orientation and depth of insertion of the voltage-sensing S4 helix of a potassium channel in lipid bilayers. Journal of Molecular Biology. 401: 642-52. PMID 20600109 DOI: 10.1016/J.Jmb.2010.06.048 |
0.698 |
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2010 |
Su Y, Waring AJ, Ruchala P, Hong M. Membrane-bound dynamic structure of an arginine-rich cell-penetrating peptide, the protein transduction domain of HIV TAT, from solid-state NMR. Biochemistry. 49: 6009-20. PMID 20550193 DOI: 10.1021/Bi100642N |
0.712 |
|
2010 |
Su Y, DeGrado WF, Hong M. Orientation, dynamics, and lipid interaction of an antimicrobial arylamide investigated by 19F and 31P solid-state NMR spectroscopy. Journal of the American Chemical Society. 132: 9197-205. PMID 20536141 DOI: 10.1021/Ja103658H |
0.693 |
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2010 |
Li S, Su Y, Luo W, Hong M. Water-protein interactions of an arginine-rich membrane peptide in lipid bilayers investigated by solid-state nuclear magnetic resonance spectroscopy. The Journal of Physical Chemistry. B. 114: 4063-9. PMID 20199036 DOI: 10.1021/Jp912283R |
0.766 |
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2010 |
Cady SD, Schmidt-Rohr K, Wang J, Soto CS, Degrado WF, Hong M. Structure of the amantadine binding site of influenza M2 proton channels in lipid bilayers. Nature. 463: 689-92. PMID 20130653 DOI: 10.1038/Nature08722 |
0.806 |
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2010 |
Luo W, Hong M. Conformational changes of an ion channel detected through water-protein interactions using solid-state NMR spectroscopy. Journal of the American Chemical Society. 132: 2378-84. PMID 20112896 DOI: 10.1021/Ja9096219 |
0.626 |
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2010 |
Zhang Y, Doherty T, Li J, Lu W, Barinka C, Lubkowski J, Hong M. Resonance assignment and three-dimensional structure determination of a human alpha-defensin, HNP-1, by solid-state NMR. Journal of Molecular Biology. 397: 408-22. PMID 20097206 DOI: 10.1016/J.Jmb.2010.01.030 |
0.488 |
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2010 |
Cady S, Schmidt-Rohr K, Wang J, Soto C, DeGrado W, Hong M. Solid-state NMR structure of the M2 transmembrane peptide of the influenza A virus in DMPC lipid bilayers bound to deuterated amantadine Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.2210/Pdb2Kqt/Pdb |
0.805 |
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2009 |
Li S, Zhang Y, Hong M. 3D (13)C-(13)C-(13)C correlation NMR for de novo distance determination of solid proteins and application to a human alpha-defensin. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 202: 203-10. PMID 19963419 DOI: 10.1016/J.Jmr.2009.11.011 |
0.426 |
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2009 |
Cady SD, Hong M. Effects of amantadine on the dynamics of membrane-bound influenza A M2 transmembrane peptide studied by NMR relaxation. Journal of Biomolecular Nmr. 45: 185-96. PMID 19633911 DOI: 10.1007/S10858-009-9352-9 |
0.784 |
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2009 |
Cady SD, Luo W, Hu F, Hong M. Structure and function of the influenza A M2 proton channel. Biochemistry. 48: 7356-64. PMID 19601584 DOI: 10.1021/Bi9008837 |
0.796 |
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2009 |
Doherty T, Hong M. High-resolution solid-state NMR of anisotropically mobile molecules under very low-power (1)H decoupling and moderate magic-angle spinning. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 199: 225-32. PMID 19501003 DOI: 10.1016/J.Jmr.2009.05.006 |
0.464 |
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2009 |
Luo W, Cady SD, Hong M. Immobilization of the influenza A M2 transmembrane peptide in virus envelope-mimetic lipid membranes: a solid-state NMR investigation. Biochemistry. 48: 6361-8. PMID 19489611 DOI: 10.1021/Bi900716S |
0.823 |
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2009 |
Wang J, Cady SD, Balannik V, Pinto LH, DeGrado WF, Hong M. Discovery of spiro-piperidine inhibitors and their modulation of the dynamics of the M2 proton channel from influenza A virus. Journal of the American Chemical Society. 131: 8066-76. PMID 19469531 DOI: 10.1021/Ja900063S |
0.755 |
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2009 |
Hong M, Mishanina TV, Cady SD. Accurate measurement of methyl 13C chemical shifts by solid-state NMR for the determination of protein side chain conformation: the influenza a M2 transmembrane peptide as an example. Journal of the American Chemical Society. 131: 7806-16. PMID 19441789 DOI: 10.1021/Ja901550Q |
0.774 |
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2009 |
Tang M, Hong M. Structure and mechanism of beta-hairpin antimicrobial peptides in lipid bilayers from solid-state NMR spectroscopy. Molecular Biosystems. 5: 317-22. PMID 19396367 DOI: 10.1039/b820398a |
0.511 |
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2009 |
Su Y, Doherty T, Waring AJ, Ruchala P, Hong M. 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: 4587-95. PMID 19364134 DOI: 10.1021/Bi900080D |
0.71 |
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2009 |
Cady SD, Mishanina TV, Hong M. 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. Journal of Molecular Biology. 385: 1127-41. PMID 19061899 DOI: 10.1016/J.Jmb.2008.11.022 |
0.801 |
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2009 |
Tang M, Waring AJ, Hong M. Effects of arginine density on the membrane-bound structure of a cationic antimicrobial peptide from solid-state NMR. Biochimica Et Biophysica Acta. 1788: 514-21. PMID 19059201 DOI: 10.1016/J.Bbamem.2008.10.027 |
0.541 |
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2008 |
Doherty T, Hong M. 2D 1H-31P solid-state NMR studies of the dependence of inter-bilayer water dynamics on lipid headgroup structure and membrane peptides. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 196: 39-47. PMID 18938095 DOI: 10.1016/J.Jmr.2008.10.001 |
0.436 |
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2008 |
Su Y, Mani R, Doherty T, Waring AJ, Hong M. Reversible sheet-turn conformational change of a cell-penetrating peptide in lipid bilayers studied by solid-state NMR. Journal of Molecular Biology. 381: 1133-44. PMID 18656895 DOI: 10.1016/J.Jmb.2008.06.007 |
0.792 |
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2008 |
Hua YJ, Chen MY, Hong MH, Zhao C, Guo L, Han F, Luo W, Sun R, Chen YY, Liu H. [Short-term efficacy of endoscopy-guided debridement on radiation-related nasopharyngeal necrosis in 20 nasopharyngeal carcinoma patients after radiotherapy]. Ai Zheng = Aizheng = Chinese Journal of Cancer. 27: 729-33. PMID 18606066 |
0.413 |
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2008 |
Su Y, Mani R, Hong M. Asymmetric insertion of membrane proteins in lipid bilayers by solid-state NMR paramagnetic relaxation enhancement: a cell-penetrating Peptide example. Journal of the American Chemical Society. 130: 8856-64. PMID 18597439 DOI: 10.1021/Ja802383T |
0.776 |
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2008 |
Tang M, Waring AJ, Hong M. Arginine dynamics in a membrane-bound cationic beta-hairpin peptide from solid-state NMR. Chembiochem : a European Journal of Chemical Biology. 9: 1487-92. PMID 18442147 DOI: 10.1002/Cbic.200800005 |
0.581 |
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2008 |
Tang M, Waring AJ, Lehrer RI, Hong M. Effects of guanidinium-phosphate hydrogen bonding on the membrane-bound structure and activity of an arginine-rich membrane peptide from solid-state NMR spectroscopy. Angewandte Chemie (International Ed. in English). 47: 3202-5. PMID 18338418 DOI: 10.1002/Anie.200705993 |
0.597 |
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2008 |
Cady SD, Hong M. Amantadine-induced conformational and dynamical changes of the influenza M2 transmembrane proton channel. Proceedings of the National Academy of Sciences of the United States of America. 105: 1483-8. PMID 18230730 DOI: 10.1073/Pnas.0711500105 |
0.786 |
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2008 |
Cady SD, Hong M. Simultaneous extraction of multiple orientational constraints of membrane proteins by 13C-detected N-H dipolar couplings under magic angle spinning. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 191: 219-25. PMID 18221902 DOI: 10.1016/J.Jmr.2008.01.001 |
0.779 |
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2007 |
Doherty T, Waring AJ, Hong M. Dynamic structure of disulfide-removed linear analogs of tachyplesin-I in the lipid bilayer from solid-state NMR. Biochemistry. 47: 1105-16. PMID 18163648 DOI: 10.1021/Bi701390T |
0.512 |
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2007 |
Mani R, Waring AJ, Hong M. Conformation, dynamics, and insertion of a noncysteine-containing protegrin-1 analogue in lipid membranes from solid-state NMR spectroscopy. Chembiochem : a European Journal of Chemical Biology. 8: 1877-84. PMID 17868158 DOI: 10.1002/Cbic.200700335 |
0.712 |
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2007 |
Tang M, Waring AJ, Hong M. Phosphate-mediated arginine insertion into lipid membranes and pore formation by a cationic membrane peptide from solid-state NMR. Journal of the American Chemical Society. 129: 11438-46. PMID 17705480 DOI: 10.1021/Ja072511S |
0.576 |
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2007 |
Luo W, Mani R, Hong M. Side-chain conformation of the M2 transmembrane peptide proton channel of influenza a virus from 19F solid-state NMR. The Journal of Physical Chemistry. B. 111: 10825-32. PMID 17705425 DOI: 10.1021/Jp073823K |
0.728 |
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2007 |
Hong M. Structure, topology, and dynamics of membrane peptides and proteins from solid-state NMR spectroscopy. The Journal of Physical Chemistry. B. 111: 10340-51. PMID 17685648 DOI: 10.1021/jp073652j |
0.38 |
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2007 |
Cady SD, Goodman C, Tatko CD, DeGrado WF, Hong M. Determining the orientation of uniaxially rotating membrane proteins using unoriented samples: a 2H, 13C, AND 15N solid-state NMR investigation of the dynamics and orientation of a transmembrane helical bundle. Journal of the American Chemical Society. 129: 5719-29. PMID 17417850 DOI: 10.1021/Ja070305E |
0.8 |
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2007 |
Tang M, Waring AJ, Hong M. Trehalose-protected lipid membranes for determining membrane protein structure and insertion. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 184: 222-7. PMID 17084650 DOI: 10.1016/J.Jmr.2006.10.006 |
0.528 |
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2007 |
Hong M. Structure, topology, and dynamics of membrane peptides and proteins from solid-state NMR spectroscopy Journal of Physical Chemistry B. 111: 10340-10351. DOI: 10.1021/Jp073652J |
0.48 |
|
2006 |
Hong M. Oligomeric Structure, Dynamics, and Orientation of Membrane Proteins from Solid-State NMR Structure. 14: 1731-1740. PMID 17161364 DOI: 10.1016/J.Str.2006.10.002 |
0.428 |
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2006 |
Doherty T, Waring aAJ, Hong M. Membrane-bound conformation and topology of the antimicrobial peptide tachyplesin I by solid-state NMR. Biochemistry. 45: 13323-13330. PMID 17073453 DOI: 10.1021/Bi061424U |
0.475 |
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2006 |
Mani R, Cady SD, Tang M, Waring AJ, Lehrer RI, Hong M. Membrane-dependent oligomeric structure and pore formation of a beta-hairpin antimicrobial peptide in lipid bilayers from solid-state NMR. Proceedings of the National Academy of Sciences of the United States of America. 103: 16242-7. PMID 17060626 DOI: 10.1073/Pnas.0605079103 |
0.819 |
|
2006 |
Mani R, Tang M, Wu X, Buffy JJ, Waring AJ, Sherman MA, Hong M. Membrane-bound dimer structure of a beta-hairpin antimicrobial peptide from rotational-echo double-resonance solid-state NMR. Biochemistry. 45: 8341-9. PMID 16819833 DOI: 10.1021/Bi060305B |
0.754 |
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2006 |
Luo W, Hong M. Determination of the oligomeric number and intermolecular distances of membrane protein assemblies by anisotropic 1H-driven spin diffusion NMR spectroscopy. Journal of the American Chemical Society. 128: 7242-51. PMID 16734478 DOI: 10.1021/Ja0603406 |
0.603 |
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2006 |
Doherty T, Waring AJ, Hong M. Peptide-lipid interactions of the beta-hairpin antimicrobial peptide tachyplesin and its linear derivatives from solid-state NMR. Biochimica Et Biophysica Acta. 1758: 1285-91. PMID 16678119 DOI: 10.1016/J.Bbamem.2006.03.016 |
0.435 |
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2006 |
Hong M. Solid-state NMR studies of the structure, dynamics, and assembly of β-sheet membrane peptides and α-helical membrane proteins with antibiotic activities Accounts of Chemical Research. 39: 176-183. PMID 16548506 DOI: 10.1021/Ar040037E |
0.468 |
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2006 |
Tang M, Waring AJ, Lehrer RI, Hong M. Orientation of a beta-hairpin antimicrobial peptide in lipid bilayers from two-dimensional dipolar chemical-shift correlation NMR. Biophysical Journal. 90: 3616-24. PMID 16500957 DOI: 10.1529/Biophysj.105.062075 |
0.572 |
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2006 |
Yao XL, Hong M. Effects of anionic lipid and ion concentrations on the topology and segmental mobility of colicin Ia channel domain from solid-state NMR. Biochemistry. 45: 289-95. PMID 16388605 DOI: 10.1021/bi051540h |
0.582 |
|
2006 |
Luo W, Hong M. A 1D sensitivity-enhanced 1H spin diffusion experiment for determining membrane protein topology. Solid State Nuclear Magnetic Resonance. 29: 163-9. PMID 16203122 DOI: 10.1016/J.Ssnmr.2005.08.007 |
0.641 |
|
2005 |
Marasinghe PA, Buffy JJ, Schmidt-Rohr K, Hong M. Membrane curvature change induced by an antimicrobial peptide detected by 31P exchange NMR. The Journal of Physical Chemistry. B. 109: 22036-44. PMID 16853861 DOI: 10.1021/Jp054396I |
0.609 |
|
2005 |
Tang M, Waring AJ, Hong M. Intermolecular packing and alignment in an ordered beta-hairpin antimicrobial peptide aggregate from 2D solid-state NMR. Journal of the American Chemical Society. 127: 13919-27. PMID 16201813 DOI: 10.1021/Ja0526665 |
0.557 |
|
2005 |
Mani R, Waring AJ, Lehrer RI, Hong M. Membrane-disruptive abilities of beta-hairpin antimicrobial peptides correlate with conformation and activity: a 31P and 1H NMR study. Biochimica Et Biophysica Acta. 1716: 11-8. PMID 16182236 DOI: 10.1016/J.Bbamem.2005.08.008 |
0.663 |
|
2005 |
Liu XK, Zeng ZY, Hong MH, Cui NJ, Su Y, Mai HQ, Chen FJ. [Primary effect of submandibular salivary gland transfer in preventing radiation-induced xerostomia of nasopharyngeal carcinoma]. Ai Zheng = Aizheng = Chinese Journal of Cancer. 24: 577-81. PMID 15890101 |
0.525 |
|
2005 |
Wi S, Sun H, Oldfield E, Hong M. Solid-state NMR and quantum chemical investigations of 13Calpha shielding tensor magnitudes and orientations in peptides: determining phi and psi torsion angles. Journal of the American Chemical Society. 127: 6451-8. PMID 15853353 DOI: 10.1021/Ja042935B |
0.445 |
|
2005 |
Luo W, Yao X, Hong M. Large structure rearrangement of colicin ia channel domain after membrane binding from 2D 13C spin diffusion NMR. Journal of the American Chemical Society. 127: 6402-8. PMID 15853348 DOI: 10.1021/Ja0433121 |
0.751 |
|
2005 |
Buffy JJ, Waring AJ, Hong M. Determination of peptide oligomerization in lipid bilayers using 19F spin diffusion NMR. Journal of the American Chemical Society. 127: 4477-83. PMID 15783230 DOI: 10.1021/Ja043621R |
0.432 |
|
2005 |
Harris DJ, Bonagamba TJ, Hong M, Schmidt-Rohr K. Two-dimensional solid-state NMR studies of crystalline poly(ethylene oxide): Conformations and chemical shifts Polymer. 46: 11737-11743. DOI: 10.1016/J.Polymer.2005.09.035 |
0.584 |
|
2004 |
Mani R, Buffy JJ, Waring AJ, Lehrer RI, Hong M. Solid-state NMR investigation of the selective disruption of lipid membranes by protegrin-1. Biochemistry. 43: 13839-48. PMID 15504046 DOI: 10.1021/Bi048650T |
0.685 |
|
2004 |
Wi S, Sinha N, Hong M. Long-range 1H-19F distance measurement in peptides by solid-state NMR. Journal of the American Chemical Society. 126: 12754-5. PMID 15469252 DOI: 10.1021/Ja0462732 |
0.356 |
|
2004 |
Buffy JJ, McCormick MJ, Wi S, Waring A, Lehrer RI, Hong M. Solid-state NMR investigation of the selective perturbation of lipid bilayers by the cyclic antimicrobial peptide RTD-1. Biochemistry. 43: 9800-12. PMID 15274634 DOI: 10.1021/Bi036243W |
0.484 |
|
2004 |
Gallagher GJ, Hong M, Thompson LK. Solid-state NMR spin diffusion for measurement of membrane-bound peptide structure: gramicidin A. Biochemistry. 43: 7899-906. PMID 15196034 DOI: 10.1021/Bi0356101 |
0.677 |
|
2004 |
Sinha N, Schmidt-Rohr K, Hong M. Compensation for pulse imperfections in rotational-echo double-resonance NMR by composite pulses and EXORCYCLE. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 168: 358-65. PMID 15140448 DOI: 10.1016/J.Jmr.2004.03.025 |
0.539 |
|
2004 |
Yao XL, Hong M. Structure distribution in an elastin-mimetic peptide (VPGVG)3 investigated by solid-state NMR. Journal of the American Chemical Society. 126: 4199-210. PMID 15053609 DOI: 10.1021/ja036686n |
0.592 |
|
2004 |
Yao XL, Conticello VP, Hong M. Investigation of the dynamics of an elastin-mimetic polypeptide using solid-state NMR. Magnetic Resonance in Chemistry : Mrc. 42: 267-75. PMID 14745807 DOI: 10.1002/Mrc.1330 |
0.609 |
|
2003 |
Buffy JJ, Waring AJ, Lehrer RI, Hong M. Immobilization and aggregation of the antimicrobial peptide protegrin-1 in lipid bilayers investigated by solid-state NMR. Biochemistry. 42: 13725-34. PMID 14622019 DOI: 10.1021/Bi035187W |
0.476 |
|
2003 |
Hong M, Isailovic D, McMillan RA, Conticello VP. Structure of an elastin-mimetic polypeptide by solid-state NMR chemical shift analysis. Biopolymers. 70: 158-68. PMID 14517905 DOI: 10.1002/Bip.10431 |
0.462 |
|
2003 |
Buffy JJ, Hong T, Yamaguchi S, Waring AJ, Lehrer RI, Hong M. Solid-state NMR investigation of the depth of insertion of protegrin-1 in lipid bilayers using paramagnetic Mn2+. Biophysical Journal. 85: 2363-73. PMID 14507700 DOI: 10.1016/S0006-3495(03)74660-8 |
0.457 |
|
2003 |
Schmidt-Rohr K, Hong M. Measurements of carbon to amide-proton distances by C-H dipolar recoupling with 15N NMR detection. Journal of the American Chemical Society. 125: 5648-9. PMID 12733900 DOI: 10.1021/Ja0344415 |
0.625 |
|
2003 |
Hong M, Yao X. Homonuclear decoupled 13C chemical shift anisotropy in 13C doubly labeled peptides by selective-pulse solid-state NMR. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 160: 114-9. PMID 12615151 DOI: 10.1016/S1090-7807(02)00140-4 |
0.636 |
|
2003 |
Petkova AT, Baldus M, Belenky M, Hong M, Griffin RG, Herzfeld J. Backbone and side chain assignment strategies for multiply labeled membrane peptides and proteins in the solid state. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 160: 1-12. PMID 12565042 DOI: 10.1016/S1090-7807(02)00137-4 |
0.672 |
|
2003 |
Sinha N, Hong M. X–1H rotational-echo double-resonance NMR for torsion angle determination of peptides Chemical Physics Letters. 380: 742-748. DOI: 10.1016/J.Cplett.2003.09.088 |
0.443 |
|
2002 |
Yao X, Yamaguchi S, Hong M. C(alpha) chemical shift tensors in helical peptides by dipolar-modulated chemical shift recoupling NMR. Journal of Biomolecular Nmr. 24: 51-62. PMID 12449418 DOI: 10.1023/A:1020626802472 |
0.581 |
|
2002 |
Yamaguchi S, Hong T, Waring A, Lehrer RI, Hong M. Solid-state NMR investigations of peptide-lipid interaction and orientation of a beta-sheet antimicrobial peptide, protegrin. Biochemistry. 41: 9852-62. PMID 12146951 DOI: 10.1021/Bi0257991 |
0.472 |
|
2002 |
Yamaguchi S, Hong M. Determination of membrane peptide orientation by 1H-detected 2H NMR spectroscopy Journal of Magnetic Resonance. 155: 244-250. PMID 12036335 DOI: 10.1006/Jmre.2002.2517 |
0.452 |
|
2002 |
Huster D, Yao X, Jakes K, Hong M. Conformational changes of colicin Ia channel-forming domain upon membrane binding: a solid-state NMR study. Biochimica Et Biophysica Acta. 1561: 159-70. PMID 11997116 DOI: 10.1016/S0005-2736(02)00340-1 |
0.742 |
|
2002 |
Yao X, Hong M. Determination of calpha chemical shift tensor orientation in peptides by dipolar-modulated chemical shift recoupling NMR spectroscopy. Journal of the American Chemical Society. 124: 2730-8. PMID 11890824 |
0.598 |
|
2002 |
Hong M, McMillan RA, Conticello VP. Measurement of conformational constraints in an elastin-mimetic protein by residue-pair selected solid-state NMR. Journal of Biomolecular Nmr. 22: 175-9. PMID 11883778 DOI: 10.1023/A:1014291305148 |
0.423 |
|
2002 |
Huster D, Yao X, Hong M. Membrane protein topology probed by (1)H spin diffusion from lipids using solid-state NMR spectroscopy. Journal of the American Chemical Society. 124: 874-83. PMID 11817963 DOI: 10.1021/Ja017001R |
0.722 |
|
2002 |
Hong M, Yao X, Jakes K, Huster D. Investigation of molecular motions by Lee-Goldburg cross-polarization NMR spectroscopy Journal of Physical Chemistry B. 106: 7355-7364. DOI: 10.1021/Jp0156064 |
0.709 |
|
2001 |
Yamaguchi S, Huster D, Waring A, Lehrer RI, Kearney W, Tack BF, Hong M. Orientation and Dynamics of an Antimicrobial Peptide in the Lipid Bilayer by Solid-State NMR Spectroscopy Biophysical Journal. 81: 2203-2214. PMID 11566791 DOI: 10.1016/S0006-3495(01)75868-7 |
0.643 |
|
2001 |
Yao XL, Hong M. Dipolar filtered 1H-13C heteronuclear correlation spectroscopy for resonance assignment of proteins. Journal of Biomolecular Nmr. 20: 263-74. PMID 11519749 DOI: 10.1023/A:1011251924874 |
0.615 |
|
2001 |
Schmidt-Rohr K, Saalwächter K, Liu SF, Hong M. High-sensitivity 2H NMR in solids by 1H detection. Journal of the American Chemical Society. 123: 7168-9. PMID 11459501 DOI: 10.1021/Ja002787Z |
0.535 |
|
2001 |
Huster D, Xiao L, Hong M. Solid-State NMR Investigation of the Dynamics of the Soluble and Membrane-Bound Colicin Ia Channel-Forming Domain† Biochemistry. 40: 7662-7674. PMID 11412120 DOI: 10.1021/Bi0027231 |
0.616 |
|
2001 |
Hong M, Yamaguchi S. Sensitivity-enhanced static 15N NMR of solids by 1H indirect detection Journal of Magnetic Resonance. 150: 43-48. PMID 11330982 DOI: 10.1006/Jmre.2001.2309 |
0.385 |
|
2001 |
Kennedy SB, DeAzevedo ER, Petka WA, Russell TP, Tirrell DA, Hong M. Dynamic structure of a protein hydrogel: A solid-state NMR study Macromolecules. 34: 8675-8685. DOI: 10.1021/Ma010768J |
0.387 |
|
2001 |
Yao XL, Schmidt-Rohr K, Hong M. Medium- and long-distance 1H-13C heteronuclear correlation NMR in solids Journal of Magnetic Resonance. 149: 139-143. DOI: 10.1006/Jmre.2001.2285 |
0.604 |
|
2000 |
Harris DJ, Bonagamba TJ, Hong M, Schmidt-Rohr K. Conformation of poly(ethylene oxide)-hydroxybenzene molecular complexes studied by solid-state NMR Macromolecules. 33: 3375-3381. DOI: 10.1021/Ma992087I |
0.59 |
|
2000 |
Hong M. Solid-state NMR determination of 13Cα chemical shift anisotropies for the identification of protein secondary structure Journal of the American Chemical Society. 122: 3762-3770. DOI: 10.1021/ja994119n |
0.384 |
|
2000 |
Huster D, Yamaguchi S, Hong M. Efficient β-Sheet Identification in Proteins by Solid-State NMR Spectroscopy Journal of the American Chemical Society. 122: 11320-11327. DOI: 10.1021/Ja001674C |
0.583 |
|
2000 |
Rienstra CM, Hohwy M, Hong M, Griffin RG. 2D and 3D 15N-13C-13C NMR chemical shift correlation spectroscopy of solids: Assignment of MAS spectra of peptides Journal of the American Chemical Society. 122: 10979-10990. DOI: 10.1021/Ja001092V |
0.746 |
|
2000 |
deAzevedo ER, Kennedy SB, Hong M. Determination of slow motions in extensively isotopically labeled proteins by magic-angle-spinning 13C-detected 15N exchange NMR Chemical Physics Letters. 321: 43-48. DOI: 10.1016/S0009-2614(00)00310-9 |
0.419 |
|
1999 |
Hong M. Resonance assignment of 13C/15N labeled solid proteins by two- and three-dimensional magic-angle-spinning NMR Journal of Biomolecular Nmr. 15: 1-14. PMID 10549131 DOI: 10.1023/A:1008334204412 |
0.434 |
|
1999 |
Hong M. Determination of Multiple φ-Torsion Angles in Proteins by Selective and Extensive 13C Labeling and Two-Dimensional Solid-State NMR Journal of Magnetic Resonance. 139: 389-401. PMID 10423377 DOI: 10.1006/Jmre.1999.1805 |
0.436 |
|
1999 |
Hong M, Jakes K. Selective and extensive 13C labeling of a membrane protein for solid- state NMR investigations Journal of Biomolecular Nmr. 14: 71-74. PMID 10382307 DOI: 10.1023/A:1008334930603 |
0.402 |
|
1999 |
Hong M. Solid-State Dipolar INADEQUATE NMR Spectroscopy with a Large Double-Quantum Spectral Width Journal of Magnetic Resonance. 136: 86-91. PMID 9887293 DOI: 10.1006/Jmre.1998.1631 |
0.381 |
|
1999 |
Sandström D, Hong M, Schmidt-Rohr K. Identification and mobility of deuterated residues in peptides and proteins by – solid-state NMR Chemical Physics Letters. 300: 213-220. DOI: 10.1016/S0009-2614(98)01325-6 |
0.655 |
|
1998 |
Hong M, Gross JD, Hu W, Griffin RG. Determination of the peptide torsion angle phi by 15N chemical shift and 13Calpha-1Halpha dipolar tensor correlation in solid-state MAS NMR. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 135: 169-77. PMID 9799691 DOI: 10.1006/Jmre.1998.1573 |
0.768 |
|
1998 |
Hong M, Griffin RG. Resonance Assignments for Solid Peptides by Dipolar-Mediated13C/15N Correlation Solid-State NMR Journal of the American Chemical Society. 120: 7113-7114. DOI: 10.1021/Ja980775W |
0.644 |
|
1997 |
Hong M, Gross JD, Rienstra CM, Griffin RG, Kumashiro KK, Schmidt-Rohr K. Coupling amplification in 2D MAS NMR and its application to torsion angle determination in peptides. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 129: 85-92. PMID 9405219 DOI: 10.1006/Jmre.1997.1242 |
0.818 |
|
1997 |
Hong M, Gross JD, Griffin RG. Site-Resolved Determination of Peptide Torsion Angle φ from the Relative Orientations of Backbone N−H and C−H Bonds by Solid-State NMR The Journal of Physical Chemistry B. 101: 5869-5874. DOI: 10.1021/Jp970887U |
0.65 |
|
1997 |
Costa P, Gross J, Hong M, Griffin R. Solid-state NMR measurement of Ψ in peptides: a NCCN 2Q-heteronuclear local field experiment Chemical Physics Letters. 280: 95-103. DOI: 10.1016/S0009-2614(97)01107-X |
0.746 |
|
1996 |
Caldarelli S, Hong M, Emsley L, Pines A. Measurement of Carbon−Proton Dipolar Couplings in Liquid Crystals by Local Dipolar Field NMR Spectroscopy The Journal of Physical Chemistry. 100: 18696-18701. DOI: 10.1021/Jp962023Z |
0.628 |
|
1996 |
Hong M, Pines A, Caldarelli S. Measurement and Assignment of Long-Range C−H Dipolar Couplings in Liquid Crystals by Two-Dimensional NMR Spectroscopy The Journal of Physical Chemistry. 100: 14815-14822. DOI: 10.1021/Jp960972M |
0.526 |
|
1996 |
Schmidt-Rohr K, Hong M. Information on Bond Orientation Distributions in Lipids and Liquid Crystals from Segmental Order Parameters The Journal of Physical Chemistry. 100: 3861-3867. DOI: 10.1021/Jp952788R |
0.537 |
|
1995 |
Hong M, Schmidt-Rohr K, Pines A. NMR Measurement of Signs and Magnitudes of C-H Dipolar Couplings in Lecithin Journal of the American Chemical Society. 117: 3310-3311. DOI: 10.1021/Ja00116A051 |
0.662 |
|
1995 |
Hong M, Schmidt-Rohr K. DISTINCT NMR for Sign Determination of C-H Dipolar Couplings in Liquid-Crystalline Lipids Journal of Magnetic Resonance, Series B. 109: 284-290. DOI: 10.1006/Jmrb.1995.9993 |
0.59 |
|
1995 |
Nanz D, Ernst M, Hong M, Ziegeweid M, Schmidtrohr K, Pines A. Low-Power Decoupling Sequences for High-Resolution Chemical-Shift and Local-Field NMR Spectra of Liquid Crystals Journal of Magnetic Resonance, Series A. 113: 169-176. DOI: 10.1006/jmra.1995.1077 |
0.417 |
|
1994 |
Min H, Hong M, Ma J, Zhang E, Zheng Q, Zhang J, Zhang J, Zhang F, Su Y, Qiu F. A new staging system for nasopharyngeal carcinoma in China. International Journal of Radiation Oncology, Biology, Physics. 30: 1037-42. PMID 7961009 |
0.514 |
|
1994 |
Lee YK, Emsley L, Larsen RG, Schmidt‐Rohr K, Hong M, Frydman L, Chingas GC, Pines A. Three‐dimensional variable‐angle nuclear magnetic resonance exchange spectroscopy without rotor axis hopping The Journal of Chemical Physics. 101: 1852-1864. DOI: 10.1063/1.467696 |
0.713 |
|
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