Year |
Citation |
Score |
2024 |
Yekefallah M, van Aalst EJ, van Beekveld RAM, Eason IR, Breukink E, Weingarth M, Wylie BJ. Cooperative Gating of a K Channel by Unmodified Biological Anionic Lipids Viewed by Solid-State NMR Spectroscopy. Journal of the American Chemical Society. 146: 4421-4432. PMID 38334076 DOI: 10.1021/jacs.3c09266 |
0.327 |
|
2023 |
van Aalst EJ, Jang J, Halligan TC, Wylie BJ. Strategies for acquisition of resonance assignment spectra of highly dynamic membrane proteins: a GPCR case study. Journal of Biomolecular Nmr. PMID 37493866 DOI: 10.1007/s10858-023-00421-8 |
0.313 |
|
2023 |
van Aalst EJ, McDonald CJ, Wylie BJ. Cholesterol Biases the Conformational Landscape of the Chemokine Receptor CCR3: A MAS SSNMR-Filtered Molecular Dynamics Study. Journal of Chemical Information and Modeling. 63: 3068-3085. PMID 37127541 DOI: 10.1021/acs.jcim.2c01546 |
0.313 |
|
2022 |
Yekefallah M, Rasberry CA, van Aalst EJ, Browning HP, Amani R, Versteeg DB, Wylie BJ. Mutational Insight into Allosteric Regulation of Kir Channel Activity. Acs Omega. 7: 43621-43634. PMID 36506180 DOI: 10.1021/acsomega.2c04456 |
0.551 |
|
2022 |
Borcik CG, Eason IR, Vanderloop B, Wylie BJ. H,C-Cholesterol for Dynamics and Structural Studies of Biological Membranes. Acs Omega. 7: 17151-17160. PMID 35647452 DOI: 10.1021/acsomega.2c00796 |
0.749 |
|
2022 |
van Aalst EJ, Borcik CG, Wylie BJ. Spectroscopic signatures of bilayer ordering in native biological membranes. Biochimica Et Biophysica Acta. Biomembranes. 183891. PMID 35217001 DOI: 10.1016/j.bbamem.2022.183891 |
0.746 |
|
2022 |
Borcik CG, Eason IR, Yekefellah M, Amani R, Han R, Vanderloop BH, Wylie B. A Cholesterol Dimer Stabilizes the Inactivated State of an Inward-rectifier Potassium Channel. Angewandte Chemie (International Ed. in English). PMID 34985791 DOI: 10.1002/anie.202112232 |
0.8 |
|
2021 |
Amani R, Schwieters CD, Borcik CG, Eason IR, Han R, Harding BD, Wylie BJ. Water Accessibility Refinement of the Extended Structure of KirBac1.1 in the Closed State. Frontiers in Molecular Biosciences. 8: 772855. PMID 34917650 DOI: 10.3389/fmolb.2021.772855 |
0.823 |
|
2021 |
Hu J, Zanca F, McManus GJ, Riha IA, Nguyen HGT, Shirley W, Borcik CG, Wylie BJ, Benamara M, van Zee RD, Moghadam PZ, Beyzavi H. Catalyst-Enabled Linkage Reduction in Imine Covalent Organic Frameworks. Acs Applied Materials & Interfaces. PMID 33913321 DOI: 10.1021/acsami.1c02709 |
0.697 |
|
2021 |
Do HQ, Hewetson A, Borcik CG, Hastert MC, Whelly S, Wylie BJ, Sutton RB, Cornwall GA. Cross-seeding Between the Functional Amyloidogenic CRES and CRES3 Family Members and their Regulation of Aβ Assembly. The Journal of Biological Chemistry. 100250. PMID 33428930 DOI: 10.1074/jbc.RA120.015307 |
0.702 |
|
2020 |
Do HQ, Hewetson A, Borcik CG, Hastert MC, Whelly S, Wylie BJ, Sutton RB, Cornwall GA. Cross-seeding Between the Functional Amyloidogenic CRES and CRES3 Family Members and their Regulation of Aβ Assembly. The Journal of Biological Chemistry. PMID 33384380 DOI: 10.1074/jbc.RA120.015307 |
0.702 |
|
2020 |
Borcik CG, Versteeg DB, Amani R, Yekefallah M, Khan NH, Wylie BJ. The Lipid Activation Mechanism of a Transmembrane Potassium Channel. Journal of the American Chemical Society. PMID 32702990 DOI: 10.1021/Jacs.0C01991 |
0.781 |
|
2020 |
Hewetson A, Khan NH, Dominguez MJ, Do HQ, Kusko RE, Borcik CG, Rigden DJ, Keegan RM, Sutton RB, Latham MP, Wylie BJ, Cornwall GA. Maturation of the functional mouse CRES amyloid from globular form. Proceedings of the National Academy of Sciences of the United States of America. PMID 32601205 DOI: 10.1073/Pnas.2006887117 |
0.733 |
|
2020 |
van Aalst E, Yekefallah M, Mehta AK, Eason I, Wylie B. Codon Harmonization of a Kir3.1-KirBac1.3 Chimera for Structural Study Optimization. Biomolecules. 10. PMID 32164257 DOI: 10.3390/biom10030430 |
0.386 |
|
2020 |
Amani R, Borcik CG, Khan NH, Versteeg DB, Yekefallah M, Do HQ, Coats HR, Wylie BJ. Conformational changes upon gating of KirBac1.1 into an open-activated state revealed by solid-state NMR and functional assays. Proceedings of the National Academy of Sciences of the United States of America. PMID 31980523 DOI: 10.1073/Pnas.1915010117 |
0.795 |
|
2019 |
Borcik CG, Versteeg DB, Wylie BJ. An Inward-Rectifier Potassium Channel Coordinates the Properties of Biologically Derived Membranes. Biophysical Journal. 116: 1701-1718. PMID 31010661 DOI: 10.1016/J.Bpj.2019.03.023 |
0.751 |
|
2018 |
Wylie B, Borcik C, Hardy E. The Functional Relationship between a Kir Channel and the Lipid Membrane Biophysical Journal. 114: 610a. DOI: 10.1016/J.Bpj.2017.11.3334 |
0.726 |
|
2016 |
Harris MJ, Struppe JO, Wylie BJ, McDermott AE, Thompson LK. Multidimensional Solid-State NMR of a Functional Multiprotein Chemoreceptor Array. Biochemistry. PMID 27295350 DOI: 10.1021/Acs.Biochem.6B00234 |
0.636 |
|
2016 |
Wylie BJ, Do HQ, Borcik CG, Hardy EP. Advances in solid-state NMR of membrane proteins Molecular Physics. 114: 3598-3609. DOI: 10.1080/00268976.2016.1252470 |
0.768 |
|
2015 |
Wylie BJ, Dzikovski BG, Pawsey S, Caporini M, Rosay M, Freed JH, McDermott AE. Dynamic nuclear polarization of membrane proteins: covalently bound spin-labels at protein-protein interfaces. Journal of Biomolecular Nmr. 61: 361-7. PMID 25828256 DOI: 10.1007/S10858-015-9919-6 |
0.61 |
|
2014 |
Wylie BJ, Bhate MP, McDermott AE. Transmembrane allosteric coupling of the gates in a potassium channel Proceedings of the National Academy of Sciences of the United States of America. 111: 185-190. PMID 24344306 DOI: 10.1073/Pnas.1319577110 |
0.526 |
|
2014 |
Harris MJ, Weis RM, Struppe JO, Wylie BJ, McDermott AE, Thompson LK. Multidimensional Solid-State NMR of Functional Chemotaxis Receptor Signaling Complexes Biophysical Journal. 106: 104a. DOI: 10.1016/J.Bpj.2013.11.645 |
0.623 |
|
2013 |
Bhate MP, Wylie BJ, Thompson A, Tian L, Nimigean C, McDermott AE. Preparation of uniformly isotope labeled KcsA for solid state NMR: Expression, purification, reconstitution into liposomes and functional assay Protein Expression and Purification. 91: 119-124. PMID 23916531 DOI: 10.1016/J.Pep.2013.07.013 |
0.633 |
|
2012 |
Mollica L, Baias M, Lewandowski JR, Wylie BJ, Sperling LJ, Rienstra CM, Emsley L, Blackledge M. Atomic-Resolution Structural Dynamics in Crystalline Proteins from NMR and Molecular Simulation. The Journal of Physical Chemistry Letters. 3: 3657-62. PMID 26291002 DOI: 10.1021/Jz3016233 |
0.79 |
|
2012 |
Mollica L, Baias M, Lewandowski JR, Wylie BJ, Sperling LJ, Rienstra CM, Emsley L, Blackledge M. Atomic-resolution structural dynamics in crystalline proteins from NMR and molecular simulation Journal of Physical Chemistry Letters. 3: 3657-3662. DOI: 10.1021/jz3016233 |
0.784 |
|
2011 |
Wylie BJ, Sperling LJ, Nieuwkoop AJ, Franks WT, Oldfield E, Rienstra CM. Ultrahigh resolution protein structures using NMR chemical shift tensors. Proceedings of the National Academy of Sciences of the United States of America. 108: 16974-9. PMID 21969532 DOI: 10.1073/Pnas.1103728108 |
0.792 |
|
2010 |
Bhate MP, Wylie BJ, Tian L, McDermott AE. Conformational dynamics in the selectivity filter of KcsA in response to potassium ion concentration Journal of Molecular Biology. 401: 155-166. PMID 20600123 DOI: 10.1016/J.Jmb.2010.06.031 |
0.553 |
|
2010 |
Bhate M, Wylie B, Tian L, McDermott A. [K+] Induced Conformational Dynamics of the Selectivity Filter of KcsA Monitored by Solid-State NMR Biophysical Journal. 98: 331a. DOI: 10.1016/J.Bpj.2009.12.1799 |
0.611 |
|
2009 |
Nieuwkoop AJ, Wylie BJ, Franks WT, Shah GJ, Rienstra CM. Atomic resolution protein structure determination by three-dimensional transferred echo double resonance solid-state nuclear magnetic resonance spectroscopy. The Journal of Chemical Physics. 131: 095101. PMID 19739873 DOI: 10.1063/1.3211103 |
0.822 |
|
2009 |
Wylie BJ, Schwieters CD, Oldfield E, Rienstra CM. Protein structure refinement using 13C alpha chemical shift tensors. Journal of the American Chemical Society. 131: 985-92. PMID 19123862 DOI: 10.1021/Ja804041P |
0.618 |
|
2008 |
Franks WT, Wylie BJ, Schmidt HL, Nieuwkoop AJ, Mayrhofer RM, Shah GJ, Graesser DT, Rienstra CM. Dipole tensor-based atomic-resolution structure determination of a nanocrystalline protein by solid-state NMR. Proceedings of the National Academy of Sciences of the United States of America. 105: 4621-6. PMID 18344321 DOI: 10.1073/Pnas.0712393105 |
0.817 |
|
2008 |
Wylie BJ, Rienstra CM. Multidimensional solid state NMR of anisotropic interactions in peptides and proteins. The Journal of Chemical Physics. 128: 052207. PMID 18266412 DOI: 10.1063/1.2834735 |
0.647 |
|
2008 |
Wylie BJ, Sperling LJ, Rienstra CM. Isotropic chemical shifts in magic-angle spinning NMR spectra of proteins. Physical Chemistry Chemical Physics : Pccp. 10: 405-13. PMID 18174982 DOI: 10.1039/B710736F |
0.801 |
|
2007 |
Graesser DT, Wylie BJ, Nieuwkoop AJ, Franks WT, Rienstra CM. Long-range 19F-15N distance measurements in highly-13C, 15N-enriched solid proteins with 19F-dephased REDOR shift (FRESH) spectroscopy. Magnetic Resonance in Chemistry : Mrc. 45: S129-34. PMID 18157807 DOI: 10.1002/Mrc.2126 |
0.796 |
|
2007 |
Schmidt HL, Sperling LJ, Gao YG, Wylie BJ, Boettcher JM, Wilson SR, Rienstra CM. Crystal polymorphism of protein GB1 examined by solid-state NMR spectroscopy and X-ray diffraction. The Journal of Physical Chemistry. B. 111: 14362-9. PMID 18052145 DOI: 10.1021/Jp075531P |
0.785 |
|
2007 |
Zhou DH, Shea JJ, Nieuwkoop AJ, Franks WT, Wylie BJ, Mullen C, Sandoz D, Rienstra CM. Solid-state protein-structure determination with proton-detected triple-resonance 3D magic-angle-spinning NMR spectroscopy. Angewandte Chemie (International Ed. in English). 46: 8380-3. PMID 17907259 DOI: 10.1002/Anie.200702905 |
0.821 |
|
2007 |
Franks WT, Kloepper KD, Wylie BJ, Rienstra CM. Four-dimensional heteronuclear correlation experiments for chemical shift assignment of solid proteins. Journal of Biomolecular Nmr. 39: 107-31. PMID 17687624 DOI: 10.1007/S10858-007-9179-1 |
0.808 |
|
2007 |
Wylie BJ, Sperling LJ, Frericks HL, Shah GJ, Franks WT, Rienstra CM. Chemical-shift anisotropy measurements of amide and carbonyl resonances in a microcrystalline protein with slow magic-angle spinning NMR spectroscopy. Journal of the American Chemical Society. 129: 5318-9. PMID 17425317 DOI: 10.1021/Ja0701199 |
0.812 |
|
2007 |
Zhou D, Shea J, Nieuwkoop A, Franks WT, Wylie B, Mullen C, Sandoz D, Rienstra C. Solid-State Protein Structure Determination with Proton-Detected TripleResonance 3D Magic-Angle Spinning NMR Spectroscopy: Beta-1 ImmunoglobulinBinding Domain of Protein G (GB1) Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr15156 |
0.791 |
|
2006 |
Wylie BJ, Franks WT, Rienstra CM. Determinations of 15N chemical shift anisotropy magnitudes in a uniformly 15N,13C-labeled microcrystalline protein by three-dimensional magic-angle spinning nuclear magnetic resonance spectroscopy. The Journal of Physical Chemistry. B. 110: 10926-36. PMID 16771346 DOI: 10.1021/Jp060507H |
0.791 |
|
2006 |
Franks WT, Wylie BJ, Stellfox SA, Rienstra CM. Backbone conformational constraints in a microcrystalline U-15N-labeled protein by 3D dipolar-shift solid-state NMR spectroscopy. Journal of the American Chemical Society. 128: 3154-5. PMID 16522090 DOI: 10.1021/Ja058292X |
0.793 |
|
2006 |
Li Y, Wylie BJ, Rienstra CM. Selective refocusing pulses in magic-angle spinning NMR: characterization and applications to multi-dimensional protein spectroscopy. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 179: 206-16. PMID 16406627 DOI: 10.1016/J.Jmr.2005.12.003 |
0.606 |
|
2005 |
Franks WT, Zhou DH, Wylie BJ, Money BG, Graesser DT, Frericks HL, Sahota G, Rienstra CM. Magic-angle spinning solid-state NMR spectroscopy of the beta1 immunoglobulin binding domain of protein G (GB1): 15N and 13C chemical shift assignments and conformational analysis. Journal of the American Chemical Society. 127: 12291-305. PMID 16131207 DOI: 10.1021/Ja044497E |
0.804 |
|
2005 |
Wylie BJ, Franks WT, Graesser DT, Rienstra CM. Site-specific 13C chemical shift anisotropy measurements in a uniformly 15N,13C-labeled microcrystalline protein by 3D magic-angle spinning NMR spectroscopy. Journal of the American Chemical Society. 127: 11946-7. PMID 16117526 DOI: 10.1021/Ja053862E |
0.797 |
|
Show low-probability matches. |