Year |
Citation |
Score |
2021 |
Xiang X, Hansen AL, Yu L, Jameson G, Bruschweiler-Li L, Yuan C, Brüschweiler R. Observation of Sub-Microsecond Protein Methyl-Side Chain Dynamics by Nanoparticle-Assisted NMR Spin Relaxation. Journal of the American Chemical Society. PMID 34428032 DOI: 10.1021/jacs.1c04687 |
0.309 |
|
2019 |
Jameson G, Hansen AL, Li D, Bruschweiler-Li L, Bruschweiler R. Extreme Non-Uniform Sampling for Protein NMR Dynamics Studies in Minimal Time. Journal of the American Chemical Society. PMID 31560199 DOI: 10.1021/Jacs.9B08032 |
0.366 |
|
2019 |
Xie M, Yu L, Bruschweiler-Li L, Xiang X, Hansen AL, Brüschweiler R. Functional protein dynamics on uncharted time scales detected by nanoparticle-assisted NMR spin relaxation. Science Advances. 5: eaax5560. PMID 31453342 DOI: 10.1126/Sciadv.Aax5560 |
0.399 |
|
2019 |
Timari I, Wang C, Hansen AL, Costa Dos Santos G, Yoon SO, Bruschweiler-Li L, Bruschweiler R. Real-Time Pure Shift HSQC NMR for Untargeted Metabolomics. Analytical Chemistry. PMID 30608652 DOI: 10.1021/Acs.Analchem.8B04928 |
0.376 |
|
2019 |
Larion M, Hansen A, Bruschweiler-Li L, Tugarinov V, Brüschweiler R, Miller B. Specific 13CH3 Labeling and NMR Reveal the Role of Structural Dynamics to Enzymatic Function Biophysical Journal. 116: 470a. DOI: 10.1016/J.Bpj.2018.11.2540 |
0.344 |
|
2018 |
Bowles DP, Yuan C, Stephany KR, Lavinder JJ, Hansen AL, Magliery TJ. Resonance assignments of wild-type and two cysteine-free variants of the four-helix bundle protein, Rop. Biomolecular Nmr Assignments. PMID 30159810 DOI: 10.1007/S12104-018-9837-0 |
0.365 |
|
2018 |
Penumutchu S, Chiu LY, Meagher JL, Hansen AL, Stuckey JA, Tolbert BS. Differential Conformational Dynamics Encoded by the Inter-qRRM linker of hnRNP H. Journal of the American Chemical Society. PMID 30122033 DOI: 10.1021/jacs.8b05366 |
0.457 |
|
2018 |
Li D, Hansen A, Bruschweiler-Li L, Bruschweiler R. Non-Uniform and Absolute Minimal Sampling for High-Throughput Multidimensional NMR Applications. Chemistry (Weinheim An Der Bergstrasse, Germany). PMID 29566285 DOI: 10.1002/Chem.201800954 |
0.356 |
|
2018 |
Li D, Hansen AL, Bruschweiler‐Li L, Brüschweiler R. Frontispiece: Non‐Uniform and Absolute Minimal Sampling for High‐Throughput Multidimensional NMR Applications Chemistry – a European Journal. 24. DOI: 10.1002/Chem.201884563 |
0.333 |
|
2017 |
Hansen A, Li DW, Wang C, Bruschweiler R. Absolute Minimal Sampling of Homonuclear 2D NMR TOCSY Spectra for High-Throughput Applications of Complex Mixtures. Angewandte Chemie (International Ed. in English). PMID 28543988 DOI: 10.1002/Anie.201703587 |
0.321 |
|
2017 |
Peng Y, Hansen AL, Bruschweiler-Li L, Davulcu O, Skalicky JJ, Chapman MS, Bruschweiler R. The Michaelis Complex of Arginine Kinase Samples the Transition State at a Frequency that Matches the Catalytic Rate. Journal of the American Chemical Society. PMID 28287709 DOI: 10.1021/Jacs.7B00236 |
0.345 |
|
2016 |
Hansen AL, Brüschweiler R. Absolute Minimal Sampling in High-Dimensional NMR Spectroscopy. Angewandte Chemie (International Ed. in English). PMID 27723193 DOI: 10.1002/Anie.201608048 |
0.335 |
|
2016 |
Gu Y, Hansen AL, Peng Y, Brüschweiler R. Rapid Determination of Fast Protein Dynamics from NMR Chemical Exchange Saturation Transfer Data. Angewandte Chemie (International Ed. in English). PMID 26821600 DOI: 10.1002/Anie.201511711 |
0.4 |
|
2015 |
Larion M, Hansen AL, Zhang F, Bruschweiler-Li L, Tugarinov V, Miller BG, Brüschweiler R. Kinetic Cooperativity in Human Pancreatic Glucokinase Originates from Millisecond Dynamics of the Small Domain. Angewandte Chemie (International Ed. in English). 54: 8129-32. PMID 26013420 DOI: 10.1002/Anie.201501204 |
0.311 |
|
2014 |
Hansen AL, Kay LE. Measurement of histidine pKa values and tautomer populations in invisible protein states. Proceedings of the National Academy of Sciences of the United States of America. 111: E1705-12. PMID 24733918 DOI: 10.1073/Pnas.1400577111 |
0.368 |
|
2014 |
Zhao B, Hansen AL, Zhang Q. Characterizing slow chemical exchange in nucleic acids by carbon CEST and low spin-lock field R(1Ï) NMR spectroscopy. Journal of the American Chemical Society. 136: 20-3. PMID 24299272 DOI: 10.1021/Ja409835Y |
0.498 |
|
2013 |
Kim TH, Chung KY, Manglik A, Hansen AL, Dror RO, Mildorf TJ, Shaw DE, Kobilka BK, Prosser RS. The role of ligands on the equilibria between functional states of a G protein-coupled receptor. Journal of the American Chemical Society. 135: 9465-74. PMID 23721409 DOI: 10.1021/Ja404305K |
0.305 |
|
2013 |
Hansen AL, Bouvignies G, Kay LE. Probing slowly exchanging protein systems via ¹³Cα-CEST: monitoring folding of the Im7 protein. Journal of Biomolecular Nmr. 55: 279-89. PMID 23386228 DOI: 10.1007/S10858-013-9711-4 |
0.303 |
|
2012 |
Hansen AL, Lundström P, Velyvis A, Kay LE. Quantifying millisecond exchange dynamics in proteins by CPMG relaxation dispersion NMR using side-chain 1H probes. Journal of the American Chemical Society. 134: 3178-89. PMID 22300166 DOI: 10.1021/Ja210711V |
0.369 |
|
2011 |
Bothe JR, Nikolova EN, Eichhorn CD, Chugh J, Hansen AL, Al-Hashimi HM. Characterizing RNA dynamics at atomic resolution using solution-state NMR spectroscopy. Nature Methods. 8: 919-31. PMID 22036746 DOI: 10.1038/Nmeth.1735 |
0.65 |
|
2011 |
Hansen AL, Kay LE. Quantifying millisecond time-scale exchange in proteins by CPMG relaxation dispersion NMR spectroscopy of side-chain carbonyl groups. Journal of Biomolecular Nmr. 50: 347-55. PMID 21681650 DOI: 10.1007/S10858-011-9520-6 |
0.377 |
|
2011 |
Korzhnev DM, Vernon RM, Religa TL, Hansen AL, Baker D, Fersht AR, Kay LE. Nonnative interactions in the FF domain folding pathway from an atomic resolution structure of a sparsely populated intermediate: an NMR relaxation dispersion study. Journal of the American Chemical Society. 133: 10974-82. PMID 21639149 DOI: 10.1021/Ja203686T |
0.388 |
|
2010 |
Dethoff EA, Hansen AL, Zhang Q, Al-Hashimi HM. Variable helix elongation as a tool to modulate RNA alignment and motional couplings. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 202: 117-21. PMID 19854083 DOI: 10.1016/J.Jmr.2009.09.022 |
0.775 |
|
2009 |
Hansen AL, Nikolova EN, Casiano-Negroni A, Al-Hashimi HM. Extending the range of microsecond-to-millisecond chemical exchange detected in labeled and unlabeled nucleic acids by selective carbon R(1rho) NMR spectroscopy. Journal of the American Chemical Society. 131: 3818-9. PMID 19243182 DOI: 10.1021/Ja8091399 |
0.737 |
|
2008 |
Dethoff EA, Hansen AL, Musselman C, Watt ED, Andricioaei I, Al-Hashimi HM. Characterizing complex dynamics in the transactivation response element apical loop and motional correlations with the bulge by NMR, molecular dynamics, and mutagenesis. Biophysical Journal. 95: 3906-15. PMID 18621815 DOI: 10.1529/Biophysj.108.140285 |
0.731 |
|
2007 |
Hansen AL, Al-Hashimi HM. Dynamics of large elongated RNA by NMR carbon relaxation. Journal of the American Chemical Society. 129: 16072-82. PMID 18047338 DOI: 10.1021/Ja0757982 |
0.706 |
|
2007 |
Bailor MH, Musselman C, Hansen AL, Gulati K, Patel DJ, Al-Hashimi HM. Characterizing the relative orientation and dynamics of RNA A-form helices using NMR residual dipolar couplings. Nature Protocols. 2: 1536-46. PMID 17571061 DOI: 10.1038/Nprot.2007.221 |
0.713 |
|
2006 |
Hansen AL, Al-Hashimi HM. Insight into the CSA tensors of nucleobase carbons in RNA polynucleotides from solution measurements of residual CSA: towards new long-range orientational constraints. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 179: 299-307. PMID 16431143 DOI: 10.1016/J.Jmr.2005.12.012 |
0.636 |
|
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