Year |
Citation |
Score |
2022 |
Zhao S, Li X, Wen Z, Zou M, Yu G, Liu X, Mao J, Zhang L, Xue Y, Fu R, Wang S. Dynamics of base pairs with low stability in RNA by solid-state nuclear magnetic resonance exchange spectroscopy. Iscience. 25: 105322. PMID 36325062 DOI: 10.1016/j.isci.2022.105322 |
0.339 |
|
2022 |
Han G, Xue Y. Rational design of hairpin RNA excited states reveals multi-step transitions. Nature Communications. 13: 1523. PMID 35314698 DOI: 10.1038/s41467-022-29194-8 |
0.335 |
|
2021 |
Cao J, Xue Y. Characteristic chemical probing patterns of loop motifs improve prediction accuracy of RNA secondary structures. Nucleic Acids Research. 49: 4294-4307. PMID 33849076 DOI: 10.1093/nar/gkab250 |
0.301 |
|
2021 |
Wang Y, Han G, Jiang X, Yuwen T, Xue Y. Chemical shift prediction of RNA imino groups: application toward characterizing RNA excited states. Nature Communications. 12: 1595. PMID 33707433 DOI: 10.1038/s41467-021-21840-x |
0.301 |
|
2019 |
Zhou H, Sathyamoorthy B, Stelling A, Xu Y, Xue Y, Pigli YZ, Case DA, Rice PA, Al-Hashimi HM. Characterizing Watson-Crick versus Hoogsteen Base Pairing in a DNA-Protein Complex Using Nuclear Magnetic Resonance and Site-Specifically C- and N-Labeled DNA. Biochemistry. PMID 30950607 DOI: 10.1021/Acs.Biochem.9B00027 |
0.763 |
|
2018 |
Kimsey IJ, Szymanski ES, Zahurancik WJ, Shakya A, Xue Y, Chu CC, Sathyamoorthy B, Suo Z, Al-Hashimi HM. Dynamic basis for dG•dT misincorporation via tautomerization and ionization. Nature. 554: 195-201. PMID 29420478 DOI: 10.1038/Nature25487 |
0.65 |
|
2017 |
Kurauskas V, Izmailov SA, Rogacheva ON, Hessel A, Ayala I, Woodhouse J, Shilova A, Xue Y, Yuwen T, Coquelle N, Colletier JP, Skrynnikov NR, Schanda P. Slow conformational exchange and overall rocking motion in ubiquitin protein crystals. Nature Communications. 8: 145. PMID 28747759 DOI: 10.1038/S41467-017-00165-8 |
0.387 |
|
2017 |
Sathyamoorthy B, Shi H, Zhou H, Xue Y, Rangadurai A, Merriman DK, Al-Hashimi HM. Insights into Watson-Crick/Hoogsteen breathing dynamics and damage repair from the solution structure and dynamic ensemble of DNA duplexes containing m1A. Nucleic Acids Research. PMID 28369571 DOI: 10.1093/Nar/Gkx186 |
0.698 |
|
2016 |
Gracia B, Xue Y, Bisaria N, Herschlag D, Al-Hashimi HM, Russell R. RNA Structural Modules Control the Rate and Pathway of RNA Folding and Assembly. Journal of Molecular Biology. PMID 27452365 DOI: 10.1016/J.Jmb.2016.07.013 |
0.624 |
|
2016 |
Xue Y, Gracia B, Herschlag D, Russell R, Al-Hashimi HM. Visualizing the formation of an RNA folding intermediate through a fast highly modular secondary structure switch. Nature Communications. 7: ncomms11768. PMID 27292179 DOI: 10.1038/Ncomms11768 |
0.632 |
|
2016 |
Merriman DK, Xue Y, Yang S, Kimsey IJ, Shakya A, Clay MC, Al-Hashimi HM. Shortening the HIV-1 TAR RNA Bulge by a Single Nucleotide Preserves Motional Modes Over a Broad Range of Timescales. Biochemistry. PMID 27232530 DOI: 10.1021/Acs.Biochem.6B00285 |
0.708 |
|
2016 |
Yuwen T, Xue Y, Skrynnikov NR. Role of electrostatic interactions in binding of peptides and intrinsically disordered proteins to their folded targets. 2. The model of encounter complex involving the double mutant of the c-Crk N-SH3 domain and peptide Sos. Biochemistry. PMID 26910732 DOI: 10.1021/Acs.Biochem.5B01283 |
0.348 |
|
2015 |
Ren A, Xue Y, Peselis A, Serganov A, Al-Hashimi HM, Patel DJ. Structural and Dynamic Basis for Low-Affinity, High-Selectivity Binding of L-Glutamine by the Glutamine Riboswitch. Cell Reports. 13: 1800-1813. PMID 26655897 DOI: 10.1016/J.Celrep.2015.10.062 |
0.656 |
|
2015 |
Shakya A, Dougherty CA, Xue Y, Al-Hashimi HM, Banaszak Holl MM. Rapid Exchange Between Free and Bound States in RNA-Dendrimer Polyplexes: Implications on the Mechanism of Delivery and Release. Biomacromolecules. PMID 26595195 DOI: 10.1021/Acs.Biomac.5B01280 |
0.785 |
|
2015 |
Swanson MD, Boudreaux DM, Salmon L, Chugh J, Winter HC, Meagher JL, André S, Murphy PV, Oscarson S, Roy R, King S, Kaplan MH, Goldstein IJ, Tarbet EB, Hurst BL, ... ... Xue Y, et al. Engineering a Therapeutic Lectin by Uncoupling Mitogenicity from Antiviral Activity. Cell. 163: 746-58. PMID 26496612 DOI: 10.1016/J.Cell.2015.09.056 |
0.733 |
|
2015 |
Ma P, Xue Y, Coquelle N, Haller JD, Yuwen T, Ayala I, Mikhailovskii O, Willbold D, Colletier JP, Skrynnikov NR, Schanda P. Observing the overall rocking motion of a protein in a crystal. Nature Communications. 6: 8361. PMID 26436197 DOI: 10.1038/Ncomms9361 |
0.302 |
|
2015 |
Xue Y, Kellogg D, Kimsey IJ, Sathyamoorthy B, Stein ZW, McBrairty M, Al-Hashimi HM. Characterizing RNA Excited States Using NMR Relaxation Dispersion. Methods in Enzymology. 558: 39-73. PMID 26068737 DOI: 10.1016/Bs.Mie.2015.02.002 |
0.752 |
|
2014 |
Xue Y, Yuwen T, Zhu F, Skrynnikov NR. Role of electrostatic interactions in binding of peptides and intrinsically disordered proteins to their folded targets. 1. NMR and MD characterization of the complex between the c-Crk N-SH3 domain and the peptide Sos. Biochemistry. 53: 6473-95. PMID 25207671 DOI: 10.1021/Bi500904F |
0.39 |
|
2014 |
del Amo JM, Agarwal V, Sarkar R, Porter J, Asami S, Rübbelke M, Fink U, Xue Y, Lange OF, Reif B. Site-specific analysis of heteronuclear Overhauser effects in microcrystalline proteins. Journal of Biomolecular Nmr. 59: 241-9. PMID 24989039 DOI: 10.1007/S10858-014-9843-1 |
0.316 |
|
2014 |
Xue Y, Skrynnikov NR. Ensemble MD simulations restrained via crystallographic data: accurate structure leads to accurate dynamics. Protein Science : a Publication of the Protein Society. 23: 488-507. PMID 24452989 DOI: 10.1002/Pro.2433 |
0.38 |
|
2012 |
Xue Y, Ward JM, Yuwen T, Podkorytov IS, Skrynnikov NR. Microsecond time-scale conformational exchange in proteins: using long molecular dynamics trajectory to simulate NMR relaxation dispersion data. Journal of the American Chemical Society. 134: 2555-62. PMID 22206299 DOI: 10.1021/Ja206442C |
0.423 |
|
2011 |
Xue Y, Skrynnikov NR. Motion of a disordered polypeptide chain as studied by paramagnetic relaxation enhancements, 15N relaxation, and molecular dynamics simulations: how fast is segmental diffusion in denatured ubiquitin? Journal of the American Chemical Society. 133: 14614-28. PMID 21819149 DOI: 10.1021/Ja201605C |
0.403 |
|
2010 |
Chevelkov V, Xue Y, Linser R, Skrynnikov NR, Reif B. Comparison of solid-state dipolar couplings and solution relaxation data provides insight into protein backbone dynamics. Journal of the American Chemical Society. 132: 5015-7. PMID 20297847 DOI: 10.1021/Ja100645K |
0.427 |
|
2010 |
Chevelkov V, Xue Y, Rao DK, Forman-Kay JD, Skrynnikov NR. 15N H/D-SOLEXSY experiment for accurate measurement of amide solvent exchange rates: application to denatured drkN SH3. Journal of Biomolecular Nmr. 46: 227-44. PMID 20195703 DOI: 10.1007/S10858-010-9398-8 |
0.388 |
|
2009 |
Mo H, Harwood J, Zhang S, Xue Y, Santini R, Raftery D. R: A quantitative measure of NMR signal receiving efficiency. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 200: 239-44. PMID 19647457 DOI: 10.1016/J.Jmr.2009.07.004 |
0.316 |
|
2009 |
Xu J, Xue Y, Skrynnikov NR. Detection of nanosecond time scale side-chain jumps in a protein dissolved in water/glycerol solvent. Journal of Biomolecular Nmr. 45: 57-72. PMID 19582374 DOI: 10.1007/S10858-009-9336-9 |
0.347 |
|
2009 |
Xue Y, Podkorytov IS, Rao DK, Benjamin N, Sun H, Skrynnikov NR. Paramagnetic relaxation enhancements in unfolded proteins: theory and application to drkN SH3 domain. Protein Science : a Publication of the Protein Society. 18: 1401-24. PMID 19544584 DOI: 10.1002/Pro.153 |
0.362 |
|
2008 |
Agarwal V, Xue Y, Reif B, Skrynnikov NR. Protein side-chain dynamics as observed by solution- and solid-state NMR spectroscopy: a similarity revealed. Journal of the American Chemical Society. 130: 16611-21. PMID 19049457 DOI: 10.1021/Ja804275P |
0.427 |
|
2007 |
Chevelkov V, Zhuravleva AV, Xue Y, Reif B, Skrynnikov NR. Combined analysis of (15)N relaxation data from solid- and solution-state NMR spectroscopy. Journal of the American Chemical Society. 129: 12594-5. PMID 17902660 DOI: 10.1021/Ja073234S |
0.415 |
|
2007 |
Xue Y, Pavlova MS, Ryabov YE, Reif B, Skrynnikov NR. Methyl rotation barriers in proteins from 2H relaxation data. Implications for protein structure. Journal of the American Chemical Society. 129: 6827-38. PMID 17488010 DOI: 10.1021/Ja0702061 |
0.368 |
|
2006 |
Reif B, Xue Y, Agarwal V, Pavlova MS, Hologne M, Diehl A, Ryabov YE, Skrynnikov NR. Protein side-chain dynamics observed by solution- and solid-state NMR: comparative analysis of methyl 2H relaxation data. Journal of the American Chemical Society. 128: 12354-5. PMID 16984151 DOI: 10.1021/Ja062808A |
0.425 |
|
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