| Year |
Citation |
Score |
| 2022 |
Gauto DF, Lebedenko OO, Becker LM, Ayala I, Lichtenecker R, Skrynnikov NR, Schanda P. Aromatic ring flips in differently packed ubiquitin protein crystals from MAS NMR and MD. Journal of Structural Biology: X. 7: 100079. PMID 36578472 DOI: 10.1016/j.yjsbx.2022.100079 |
0.301 |
|
| 2020 |
Izmailov SA, Rabdano SO, Hasanbasri Z, Podkorytov IS, Saxena S, Skrynnikov NR. Structural and dynamic origins of ESR lineshapes in spin-labeled GB1 domain: the insights from spin dynamics simulations based on long MD trajectories. Scientific Reports. 10: 957. PMID 31969574 DOI: 10.1038/S41598-019-56750-Y |
0.484 |
|
| 2019 |
Luzik DA, Rogacheva ON, Izmailov SA, Indeykina MI, Kononikhin AS, Skrynnikov NR. Molecular Dynamics model of peptide-protein conjugation: case study of covalent complex between Sos1 peptide and N-terminal SH3 domain from Grb2. Scientific Reports. 9: 20219. PMID 31882608 DOI: 10.1038/S41598-019-56078-7 |
0.364 |
|
| 2018 |
Kämpf K, Izmailov SA, Rabdano SO, Groves AT, Podkorytov IS, Skrynnikov NR. What Drives N Spin Relaxation in Disordered Proteins? Combined NMR/MD Study of the H4 Histone Tail. Biophysical Journal. 115: 2348-2367. PMID 30527335 DOI: 10.1016/J.Bpj.2018.11.017 |
0.445 |
|
| 2018 |
Skrynnikov NR, Izmailov SA, Slipchenko LV, Rogacheva ON. Analysis of crystallographic structures and DFT calculations reveal a new structural arrangement in proteins involving lysine NH3
+ group and carbonyl Acta Crystallographica Section a Foundations and Advances. 74: a175-a175. DOI: 10.1107/S0108767318098240 |
0.344 |
|
| 2017 |
Rogacheva ON, Izmailov SA, Slipchenko LV, Skrynnikov NR. A new structural arrangement in proteins involving lysine NH3+ group and carbonyl. Scientific Reports. 7: 16402. PMID 29180642 DOI: 10.1038/S41598-017-16584-Y |
0.33 |
|
| 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 |
0.301 |
|
| 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 |
0.425 |
|
| 2016 |
Izmailov SA, Podkorytov IS, Skrynnikov NR. MD Modeling of Oxidative Folding in Peptides and Proteins Biophysical Journal. 110: 644a-645a. DOI: 10.1016/J.Bpj.2015.11.3449 |
0.335 |
|
| 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 |
0.33 |
|
| 2015 |
Skrynnikov NR, Tycko R. Interview with Robert Tycko: On amyloids, Alzheimer disease, and solid-state NMR Concepts in Magnetic Resonance Part a: Bridging Education and Research. 44: 182-189. DOI: 10.1002/Cmr.A.21353 |
0.324 |
|
| 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 |
0.416 |
|
| 2014 |
Yuwen T, Skrynnikov NR. CP-HISQC: a better version of HSQC experiment for intrinsically disordered proteins under physiological conditions. Journal of Biomolecular Nmr. 58: 175-92. PMID 24496557 DOI: 10.1007/S10858-014-9815-5 |
0.455 |
|
| 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 |
0.41 |
|
| 2014 |
Yuwen T, Skrynnikov NR. Proton-decoupled CPMG: a better experiment for measuring (15)N R2 relaxation in disordered proteins. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 241: 155-69. PMID 24120537 DOI: 10.1016/J.Jmr.2013.08.008 |
0.446 |
|
| 2012 |
Ward JM, Skrynnikov NR. Very large residual dipolar couplings from deuterated ubiquitin. Journal of Biomolecular Nmr. 54: 53-67. PMID 22828737 DOI: 10.1007/S10858-012-9651-4 |
0.411 |
|
| 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 |
0.432 |
|
| 2011 |
Yuwen T, Post CB, Skrynnikov NR. Domain cooperativity in multidomain proteins: what can we learn from molecular alignment in anisotropic media? Journal of Biomolecular Nmr. 51: 131-50. PMID 21947922 DOI: 10.1007/S10858-011-9548-7 |
0.39 |
|
| 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 |
0.434 |
|
| 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 |
0.472 |
|
| 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 |
0.457 |
|
| 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 |
0.428 |
|
| 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 |
0.504 |
|
| 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 |
0.499 |
|
| 2007 |
Skrynnikov NR. Asymmetric doublets in MAS NMR: coherent and incoherent mechanisms. Magnetic Resonance in Chemistry : Mrc. 45: S161-73. PMID 18157846 DOI: 10.1002/Mrc.2162 |
0.462 |
|
| 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 |
0.443 |
|
| 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 |
0.41 |
|
| 2007 |
Podkorytov IS, Skrynnikov NR. Transient NOE-exchange-relay experiment: application to ligand-protein binding under slow exchange conditions. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 187: 44-51. PMID 17449307 DOI: 10.1016/J.Jmr.2007.02.016 |
0.395 |
|
| 2007 |
Eichmüller C, Skrynnikov NR. Observation of microsecond time-scale protein dynamics in the presence of Ln3+ ions: application to the N-terminal domain of cardiac troponin C. Journal of Biomolecular Nmr. 37: 79-95. PMID 17180551 DOI: 10.1007/S10858-006-9105-Y |
0.418 |
|
| 2006 |
Agarwal V, Diehl A, Skrynnikov N, Reif B. High resolution 1H detected 1H,13C correlation spectra in MAS solid-state NMR using deuterated proteins with selective1H,2H isotopic labeling of methyl groups Journal of the American Chemical Society. 128: 12620-12621. PMID 17002335 DOI: 10.1021/Ja064379M |
0.382 |
|
| 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 |
0.465 |
|
| 2006 |
Kanelis V, Bruce MC, Skrynnikov NR, Rotin D, Forman-Kay JD. Structural determinants for high-affinity binding in a Nedd4 WW3* domain-Comm PY motif complex. Structure (London, England : 1993). 14: 543-53. PMID 16531238 DOI: 10.1016/J.Str.2005.11.018 |
0.364 |
|
| 2005 |
Simon K, Xu J, Kim C, Skrynnikov NR. Estimating the accuracy of protein structures using residual dipolar couplings. Journal of Biomolecular Nmr. 33: 83-93. PMID 16258827 DOI: 10.1007/S10858-005-2601-7 |
0.426 |
|
| 2005 |
Ollerenshaw JE, Tugarinov V, Skrynnikov NR, Kay LE. Comparison of 13CH3, 13CH2D, and 13CHD2 methyl labeling strategies in proteins. Journal of Biomolecular Nmr. 33: 25-41. PMID 16222555 DOI: 10.1007/S10858-005-2614-2 |
0.493 |
|
| 2005 |
Eichmüller C, Skrynnikov NR. A new amide proton R1rho experiment permits accurate characterization of microsecond time-scale conformational exchange. Journal of Biomolecular Nmr. 32: 281-93. PMID 16211482 DOI: 10.1007/S10858-005-0658-Y |
0.439 |
|
| 2005 |
Xu J, Millet O, Kay LE, Skrynnikov NR. A new spin probe of protein dynamics: nitrogen relaxation in 15N-2H amide groups. Journal of the American Chemical Society. 127: 3220-9. PMID 15740163 DOI: 10.1021/Ja040215Z |
0.552 |
|
| 2004 |
Podkorytov IS, Skrynnikov NR. Microsecond time-scale dynamics from relaxation in the rotating frame: experiments using spin lock with alternating phase. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 169: 164-73. PMID 15183365 DOI: 10.1016/J.Jmr.2004.04.011 |
0.395 |
|
| 2004 |
Skrynnikov NR. Orienting molecular fragments and molecules with residual dipolar couplings Comptes Rendus Physique. 5: 359-375. DOI: 10.1016/J.Crhy.2004.02.006 |
0.447 |
|
| 2002 |
Mal TK, Skrynnikov NR, Yap KL, Kay LE, Ikura M. Detecting protein kinase recognition modes of calmodulin by residual dipolar couplings in solution NMR. Biochemistry. 41: 12899-906. PMID 12390014 DOI: 10.1021/Bi0264162 |
0.488 |
|
| 2002 |
Skrynnikov NR, Dahlquist FW, Kay LE. Reconstructing NMR spectra of "invisible" excited protein states using HSQC and HMQC experiments. Journal of the American Chemical Society. 124: 12352-60. PMID 12371879 DOI: 10.1021/Ja0207089 |
0.563 |
|
| 2002 |
Korzhnev DM, Skrynnikov NR, Millet O, Torchia DA, Kay LE. An NMR experiment for the accurate measurement of heteronuclear spin-lock relaxation rates. Journal of the American Chemical Society. 124: 10743-53. PMID 12207529 DOI: 10.1021/Ja0204776 |
0.588 |
|
| 2002 |
Skrynnikov NR, Millet O, Kay LE. Deuterium spin probes of side-chain dynamics in proteins. 2. Spectral density mapping and identification of nanosecond time-scale side-chain motions. Journal of the American Chemical Society. 124: 6449-60. PMID 12033876 DOI: 10.1021/Ja012498Q |
0.562 |
|
| 2002 |
Millet O, Muhandiram DR, Skrynnikov NR, Kay LE. Deuterium spin probes of side-chain dynamics in proteins. 1. Measurement of five relaxation rates per deuteron in (13)C-labeled and fractionally (2)H-enriched proteins in solution. Journal of the American Chemical Society. 124: 6439-48. PMID 12033875 DOI: 10.1021/Ja012497Y |
0.616 |
|
| 2002 |
Boyd J, Skrynnikov NR. Calculations of the contribution of ring currents to the chemical shielding anisotropy. Journal of the American Chemical Society. 124: 1832-3. PMID 11866578 DOI: 10.1021/Ja016476F |
0.312 |
|
| 2001 |
Tollinger M, Skrynnikov NR, Mulder FA, Forman-Kay JD, Kay LE. Slow dynamics in folded and unfolded states of an SH3 domain. Journal of the American Chemical Society. 123: 11341-52. PMID 11707108 DOI: 10.1021/Ja011300Z |
0.737 |
|
| 2001 |
Donaldson LW, Skrynnikov NR, Choy WY, Muhandiram DR, Sarkar B, Forman-Kay JD, Kay LE. Structural characterization of proteins with an attached ATCUN motif by paramagnetic relaxation enhancement NMR spectroscopy. Journal of the American Chemical Society. 123: 9843-7. PMID 11583547 DOI: 10.1021/Ja011241P |
0.57 |
|
| 2001 |
Skrynnikov NR, Mulder FA, Hon B, Dahlquist FW, Kay LE. Probing slow time scale dynamics at methyl-containing side chains in proteins by relaxation dispersion NMR measurements: application to methionine residues in a cavity mutant of T4 lysozyme. Journal of the American Chemical Society. 123: 4556-66. PMID 11457242 DOI: 10.1021/Ja004179P |
0.739 |
|
| 2001 |
Mulder FA, Skrynnikov NR, Hon B, Dahlquist FW, Kay LE. Measurement of slow (micros-ms) time scale dynamics in protein side chains by (15)N relaxation dispersion NMR spectroscopy: application to Asn and Gln residues in a cavity mutant of T4 lysozyme. Journal of the American Chemical Society. 123: 967-75. PMID 11456632 DOI: 10.1021/Ja003447G |
0.748 |
|
| 2001 |
Hwang PM, Skrynnikov NR, Kay LE. Domain orientation in beta-cyclodextrin-loaded maltose binding protein: diffusion anisotropy measurements confirm the results of a dipolar coupling study. Journal of Biomolecular Nmr. 20: 83-8. PMID 11430759 DOI: 10.1023/A:1011226512421 |
0.579 |
|
| 2001 |
Evenäs J, Tugarinov V, Skrynnikov NR, Goto NK, Muhandiram R, Kay LE. Ligand-induced structural changes to maltodextrin-binding protein as studied by solution NMR spectroscopy. Journal of Molecular Biology. 309: 961-74. PMID 11399072 DOI: 10.1006/Jmbi.2001.4695 |
0.745 |
|
| 2001 |
Goto NK, Skrynnikov NR, Dahlquist FW, Kay LE. What is the average conformation of bacteriophage T4 lysozyme in solution? A domain orientation study using dipolar couplings measured by solution NMR. Journal of Molecular Biology. 308: 745-64. PMID 11350172 DOI: 10.1006/Jmbi.2001.4614 |
0.732 |
|
| 2001 |
Evenas J, Tugarinov V, Skrynnikov N, Goto N, Muhandiram R, Kay L. Backbone 1H,13C and 15N chemical shift assignment for the maltotriose-bound state of 2H,13C,15N-labeled maltodextrin-binding protein Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr4987 |
0.522 |
|
| 2000 |
Skrynnikov NR, Kay LE. Assessment of molecular structure using frame-independent orientational restraints derived from residual dipolar couplings. Journal of Biomolecular Nmr. 18: 239-52. PMID 11142514 DOI: 10.1023/A:1026501101716 |
0.554 |
|
| 2000 |
Mueller GA, Choy WY, Skrynnikov NR, Kay LE. A method for incorporating dipolar couplings into structure calculations in cases of (near) axial symmetry of alignment. Journal of Biomolecular Nmr. 18: 183-8. PMID 11142508 DOI: 10.1023/A:1026788430236 |
0.596 |
|
| 2000 |
Skrynnikov NR, Goto NK, Yang D, Choy WY, Tolman JR, Mueller GA, Kay LE. Orienting domains in proteins using dipolar couplings measured by liquid-state NMR: differences in solution and crystal forms of maltodextrin binding protein loaded with beta-cyclodextrin. Journal of Molecular Biology. 295: 1265-73. PMID 10653702 DOI: 10.1006/Jmbi.1999.3430 |
0.759 |
|
| 2000 |
Separovic F, Skrynnikov NR, Sanctuary BC. Selective on-resonance N.M.R. irradiation of a dipolar doublet Australian Journal of Chemistry. 53: 355-361. DOI: 10.1071/Ch00044 |
0.618 |
|
| 2000 |
Skrynnikov NR, Konrat R, Muhandiram DR, Kay LE. Relative orientation of peptide planes in proteins is reflected in carbonyl - Carbonyl chemical shift anisotropy cross-correlated spin relaxation Journal of the American Chemical Society. 122: 7059-7071. DOI: 10.1021/Ja0000201 |
0.596 |
|
| 1999 |
Skrynnikov NR, Ernst RR. Detection of intermolecular chemical exchange through decorrelation of two-spin order. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 137: 276-80. PMID 10053160 DOI: 10.1006/Jmre.1998.1666 |
0.546 |
|
| 1999 |
Scheurer C, Skrynnikov NR, Lienin SF, Straus SK, Brüschweiler R, Ernst RR. Effects of dynamics and environment on 15N chemical shielding anisotropy in proteins. A combination of density functional theory, molecular dynamics simulation, and NMR relaxation Journal of the American Chemical Society. 121: 4242-4251. DOI: 10.1021/Ja984159B |
0.584 |
|
| 1998 |
Brutscher B, Skrynnikov NR, Bremi T, BrYschweiler R, Ernst RR. Quantitative investigation of dipole-CSA cross-correlated relaxation by ZQ/DQ spectroscopy. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 130: 346-51. PMID 9500898 DOI: 10.1006/Jmre.1997.1312 |
0.546 |
|
| 1998 |
Skrynnikov NR, Lienin SF, Brüschweiler R, Ernst RR. Efficient scalar spin relaxation in the rotating frame for matched radio-frequency fields Journal of Chemical Physics. 108: 7662-7669. DOI: 10.1063/1.476202 |
0.558 |
|
| 1997 |
Skrynnikov NR, Khazanovich TN, Sanctuary BC. Intermolecular relaxation involving coupled spin systems: A simplified approach to solvent induced relaxation Molecular Physics. 91: 977-992. DOI: 10.1080/002689797170743 |
0.645 |
|
| 1997 |
Skrynnikov NR, Brüschweiler R. Comment on “Nuclear spin relaxation and non-ergodic quasi-equilibria” Chemical Physics Letters. 281: 239-242. DOI: 10.1016/S0009-2614(97)01064-6 |
0.385 |
|
| 1995 |
Khazanovich TN, Skrynnikov NR. External random field model for intermolecular spin interactions: Accuracy evaluation for the coupled relaxation of two-spin molecules in a pulse responsive solvent Journal of the Physical Society of Japan. 64: 636-642. DOI: 10.1143/Jpsj.64.631 |
0.425 |
|
| 1994 |
Skrynnikov NR, Zhou J, Sanctuary BC. Classification of cyclic initial states and geometric phase for the spin-j system Journal of Physics a: General Physics. 27: 6253-6265. DOI: 10.1088/0305-4470/27/18/033 |
0.627 |
|
| 1994 |
Skrynnikov NR, Sanctuary BC. Geometric phase in NMR interferometry experiment Molecular Physics. 83: 1133-1144. DOI: 10.1080/00268979400101831 |
0.605 |
|
| Low-probability matches (unlikely to be authored by this person) |
| 2007 |
Xue Y, Pavlova M, Ryabov Y, Reif B, Skrynnikov N. Side-chain relaxation in SH3 domain from alpha-spectrin measured at multiple temperatures Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr15144 |
0.299 |
|
| 2023 |
Lebedenko OO, Salikov VA, Izmailov SA, Podkorytov IS, Skrynnikov NR. Using NMR diffusion data to validate MD models of disordered proteins: Test case of N-terminal tail of histone H4. Biophysical Journal. 123: 80-100. PMID 37990496 DOI: 10.1016/j.bpj.2023.11.020 |
0.276 |
|
| 2018 |
Case DA, Skrynnikov NR. Interview with David A. Case: On force fields, biomolecular modeling, and NMR Concepts in Magnetic Resonance Part A. DOI: 10.1002/Cmr.A.21403 |
0.256 |
|
| 1996 |
Skrynnikov NR. Comment on "Intermolecular translational-rotational contribution to nuclear-spin relaxation in liquids" Physical Review. A. 53: 4611-4612. PMID 9913443 |
0.254 |
|
| 2023 |
Liu N, Mikhailovskii O, Skrynnikov NR, Xue Y. Simulating diffraction photographs based on molecular dynamics trajectories of a protein crystal: a new option to examine structure-solving strategies in protein crystallography. Iucrj. 10: 16-26. PMID 36598499 DOI: 10.1107/S2052252522011198 |
0.249 |
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| 2022 |
Mikhailovskii O, Xue Y, Skrynnikov NR. Modeling a unit cell: crystallographic refinement procedure using the biomolecular MD simulation platform . Iucrj. 9: 114-133. PMID 35059216 DOI: 10.1107/S2052252521011891 |
0.246 |
|
| 2019 |
Mikhailovskii O, Xue Y, Skrynnikov N. MD-assisted refinement of X-ray coordinates Acta Crystallographica Section a Foundations and Advances. 75: a455-a455. DOI: 10.1107/S0108767319095576 |
0.239 |
|
| 2021 |
Sheedlo MJ, Kenny S, Podkorytov IS, Brown K, Ma J, Iyer S, Hewitt CS, Arbough T, Mikhailovskii O, Flaherty DP, Wilson MA, Skrynnikov NR, Das C. Insights into Ubiquitin Product Release in Hydrolysis Catalyzed by the Bacterial Deubiquitinase SdeA. Biochemistry. PMID 33583181 DOI: 10.1021/acs.biochem.0c00760 |
0.238 |
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| 2023 |
Mikhailovskii O, Izmailov SA, Xue Y, Case DA, Skrynnikov NR. X-ray Crystallography Module in MD Simulation Program Amber 2023. Refining the Models of Protein Crystals. Journal of Chemical Information and Modeling. 64: 18-25. PMID 38147516 DOI: 10.1021/acs.jcim.3c01531 |
0.237 |
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| 2017 |
Izmailov SA, Podkorytov IS, Skrynnikov NR. Simple MD-based model for oxidative folding of peptides and proteins. Scientific Reports. 7: 9293. PMID 28839177 DOI: 10.1038/s41598-017-09229-7 |
0.23 |
|
| 2023 |
Sun W, Lebedenko OO, Salguero NG, Shannon MD, Zandian M, Poirier MG, Skrynnikov NR, Jaroniec CP. Conformational and Interaction Landscape of Histone H4 Tails in Nucleosomes Probed by Paramagnetic NMR Spectroscopy. Journal of the American Chemical Society. PMID 37943892 DOI: 10.1021/jacs.3c10340 |
0.224 |
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| 2022 |
Podkorytov IS, Skrynnikov NR. Effect of rotation in NMR diffusion experiments on micron-sized particles: A generalized theoretical treatment. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 344: 107303. PMID 36242795 DOI: 10.1016/j.jmr.2022.107303 |
0.222 |
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| 2007 |
Ryabov Y, White C, Xue Y, Skrynnikov NR. Introducing color into stacking gels makes sample loading easy. Analytical Biochemistry. 366: 111-2. PMID 17490595 DOI: 10.1016/J.Ab.2007.04.002 |
0.213 |
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| 2021 |
Rabdano S, Shannon MD, Izmailov SA, Gonzalez Salguero N, Zandian M, Purusottam RN, Poirier MG, Skrynnikov NR, Jaroniec CP. Histone H4 tails in nucleosomes: a fuzzy interaction with DNA. Angewandte Chemie (International Ed. in English). PMID 33522067 DOI: 10.1002/anie.202012046 |
0.209 |
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| 2017 |
Rabdano SO, Izmailov SA, Luzik DA, Groves A, Podkorytov IS, Skrynnikov NR. Onset of disorder and protein aggregation due to oxidation-induced intermolecular disulfide bonds: case study of RRM2 domain from TDP-43. Scientific Reports. 7: 11161. PMID 28894122 DOI: 10.1038/s41598-017-10574-w |
0.206 |
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| 2021 |
Kharkov BB, Podkorytov IS, Bondarev SA, Belousov MV, Salikov VA, Zhouravleva GA, Skrynnikov NR. Role of rotational motion in diffusion NMR experiments on supramolecular assemblies: application to Sup35NM fibrils. Angewandte Chemie (International Ed. in English). PMID 33891789 DOI: 10.1002/anie.202102408 |
0.191 |
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| 2016 |
Rabdano SO, Podkorytov IS, Izmailov SA, Pivovarova YV, Yakimov AP, Yuwen T, Groves A, Skrynnikov NR. Loss of Protein Stability due to Formation of Intermolecular Disulfide Bonds under the Effect of Oxidative Stress: Case Study of the RRM2 Domain from Neuropathological Protein TDP-43 Biophysical Journal. 110: 210a. DOI: 10.1016/j.bpj.2015.11.1167 |
0.171 |
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| 2021 |
Skrynnikov NR. Toward a proper interpretation of hydrogen exchange data in disordered proteins. Biophysical Journal. PMID 34416173 DOI: 10.1016/j.bpj.2021.08.004 |
0.132 |
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| 2017 |
Tyuryaeva II, Lyublinskaya OG, Podkorytov IS, Skrynnikov NR. Origin of anti-tumor activity of the cysteine-containing GO peptides and further optimization of their cytotoxic properties. Scientific Reports. 7: 40217. PMID 28091523 DOI: 10.1038/srep40217 |
0.103 |
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| Hide low-probability matches. |
