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Volumn 58, Issue 2, 2014, Pages 129-139

Time-resolved multidimensional NMR with non-uniform sampling

Author keywords

BEST TROSY; CD79; IDP; ITAM; MDD; NUS; PARAFAC; Post translational modification; Real time

Indexed keywords

CD79B ANTIGEN; TYROSINE;

EID: 84896723382     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-013-9811-1     Document Type: Article
Times cited : (80)

References (64)
  • 1
    • 84884700421 scopus 로고    scopus 로고
    • Multi-phosphorylation of the Intrinsically disordered unique domain of c-Src studied by in-cell and real-time NMR spectroscopy
    • doi:10.1002/cbic.201300139
    • Amata I, Maffei M, Igea A, Gay M, Vilaseca M, Nebreda AR, Pons M (2013) Multi-phosphorylation of the Intrinsically disordered unique domain of c-Src studied by in-cell and real-time NMR spectroscopy. ChemBioChem 14(14):1820-1827. doi:10.1002/cbic.201300139
    • (2013) ChemBioChem , vol.14 , Issue.14 , pp. 1820-1827
    • Amata, I.1    Maffei, M.2    Igea, A.3    Gay, M.4    Vilaseca, M.5    Nebreda, A.R.6    Pons, M.7
  • 4
    • 70350348011 scopus 로고    scopus 로고
    • NMR spectroscopy brings invisible protein states into focus
    • doi:10.1038/nchembio.238
    • Baldwin AJ, Kay LE (2009) NMR spectroscopy brings invisible protein states into focus. Nat Chem Biol 5(11):808-814. doi:10.1038/nchembio.238
    • (2009) Nat Chem Biol , vol.5 , Issue.11 , pp. 808-814
    • Baldwin, A.J.1    Kay, L.E.2
  • 5
    • 0033377656 scopus 로고    scopus 로고
    • Random-coil chemical shifts of phosphorylated amino acids
    • DOI 10.1023/A:1008375029746
    • Bienkiewicz EA, Lumb KJ (1999) Random-coil chemical shifts of phosphorylated amino acids. J Biomol NMR 15(3):203-206. doi:10.1023/A: 1008375029746 (Pubitemid 30016118)
    • (1999) Journal of Biomolecular NMR , vol.15 , Issue.3 , pp. 203-206
    • Bienkiewicz, E.A.1    Lumb, K.J.2
  • 7
    • 1442355435 scopus 로고    scopus 로고
    • Quantitation of rapid proton-deuteron amide exchange using hadamard spectroscopy
    • doi:10.1023/B:JNMR.0000015406.66725.30
    • Bougault C, Feng L, Glushka J (2004) Quantitation of rapid proton-deuteron amide exchange using hadamard spectroscopy. J Biomol NMR 28(4):6. doi:10.1023/B:JNMR.0000015406.66725.30
    • (2004) J Biomol NMR , vol.28 , Issue.4 , pp. 6
    • Bougault, C.1    Feng, L.2    Glushka, J.3
  • 8
    • 84869414047 scopus 로고    scopus 로고
    • Rapid protein global fold determination using ultrasparse sampling, high-dynamic range artifact suppression, and time-shared NOESY
    • doi:10.1021/ja307445y
    • Coggins BE, Werner-Allen JW, Yan A, Zhou P (2012) Rapid protein global fold determination using ultrasparse sampling, high-dynamic range artifact suppression, and time-shared NOESY. J Am Chem Soc 134(45):18619-18630. doi:10.1021/ja307445y
    • (2012) J Am Chem Soc , vol.134 , Issue.45 , pp. 18619-18630
    • Coggins, B.E.1    Werner-Allen, J.W.2    Yan, A.3    Zhou, P.4
  • 10
    • 0037137617 scopus 로고    scopus 로고
    • Automated analysis of large sets of heteronuclear correlation spectra in NMR-based drug discovery
    • DOI 10.1021/jm020866a
    • Damberg CS, Orekhov VY, Billeter M (2002) Automated analysis of large sets of heteronuclear correlation spectra in NMR-based drug discovery. J Med Chem 45(26):5649-5654. doi:10.1021/jm020866a (Pubitemid 35453757)
    • (2002) Journal of Medicinal Chemistry , vol.45 , Issue.26 , pp. 5649-5654
    • Damberg, C.S.1    Orekhov, V.Y.2    Billeter, M.3
  • 11
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • doi:10.1007/BF00197809
    • Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6(3):277-293. doi:10.1007/BF00197809
    • (1995) J Biomol NMR , vol.6 , Issue.3 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 12
    • 0035928606 scopus 로고    scopus 로고
    • Hydrogen exchange in peptides and proteins using NMR spectroscopy
    • doi:10.1016/S0079-6565(01)00032-2
    • Dempsey EC (2001) Hydrogen exchange in peptides and proteins using NMR spectroscopy. Progr Nucl NMR Spectrosc 39:135-170. doi:10.1016/S0079-6565(01) 00032-2
    • (2001) Progr Nucl NMR Spectrosc , vol.39 , pp. 135-170
    • Dempsey, E.C.1
  • 13
    • 4344707281 scopus 로고    scopus 로고
    • Unfolded proteins and protein folding studied by NMR
    • doi:10.1021/cr030403s
    • Dyson HJ, Wright PE (2004) Unfolded proteins and protein folding studied by NMR. Chem Rev 104(8):3607-3622. doi:10.1021/cr030403s
    • (2004) Chem Rev , vol.104 , Issue.8 , pp. 3607-3622
    • Dyson, H.J.1    Wright, P.E.2
  • 14
    • 79951549811 scopus 로고    scopus 로고
    • Recovering lost magnetization: Polarization enhancement in biomolecular NMR
    • doi:10.1007/s10858-010-9461-5
    • Favier A, Brutscher B (2011) Recovering lost magnetization: polarization enhancement in biomolecular NMR. J Biomol NMR 49(1):9-15. doi:10.1007/s10858- 010-9461-5
    • (2011) J Biomol NMR , vol.49 , Issue.1 , pp. 9-15
    • Favier, A.1    Brutscher, B.2
  • 15
    • 0027489831 scopus 로고
    • NMR and protein folding: Equilibrium and stopped-flow studies
    • Frieden C, Hoeltzli SD, Ropson IJ (1993) NMR and protein folding: equilibrium and stopped-flow studies. Protein Sci 2(12):2007-2014. doi:10.1002/pro.5560021202 (Pubitemid 23354705)
    • (1993) Protein Science , vol.2 , Issue.12 , pp. 2007-2014
    • Frieden, C.1    Hoeltzli, S.D.2    Ropson, I.J.3
  • 17
    • 31444443367 scopus 로고    scopus 로고
    • Real-time monitoring of chemical transformations by ultrafast 2D NMR spectroscopy
    • DOI 10.1021/ja0564158
    • Gal M, Frydman L (2006) Real-time monitoring of chemical transformations by ultrafast 2D NMR spectroscopy. J Am Chem Soc 128(3):951-956. doi:10.1021/ja0564158 (Pubitemid 43153044)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.3 , pp. 951-956
    • Gal, M.1    Mishkovsky, M.2    Frydman, L.3
  • 18
    • 33846785314 scopus 로고    scopus 로고
    • UltraSOFAST HMQC NMR and the repetitive acquisition of 2D protein spectra at Hz rates
    • DOI 10.1021/ja066915g
    • Gal M, Schanda P, Brutscher B, Frydman L (2007) UltraSOFAST HMQC NMR and the repetitive acquisition of 2D protein spectra at Hz rates. J Am Chem Soc 129(5):1372-1377. doi:10.1021/ja066915g (Pubitemid 46208609)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.5 , pp. 1372-1377
    • Gal, M.1    Schanda, P.2    Brutscher, B.3    Frydman, L.4
  • 19
    • 57549118920 scopus 로고    scopus 로고
    • An improved ultrafast 2D NMR experiment: Towards atom-resolved real-time studies of protein kinetics at multi-Hz rates
    • doi:10.1007/s10858-008-9284-9
    • Gal M, Kern T, Schanda P, Frydman L, Brutscher B (2009) An improved ultrafast 2D NMR experiment: towards atom-resolved real-time studies of protein kinetics at multi-Hz rates. J Biomol NMR 43(1):1-10. doi:10.1007/s10858-008- 9284-9
    • (2009) J Biomol NMR , vol.43 , Issue.1 , pp. 1-10
    • Gal, M.1    Kern, T.2    Schanda, P.3    Frydman, L.4    Brutscher, B.5
  • 20
    • 1242332383 scopus 로고    scopus 로고
    • Accurate relaxation parameters for large proteins
    • doi:10.1016/j.jmr.2003.12.002
    • Gutmanas A, Luan T, Orekhov VY, Billeter M (2004) Accurate relaxation parameters for large proteins. J Magn Reson 167(1):107-113. doi:10.1016/j.jmr. 2003.12.002
    • (2004) J Magn Reson , vol.167 , Issue.1 , pp. 107-113
    • Gutmanas, A.1    Luan, T.2    Orekhov, V.Y.3    Billeter, M.4
  • 22
    • 70349145444 scopus 로고    scopus 로고
    • Coupled decomposition of four-dimensional NOESY Spectra
    • doi:10.1021/ja902012x
    • Hiller S, Ibraghimov I, Wagner G, Orekhov VY (2009) Coupled decomposition of four-dimensional NOESY Spectra. J Am Chem Soc 131(36):12970-12978. doi:10.1021/ja902012x
    • (2009) J Am Chem Soc , vol.131 , Issue.36 , pp. 12970-12978
    • Hiller, S.1    Ibraghimov, I.2    Wagner, G.3    Orekhov, V.Y.4
  • 23
    • 0034917883 scopus 로고    scopus 로고
    • Maximum entropy reconstruction, spectrum analysis and deconvolution in multidimensional nuclear magnetic resonance
    • DOI 10.1016/S0076-6879(02)38219-3
    • Hoch JC, Stern AS (2001) Maximum entropy reconstruction, spectrum analysis and deconvolution in multidimensional nuclear magnetic resonance. Method Enzymol 338:159-178 (Pubitemid 32666578)
    • (2001) Methods in Enzymology , vol.338 , pp. 159-178
    • Hoch, J.C.1    Stern, A.S.2
  • 24
    • 79959974154 scopus 로고    scopus 로고
    • Fast multidimensional NMR spectroscopy using compressed sensing
    • doi:10.1002/anie.201100440
    • Holland DJ, Bostock MJ, Gladden LF, Nietlispach D (2011) Fast multidimensional NMR spectroscopy using compressed sensing. Angew Chem Int Ed 50(29):6548-6551. doi:10.1002/anie.201100440
    • (2011) Angew Chem Int Ed , vol.50 , Issue.29 , pp. 6548-6551
    • Holland, D.J.1    Bostock, M.J.2    Gladden, L.F.3    Nietlispach, D.4
  • 26
    • 84877147584 scopus 로고    scopus 로고
    • Highly efficient NMR assignment of intrinsically disordered proteins: Application to B- and T cell receptor domains
    • doi:10.1371/journal.pone.0062947
    • Isaksson L, Mayzel M, Saline M, Pedersen A, Rosenlöw J, Brutscher B, Karlsson BG, Orekhov VY (2013) Highly efficient NMR assignment of intrinsically disordered proteins: application to B- and T cell receptor domains. PLoS One 8(5):e62947. doi:10.1371/journal.pone.0062947
    • (2013) PLoS One , vol.8 , Issue.5
    • Isaksson, L.1    Mayzel, M.2    Saline, M.3    Pedersen, A.4    Rosenlöw, J.5    Brutscher, B.6    Karlsson, B.G.7    Orekhov, V.Y.8
  • 27
    • 33746403404 scopus 로고    scopus 로고
    • Removal of a time barrier for high-resolution multidimensional NMR spectroscopy
    • DOI 10.1038/nmeth900, PII NMETH900
    • Jaravine V, Ibraghimov I, Orekhov VY (2006) Removal of time barrier for high-resolution multidimensional NMR spectroscopy. Nat Method 3(8):605-607. doi:10.1038/nmeth900 (Pubitemid 44123426)
    • (2006) Nature Methods , vol.3 , Issue.8 , pp. 605-607
    • Jaravine, V.1    Ibraghimov, I.2    Orekhov, V.Y.3
  • 29
    • 0028793187 scopus 로고
    • Phosphorylated immunoreceptor signaling motifs (ITAMs) exhibit unique abilities to bind and activate lyn and syk tyrosine kinases
    • Johnson SA, Pleiman CM, Pao L, Schneringer J, Hippen K, Cambier JC (1995) Phosphorylated immunoreceptor signaling motifs (ITAMs) exhibit unique abilities to bind and activate lyn and syk tyrosine kinases. J Immunol 155(10):4596-4603
    • (1995) J Immunol , vol.155 , Issue.10 , pp. 4596-4603
    • Johnson, S.A.1    Pleiman, C.M.2    Pao, L.3    Schneringer, J.4    Hippen, K.5    Cambier, J.C.6
  • 30
    • 79958040716 scopus 로고    scopus 로고
    • Accelerated NMR spectroscopy by using compressed sensing
    • doi:10.1002/anie.201100370
    • Kazimierczuk K, Orekhov VY (2011) Accelerated NMR spectroscopy by using compressed sensing. Angew Chem Int Ed 50(24):5556-5559. doi:10.1002/anie. 201100370
    • (2011) Angew Chem Int Ed , vol.50 , Issue.24 , pp. 5556-5559
    • Kazimierczuk, K.1    Orekhov, V.Y.2
  • 31
    • 84865646289 scopus 로고    scopus 로고
    • A comparison of convex and non-convex compressed sensing applied to multidimensional NMR
    • doi:10.1016/j.jmr.2012.08.001
    • Kazimierczuk K, Orekhov VY (2012) A comparison of convex and non-convex compressed sensing applied to multidimensional NMR. J Magn Reson 223:1-10. doi:10.1016/j.jmr.2012.08.001
    • (2012) J Magn Reson , vol.223 , pp. 1-10
    • Kazimierczuk, K.1    Orekhov, V.Y.2
  • 32
    • 84884232013 scopus 로고    scopus 로고
    • High-dimensional NMR Spectra for structural studies of biomolecules
    • doi:10.1002/cphc.201300277
    • Kazimierczuk K, Stanek J, Zawadzka-Kazimierczuk A, Koźmin̈ski W (2013) High-dimensional NMR Spectra for structural studies of biomolecules. ChemPhysChem 14(13):3015-3025. doi:10.1002/cphc.201300277
    • (2013) ChemPhysChem , vol.14 , Issue.13 , pp. 3015-3025
    • Kazimierczuk, K.1    Stanek, J.2    Zawadzka-Kazimierczuk, A.3    Koźmin̈ski, W.4
  • 33
    • 0035211558 scopus 로고    scopus 로고
    • MUNIN: Application of three-way decomposition to the analysis of heteronuclear NMR relaxation data
    • DOI 10.1023/A:1012982830367
    • Korzhnev DM, Ibraghimov IV, Billeter M, Orekhov VY (2001) MUNIN: application of three-way decomposition to the analysis of heteronuclear NMR relaxation data. J Biomol NMR 21(3):263-268. doi:10.1023/A:1012982830367 (Pubitemid 33133426)
    • (2001) Journal of Biomolecular NMR , vol.21 , Issue.3 , pp. 263-268
    • Korzhnev, D.M.1    Ibraghimov, I.V.2    Billeter, M.3    Orekhov, V.Y.4
  • 34
    • 0041859673 scopus 로고    scopus 로고
    • Hadamard NMR spectroscopy
    • doi:10.1016/S0079-6565(03)00022-0
    • Kupce E, Nishida T, Freeman R (2003) Hadamard NMR spectroscopy. Prog Nucl Magn Reson Spectrosc 42(3-4):95-122. doi:10.1016/S0079-6565(03)00022-0
    • (2003) Prog Nucl Magn Reson Spectrosc , vol.42 , Issue.3-4 , pp. 95-122
    • Kupce, E.1    Nishida, T.2    Freeman, R.3
  • 36
    • 84884686475 scopus 로고    scopus 로고
    • Fast automated protein NMR data collection and assignment by ADAPT-NMR on Bruker spectrometers
    • doi:10.1016/j.jmr.2013.08.010
    • Lee W, Hu K, Tonelli M, Bahrami A, Neuhardt E, Glass KC, Markley JL (2013) Fast automated protein NMR data collection and assignment by ADAPT-NMR on Bruker spectrometers. J Magn Reson 236:83-88. doi:10.1016/j.jmr.2013.08.010
    • (2013) J Magn Reson , vol.236 , pp. 83-88
    • Lee, W.1    Hu, K.2    Tonelli, M.3    Bahrami, A.4    Neuhardt, E.5    Glass, K.C.6    Markley, J.L.7
  • 37
    • 79951553142 scopus 로고    scopus 로고
    • A novel strategy for NMR resonance assignment and protein structure determination
    • doi:10.1007/s10858-010-9458-0
    • Lemak A, Gutmanas A, Chitayat S, Karra M, Farès C, Sunnerhagen M, Arrowsmith CH (2010) A novel strategy for NMR resonance assignment and protein structure determination. J Biomol NMR 49(1):27-38. doi:10.1007/s10858-010-9458-0
    • (2010) J Biomol NMR , vol.49 , Issue.1 , pp. 27-38
    • Lemak, A.1    Gutmanas, A.2    Chitayat, S.3    Karra, M.4    Farès, C.5    Sunnerhagen, M.6    Arrowsmith, C.H.7
  • 38
    • 77958493434 scopus 로고    scopus 로고
    • Simultaneous detection of protein phosphorylation and acetylation by high-resolution NMR spectroscopy
    • doi:10.1021/ja106764y
    • Liokatis S, Dose A, Schwarzer D, Selenko P (2010) Simultaneous detection of protein phosphorylation and acetylation by high-resolution NMR spectroscopy. J Am Chem Soc 132(42):14704-14705. doi:10.1021/ja106764y
    • (2010) J Am Chem Soc , vol.132 , Issue.42 , pp. 14704-14705
    • Liokatis, S.1    Dose, A.2    Schwarzer, D.3    Selenko, P.4
  • 40
    • 27644584200 scopus 로고    scopus 로고
    • Optimization of resolution and sensitivity of 4D NOESY using Multi-dimensional Decomposition
    • DOI 10.1007/s10858-005-1363-6
    • Luan T, Jaravine V, Yee A, Arrowsmith CH, Orekhov VY (2005a) Optimization of resolution and sensitivity of 4D NOESY using multi-dimensional decomposition. J Biomol NMR 33(1):1-14. doi:10.1007/S10858-005-1363-6 (Pubitemid 41573965)
    • (2005) Journal of Biomolecular NMR , vol.33 , Issue.1 , pp. 1-14
    • Luan, T.1    Jaravine, V.2    Yee, A.3    Arrowsmith, C.H.4    Orekhov, V.Yu.5
  • 41
    • 17644415359 scopus 로고    scopus 로고
    • Accuracy and robustness of three-way decomposition applied to NMR data
    • DOI 10.1016/j.jmr.2005.02.009, PII S1090780705000339
    • Luan T, Orekhov VY, Gutmanas A, Billeter M (2005b) Accuracy and robustness of three-way decomposition applied to NMR data. J Magn Reson 174(2):188-199. doi:10.1016/j.jmr.2005.02.009 (Pubitemid 40557702)
    • (2005) Journal of Magnetic Resonance , vol.174 , Issue.2 , pp. 188-199
    • Luan, T.1    Orekhov, V.Yu.2    Gutmanas, A.3    Billeter, M.4
  • 42
    • 81555196391 scopus 로고    scopus 로고
    • Boosting protein dynamics studies using quantitative nonuniform sampling NMR spectroscopy
    • doi:10.1021/jp2081116
    • Matsuki Y, Konuma T, Fujiwara T, Sugase K (2011) Boosting protein dynamics studies using quantitative nonuniform sampling NMR spectroscopy. J Phys Chem B 115(46):13740-13745. doi:10.1021/jp2081116
    • (2011) J Phys Chem B , vol.115 , Issue.46 , pp. 13740-13745
    • Matsuki, Y.1    Konuma, T.2    Fujiwara, T.3    Sugase, K.4
  • 44
    • 33645310982 scopus 로고    scopus 로고
    • ITAM-mediated tonic signalling through pre-BCR and BCR complexes
    • doi:10.1038/nri1808
    • Monroe JG (2006) ITAM-mediated tonic signalling through pre-BCR and BCR complexes. Nature Rev Immunol 6(4):283-294. doi:10.1038/nri1808
    • (2006) Nature Rev Immunol , vol.6 , Issue.4 , pp. 283-294
    • Monroe, J.G.1
  • 45
    • 0034981892 scopus 로고    scopus 로고
    • MUNIN: A new approach to multi-dimensional NMR spectra interpretation
    • DOI 10.1023/A:1011234126930
    • Orekhov VY, Ibraghimov IV, Billeter M (2001) MUNIN: a new approach to multi-dimensional NMR spectra interpretation. J Biomol NMR 20(1):49-60. doi:10.1023/A:1011234126930 (Pubitemid 32519654)
    • (2001) Journal of Biomolecular NMR , vol.20 , Issue.1 , pp. 49-60
    • Orekhov, V.Y.1    Ibraghimov, I.V.2    Billeter, M.3
  • 46
    • 80052810923 scopus 로고    scopus 로고
    • Analysis of non-uniformly sampled spectra with multi-dimensional decomposition
    • doi:10.1016/j.pnmrs.2011.02.002
    • Orekhov VY, Jaravine VA (2011) Analysis of non-uniformly sampled spectra with multi-dimensional decomposition. Prog Nucl Magn Reson Spectrosc 59(3):271-292. doi:10.1016/j.pnmrs.2011.02.002
    • (2011) Prog Nucl Magn Reson Spectrosc , vol.59 , Issue.3 , pp. 271-292
    • Orekhov, V.Y.1    Jaravine, V.A.2
  • 47
    • 0026460815 scopus 로고
    • Hydrogen exchange in native and alcohol forms of ubiquitin
    • doi:10.1021/bi00161a019
    • Pan Y, Briggs MS (1992) Hydrogen exchange in native and alcohol forms of ubiquitin. Biochemistry 31(46):11405-11412. doi:10.1021/bi00161a019
    • (1992) Biochemistry , vol.31 , Issue.46 , pp. 11405-11412
    • Pan, Y.1    Briggs, M.S.2
  • 49
    • 84862059639 scopus 로고    scopus 로고
    • Real-time NMR characterization of structure and dynamics in a transiently populated protein folding intermediate
    • doi:10.1021/ja302598j
    • Rennella E, Cutuil T, Schanda P, Ayala I, Forge V, Brutscher B (2012b) Real-time NMR characterization of structure and dynamics in a transiently populated protein folding intermediate. J Am Chem Soc 134(19):8066-8069. doi:10.1021/ja302598j
    • (2012) J Am Chem Soc , vol.134 , Issue.19 , pp. 8066-8069
    • Rennella, E.1    Cutuil, T.2    Schanda, P.3    Ayala, I.4    Forge, V.5    Brutscher, B.6
  • 50
    • 84885120689 scopus 로고    scopus 로고
    • Effect of internal cavities on folding rates and routes revealed by real-time pressure-jump NMR spectroscopy
    • doi:10.1021/ja406682e
    • Roche J, Dellarole M, Caro JA, Norberto DR, Garcia AE, García-Moreno EB, Roumestand C, Royer CA (2013) Effect of internal cavities on folding rates and routes revealed by real-time pressure-jump NMR spectroscopy. J Am Chem Soc 135(39):14610-14618. doi:10.1021/ja406682e
    • (2013) J Am Chem Soc , vol.135 , Issue.39 , pp. 14610-14618
    • Roche, J.1    Dellarole, M.2    Caro, J.A.3    Norberto, D.R.4    Garcia, A.E.5    García-Moreno, E.B.6    Roumestand, C.7    Royer, C.A.8
  • 51
    • 20444393525 scopus 로고    scopus 로고
    • Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds
    • DOI 10.1021/ja051306e
    • Schanda P, Brutscher B (2005) Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds. J Am Chem Soc 127(22):8014-8015. doi:10.1021/ja051306e (Pubitemid 40799646)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.22 , pp. 8014-8015
    • Schanda, P.1    Brutscher, B.2
  • 53
    • 84875233112 scopus 로고    scopus 로고
    • NMR-based functional profiling of RASopathies and oncogenic RAS mutations
    • doi:10.1073/pnas.1218173110
    • Smith MJ, Neel BG, Ikura M (2013) NMR-based functional profiling of RASopathies and oncogenic RAS mutations. Proc Nat Acad Sci 110(12):4574-4579. doi:10.1073/pnas.1218173110
    • (2013) Proc Nat Acad Sci , vol.110 , Issue.12 , pp. 4574-4579
    • Smith, M.J.1    Neel, B.G.2    Ikura, M.3
  • 54
    • 84876469036 scopus 로고    scopus 로고
    • Probing local backbone geometries in intrinsically disordered proteins by cross-correlated NMR relaxation
    • doi:10.1002/anie.201210005
    • Stanek J, Saxena S, Geist L, Konrat R, Koźmiński W (2013) Probing local backbone geometries in intrinsically disordered proteins by cross-correlated NMR relaxation. Angew Chem Int Ed 52(17):4604-4606. doi:10.1002/anie.201210005
    • (2013) Angew Chem Int Ed , vol.52 , Issue.17 , pp. 4604-4606
    • Stanek, J.1    Saxena, S.2    Geist, L.3    Konrat, R.4    Koźmiński, W.5
  • 55
    • 84870039330 scopus 로고    scopus 로고
    • A time-saving strategy for MAS NMR spectroscopy by combining nonuniform sampling and paramagnetic relaxation assisted condensed data collection
    • doi:10.1021/jp3005794
    • Sun S, Yan S, Guo C, Li M, Hoch JC, Williams JC, Polenova T (2012) A time-saving strategy for MAS NMR spectroscopy by combining nonuniform sampling and paramagnetic relaxation assisted condensed data collection. J Phys Chem B 116(46):13585-13596. doi:10.1021/jp3005794
    • (2012) J Phys Chem B , vol.116 , Issue.46 , pp. 13585-13596
    • Sun, S.1    Yan, S.2    Guo, C.3    Li, M.4    Hoch, J.C.5    Williams, J.C.6    Polenova, T.7
  • 56
    • 77949382937 scopus 로고    scopus 로고
    • High-resolution 3D CANCA NMR experiments for complete mainchain assignments using C-alpha direct detection
    • doi:10.1021/ja907717b
    • Takeuchi K, Frueh DP, Hyberts SG, Sun ZYJ, Wagner G (2010) High-resolution 3D CANCA NMR experiments for complete mainchain assignments using C-alpha direct detection. J Am Chem Soc 132(9):2945-2951. doi:10.1021/ja907717b
    • (2010) J Am Chem Soc , vol.132 , Issue.9 , pp. 2945-2951
    • Takeuchi, K.1    Frueh, D.P.2    Hyberts, S.G.3    Sun, Z.Y.J.4    Wagner, G.5
  • 57
    • 84860869186 scopus 로고    scopus 로고
    • Site-specific mapping and time-resolved monitoring of lysine methylation by high-resolution NMR spectroscopy
    • doi:10.1021/ja301895f
    • Theillet F-X, Liokatis S, Jost JO, Bekei B, Rose HM, Binolfi A, Schwarzer D, Selenko P (2012a) Site-specific mapping and time-resolved monitoring of lysine methylation by high-resolution NMR spectroscopy. J Am Chem Soc 134(18):7616-7619. doi:10.1021/ja301895f
    • (2012) J Am Chem Soc , vol.134 , Issue.18 , pp. 7616-7619
    • Theillet, F.-X.1    Liokatis, S.2    Jost, J.O.3    Bekei, B.4    Rose, H.M.5    Binolfi, A.6    Schwarzer, D.7    Selenko, P.8
  • 59
    • 84886779808 scopus 로고    scopus 로고
    • Site-specific NMR mapping and time-resolved monitoring of serine and threonine phosphorylation in reconstituted kinase reactions and mammalian cell extracts
    • doi:10.1038/nprot.2013.083
    • Theillet F-X, Rose HM, Liokatis S, Binolfi A, Thongwichian R, Stuiver M, Selenko P (2013) Site-specific NMR mapping and time-resolved monitoring of serine and threonine phosphorylation in reconstituted kinase reactions and mammalian cell extracts. Nat Protoc 8(7):1416-1432. doi:10.1038/nprot.2013.083
    • (2013) Nat Protoc , vol.8 , Issue.7 , pp. 1416-1432
    • Theillet, F.-X.1    Rose, H.M.2    Liokatis, S.3    Binolfi, A.4    Thongwichian, R.5    Stuiver, M.6    Selenko, P.7
  • 60
    • 84858336677 scopus 로고    scopus 로고
    • Speeding up the measurement of one-bond scalar (1J) and residual dipolar couplings (1D) by using non-uniform sampling (NUS)
    • doi:10.1016/j.jmr.2012.01.008
    • Thiele CM, Bermel W (2012) Speeding up the measurement of one-bond scalar (1J) and residual dipolar couplings (1D) by using non-uniform sampling (NUS). J Magn Reson 216:134-143. doi:10.1016/j.jmr.2012.01.008
    • (2012) J Magn Reson , vol.216 , pp. 134-143
    • Thiele, C.M.1    Bermel, W.2
  • 61
    • 14744278812 scopus 로고    scopus 로고
    • 13C NOE spectroscopy using methyl-TROSY, sparse data acquisition, and multidimensional decomposition
    • DOI 10.1021/ja044032o
    • Tugarinov V, Kay LE, Ibraghimov I, Orekhov VY (2005) High-resolution four-dimensional H-1-C-13 NOE spectroscopy using methyl-TROSY, sparse data acquisition, and multidimensional decomposition. J Am Chem Soc 127(8):2767-2775. doi:10.1021/Ja04032o (Pubitemid 40327839)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.8 , pp. 2767-2775
    • Tugarinov, V.1    Kay, L.E.2    Ibraghimov, I.3    Orekhov, V.Yu.4
  • 62
    • 40049096760 scopus 로고    scopus 로고
    • Characterization of folding the four-helix bundle protein Rop by real-time NMR
    • DOI 10.1093/protein/gzm081
    • van Nuland NAJ, Dobson CM, Regan L (2008) Characterization of folding the four-helix bundle protein Rop by real-time NMR. Protein Eng Des Sel 21(3):165-170. doi:10.1093/protein/gzm081 (Pubitemid 351323354)
    • (2008) Protein Engineering, Design and Selection , vol.21 , Issue.3 , pp. 165-170
    • Van Nuland, N.A.J.1    Dobson, C.M.2    Regan, L.3
  • 63
    • 3342898158 scopus 로고    scopus 로고
    • Protein folding studied by real-time NMR spectroscopy
    • doi:10.1016/j.ymeth.2004.03.014
    • Zeeb M (2004) Protein folding studied by real-time NMR spectroscopy. Methods 34(1):65-74. doi:10.1016/j.ymeth.2004.03.014
    • (2004) Methods , vol.34 , Issue.1 , pp. 65-74
    • Zeeb, M.1
  • 64
    • 6044266177 scopus 로고    scopus 로고
    • Indirect covariance NMR spectroscopy
    • DOI 10.1021/ja047241h
    • Zhang F, Brüschweiler R (2004) Indirect covariance NMR spectroscopy. J Am Chem Soc 126(41):13180-13181. doi:10.1021/ja047241h (Pubitemid 39382718)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.41 , pp. 13180-13181
    • Zhang, F.1    Bruschweiler, R.2


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