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Volumn 42, Issue 2, 2008, Pages 77-86

Automatic assignment of protein backbone resonances by direct spectrum inspection in targeted acquisition of NMR data

Author keywords

Automatic resonance assignment; MDD; Nonlinear data sampling; Targeted NMR data acquisition

Indexed keywords

CHAPERONE; PROTEIN CCME; UNCLASSIFIED DRUG;

EID: 54049119553     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-008-9269-8     Document Type: Article
Times cited : (5)

References (53)
  • 1
    • 13444256166 scopus 로고    scopus 로고
    • Rapid high-resolution four-dimensional NMR spectroscopy using the filter diagonalization method and its advantages for detailed structural elucidation of oligosaccharides
    • Armstrong GS, Mandelshtam VA, Shaka AJ, Bendiak B (2005) Rapid high-resolution four-dimensional NMR spectroscopy using the filter diagonalization method and its advantages for detailed structural elucidation of oligosaccharides. J Magn Reson 173:160-168
    • (2005) J Magn Reson , vol.173 , pp. 160-168
    • Armstrong, G.S.1    Mandelshtam, V.A.2    Shaka, A.J.3    Bendiak, B.4
  • 2
    • 0033947784 scopus 로고    scopus 로고
    • A tracked approach for automated NMR assignments in proteins (TATAPRO)
    • Atreya HS, Sahu SC, Chary KVR, Govil G (2000) A tracked approach for automated NMR assignments in proteins (TATAPRO). J Biomol NMR 17:125-136
    • (2000) J Biomol NMR , vol.17 , pp. 125-136
    • Atreya, H.S.1    Sahu, S.C.2    Chary, K.V.R.3    Govil, G.4
  • 3
    • 0345807594 scopus 로고    scopus 로고
    • Automated NMR assignments of proteins for high throughput structure determination: TATAPRO II
    • Atreya HS, Chary KVR, Govil G (2002) Automated NMR assignments of proteins for high throughput structure determination: TATAPRO II. Curr Sci 83:1372-1376
    • (2002) Curr Sci , vol.83 , pp. 1372-1376
    • Atreya, H.S.1    Chary, K.V.R.2    Govil, G.3
  • 4
    • 33846410688 scopus 로고    scopus 로고
    • J-GFT NMR for precise measurement of mutually correlated nuclear spin-spin couplings
    • Atreya HS, Garcia E, Shen Y, Szyperski T (2007) J-GFT NMR for precise measurement of mutually correlated nuclear spin-spin couplings. J Am Chem Soc 129:680-692
    • (2007) J Am Chem Soc , vol.129 , pp. 680-692
    • Atreya, H.S.1    Garcia, E.2    Shen, Y.3    Szyperski, T.4
  • 5
    • 0343459675 scopus 로고
    • The Program Xeasy for computer-supported nmr spectral-analysis of biological macromolecules
    • Bartels C, Xia TH, Billeter M, Güntert P, Wüthrich K (1995) The Program Xeasy for computer-supported nmr spectral-analysis of biological macromolecules. J Biomol NMR 6:1-10
    • (1995) J Biomol NMR , vol.6 , pp. 1-10
    • Bartels, C.1    Xia, T.H.2    Billeter, M.3    Güntert, P.4    Wüthrich, K.5
  • 7
    • 0038663223 scopus 로고    scopus 로고
    • PACES: Protein sequential assignment by computer-assisted exhaustive search
    • Coggins BE, Zhou P (2003) PACES: Protein sequential assignment by computer-assisted exhaustive search. J Biomol NMR 26:93-111
    • (2003) J Biomol NMR , vol.26 , pp. 93-111
    • Coggins, B.E.1    Zhou, P.2
  • 9
    • 24744454144 scopus 로고    scopus 로고
    • High-resolution iterative frequency identification for NMR as a general strategy for multidimensional data collection
    • Eghbalnia HR, Bahrami A, Tonelli M, Hallenga K, Markley JL (2005a) High-resolution iterative frequency identification for NMR as a general strategy for multidimensional data collection. J Am Chem Soc 127:12528-12536
    • (2005) J Am Chem Soc , vol.127 , pp. 12528-12536
    • Eghbalnia, H.R.1    Bahrami, A.2    Tonelli, M.3    Hallenga, K.4    Markley, J.L.5
  • 10
    • 24344440618 scopus 로고    scopus 로고
    • Probabilistic identification of spin systems and their assignments including coil-helix inference as output (PISTACHIO)
    • Eghbalnia HR, Bahrami A, Wang LY, Assadi A, Markley JL (2005b) Probabilistic identification of spin systems and their assignments including coil-helix inference as output (PISTACHIO). J Biomol NMR 32:219-233
    • (2005) J Biomol NMR , vol.32 , pp. 219-233
    • Eghbalnia, H.R.1    Bahrami, A.2    Wang, L.Y.3    Assadi, A.4    Markley, J.L.5
  • 11
    • 0036849827 scopus 로고    scopus 로고
    • NMR structure of the heme chaperone CcmE reveals a novel functional motif
    • Enggist E, Thony-Meyer L, Güntert P, Pervushin K (2002) NMR structure of the heme chaperone CcmE reveals a novel functional motif. Structure 10:1551-1557
    • (2002) Structure , vol.10 , pp. 1551-1557
    • Enggist, E.1    Thony-Meyer, L.2    Güntert, P.3    Pervushin, K.4
  • 12
    • 33745364809 scopus 로고    scopus 로고
    • Automated resonance assignment of proteins: 6D APSY-NMR
    • Fiorito F, Hiller S, Wider G, Wüthrich K (2006) Automated resonance assignment of proteins: 6D APSY-NMR. J Biomol NMR 35:27-37
    • (2006) J Biomol NMR , vol.35 , pp. 27-37
    • Fiorito, F.1    Hiller, S.2    Wider, G.3    Wüthrich, K.4
  • 13
    • 33646574966 scopus 로고    scopus 로고
    • Non-uniformly sampled double-TROSY hNcaNH experiments for NMR sequential assignments of large proteins
    • Frueh DP, Sun ZY, Vosburg DA, Walsh CT, Hoch JC, Wagner G (2006) Non-uniformly sampled double-TROSY hNcaNH experiments for NMR sequential assignments of large proteins. J Am Chem Soc 128:5757-5763
    • (2006) J Am Chem Soc , vol.128 , pp. 5757-5763
    • Frueh, D.P.1    Sun, Z.Y.2    Vosburg, D.A.3    Walsh, C.T.4    Hoch, J.C.5    Wagner, G.6
  • 14
    • 0042868578 scopus 로고    scopus 로고
    • Principles and features of single-scan two-dimensional NMR spectroscopy
    • Frydman L, Lupulescu A, Scherf T (2003) Principles and features of single-scan two-dimensional NMR spectroscopy. J Am Chem Soc 125:9204-9217
    • (2003) J Am Chem Soc , vol.125 , pp. 9204-9217
    • Frydman, L.1    Lupulescu, A.2    Scherf, T.3
  • 15
    • 33846785314 scopus 로고    scopus 로고
    • UltraSOFAST HMQC NMR and the repetitive acquisition of 2D protein spectra at Hz rates
    • 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 129:1372-1377
    • (2007) J Am Chem Soc , vol.129 , pp. 1372-1377
    • Gal, M.1    Schanda, P.2    Brutscher, B.3    Frydman, L.4
  • 16
    • 1242295376 scopus 로고    scopus 로고
    • BACUS: A Bayesian protocol for the identification of protein NOESY spectra via unassigned spin systems
    • Grishaev A, Llinas M (2004) BACUS: A Bayesian protocol for the identification of protein NOESY spectra via unassigned spin systems. J Biomol NMR 28:1-10
    • (2004) J Biomol NMR , vol.28 , pp. 1-10
    • Grishaev, A.1    Llinas, M.2
  • 17
    • 24344445864 scopus 로고    scopus 로고
    • ABACUS, a direct method for protein NMR structure computation via assembly of fragments
    • Grishaev A, Steren CA, Wu B, Pineda-Lucena A, Arrowsmith C, Llinas M (2005) ABACUS, a direct method for protein NMR structure computation via assembly of fragments. Proteins 61:36-43
    • (2005) Proteins , vol.61 , pp. 36-43
    • Grishaev, A.1    Steren, C.A.2    Wu, B.3    Pineda-Lucena, A.4    Arrowsmith, C.5    Llinas, M.6
  • 18
    • 0036873589 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS
    • Herrmann T, Güntert P, Wührich K (2002a) Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS. J Biomol NMR 24:171-189
    • (2002) J Biomol NMR , vol.24 , pp. 171-189
    • Herrmann, T.1    Güntert, P.2    Wührich, K.3
  • 19
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • Herrmann T, Güntert P, Wüthrich K (2002b) Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J Mol Biol 319:209-227
    • (2002) J Mol Biol , vol.319 , pp. 209-227
    • Herrmann, T.1    Güntert, P.2    Wüthrich, K.3
  • 21
    • 34848903007 scopus 로고    scopus 로고
    • Sequence-specific resonance assignment of soluble nonglobular proteins by 7D APSY-NMR spectroscopy
    • Hiller S, Wasmer C, Wider G, Wüthrich K (2007) Sequence-specific resonance assignment of soluble nonglobular proteins by 7D APSY-NMR spectroscopy. J Am Chem Soc 129:10823-10828
    • (2007) J Am Chem Soc , vol.129 , pp. 10823-10828
    • Hiller, S.1    Wasmer, C.2    Wider, G.3    Wüthrich, K.4
  • 22
    • 0037266406 scopus 로고    scopus 로고
    • MONTE: An automated Monte Carlo based approach to nuclear magnetic resonance assignment of proteins
    • Hitchens TK, Lukin JA, Zhan YP, McCallum SA, Rule GS (2003) MONTE: An automated Monte Carlo based approach to nuclear magnetic resonance assignment of proteins. J Biomol NMR 25:1-9
    • (2003) J Biomol NMR , vol.25 , pp. 1-9
    • Hitchens, T.K.1    Lukin, J.A.2    Zhan, Y.P.3    McCallum, S.A.4    Rule, G.S.5
  • 23
    • 33750057379 scopus 로고    scopus 로고
    • Targeted acquisition for real-time NMR spectroscopy
    • Jaravine V, Orekhov V (2006) Targeted acquisition for real-time NMR spectroscopy. J Am Chem Soc 128:13421-13426
    • (2006) J Am Chem Soc , vol.128 , pp. 13421-13426
    • Jaravine, V.1    Orekhov, V.2
  • 24
    • 33746403404 scopus 로고    scopus 로고
    • Removal of a time barrier for high-resolution multidimensional NMR spectroscopy
    • Jaravine VA, Ibraghimov I, Orekhov VY (2006) Removal of a time barrier for high-resolution multidimensional NMR spectroscopy. Nat Methods 3:605-607
    • (2006) Nat Methods , vol.3 , pp. 605-607
    • Jaravine, V.A.1    Ibraghimov, I.2    Orekhov, V.Y.3
  • 26
    • 4644234334 scopus 로고    scopus 로고
    • Mars - Robust automatic backbone assignment of proteins
    • Jung YS, Zweckstetter M (2004) Mars - robust automatic backbone assignment of proteins. J Biomol NMR 30:11-23
    • (2004) J Biomol NMR , vol.30 , pp. 11-23
    • Jung, Y.S.1    Zweckstetter, M.2
  • 27
    • 33645856186 scopus 로고    scopus 로고
    • Two-dimensional Fourier transform of arbitrarily sampled NMR data sets
    • Kazimierczuk K, Kozminski W, Zhukov I (2006a) Two-dimensional Fourier transform of arbitrarily sampled NMR data sets. J Magn Reson 179:323-328
    • (2006) J Magn Reson , vol.179 , pp. 323-328
    • Kazimierczuk, K.1    Kozminski, W.2    Zhukov, I.3
  • 28
    • 33750998508 scopus 로고    scopus 로고
    • Random sampling of evolution time space and Fourier transform processing
    • Kazimierczuk K, Zawadzka A, Kozminski W, Zhukov I (2006b) Random sampling of evolution time space and Fourier transform processing. J Biomol NMR 36:157-168
    • (2006) J Biomol NMR , vol.36 , pp. 157-168
    • Kazimierczuk, K.1    Zawadzka, A.2    Kozminski, W.3    Zhukov, I.4
  • 29
    • 0037419802 scopus 로고    scopus 로고
    • GFT NMR, a new approach to rapidly obtain precise high-dimensional NMR spectral information
    • Kim S, Szyperski T (2003) GFT NMR, a new approach to rapidly obtain precise high-dimensional NMR spectral information. J Am Chem Soc 125:1385-1393
    • (2003) J Am Chem Soc , vol.125 , pp. 1385-1393
    • Kim, S.1    Szyperski, T.2
  • 30
    • 2442687868 scopus 로고    scopus 로고
    • Projection-reconstruction technique for speeding up multidimensional NMR spectroscopy
    • Kupce E, Freeman R (2004) Projection-reconstruction technique for speeding up multidimensional NMR spectroscopy. J Am Chem Soc 126:6429-6440
    • (2004) J Am Chem Soc , vol.126 , pp. 6429-6440
    • Kupce, E.1    Freeman, R.2
  • 31
    • 33845922962 scopus 로고    scopus 로고
    • Fast multidimensional NMR by polarization sharing
    • Kupce E, Freeman R (2007) Fast multidimensional NMR by polarization sharing. Magn Reson Chem 45:2-4
    • (2007) Magn Reson Chem , vol.45 , pp. 2-4
    • Kupce, E.1    Freeman, R.2
  • 32
    • 1842555458 scopus 로고    scopus 로고
    • An expectation/maximization nuclear vector replacement algorithm for automated NMR resonance assignments
    • Langmead CJ, Donald BR (2004) An expectation/maximization nuclear vector replacement algorithm for automated NMR resonance assignments. J Biomol NMR 29:111-138
    • (2004) J Biomol NMR , vol.29 , pp. 111-138
    • Langmead, C.J.1    Donald, B.R.2
  • 33
    • 23344434597 scopus 로고    scopus 로고
    • GANA - A genetic algorithm for NMR backbone resonance assignment
    • Lin HN, Wu KP, Chang JM, Sung TY, Hsu WL (2005) GANA - a genetic algorithm for NMR backbone resonance assignment. Nucleic Acids Res 33:4593-4601
    • (2005) Nucleic Acids Res , vol.33 , pp. 4593-4601
    • Lin, H.N.1    Wu, K.P.2    Chang, J.M.3    Sung, T.Y.4    Hsu, W.L.5
  • 34
    • 27644584200 scopus 로고    scopus 로고
    • Optimization of resolution and sensitivity of 4D NOESY using multi-dimensional decomposition
    • Luan T, Jaravine V, Yee A, Arrowsmith CH, Orekhov VY (2005) Optimization of resolution and sensitivity of 4D NOESY using multi-dimensional decomposition. J Biomol NMR 33:1-14
    • (2005) J Biomol NMR , vol.33 , pp. 1-14
    • Luan, T.1    Jaravine, V.2    Yee, A.3    Arrowsmith, C.H.4    Orekhov, V.Y.5
  • 35
    • 0034199794 scopus 로고    scopus 로고
    • The multidimensional filter diagonalization method
    • Mandelshtam VA (2000) The multidimensional filter diagonalization method. J Magn Reson 144:343-356
    • (2000) J Magn Reson , vol.144 , pp. 343-356
    • Mandelshtam, V.A.1
  • 36
    • 0000188085 scopus 로고    scopus 로고
    • Application of the filter diagonalization method to one- and two-dimensional NMR spectra
    • Mandelshtam VA, Taylor HS, Shaka AJ (1998) Application of the filter diagonalization method to one- and two-dimensional NMR spectra. J Magn Reson 133:304-312
    • (1998) J Magn Reson , vol.133 , pp. 304-312
    • Mandelshtam, V.A.1    Taylor, H.S.2    Shaka, A.J.3
  • 37
    • 23344443316 scopus 로고    scopus 로고
    • Fast acquisition of NMR spectra using Fourier transform of non-equispaced data
    • Marion D (2005) Fast acquisition of NMR spectra using Fourier transform of non-equispaced data. J Biomol NMR 32:141-150
    • (2005) J Biomol NMR , vol.32 , pp. 141-150
    • Marion, D.1
  • 38
    • 15844385659 scopus 로고    scopus 로고
    • AutoLink: Automated sequential resonance assignment of biopolymers from NMR data by relative-hypothesis-prioritization-based simulated logic
    • Masse JE, Keller R (2005) AutoLink: Automated sequential resonance assignment of biopolymers from NMR data by relative-hypothesis-prioritization-based simulated logic. J Magn Reson 174:133-151
    • (2005) J Magn Reson , vol.174 , pp. 133-151
    • Masse, J.E.1    Keller, R.2
  • 39
    • 33744991036 scopus 로고    scopus 로고
    • SideLink: Automated side-chain assignment of biopolymers from NMR data by relative-hypothesis-prioritization-based simulated logic
    • Masse JE, Keller R, Pervushin K (2006) SideLink: Automated side-chain assignment of biopolymers from NMR data by relative-hypothesis-prioritization-based simulated logic. J Magn Reson 181:45-67
    • (2006) J Magn Reson , vol.181 , pp. 45-67
    • Masse, J.E.1    Keller, R.2    Pervushin, K.3
  • 40
    • 34547217312 scopus 로고    scopus 로고
    • Ultrafast-based projection-reconstruction three-dimensional nuclear magnetic resonance spectroscopy
    • Mishkovsky M, Kupce E, Frydman L (2007) Ultrafast-based projection-reconstruction three-dimensional nuclear magnetic resonance spectroscopy. J Chem Phys 127:034507
    • (2007) J Chem Phys , vol.127 , pp. 034507
    • Mishkovsky, M.1    Kupce, E.2    Frydman, L.3
  • 41
    • 0031566434 scopus 로고    scopus 로고
    • Automated NOESY interpretation with ambiguous distance restraints: The refined NMR solution structure of the pleckstrin homology domain from beta-spectrin
    • Nilges M, Macias MJ, Odonoghue SI, Oschkinat H (1997) Automated NOESY interpretation with ambiguous distance restraints: The refined NMR solution structure of the pleckstrin homology domain from beta-spectrin. J Mol Biol 269:408-422
    • (1997) J Mol Biol , vol.269 , pp. 408-422
    • Nilges, M.1    Macias, M.J.2    Odonoghue, S.I.3    Oschkinat, H.4
  • 42
    • 0034981892 scopus 로고    scopus 로고
    • MUNIN: A new approach to multi-dimensional NMR spectra interpretation
    • Orekhov VY, Ibraghimov IV, Billeter M (2001) MUNIN: A new approach to multi-dimensional NMR spectra interpretation. J Biomol NMR 20:49-60
    • (2001) J Biomol NMR , vol.20 , pp. 49-60
    • Orekhov, V.Y.1    Ibraghimov, I.V.2    Billeter, M.3
  • 43
    • 0037202215 scopus 로고    scopus 로고
    • Longitudinal H-1 relaxation optimization in TROSY NMR spectroscopy
    • Pervushin K, Vogeli B, Eletsky A (2002) Longitudinal H-1 relaxation optimization in TROSY NMR spectroscopy. J Am Chem Soc 124:12898-12902
    • (2002) J Am Chem Soc , vol.124 , pp. 12898-12902
    • Pervushin, K.1    Vogeli, B.2    Eletsky, A.3
  • 44
    • 0036462495 scopus 로고    scopus 로고
    • Semiautomatic sequence-specific assignment of proteins based on the tertiary structure - The program st2nmr
    • Pristovsek P, Ruterjans H, Jerala R (2002) Semiautomatic sequence-specific assignment of proteins based on the tertiary structure - the program st2nmr. J Comput Chem 23:335-340
    • (2002) J Comput Chem , vol.23 , pp. 335-340
    • Pristovsek, P.1    Ruterjans, H.2    Jerala, R.3
  • 45
    • 4243138246 scopus 로고    scopus 로고
    • Accelerated acquisition of high resolution triple-resonance spectra using non-uniform sampling and maximum entropy reconstruction
    • Rovnyak D, Frueh DP, Sastry M, Sun ZY, Stern AS, Hoch JC, Wagner G (2004) Accelerated acquisition of high resolution triple-resonance spectra using non-uniform sampling and maximum entropy reconstruction. J Magn Reson 170:15-21
    • (2004) J Magn Reson , vol.170 , pp. 15-21
    • Rovnyak, D.1    Frueh, D.P.2    Sastry, M.3    Sun, Z.Y.4    Stern, A.S.5    Hoch, J.C.6    Wagner, G.7
  • 46
    • 30844456535 scopus 로고    scopus 로고
    • SOFAST-HMQC experiments for recording two-dimensional heteronuclear correlation spectra of proteins within a few seconds
    • Schanda P, Kupce E, Brutscher B (2005) SOFAST-HMQC experiments for recording two-dimensional heteronuclear correlation spectra of proteins within a few seconds. J Biomol NMR 33:199-211
    • (2005) J Biomol NMR , vol.33 , pp. 199-211
    • Schanda, P.1    Kupce, E.2    Brutscher, B.3
  • 47
    • 36448973470 scopus 로고    scopus 로고
    • Resolution-enhanced 4D 15 N/13C NOESY protein NMR spectroscopy by application of the covariance transform
    • Snyder DA, Xu Y, Yang D, Brüschweiler R (2007a) Resolution-enhanced 4D 15 N/13C NOESY protein NMR spectroscopy by application of the covariance transform. J Am Chem Soc 129:14126-14127
    • (2007) J Am Chem Soc , vol.129 , pp. 14126-14127
    • Snyder, D.A.1    Xu, Y.2    Yang, D.3    Brüschweiler, R.4
  • 48
    • 35448988389 scopus 로고    scopus 로고
    • Covariance NMR in higher dimensions: Application to 4D NOESY spectroscopy of proteins
    • Snyder DA, Zhang F, Brüschweiler R (2007b) Covariance NMR in higher dimensions: Application to 4D NOESY spectroscopy of proteins. J Biomol NMR 39:165-175
    • (2007) J Biomol NMR , vol.39 , pp. 165-175
    • Snyder, D.A.1    Zhang, F.2    Brüschweiler, R.3
  • 49
    • 39149093421 scopus 로고    scopus 로고
    • Automated structure determination of proteins with the SAIL-FLYA NMR method
    • Takeda M, Ikeya T, Güntert P, Kainosho M (2007) Automated structure determination of proteins with the SAIL-FLYA NMR method. Nat Protocol 2:2896-2902
    • (2007) Nat Protocol , vol.2 , pp. 2896-2902
    • Takeda, M.1    Ikeya, T.2    Güntert, P.3    Kainosho, M.4
  • 50
    • 0035965759 scopus 로고    scopus 로고
    • A dipolar coupling based strategy for simultaneous resonance assignment and structure determination of protein backbones
    • Tian F, Valafar H, Prestegard JH (2001) A dipolar coupling based strategy for simultaneous resonance assignment and structure determination of protein backbones. J Am Chem Soc 123:11791-11796
    • (2001) J Am Chem Soc , vol.123 , pp. 11791-11796
    • Tian, F.1    Valafar, H.2    Prestegard, J.H.3
  • 51
    • 14744278812 scopus 로고    scopus 로고
    • High-resolution four-dimensional H-1-C-13 NOE spectroscopy using methyl-TROSY, sparse data acquisition, and multidimensional decomposition
    • 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 127:2767-2775
    • (2005) J Am Chem Soc , vol.127 , pp. 2767-2775
    • Tugarinov, V.1    Kay, L.E.2    Ibraghimov, I.3    Orekhov, V.Y.4
  • 53
    • 6044266177 scopus 로고    scopus 로고
    • Indirect covariance NMR spectroscopy
    • Zhang F, Brüschweiler R (2004) Indirect covariance NMR spectroscopy. J Am Chem Soc 126:13180-13181
    • (2004) J Am Chem Soc , vol.126 , pp. 13180-13181
    • Zhang, F.1    Brüschweiler, R.2


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