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Volumn , Issue , 2013, Pages 1-431

Structural biology: Practical NMR applications

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EID: 84955133213     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-1-4614-3964-6     Document Type: Book
Times cited : (48)

References (404)
  • 2
    • 4043165350 scopus 로고
    • Removal of dipolar broadening of nuclear magnetic resonance spectra of solids by specimen rotation
    • Andrew ER, Bradburg A, Eades RG (1959) Removal of dipolar broadening of nuclear magnetic resonance spectra of solids by specimen rotation. Nature 183:1802-1803
    • (1959) Nature , vol.183 , pp. 1802-1803
    • Andrew, E.R.1    Bradburg, A.2    Eades, R.G.3
  • 3
    • 0033054043 scopus 로고    scopus 로고
    • High precision solution structure of the c-terminal kh domain of heterogeneous nuclear ribonucleoprotein k, a c- myc transcription factor
    • Baber JL, Libutti D, Levens D, Tjandra N (1999) High precision solution structure of the C-terminal KH domain of heterogeneous nuclear ribonucleoprotein K, a c- myc transcription factor. J Mol Biol 289:949-962
    • (1999) J Mol Biol , vol.289 , pp. 949-962
    • Baber, J.L.1    Libutti, D.2    Levens, D.3    Tjandra, N.4
  • 4
    • 48749142077 scopus 로고
    • Coherence levels and coherence pathways in nmr: A simple way to design phase cycling procedures
    • Bain AD (1984) Coherence levels and coherence pathways in NMR: a simple way to design phase cycling procedures. J Magn Reson 56:418-427
    • (1984) J Magn Reson , vol.56 , pp. 418-427
    • Bain, A.D.1
  • 5
    • 46549098296 scopus 로고
    • Retrieval of frequencies, amplitudes, damping factors, and phases from time-domain signals using a linear least-squares procedure
    • Barkhuusen H, De Beer R, Bovee WMMJ, VanOrmondt D (1985) Retrieval of frequencies, amplitudes, damping factors, and phases from time-domain signals using a linear least-squares procedure. J Magn Reson 61:465-481
    • (1985) J Magn Reson , vol.61 , pp. 465-481
    • Barkhuusen, H.1    De Beer, R.2    Bovee, W.3    Van Ormondt, D.4
  • 6
    • 0034919243 scopus 로고    scopus 로고
    • Dipolar couplings in macromolecular structure determination
    • Bax A, Kontaxis G, Tjandra N (2001) Dipolar couplings in macromolecular structure determination. Meth Enzymol 339:127-174
    • (2001) Meth Enzymol , vol.339 , pp. 127-174
    • Bax, A.1    Kontaxis, G.2    Tjandra, N.3
  • 7
    • 50849149934 scopus 로고
    • Complete accurate editing of decoupled 13c spectra using dept and a quaternary-only sequence
    • Bendal MR, Pegg DT (1983) Complete accurate editing of decoupled 13C spectra using DEPT and a quaternary-only sequence. J Magn Reson 53:272-296
    • (1983) J Magn Reson , vol.53 , pp. 272-296
    • Bendal, M.R.1    Pegg, D.T.2
  • 8
    • 0011327448 scopus 로고
    • Nuclear induction
    • Bloch F (1946) Nuclear induction. Phys Rev 70:460-474
    • (1946) Phys Rev , vol.70 , pp. 460-474
    • Bloch, F.1
  • 9
    • 48549112001 scopus 로고
    • Selection of coherence-transfer pathways in nmr pulse experiments
    • Bodenhausen G, Kogler H, Ernst RR (1984) Selection of coherence-transfer pathways in NMR pulse experiments. J Magn Reson 58:370-388
    • (1984) J Magn Reson , vol.58 , pp. 370-388
    • Bodenhausen, G.1    Kogler, H.2    Ernst, R.R.3
  • 11
    • 0034418635 scopus 로고    scopus 로고
    • Principles and applications of cross-correlated relaxation in biomolecules
    • Brutscher B (2000) Principles and applications of cross-correlated relaxation in biomolecules. Concepts Magn Reson 12:207-229
    • (2000) Concepts Magn Reson , vol.12 , pp. 207-229
    • Brutscher, B.1
  • 12
    • 33847534249 scopus 로고
    • Effects of diffusion on free precession in nuclear magnetic resonance experiments
    • Carr HY, Purcell EM (1954) Effects of diffusion on free precession in Nuclear Magnetic Resonance experiments. Phys Rev 94:630-638
    • (1954) Phys Rev , vol.94 , pp. 630-638
    • Carr, H.Y.1    Purcell, E.M.2
  • 13
    • 0037169646 scopus 로고    scopus 로고
    • Nmr dipolar couplings for the structure determination of biopolymers in solution
    • de Alba E, Tjandra N (2002) NMR dipolar couplings for the structure determination of biopolymers in solution. Prog Nucl Magn Reson Spectrosc 40:175-197
    • (2002) Prog Nucl Magn Reson Spectrosc , vol.40 , pp. 175-197
    • De Alba, E.1    Tjandra, N.2
  • 15
    • 0041045434 scopus 로고
    • Distortionless enhancement of nmr signals by polarization transfer
    • Doddrell DM, Pegg DT, Bendall MR (1982) Distortionless enhancement of NMR signals by polarization transfer. J Magn Reson 48:323-327
    • (1982) J Magn Reson , vol.48 , pp. 323-327
    • Doddrell, D.M.1    Pegg, D.T.2    Bendall, M.R.3
  • 16
    • 0001965116 scopus 로고
    • Description of states in quantum mechanics by density matrix and operator techniques
    • Fano U (1957) Description of states in quantum mechanics by density matrix and operator techniques. Rev Mod Phys 29:74-93
    • (1957) Rev Mod Phys , vol.29 , pp. 74-93
    • Fano, U.1
  • 21
    • 0000487645 scopus 로고
    • Formalisms for the description of multiple-pulse nmr experiments
    • Howarth MA, Lian LY, Hawkes GE, Sales KD (1986) Formalisms for the description of multiple-pulse NMR experiments. J Magn Reson 68:433-452
    • (1986) J Magn Reson , vol.68 , pp. 433-452
    • Howarth, M.A.1    Lian, L.Y.2    Hawkes, G.E.3    Sales, K.D.4
  • 23
    • 12244297937 scopus 로고
    • Vicinal proton coupling in nuclear magnetic resonance
    • Karplus K (1963) Vicinal proton coupling in nuclear magnetic resonance. J Am Chem Soc 85:2870-2871
    • (1963) J am Chem Soc , vol.85 , pp. 2870-2871
    • Karplus, K.1
  • 24
    • 33745356391 scopus 로고
    • Contact electron-spin interactions of nuclear magnetic moments
    • Karplus M (1959) Contact electron-spin Interactions of nuclear magnetic moments. J Phys Chem 30:11-15
    • (1959) J Phys Chem , vol.30 , pp. 11-15
    • Karplus, M.1
  • 26
  • 27
    • 36149028286 scopus 로고
    • Free induction decays of rotating solids
    • Lowe IJ (1959) Free Induction decays of rotating solids. Phys Rev Lett 2:285-287
    • (1959) Phys Rev Lett , vol.2 , pp. 285-287
    • Lowe, I.J.1
  • 28
    • 0032110340 scopus 로고    scopus 로고
    • Recommendations for the presentation of nmr structures of proteins and nucleic acids -lupac-iubmb-iupab inter-union task group on the standardization of data bases of protein and nucleic acid structures determined by nmr spectroscopy
    • Markley JL, Bax A, Arata Y, Hilbers CW, Kaptein R, Sykes BD, Wright PE, Wuthrich K (1998) Recommendations for the presentation of NMR structures of proteins and nucleic acids -lUPAC-IUBMB-IUPAB Inter-Union Task Group on the standardization of data bases of protein and nucleic acid structures determined by NMR spectroscopy. J Biomol NMR 12:1-23
    • (1998) J Biomol NMR , vol.12 , pp. 1-23
    • Markley, J.L.1    Bax, A.2    Arata, Y.3    Hilbers, C.W.4    Kaptein, R.5    Sykes, B.D.6    Wright, P.E.7    Wuthrich, K.8
  • 29
    • 0011540227 scopus 로고
    • Generalized maximum entropy deconvolution of spectral segments
    • Mazzeo AR, Delsuc MA, Kumar A, Levy GC (1989) Generalized maximum entropy deconvolution of spectral segments. J Magn Reson 81:512-519
    • (1989) J Magn Reson , vol.81 , pp. 512-519
    • Mazzeo, A.R.1    Delsuc, M.A.2    Kumar, A.3    Levy, G.C.4
  • 30
    • 33845560617 scopus 로고
    • Enhancement of nuclear magnetic resonance signals by polarization transfer
    • Morris GA, Freeman R (1979) Enhancement of nuclear magnetic resonance signals by polarization transfer. J Am Chem Soc 101:760-762
    • (1979) J am Chem Soc , vol.101 , pp. 760-762
    • Morris, G.A.1    Freeman, R.2
  • 31
    • 0242565339 scopus 로고    scopus 로고
    • Application of real time digital filters in nmr spectroscopy
    • Moskau D (2002) Application of real time digital filters in NMR spectroscopy. Concepts Magn Reson 15:164-176
    • (2002) Concepts Magn Reson , vol.15 , pp. 164-176
    • Moskau, D.1
  • 33
    • 0034480326 scopus 로고    scopus 로고
    • Nmr structures of biomolecules using field oriented media and residual dipolar couplings
    • Prestegard JH, Al-Hashimi HM, Tolman JR (2000) NMR structures of biomolecules using field oriented media and residual dipolar couplings. Quart Rev Biophys 33:371-424
    • (2000) Quart Rev Biophys , vol.33 , pp. 371-424
    • Prestegard, J.H.1    Al-Hashimi, H.M.2    Tolman, J.R.3
  • 35
    • 10144260777 scopus 로고
    • Nitrogen-15 nuclear magnetic resonance spectroscopy. Natural abundance nitrogen-15 chemical shifts of alkyl- and aryl-substituted ureas
    • Sibi MP, Lichter RL (1979) Nitrogen-15 nuclear magnetic resonance spectroscopy. Natural abundance nitrogen-15 chemical shifts of alkyl- and aryl-substituted ureas. J Org Chem 44:3017-3022
    • (1979) J Org Chem , vol.44 , pp. 3017-3022
    • Sibi, M.P.1    Lichter, R.L.2
  • 36
    • 36149008265 scopus 로고
    • Relaxation processes in a system of two spins
    • Solomon I (1955) Relaxation processes in a system of two spins. Phys Rev 99:559-565
    • (1955) Phys Rev , vol.99 , pp. 559-565
    • Solomon, I.1
  • 38
    • 0347610773 scopus 로고
    • Empirical correlation between protein backbone conformation and c. Alpha. And c.Beta. 13C nuclear magnetic resonance chemical shifts
    • Spera S, Bax A (1991) Empirical correlation between protein backbone conformation and C.alpha. And C.beta. 13C nuclear magnetic resonance chemical shifts. J Am Chem Soc 113:5490-5492
    • (1991) J am Chem Soc , vol.113 , pp. 5490-5492
    • Spera, S.1    Bax, A.2
  • 39
    • 38249011370 scopus 로고
    • A new, storage-efficient algorithm for maximum-entropy spectrum reconstruction
    • Stern AS, Hoch JC (1992) A new, storage-efficient algorithm for maximum-entropy spectrum reconstruction. J Magn Reson 97:255-270
    • (1992) J Magn Reson , vol.97 , pp. 255-270
    • Stern, A.S.1    Hoch, J.C.2
  • 40
    • 0033200220 scopus 로고    scopus 로고
    • Establishing a degree of order: Obtaining high-resolution nmr structures from molecular alignment
    • Tjandra N (1999) Establishing a degree of order: obtaining high-resolution NMR structures from molecular alignment. Structure 7:R205-R211
    • (1999) Structure , vol.7 , pp. R205-R211
    • Tjandra, N.1
  • 41
    • 0030722243 scopus 로고    scopus 로고
    • Direct measurement of distances and angles in biomolecules by nmr in a dilute liquid crystalline medium
    • Tjandra T, Bax A (1997) Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium. Science 278:1111-1114
    • (1997) Science , vol.278 , pp. 1111-1114
    • Tjandra, T.1    Bax, A.2
  • 42
    • 0029879363 scopus 로고    scopus 로고
    • Determination of the backbone dihedral angles j in human ubiquitin from reparametrized empirical karplus equations
    • Wang AC, Bax A (1996) Determination of the backbone dihedral angles j in human ubiquitin from reparametrized empirical Karplus equations. J Am Chem Soc 118:2483-2494
    • (1996) J am Chem Soc , vol.118 , pp. 2483-2494
    • Wang, A.C.1    Bax, A.2
  • 45
    • 0026410969 scopus 로고
    • Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
    • Wishart DS, Richards FM, Sykes BD (1991) Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J Mol Biol 222:311-333
    • (1991) J Mol Biol , vol.222 , pp. 311-333
    • Wishart, D.S.1    Richards, F.M.2    Sykes, B.D.3
  • 47
    • 0000517056 scopus 로고
    • Improved linear prediction for truncated signals of known phase
    • Zhu G, Bax A (1990) Improved linear prediction for truncated signals of known phase. J Magn Reson 90:405-410
    • (1990) J Magn Reson , vol.90 , pp. 405-410
    • Zhu, G.1    Bax, A.2
  • 48
    • 0001833249 scopus 로고
    • Understanding multiple-pulse experiments - an introduction to the product-operator description. I. Starting with the vector model
    • Ziessow D (1990) Understanding multiple-pulse experiments - an introduction to the product-operator description. I. Starting with the vector model. Concept Magn Reson 2:81-100
    • (1990) Concept Magn Reson , vol.2 , pp. 81-100
    • Ziessow, D.1
  • 49
    • 0002333715 scopus 로고    scopus 로고
    • Amplification of radiation damping in a 600-mhz nmr spectrometer: Application to the study of water-protein interactions
    • Abergel D, Louis-Joseph A, Lallemend JY (1996) Amplification of radiation damping in a 600-MHz NMR spectrometer: application to the study of water-protein interactions. J Biomol NMR 8:15-22
    • (1996) J Biomol NMR , vol.8 , pp. 15-22
    • Abergel, D.1    Louis-Joseph, A.2    Lallemend, J.Y.3
  • 50
    • 0037169647 scopus 로고    scopus 로고
    • Transient properties of radiation damping
    • Augustine MP (2002) Transient properties of radiation damping. Prog Nucl Magn Reson Spectrosc 40:111-150
    • (2002) Prog Nucl Magn Reson Spectrosc , vol.40 , pp. 111-150
    • Augustine, M.P.1
  • 51
    • 36149018202 scopus 로고
    • Radiation damping in magnetic resonance experiments
    • Bloembergen N, Pound RV (1954) Radiation damping in magnetic resonance experiments. Phys Rev 95:8-12
    • (1954) Phys Rev , vol.95 , pp. 8-12
    • Bloembergen, N.1    Pound, R.V.2
  • 52
    • 0001610685 scopus 로고
    • Water selective pseudo-3d noesy-tocsy experiment using ‘radiation damping’: Application to the study of the effects of scn- on the hydration of bpti
    • Bockmann A, Guittet E (1995) Water selective pseudo-3D NOESY-TOCSY experiment using ‘radiation damping’: application to the study of the effects of SCN- on the hydration of BPTI. J Chim Phys Chim Biol 92:1923-1928
    • (1995) J Chim Phys Chim Biol , vol.92 , pp. 1923-1928
    • Bockmann, A.1    Guittet, E.2
  • 53
    • 58149209498 scopus 로고
    • Suppression of radiation damping in nmr in liquids by active electronic feedback
    • Broekaert P, Jeener J (1995) Suppression of radiation damping in NMR in liquids by active electronic feedback. J Magn Reson 113A:60-64
    • (1995) J Magn Reson , vol.113 , pp. 60-64
    • Broekaert, P.1    Jeener, J.2
  • 56
    • 0001118712 scopus 로고    scopus 로고
    • An improved experimental scheme to measure self-diffusion coefficients of biomolecules with an advantageous use of radiation damping
    • Krishnan VV, Thornton KH, Cosman M (1999) An improved experimental scheme to measure self-diffusion coefficients of biomolecules with an advantageous use of radiation damping. Chem Phys Lett 302:317-323
    • (1999) Chem Phys Lett , vol.302 , pp. 317-323
    • Krishnan, V.V.1    Thornton, K.H.2    Cosman, M.3
  • 57
    • 0000389264 scopus 로고
    • Use of a water flip-back pulse in the homonuclear noesy experiment
    • Lippens G, Dhallium C, Wieruszeski JM (1995) Use of a water flip-back pulse in the homonuclear NOESY experiment. J Biomol NMR 5:327-331
    • (1995) J Biomol NMR , vol.5 , pp. 327-331
    • Lippens, G.1    Dhallium, C.2    Wieruszeski, J.M.3
  • 62
    • 0001297802 scopus 로고    scopus 로고
    • An overcoupled nmr probe for the reduction of radiation damping
    • Picard L, von Keinlin M, Decorps M (1996) An overcoupled NMR probe for the reduction of radiation damping. J Magn Reson 117A:262-266
    • (1996) J Magn Reson , vol.117A , pp. 262-266
    • Picard, L.1    Von Keinlin, M.2    Decorps, M.3
  • 64
    • 0001363358 scopus 로고
    • Radiation damping in nuclear magnetic resonance
    • Szoke A, Meiboom S (1959) Radiation damping in nuclear magnetic resonance. Phys Rev 113:585-586
    • (1959) Phys Rev , vol.113 , pp. 585-586
    • Szoke, A.1    Meiboom, S.2
  • 66
    • 0034919243 scopus 로고    scopus 로고
    • Dipolar couplings in macromolecular structure determination
    • Bax A, Kontaxis G, Tjandra N (2001) Dipolar couplings in macromolecular structure determination. Meth Enzymol 339:127-174
    • (2001) Meth Enzymol , vol.339 , pp. 127-174
    • Bax, A.1    Kontaxis, G.2    Tjandra, N.3
  • 67
    • 0000112965 scopus 로고    scopus 로고
    • Isotope-filtered nmr methods for the study of biomolecular structure and interactions
    • Breeze AL (2000) Isotope-filtered NMR methods for the study of biomolecular structure and interactions. Prog Nucl Magn Reson Spectrosc 36:323-372
    • (2000) Prog Nucl Magn Reson Spectrosc , vol.36 , pp. 323-372
    • Breeze, A.L.1
  • 68
    • 0000393431 scopus 로고
    • Theory and applications of the transferred nuclear overhauser effect to the study of the conformations of small ligands bound to proteins
    • Clore GM, Gronenbom AM (1982) Theory and applications of the transferred nuclear overhauser effect to the study of the conformations of small ligands bound to proteins. J Magn Reson 48:402-417
    • (1982) J Magn Reson , vol.48 , pp. 402-417
    • Clore, G.M.1    Gronenbom, A.M.2
  • 69
    • 0001342923 scopus 로고
    • Theory of the time dependent transferred nuclear overhauser effect: Applications to structural analysis of ligand-protein complexes in solution
    • Clore GM, Gronenborn AM (1983) Theory of the time dependent transferred nuclear Overhauser effect: applications to structural analysis of ligand-protein complexes in solution. J Magn Reson 53:423-442
    • (1983) J Magn Reson , vol.53 , pp. 423-442
    • Clore, G.M.1    Gronenborn, A.M.2
  • 70
    • 0031933143 scopus 로고    scopus 로고
    • Determining the structures of large proteins and protein complexes by nmr
    • Clore GM, Gronenborn AM (1998) Determining the structures of large proteins and protein complexes by NMR. Trends Biotech 16:22-34
    • (1998) Trends Biotech , vol.16 , pp. 22-34
    • Clore, G.M.1    Gronenborn, A.M.2
  • 71
    • 0032517327 scopus 로고    scopus 로고
    • Measurement of residual dipolar couplings of macromolecules aligned in the nematic phase of a colloidal suspension of rod-shaped viruses
    • Clore GM, Starich MR, Gronenborn AM (1998) Measurement of residual dipolar couplings of macromolecules aligned in the nematic phase of a colloidal suspension of rod-shaped viruses. J Am Chem Sco 120:10571-10572
    • (1998) J am Chem Sco , vol.120 , pp. 10571-10572
    • Clore, G.M.1    Starich, M.R.2    Gronenborn, A.M.3
  • 72
    • 0026598960 scopus 로고
    • Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex
    • de Vos AM, Ultsch M, Kossiakoff AA (1992) Human growth hormone and extracellular domain of its receptor: crystal structure of the complex. Science 255:306-312
    • (1992) Science , vol.255 , pp. 306-312
    • De Vos, A.M.1    Ultsch, M.2    Kossiakoff, A.A.3
  • 73
    • 0033566242 scopus 로고    scopus 로고
    • Millisecond-timescale motions contribute to the function of the bacterial response regulator protein spo0f
    • Feher VA, Cavanagh J (1999) Millisecond-timescale motions contribute to the function of the bacterial response regulator protein Spo0F. Nature 400:289-293
    • (1999) Nature , vol.400 , pp. 289-293
    • Feher, V.A.1    Cavanagh, J.2
  • 74
    • 0031760503 scopus 로고    scopus 로고
    • Tunable alignment of macromolecules by filamentous phage yields dipolar coupling interactions
    • Hansen MR, Mueller L, Paridi A (1998a) Tunable alignment of macromolecules by filamentous phage yields dipolar coupling interactions. Nat Struct Biol 5:1065-1074
    • (1998) Nat Struct Biol , vol.5 , pp. 1065-1074
    • Hansen, M.R.1    Mueller, L.2    Paridi, A.3
  • 75
    • 0032483695 scopus 로고    scopus 로고
    • Observation of long-range 1h—1h distances in solution by dipolar coupling interactions
    • Hansen MR, Rance M, Paridi A (1998b) Observation of long-range 1H—1H distances in solution by dipolar coupling interactions. J Am Chem Sco 120:11210-11211
    • (1998) J am Chem Sco , vol.120 , pp. 11210-11211
    • Hansen, M.R.1    Rance, M.2    Paridi, A.3
  • 76
    • 0030691041 scopus 로고    scopus 로고
    • Design of an expression system for detecting folded protein domains and mapping macromolecular interactions by nmr
    • Huth JR, Bewley CA, Jackson BM, Hinnebusch AG, Clore GM, Gronenborn AM (1997) Design of an expression system for detecting folded protein domains and mapping macromolecular interactions by NMR. Prot Sci 6:2359-2364
    • (1997) Prot Sci , vol.6 , pp. 2359-2364
    • Huth, J.R.1    Bewley, C.A.2    Jackson, B.M.3    Hinnebusch, A.G.4    Clore, G.M.5    Gronenborn, A.M.6
  • 78
    • 0032177257 scopus 로고    scopus 로고
    • Improved dilute bicelle solutions for high-resolution nmr of biological macromolecules
    • Losonczi JA, Prestegard JH (1998) Improved dilute bicelle solutions for high-resolution NMR of biological macromolecules. J Biomol NMR 12:447-451
    • (1998) J Biomol NMR , vol.12 , pp. 447-451
    • Losonczi, J.A.1    Prestegard, J.H.2
  • 79
    • 0033610476 scopus 로고    scopus 로고
    • Identification by nmr spectroscopy of residues at contact surfaces in large, slowly exchanging macromolecular complexes
    • Mastsuo H, Walters KJ, Teruya K, Tanaka T, Gassner GT, Lippard SJ, Kyogoku Y, Wagner G (1999) Identification by NMR spectroscopy of residues at contact surfaces in large, Slowly Exchanging Macromolecular Complexes. J Am Chem Sco 121:9903-9904
    • (1999) J am Chem Sco , vol.121 , pp. 9903-9904
    • Mastsuo, H.1    Walters, K.J.2    Teruya, K.3    Tanaka, T.4    Gassner, G.T.5    Lippard, S.J.6    Kyogoku, Y.7    Wagner, G.8
  • 80
    • 0030861621 scopus 로고    scopus 로고
    • The a-kinase anchoring domain of type ila camp-dependent protein kinase is highly helical
    • Newlon MG, Roy M, Hausken ZE, Scott JD, Jennings PA (1997) The A-kinase anchoring domain of Type Ila cAMP-dependent protein kinase Is highly helical. J Biol Chem 272:23637-23644
    • (1997) J Biol Chem , vol.272 , pp. 23637-23644
    • Newlon, M.G.1    Roy, M.2    Hausken, Z.E.3    Scott, J.D.4    Jennings, P.A.5
  • 81
    • 0034919312 scopus 로고    scopus 로고
    • Protein-protein interactions probed by nuclear magnetic resonance spectroscopy
    • Qin J, Vinogradova O, Gronenborn AM (2001) Protein-protein interactions probed by nuclear magnetic resonance spectroscopy. Meth Enzmol 339:377-389
    • (2001) Meth Enzmol , vol.339 , pp. 377-389
    • Qin, J.1    Vinogradova, O.2    Gronenborn, A.M.3
  • 82
    • 0034486021 scopus 로고    scopus 로고
    • Solution structure of dini provides insight into its mode of reca inactivation
    • Ramirez BE, Voloshin ON, Camerini-Otero RD, Bax A (2000) Solution structure of DinI provides insight into its mode of RecA inactivation. Prot Sci 9:2161-2169
    • (2000) Prot Sci , vol.9 , pp. 2161-2169
    • Ramirez, B.E.1    Voloshin, O.N.2    Camerini-Otero, R.D.3    Bax, A.4
  • 83
    • 0025182649 scopus 로고
    • Magnetically orientable phospholipid bilayers containing small amounts of a bile salt analogue, chapso
    • Sanders CR, Prestegard JH (1990) Magnetically orientable phospholipid bilayers containing small amounts of a bile salt analogue, CHAPSO. Biophys J 58:447-460
    • (1990) Biophys J , vol.58 , pp. 447-460
    • Sanders, C.R.1    Prestegard, J.H.2
  • 84
    • 0000265205 scopus 로고
    • Orientation and dynamics of.Beta.-dodecyl glucopyranoside in phospholipid bilayers by oriented sample nmr and order matrix analysis
    • Sanders CR, Prestegard JH (1991) Orientation and dynamics of.beta.-dodecyl glucopyranoside in phospholipid bilayers by oriented sample NMR and order matrix analysis. J Am Chem Sco 113:1987-1996
    • (1991) J am Chem Sco , vol.113 , pp. 1987-1996
    • Sanders, C.R.1    Prestegard, J.H.2
  • 85
    • 0028730634 scopus 로고
    • Magnetically-oriented phospholipid micelles as a tool for the study of membrane-associated molecules
    • Sanders CR, Hare B, Howard KP, Prestegard JH (1993) Magnetically-oriented phospholipid micelles as a tool for the study of membrane-associated molecules. Prog Nucl Magn Reson Spectrosc 26:421-444
    • (1993) Prog Nucl Magn Reson Spectrosc , vol.26 , pp. 421-444
    • Sanders, C.R.1    Hare, B.2    Howard, K.P.3    Prestegard, J.H.4
  • 86
    • 0032467377 scopus 로고    scopus 로고
    • Nmr for the design of functional mimetics of protein-protein interactions: One key is in the building of bridges
    • Song J, Ni F (1998) NMR for the design of functional mimetics of protein-protein interactions: one key is in the building of bridges. Biochem Cell Biol 76:177-188
    • (1998) Biochem Cell Biol , vol.76 , pp. 177-188
    • Song, J.1    Ni, F.2
  • 87
    • 0034051065 scopus 로고    scopus 로고
    • A novel nmr method for determining the interfaces of large protein—protein complexes
    • Takahashi H, Nahanishi T, Kami K, Arata Y, Shimada I (2000) A novel NMR method for determining the interfaces of large protein—protein complexes. Nat Struct Biol 7:220-223
    • (2000) Nat Struct Biol , vol.7 , pp. 220-223
    • Takahashi, H.1    Nahanishi, T.2    Kami, K.3    Arata, Y.4    Shimada, I.5
  • 88
    • 0030722243 scopus 로고    scopus 로고
    • Direct measurement of distances and angles in biomolecules by nmr in a dilute liquid crystalline medium
    • Tjandra T, Bax A (1997) Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium. Science 278:1111-1114
    • (1997) Science , vol.278 , pp. 1111-1114
    • Tjandra, T.1    Bax, A.2
  • 91
    • 48749142077 scopus 로고
    • Coherence levels and coherence pathways in nmr
    • J Magn Reson
    • Bain A (1984) Coherence levels and coherence pathways in NMR. A simple way to design phase cycling procedures. J Magn Reson 56:418-427
    • (1984) A Simple Way to Design phase cycling Procedures , vol.56 , pp. 418-427
    • Bain, A.1
  • 92
    • 46549098296 scopus 로고
    • Retrieval of frequencies, amplitudes, damping factors, and phases from time-domain signals using a linear least-squares procedure
    • Barkhuijsen H, de Beer R, Bovee WMJ, van Ormindt D (1985) Retrieval of frequencies, amplitudes, damping factors, and phases from time-domain signals using a linear least-squares procedure. J Magn Reson 61:465-481
    • (1985) J Magn Reson , vol.61 , pp. 465-481
    • Barkhuijsen, H.1    De Beer, R.2    Bovee, W.3    Van Ormindt, D.4
  • 94
    • 0001549644 scopus 로고
    • Broadband and adiabatic inversion of a two-level system by phase-modulated pulses
    • Baum J, Tycko R, Pines A (1985) Broadband and adiabatic inversion of a two-level system by phase-modulated pulses. Phys Rev A32:3435-3447
    • (1985) Phys Rev , vol.A32 , pp. 3435-3447
    • Baum, J.1    Tycko, R.2    Pines, A.3
  • 95
    • 5144229966 scopus 로고
    • Practical aspects of two-dimensional transverse noe spectroscopy
    • Bax A, Davis DG (1985a) Practical aspects of two-dimensional transverse NOE spectroscopy. J Magn Reson 63:207-213
    • (1985) J Magn Reson , vol.63 , pp. 207-213
    • Bax, A.1    Davis, D.G.2
  • 96
    • 5144233105 scopus 로고
    • Mlev-17-based two-dimensional homonuclear magnetization transfer spectroscopy
    • Bax A, Davis DG (1985b) MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J Magn Reson 65:355-360
    • (1985) J Magn Reson , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 97
    • 48549112001 scopus 로고
    • Selection of coherence-transfer pathways in nmr pulse experiments
    • Bodenhausen G, Kogler H, Ernst RR (1984) Selection of coherence-transfer pathways in NMR pulse experiments. J Magn Reson 58:370-388
    • (1984) J Magn Reson , vol.58 , pp. 370-388
    • Bodenhausen, G.1    Kogler, H.2    Ernst, R.R.3
  • 98
    • 0011491177 scopus 로고
    • Structure determination of a tetrasaccharide: Transient nuclear overhauser effects in the rotating frame
    • Bothner-By AA, Stephens RL, Lee J, Warren CD, Jeanloz RW (1984) Structure determination of a tetrasaccharide: transient nuclear Overhauser effects in the rotating frame. J Am Chem Soc 106:811-813
    • (1984) J am Chem Soc , vol.106 , pp. 811-813
    • Bothner-By, A.A.1    Stephens, R.L.2    Lee, J.3    Warren, C.D.4    Jeanloz, R.W.5
  • 99
    • 0344448273 scopus 로고
    • Coherence transfer by isotropic mixing: Application to proton correlation spectroscopy
    • Braunschweiler L, Ernst RR (1983) Coherence transfer by isotropic mixing: application to proton correlation spectroscopy. J Magn Reson 53:521-528
    • (1983) J Magn Reson , vol.53 , pp. 521-528
    • Braunschweiler, L.1    Ernst, R.R.2
  • 101
    • 48749146220 scopus 로고
    • A broadband radiofrequency reflected-wave detector and its application to a nuclear magnetic resonance spectrometer
    • Dykstra RW (1983) A broadband radiofrequency reflected-wave detector and its application to a nuclear magnetic resonance spectrometer. J Magn Reson 52:313-317
    • (1983) J Magn Reson , vol.52 , pp. 313-317
    • Dykstra, R.W.1
  • 102
    • 11544304059 scopus 로고
    • Gaussian pulse cascades: New analytical functions for rectangular selective inversion and in-phase excitation in nmr
    • Emsley L, Bodenhausen G (1990) Gaussian pulse cascades: new analytical functions for rectangular selective inversion and in-phase excitation in NMR. Chem Phys Lett 165:469-476
    • (1990) Chem Phys Lett , vol.165 , pp. 469-476
    • Emsley, L.1    Bodenhausen, G.2
  • 103
    • 0000894994 scopus 로고
    • Self-refocusing effect of 270° gaussian pulses. Applications to selective two-dimensional exchange spectroscopy
    • Emsley L, Bodenhausen G (1989) Self-refocusing effect of 270° Gaussian pulses. Applications to selective two-dimensional exchange spectroscopy. J Magn Reson 82:211-221
    • (1989) J Magn Reson , vol.82 , pp. 211-221
    • Emsley, L.1    Bodenhausen, G.2
  • 104
    • 0028673795 scopus 로고
    • Selective pulses and their applications to assignment and structure determination in nuclear magnetic resonance
    • Emsley L (1994) Selective pulses and their applications to assignment and structure determination in nuclear magnetic resonance. Meth Enzymol 239:207-246
    • (1994) Meth Enzymol , vol.239 , pp. 207-246
    • Emsley, L.1
  • 107
    • 0001021681 scopus 로고
    • Shaped selective pulses for coherence-transfer experiments
    • Friedrich J, Davies S, Freeman R (1987) Shaped selective pulses for coherence-transfer experiments. J Magn Reson 75:390-395
    • (1987) J Magn Reson , vol.75 , pp. 390-395
    • Friedrich, J.1    Davies, S.2    Freeman, R.3
  • 108
    • 44949280676 scopus 로고
    • Band-selective radiofrequency pulses
    • Geen H, Freeman R (1991) Band-selective radiofrequency pulses. J Magn Reson 93:93-141
    • (1991) J Magn Reson , vol.93 , pp. 93-141
    • Geen, H.1    Freeman, R.2
  • 109
    • 0001240703 scopus 로고
    • Frequency offset effects and their elimination in nmr rotating-frame cross-relaxation spectroscopy
    • Griesinger C, Ernest RR (1987) Frequency offset effects and their elimination in NMR rotating-frame cross-relaxation spectroscopy. J Magn Reson 75:261-271
    • (1987) J Magn Reson , vol.75 , pp. 261-271
    • Griesinger, C.1    Ernest, R.R.2
  • 110
    • 0027787894 scopus 로고
    • The importance of not saturating water in protein nmr. Application to sensitivity enhancement and noe measurements
    • Grzesiek S, Bax A (1993) The importance of not saturating water in protein NMR. Application to sensitivity enhancement and NOE measurements. J Am Chem Soc 115:12593-12594
    • (1993) J am Chem Soc , vol.115 , pp. 12593-12594
    • Grzesiek, S.1    Bax, A.2
  • 111
    • 0035742515 scopus 로고    scopus 로고
    • Nmr nomenclature. Nuclear spin properties and conventions for chemical shifts, pure appl
    • Harris R, Becker ED, de Menezes SMC, Goodfellow R, and Granger P, NMR Nomenclature. Nuclear Spin Properties And Conventions For Chemical Shifts, Pure Appl. Chem., Vol. 73, pp. 1795-1818, 2001
    • (2001) Chem , vol.73 , pp. 1795-1818
    • Harris, R.1    Becker, E.D.2    De Menezes, S.3    Goodfellow, R.4    Granger, P.5
  • 112
    • 36149026370 scopus 로고
    • Nuclear double resonance in the rotating frame
    • Hartmann SR, Hahn EL (1962) Nuclear double resonance in the rotating frame. Phys Rev 128:2042-2053
    • (1962) Phys Rev , vol.128 , pp. 2042-2053
    • Hartmann, S.R.1    Hahn, E.L.2
  • 113
    • 0003026536 scopus 로고
    • Practical aspects of 3d heteronuclear nmr of proteins
    • Kay LE, Marion D, Bax A (1989) Practical aspects of 3D heteronuclear NMR of proteins. J Magn Reson 84:72-84
    • (1989) J Magn Reson , vol.84 , pp. 72-84
    • Kay, L.E.1    Marion, D.2    Bax, A.3
  • 115
    • 0034917743 scopus 로고    scopus 로고
    • Applications of adiabatic pulses in biomolecular nuclear magnetic resonance
    • Kupce lí (2001) Applications of adiabatic pulses in biomolecular nuclear magnetic resonance. Meth Enzymol 338:82-111
    • (2001) Meth Enzymol , vol.338 , pp. 82-111
    • Lí, K.1
  • 116
    • 58149365834 scopus 로고
    • Adiabatic pulses for wideband inversion and broadband decoupling
    • Kupce li, Freeman R (1995) Adiabatic Pulses for wideband inversion and broadband decoupling. J Magn Reson A115:273-276
    • (1995) J Magn Reson , vol.A115 , pp. 273-276
    • Li, K.1    Freeman, R.2
  • 117
    • 20444481878 scopus 로고    scopus 로고
    • Optimized adiabatic pulses for wideband spin inversion
    • Kupce ii, Freeman R (1996) Optimized adiabatic pulses for wideband spin inversion. J Magn Reson A118:299-303
    • (1996) J Magn Reson , vol.A118 , pp. 299-303
    • Ii, K.1    Freeman, R.2
  • 118
    • 0021114895 scopus 로고
    • Application of phase sensitive two-dimensional correlated spectroscopy (Cosy) for measurements of 1h-1h spin-spin coupling constants in proteins
    • Marion D, Wuthrich K (1983) Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins. Biochem Biophys Res Comm 113:967-974
    • (1983) Biochem Biophys Res Comm , vol.113 , pp. 967-974
    • Marion, D.1    Wuthrich, K.2
  • 119
    • 0342976767 scopus 로고
    • Improved solvent suppression in one- and two-dimensional nmr spectra by convolution of time-domain data
    • Marion D, Ikura M, Bax A (1989a) Improved solvent suppression in one- and two-dimensional NMR spectra by convolution of time-domain data. J Magn Reson 84:425-430
    • (1989) J Magn Reson , vol.84 , pp. 425-430
    • Marion, D.1    Ikura, M.2    Bax, A.3
  • 120
    • 45249127991 scopus 로고
    • Rapid recording of 2d nmr spectra without phase cycling. Application to the study of hydrogen exchange in proteins
    • Marion D, Ikura M, Tschudin R, Bax A (1989b) Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins. J Magn Reson 85:393-399
    • (1989) J Magn Reson , vol.85 , pp. 393-399
    • Marion, D.1    Ikura, M.2    Tschudin, R.3    Bax, A.4
  • 121
  • 122
    • 23044533626 scopus 로고    scopus 로고
    • Adiabatic radiofrequency pulse forms in biomedical nuclear magnetic resonance
    • Norris D (2002) Adiabatic radiofrequency pulse forms in biomedical nuclear magnetic resonance. Concepts Magn Reson 14:89-101
    • (2002) Concepts Magn Reson , vol.14 , pp. 89-101
    • Norris, D.1
  • 123
    • 46149136737 scopus 로고
    • Origin of x2 and x2 ridges in 2d nmr spectra and procedures for suppression
    • Otting G, Widmer H, Wagner G, Wuthrich K (1986) Origin of x2 and x2 ridges in 2D NMR spectra and procedures for suppression. J Magn Reson 66:187-193
    • (1986) J Magn Reson , vol.66 , pp. 187-193
    • Otting, G.1    Widmer, H.2    Wagner, G.3    Wuthrich, K.4
  • 124
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum nmr spectroscopy of aqueous solutions
    • Piotto M, Saudek V, Sklenar V (1992) Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J Biomol NMR 2:661-665
    • (1992) J Biomol NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 125
    • 33845555707 scopus 로고
    • Exchangeable proton nmr without base-line distorsion, using new strong-pulse sequences
    • Plateau P, Guíéron M (1982) Exchangeable proton NMR without base-line distorsion, using new strong-pulse sequences. J AM Chem Soc 104:7310-7311
    • (1982) J AM Chem Soc , vol.104 , pp. 7310-7311
    • Plateau, P.1    Guíéron, M.2
  • 126
    • 49549139089 scopus 로고
    • Dynamic range in fourier transform proton magnetic resonance
    • Redfield AG, Kunz SD, Ralph EK (1975) Dynamic range in Fourier transform proton magnetic resonance. J Magn Reson 19:114-117
    • (1975) J Magn Reson , vol.19 , pp. 114-117
    • Redfield, A.G.1    Kunz, S.D.2    Ralph, E.K.3
  • 127
    • 0000492963 scopus 로고
    • Broadband homonuclear cross polarization in 2d N.M.R. Using dipsi-2
    • Rucker SP, Shaka AJ (1989) Broadband homonuclear cross polarization in 2D N.M.R. Using DIPSI-2. Mol Phys 68:509-517
    • (1989) Mol Phys , vol.68 , pp. 509-517
    • Rucker, S.P.1    Shaka, A.J.2
  • 128
    • 45449123980 scopus 로고
    • Iterative schemes for bilinear operators; application to spin decoupling
    • Shaka AJ, Lee CJ, Pines A (1988) Iterative schemes for bilinear operators; application to spin decoupling. J Magn Reson 77:274-293
    • (1988) J Magn Reson , vol.77 , pp. 274-293
    • Shaka, A.J.1    Lee, C.J.2    Pines, A.3
  • 129
    • 48749144559 scopus 로고
    • Evaluation of a new broadband decoupling sequence: Waltz-16
    • Shaka AJ, Keeler J, Freeman R (1983) Evaluation of a new broadband decoupling sequence: WALTZ-16. J Magn Reson 53:313-340
    • (1983) J Magn Reson , vol.53 , pp. 313-340
    • Shaka, A.J.1    Keeler, J.2    Freeman, R.3
  • 130
    • 13444269041 scopus 로고
    • Computer-optimized decoupling scheme for wideband applications and low-level operation
    • Shaka AJ, Barker PB, Freeman R (1985) Computer-optimized decoupling scheme for wideband applications and low-level operation. J Magn Reson 64:547-552
    • (1985) J Magn Reson , vol.64 , pp. 547-552
    • Shaka, A.J.1    Barker, P.B.2    Freeman, R.3
  • 131
    • 2642628181 scopus 로고
    • A two-dimensional nuclear overhauser experiment with pure absorption phase in four quadrants
    • States J, Haberkorn RA, Ruben DJ (1982) A two-dimensional nuclear overhauser experiment with pure absorption phase in four quadrants. J Magn Reson 48:286-292
    • (1982) J Magn Reson , vol.48 , pp. 286-292
    • States, J.1    Haberkorn, R.A.2    Ruben, D.J.3
  • 132
    • 0000842145 scopus 로고    scopus 로고
    • Improved performance of frequency-swept pulses using offsetindependent adiabaticity
    • Tannus A, Garwood M (1996) Improved performance of frequency-swept pulses using offsetindependent adiabaticity. J Magn Reson A120:133-137
    • (1996) J Magn Reson , vol.A120 , pp. 133-137
    • Tannus, A.1    Garwood, M.2
  • 133
    • 0009273439 scopus 로고
    • User-friendly selective pulses
    • Xu P, Wu XL, Freeman R (1992) User-friendly selective pulses. J Magn Reson 99:308-322
    • (1992) J Magn Reson , vol.99 , pp. 308-322
    • Xu, P.1    Wu, X.L.2    Freeman, R.3
  • 134
    • 0000517056 scopus 로고
    • Improved linear prediction for truncated signals of known phase
    • Zhu G, Bax A (1990) Improved linear prediction for truncated signals of known phase. J Magn Reson 90:405-410
    • (1990) J Magn Reson , vol.90 , pp. 405-410
    • Zhu, G.1    Bax, A.2
  • 135
    • 0028472014 scopus 로고
    • Heteronuclear-correlation nmr spectroscopy with simultaneous isotope filtration, quadrature detection, and sensitivity enhancement using z rotations
    • Akke M, Carr PA, Palmer AG (1994) Heteronuclear-correlation NMR spectroscopy with simultaneous isotope filtration, quadrature detection, and sensitivity enhancement using z rotations. J Magn Reson B104:298-302
    • (1994) J Magn Reson , vol.B104 , pp. 298-302
    • Akke, M.1    Carr, P.A.2    Palmer, A.G.3
  • 136
    • 44949288628 scopus 로고
    • 1h-1h correlation via isotropic mixing of 13c magnetization, a new three-dimensional approach for assigning 1h and 13c spectra of 13c-enriched proteins
    • Bax A, Clore GM, Gronenborn AM (1990a) 1H-1H correlation via isotropic mixing of 13C magnetization, a new three-dimensional approach for assigning 1H and 13C spectra of 13C-enriched proteins. J Magn Reson 88:425-431
    • (1990) J Magn Reson , vol.88 , pp. 425-431
    • Bax, A.1    Clore, G.M.2    Gronenborn, A.M.3
  • 137
    • 45149138663 scopus 로고
    • Comparison of different modes of twodimensional reverse-correlation nmr for the study of proteins
    • Bax A, Ikura M, Kay LE, Torchia DA, Tschudin R (1990b) Comparison of different modes of twodimensional reverse-correlation NMR for the study of proteins. J Magn Reson 86:304-318
    • (1990) J Magn Reson , vol.86 , pp. 304-318
    • Bax, A.1    Ikura, M.2    Kay, L.E.3    Torchia, D.A.4    Tschudin, R.5
  • 138
    • 0000195671 scopus 로고
    • Natural abundance nitrogen-15 nmr by enhanced heteronuclear spectroscopy
    • Bodenhausen G, Ruben DJ (1980) Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy. Chem Phys Lett 69:185-189
    • (1980) Chem Phys Lett , vol.69 , pp. 185-189
    • Bodenhausen, G.1    Ruben, D.J.2
  • 139
    • 44949282610 scopus 로고
    • Sensitivity improvement in proton-detected two-dimensional heteronuclear relay spectroscopy
    • Cavanagh J, Palmer AG III, Wright PE, Rance M (1991a) Sensitivity improvement in proton-detected two-dimensional heteronuclear relay spectroscopy. J Magn Reson 91:429-436
    • (1991) J Magn Reson , vol.91 , pp. 429-436
    • Cavanagh, J.1    Palmer, A.2    Wright, P.E.3    Rance, M.4
  • 140
    • 67049140677 scopus 로고
    • Sensitivity-enhanced nmr techniques for the study of biomolecules
    • Cavanagh J, Rance M (1993) Sensitivity-enhanced NMR techniques for the study of biomolecules. Annu Rep NMR Spectros 27:1-58
    • (1993) Annu Rep NMR Spectros , vol.27 , pp. 1-58
    • Cavanagh, J.1    Rance, M.2
  • 141
    • 0002848358 scopus 로고
    • A constant-time three-dimensional triple-resonance pulse scheme to correlate intraresidue 1hn, 15n, and 13c' chemical shifts in 15n—13c-labelled proteins
    • Clubb RT, Thanabal V, Wagner G (1992) A constant-time three-dimensional triple-resonance pulse scheme to correlate intraresidue 1HN, 15N, and 13C' chemical shifts in 15N—13C-labelled proteins. J Magn Reson 97:213-217
    • (1992) J Magn Reson , vol.97 , pp. 213-217
    • Clubb, R.T.1    Thanabal, V.2    Wagner, G.3
  • 142
    • 0001106617 scopus 로고
    • Selective decoupling
    • Coy MA, Mueller L (1993) Selective decoupling. J Magn Reson A101:122-130
    • (1993) J Magn Reson , vol.A101 , pp. 122-130
    • Coy, M.A.1    Mueller, L.2
  • 145
    • 11544304059 scopus 로고
    • Gaussian pulse cascades: New analytical functions for rectangular selective inversion and in-phase excitation in nmr
    • Emsley L, Bodenhausen G (1990) Gaussian pulse cascades: new analytical functions for rectangular selective inversion and in-phase excitation in NMR. Chem Phys Lett 165:469-476
    • (1990) Chem Phys Lett , vol.165 , pp. 469-476
    • Emsley, L.1    Bodenhausen, G.2
  • 146
    • 58149362646 scopus 로고
    • Sequential protein backbone resonance assignments using an improved 3d-hn(Ca)co pulse scheme
    • Engelke J, Ruterjans H (1995) Sequential protein backbone resonance assignments using an improved 3D-HN(CA)CO pulse scheme. J Magn Reson B109:318-322
    • (1995) J Magn Reson , vol.B109 , pp. 318-322
    • Engelke, J.1    Ruterjans, H.2
  • 148
    • 0025322418 scopus 로고
    • 2d and 3d nmr spectroscopy employing carbon-13/carbon-13 magnetization transfer by isotropic mixing. Spin system identification in large proteins
    • Fesik SW, Eaton HL, Olejniczak ET, Zuiderweg ERP, McIntosh LP, Dahlquist FW (1990) 2D and 3D NMR spectroscopy employing carbon-13/carbon-13 magnetization transfer by isotropic mixing. Spin system identification in large proteins. J Am Chem Soc 112:886-888
    • (1990) J am Chem Soc , vol.112 , pp. 886-888
    • Fesik, S.W.1    Eaton, H.L.2    Olejniczak, E.T.3    Zuiderweg, E.4    McIntosh, L.P.5    Dahlquist, F.W.6
  • 149
    • 44949280676 scopus 로고
    • Band-selective radiofrequency pulses
    • Geen H, Freeman R (1991) Band-selective radiofrequency pulses. J Magn Reson 93:93-141
    • (1991) J Magn Reson , vol.93 , pp. 93-141
    • Geen, H.1    Freeman, R.2
  • 150
    • 0000996315 scopus 로고
    • Chemical shift and electric field gradient tensors for the amide and carboxyl hydrogens in the model peptide n-acetyl-d, l-valine. Single-crystal deuterium nmr study
    • Gerald RE, Bernhard T, Haegberlen U, Rendell J, Opella S (1993) Chemical shift and electric field gradient tensors for the amide and carboxyl hydrogens in the model peptide N-acetyl-D, L-valine. Single-crystal deuterium NMR study. J Am Chem Soc 115:777-782
    • (1993) J am Chem Soc , vol.115 , pp. 777-782
    • Gerald, R.E.1    Bernhard, T.2    Haegberlen, U.3    Rendell, J.4    Opella, S.5
  • 151
    • 44049109615 scopus 로고
    • An efficient experiment for sequential backbone assignment of medium-sized isotopically enriched proteins
    • Grzesiek S, Bax A (1992a) An efficient experiment for sequential backbone assignment of medium-sized isotopically enriched proteins. J Magn Reson 99:201-207
    • (1992) J Magn Reson , vol.99 , pp. 201-207
    • Grzesiek, S.1    Bax, A.2
  • 152
    • 9444245493 scopus 로고
    • Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance nmr
    • Grzesiek S, Bax A (1992b) Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR. J Am Chem Soc 114:6291-6293
    • (1992) J am Chem Soc , vol.114 , pp. 6291-6293
    • Grzesiek, S.1    Bax, A.2
  • 153
    • 0027787894 scopus 로고
    • The importance of not saturating water in protein nmr. Application to sensitivity enhancement and noe measurements
    • Grzesiek S, Bax A (1993) The importance of not saturating water in protein NMR. Application to sensitivity enhancement and NOE measurements. J Am Chem Soc 115:12593-12594
    • (1993) J am Chem Soc , vol.115 , pp. 12593-12594
    • Grzesiek, S.1    Bax, A.2
  • 154
    • 43949175202 scopus 로고
    • Correlation of backbone amide and aliphatic side-chain resonances in 13c/15n-enriched proteins by isotropic mixing of 13c magnetization
    • Grzesiek S, Anglister J, Bax A (1993) Correlation of backbone amide and aliphatic side-chain resonances in 13C/15N-enriched proteins by isotropic mixing of 13C magnetization. J Magn Reson B101:114-119
    • (1993) J Magn Reson , vol.B101 , pp. 114-119
    • Grzesiek, S.1    Anglister, J.2    Bax, A.3
  • 155
    • 0344620689 scopus 로고
    • Gradient-enhanced proton-detected heteronuclear multiple-quantum coherence spectroscopy
    • Hurd RE, John BK (1991) Gradient-enhanced proton-detected heteronuclear multiple-quantum coherence spectroscopy. J Magn Reson 91:648-653
    • (1991) J Magn Reson , vol.91 , pp. 648-653
    • Hurd, R.E.1    John, B.K.2
  • 156
    • 0025341339 scopus 로고
    • A novel approach for sequential assignment of proton, carbon-13, and nitrogen-15 spectra of larger proteins: Heteronuclear triple-resonance three-dimensional nmr spectroscopy. Application to calmodulin
    • Ikura M, Kay LE, Bax A (1990a) A novel approach for sequential assignment of proton, carbon-13, and nitrogen-15 spectra of larger proteins: heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin. Biochemistry 29:4659-4667
    • (1990) Biochemistry , vol.29 , pp. 4659-4667
    • Ikura, M.1    Kay, L.E.2    Bax, A.3
  • 157
    • 0025276930 scopus 로고
    • Heteronuclear 3d nmr and isotopic labeling of calmodulin: Towards the complete assignment of the 1h nmr spectrum
    • Ikura M, Marion D, Kay LE, Shih H, Krinks M, Klee CB, Bax A (1990b) Heteronuclear 3D NMR and isotopic labeling of calmodulin: towards the complete assignment of the 1H NMR spectrum. Biochem Pharmacol 40:153-160
    • (1990) Biochem Pharmacol , vol.40 , pp. 153-160
    • Ikura, M.1    Marion, D.2    Kay, L.E.3    Shih, H.4    Krinks, M.5    Klee, C.B.6    Bax, A.7
  • 158
    • 84955054537 scopus 로고    scopus 로고
    • Johnson BA (2004) http://onemoonscientific.com/nmrview/
    • (2004)
    • Johnson, B.A.1
  • 159
    • 44949291986 scopus 로고
    • Three-dimensional triple-resonance nmr spectroscopy of isotopically enriched proteins
    • Kay LE, Ikura M, Tschudin R, Bax A (1990) Three-dimensional triple-resonance NMR spectroscopy of isotopically enriched proteins. J Magn Reson 89:496-514
    • (1990) J Magn Reson , vol.89 , pp. 496-514
    • Kay, L.E.1    Ikura, M.2    Tschudin, R.3    Bax, A.4
  • 160
    • 0000647777 scopus 로고
    • Four-dimensional heteronuclear triple-resonance nmr of isotopically enriched proteins for sequential assignment of backbone atoms
    • Kay LE, Ikura M, Zhu G, Bax A (1991) Four-dimensional heteronuclear triple-resonance NMR of isotopically enriched proteins for sequential assignment of backbone atoms. J Magn Reson 91:422-428
    • (1991) J Magn Reson , vol.91 , pp. 422-428
    • Kay, L.E.1    Ikura, M.2    Zhu, G.3    Bax, A.4
  • 161
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • Kay LE, Keifer P, Saarinen T (1992) Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J Am Chem Soc 114:10663-10665
    • (1992) J am Chem Soc , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 162
    • 34447505016 scopus 로고
    • Enhanced-sensitivity triple-resonance spectroscopy with minimal h2o saturation
    • Kay LE, Xu GY, Yamazaki T (1994) Enhanced-sensitivity triple-resonance spectroscopy with minimal H2O saturation. J Magn Reson A109:129-133
    • (1994) J Magn Reson , vol.A109 , pp. 129-133
    • Kay, L.E.1    Xu, G.Y.2    Yamazaki, T.3
  • 163
    • 0033370719 scopus 로고    scopus 로고
    • A 4d trosy-based pulse scheme for correlating 1hni,15ni,13cai,13c'i—1 chemical shifts in high molecular weight, 15n,13c, 2h labeled proteins
    • Konrat R, Yang D, Kay LE (1999) A 4D TROSY-based pulse scheme for correlating 1HNi,15Ni,13Cai,13C'i—1 chemical shifts in high molecular weight, 15N,13C, 2H labeled proteins. J Biomol NMR 15:309-313
    • (1999) J Biomol NMR , vol.15 , pp. 309-313
    • Konrat, R.1    Yang, D.2    Kay, L.E.3
  • 164
    • 0027568083 scopus 로고
    • A general method for assigning nmr spectra of denatured proteins using 3d hc(Co)nh-tocsy triple resonance experiments
    • Logan TM, Olejniczak ET, Xu RX, Fesik SW (1993) A general method for assigning NMR spectra of denatured proteins using 3D HC(CO)NH-TOCSY triple resonance experiments. J Biomol NMR 3:225-231
    • (1993) J Biomol NMR , vol.3 , pp. 225-231
    • Logan, T.M.1    Olejniczak, E.T.2    Xu, R.X.3    Fesik, S.W.4
  • 165
    • 0001590904 scopus 로고
    • An hccnh triple-resonance experiment using carbon-13 isotropic mixing for correlating backbone amide and side-chain aliphatic resonances in isotopically enriched proteins
    • Lyons BA, Montelione GT (1993) An HCCNH triple-resonance experiment using carbon-13 isotropic mixing for correlating backbone amide and side-chain aliphatic resonances in isotopically enriched proteins. J Magn Reson B101:206-209
    • (1993) J Magn Reson , vol.B101 , pp. 206-209
    • Lyons, B.A.1    Montelione, G.T.2
  • 166
    • 0000733526 scopus 로고
    • Sensitivity improvement in 2d and 3d hcch spectroscopy using heteronuclear cross-polarization
    • Majumdar A, Wang H, Morshauser RC, Zuiderweg ERP (1993) Sensitivity improvement in 2D and 3D HCCH spectroscopy using heteronuclear cross-polarization. J Biomol NMR 4:387-397
    • (1993) J Biomol NMR , vol.4 , pp. 387-397
    • Majumdar, A.1    Wang, H.2    Morshauser, R.C.3    Zuiderweg, E.4
  • 168
    • 0030265965 scopus 로고    scopus 로고
    • Increased sensitivity in hnca and hn(Co)ca experiments by selective cpdecoupling
    • Matsuo H, Kupce E, Li H, Wagner G (1996) Increased sensitivity in HNCA and HN(CO)CA experiments by selective CpDecoupling. J Magn Reson B113:91-96
    • (1996) J Magn Reson , vol.B113 , pp. 91-96
    • Matsuo, H.1    Kupce, E.2    Li, H.3    Wagner, G.4
  • 169
    • 84890928276 scopus 로고
    • An efficient triple resonance experiment using carbon-13 isotropic mixing for determining sequence-specific resonance assignments of isotopically-enriched proteins
    • Montelione GT, Lyons BA, Emerson SD, Tashiro M (1992) An efficient triple resonance experiment using carbon-13 isotropic mixing for determining sequence-specific resonance assignments of isotopically-enriched proteins. J Am Chem Soc 114:10974-10975
    • (1992) J am Chem Soc , vol.114 , pp. 10974-10975
    • Montelione, G.T.1    Lyons, B.A.2    Emerson, S.D.3    Tashiro, M.4
  • 170
    • 0002616982 scopus 로고
    • Sensitivity enhanced detection of weak nuclei using heteronuclear multiple quantum coherence
    • Mueller L (1979) Sensitivity enhanced detection of weak nuclei using heteronuclear multiple quantum coherence. J Am Chem Soc 101:4481-4484
    • (1979) J am Chem Soc , vol.101 , pp. 4481-4484
    • Mueller, L.1
  • 171
    • 0000045562 scopus 로고
    • An enhanced-sensitivity pure absorption gradient 4d 15n, 13c-edited noesy experiment
    • Muhandiram DR, Xu GY, Kay LE (1993) An enhanced-sensitivity pure absorption gradient 4D 15N, 13C-edited NOESY experiment. J Biomol NMR 3:463-470
    • (1993) J Biomol NMR , vol.3 , pp. 463-470
    • Muhandiram, D.R.1    Xu, G.Y.2    Kay, L.E.3
  • 172
    • 0001689741 scopus 로고
    • Gradient-enhanced triple-resonance three-dimensional nmr experiments with improved sensitivity
    • Muhandiram DR, Kay LE (1994) Gradient-enhanced triple-resonance three-dimensional NMR experiments with improved sensitivity. J Magn Reson B103:203-216
    • (1994) J Magn Reson , vol.B103 , pp. 203-216
    • Muhandiram, D.R.1    Kay, L.E.2
  • 173
    • 0026948921 scopus 로고
    • A 4d hcch-tocsy experiment for assigning the side chain1h and13c resonances of proteins
    • Olejniczak ET, Xu RX, Fesik SW (1992) A 4D HCCH-TOCSY experiment for assigning the side chain1H and13C resonances of proteins. J Biomol NMR 2:655-659
    • (1992) J Biomol NMR , vol.2 , pp. 655-659
    • Olejniczak, E.T.1    Xu, R.X.2    Fesik, S.W.3
  • 174
    • 0032042263 scopus 로고    scopus 로고
    • Measurement of j and dipolar couplings from simplified twodimensional nmr spectra
    • Ottiger M, Delaglio F, Bax A (1998) Measurement of J and dipolar couplings from simplified twodimensional NMR spectra. J Magn Reson 131:373-378
    • (1998) J Magn Reson , vol.131 , pp. 373-378
    • Ottiger, M.1    Delaglio, F.2    Bax, A.3
  • 175
    • 44949282610 scopus 로고
    • Sensitivity improvement in proton-detected two-dimensional heteronuclear relay spectroscopy
    • Cavanagh J, Palmer AG III, Wright PE, Rance M (1991b) Sensitivity improvement in proton-detected two-dimensional heteronuclear relay spectroscopy. J Magn Reson 91:429-436
    • (1991) J Magn Reson , vol.91 , pp. 429-436
    • Cavanagh, J.1    Palmer, A.2    Wright, P.E.3    Rance, M.4
  • 176
    • 0030612833 scopus 로고    scopus 로고
    • Attenuated t2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to nmr structures of very large biological macromolecules in solution
    • Pervushin K, Riek R, Wider G, Wuthrich K (1997) Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution. Proc Natl Acad Sci USA 94:12366-12371
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 12366-12371
    • Pervushin, K.1    Riek, R.2    Wider, G.3    Wuthrich, K.4
  • 177
    • 0033578363 scopus 로고    scopus 로고
    • The 3d noesy-[1h,15n,1h]-zq-trosy nmr experiment with diagonal peak suppression
    • Pervushin K, Wider G, Riek R, Wuthrich K (1999) The 3D NOESY-[1H,15N,1H]-ZQ-TROSY NMR experiment with diagonal peak suppression. Proc Natl Acad Sci USA 96:9607-9612
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 9607-9612
    • Pervushin, K.1    Wider, G.2    Riek, R.3    Wuthrich, K.4
  • 178
    • 58149363787 scopus 로고
    • Novel pulse sequences with sensitivity enhancement for in-phase coherence transfer employing pulsed field gradients
    • Sattler M, Schmidt P, Scleucher J, Schedletzky O, Glaser SJ, Griesinger C (1995a) Novel pulse sequences with sensitivity enhancement for in-phase coherence transfer employing pulsed field gradients. J Magn Reson B108:235-242
    • (1995) J Magn Reson , vol.B108 , pp. 235-242
    • Sattler, M.1    Schmidt, P.2    Scleucher, J.3    Schedletzky, O.4    Glaser, S.J.5    Griesinger, C.6
  • 179
    • 34249757083 scopus 로고
    • Novel strategies for sensitivity enhancement in heteronuclear multi—dimensional nmr experiments employing pulsed field gradients
    • Sattler M, Schwedinger M, Schleucher J, Griesinger C (1995b) Novel strategies for sensitivity enhancement in heteronuclear multi—dimensional NMR experiments employing pulsed field gradients. J Biomol NMR 6:11-22
    • (1995) J Biomol NMR , vol.6 , pp. 11-22
    • Sattler, M.1    Schwedinger, M.2    Schleucher, J.3    Griesinger, C.4
  • 182
    • 0001164631 scopus 로고
    • The in situ determination of the 15n chemical-shift tensor orientation in a polypeptide
    • Teng Q, Cross TA (1989) The in situ determination of the 15N chemical-shift tensor orientation in a polypeptide. J Magn Reson 85:439-447
    • (1989) J Magn Reson , vol.85 , pp. 439-447
    • Teng, Q.1    Cross, T.A.2
  • 183
    • 0000112965 scopus 로고    scopus 로고
    • Isotope-filtered nmr methods for the study of biomolecular structure and interactions
    • Breeze A (2000) Isotope-filtered NMR methods for the study of biomolecular structure and interactions. Prog Nucl Magn Reson Spectrosc 36:323-372
    • (2000) Prog Nucl Magn Reson Spectrosc , vol.36 , pp. 323-372
    • Breeze, A.1
  • 184
    • 0015861774 scopus 로고
    • Relationship between the inhibition constant (Ki) and the concentration of inhibitor which causes 50 per cent inhibition (i50) of an enzymatic reaction
    • Cheng Y, Prusoff WH (1973) Relationship between the inhibition constant (KI) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction. Biochem Pharmacol 22:3099-3108
    • (1973) Biochem Pharmacol , vol.22 , pp. 3099-3108
    • Cheng, Y.1    Prusoff, W.H.2
  • 186
    • 0000393431 scopus 로고
    • Theory and applications of the transferred nuclear overhauser effect to the study of the conformations of small ligands bound to proteins
    • Clore GM, Gronenborn AM (1982) Theory and applications of the transferred nuclear overhauser effect to the study of the conformations of small ligands bound to proteins. J Magn Reson 48:402-417
    • (1982) J Magn Reson , vol.48 , pp. 402-417
    • Clore, G.M.1    Gronenborn, A.M.2
  • 187
    • 0030782658 scopus 로고    scopus 로고
    • Analysis of biofluids and chemical mixtures in non-deuterated solvents with 1h diffusion-weighted pfg phase-sensitive double-quantum nmr spectroscopy
    • Dalvit C, Bohlen JM (1997) Analysis of biofluids and chemical mixtures in non-deuterated solvents with 1H diffusion-weighted PFG phase-sensitive double-quantum NMR spectroscopy. Nmr Biomed 10:285-291
    • (1997) NMR Biomed , vol.10 , pp. 285-291
    • Dalvit, C.1    Bohlen, J.M.2
  • 189
    • 0030854195 scopus 로고    scopus 로고
    • Leukocyte adhesion: Cd11/cd18 integrins and intercellular adhesion molecules
    • Gahmberg CG (1997) Leukocyte adhesion: CD11/CD18 integrins and intercellular adhesion molecules. Curr Opin Cell Biol 9:643-650
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 643-650
    • Gahmberg, C.G.1
  • 190
    • 0001147165 scopus 로고
    • An improved method for selectively observing protons attached to 12c in the presence of 1h-13c spin pairs
    • Gemmecker G, Olejniczak ET, Fesik S (1992) An improved method for selectively observing protons attached to 12C in the presence of 1H-13C spin pairs. J Magn Reson 96:199-204
    • (1992) J Magn Reson , vol.96 , pp. 199-204
    • Gemmecker, G.1    Olejniczak, E.T.2    Fesik, S.3
  • 194
    • 0347359145 scopus 로고    scopus 로고
    • Diffusion ordered nuclear magnetic resonance spectroscopy: Principles and applications
    • Johnson CS (1999) Diffusion ordered nuclear magnetic resonance spectroscopy: principles and applications. Prog Nucl Magn Reson Spectrosc 34:203-256
    • (1999) Prog Nucl Magn Reson Spectrosc , vol.34 , pp. 203-256
    • Johnson, C.S.1
  • 195
    • 0033538283 scopus 로고    scopus 로고
    • Detecting binding affinity to immobilized receptor proteins in compound libraries by hr-mas std nmr
    • Klein J, Meinecke R, Mayer M, Meyer B (1999) Detecting binding affinity to immobilized receptor proteins in compound libraries by HR-MAS STD NMR. J Am Chem Soc 121:5336-5337
    • (1999) J am Chem Soc , vol.121 , pp. 5336-5337
    • Klein, J.1    Meinecke, R.2    Mayer, M.3    Meyer, B.4
  • 196
    • 0035848575 scopus 로고    scopus 로고
    • Novel p-arylthio cinnamides as antagonists of leukocyte function-associated antigen-1/intracellular adhesion molecule-1 interaction. 2. Mechanism of inhibition and structure-based improvement of pharmaceutical properties
    • Liu G, Huth JR, Olejniczak ET, Mendoza R, DeVries P, Leitza S, Reilly EB, Okasinski GF, Fesik SW, von Geldern TW (2001) Novel p-arylthio cinnamides as antagonists of leukocyte function-associated antigen-1/intracellular adhesion molecule-1 interaction. 2. Mechanism of inhibition and structure-based improvement of pharmaceutical properties. J Med Chem 44:1202-1210
    • (2001) J Med Chem , vol.44 , pp. 1202-1210
    • Liu, G.1    Huth, J.R.2    Olejniczak, E.T.3    Mendoza, R.4    DeVries, P.5    Leitza, S.6    Reilly, E.B.7    Okasinski, G.F.8    Fesik, S.W.9    Von Geldern, T.W.10
  • 197
    • 0034687234 scopus 로고    scopus 로고
    • Discovery of novel p-arylthio cinnamides as antagonists of leukocyte function-associated antigen-1/intracellular adhesion molecule-1 interaction. 1. Identification of an additional binding pocket based on an anilino diaryl sulfide lead
    • Liu G, Link JT, Pei Z, Reilly EB, Leitza S, Ngygen B, Marsh KC, Okasinski GF, von Geldern TW, Ormes M, Fowler K, Gallatin M (2000) Discovery of novel p-arylthio cinnamides as antagonists of leukocyte function-associated antigen-1/intracellular adhesion molecule-1 interaction. 1. Identification of an additional binding pocket based on an anilino diaryl sulfide lead. J Med Chem 43:4025-4040
    • (2000) J Med Chem , vol.43 , pp. 4025-4040
    • Liu, G.1    Link, J.T.2    Pei, Z.3    Reilly, E.B.4    Leitza, S.5    Ngygen, B.6    Marsh, K.C.7    Okasinski, G.F.8    Von Geldern, T.W.9    Ormes, M.10    Fowler, K.11    Gallatin, M.12
  • 198
    • 0033553844 scopus 로고    scopus 로고
    • Characterization of ligand binding by saturation transfer difference nmr spectroscopy
    • Mayer M, Meyer B (1999) Characterization of ligand binding by saturation transfer difference NMR spectroscopy. Angew Chem Int Ed 38:1784-1788
    • (1999) Angew Chem Int Ed , vol.38 , pp. 1784-1788
    • Mayer, M.1    Meyer, B.2
  • 199
    • 0034823890 scopus 로고    scopus 로고
    • Group epitope mapping by saturation transfer difference nmr to identify segments of a ligand in direct contact with a protein receptor
    • Mayer M, Meyer B (2001) Group epitope mapping by saturation transfer difference NMR to identify segments of a ligand in direct contact with a protein receptor. J Am Chem Soc 123:6108-6117
    • (2001) J am Chem Soc , vol.123 , pp. 6108-6117
    • Mayer, M.1    Meyer, B.2
  • 200
    • 0030917461 scopus 로고    scopus 로고
    • Screening mixtures for biological activity by nmr
    • Meyer B, Weimar T, Peters T (1997) Screening mixtures for biological activity by NMR. Eur J Biochem 246:705-709
    • (1997) Eur J Biochem , vol.246 , pp. 705-709
    • Meyer, B.1    Weimar, T.2    Peters, T.3
  • 201
    • 0002437481 scopus 로고    scopus 로고
    • Chemical composition of escherichia coli
    • Neidhardt FC, Curtiss III R, Ingraham JL, Lin ECC, Low KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, Umbarger HE, 2nd edn. American Society for Microbiology, Washington, DC
    • Neidhardt FC, Umbarger HE (1996) Chemical composition of Escherichia coli. In: Neidhardt FC, Curtiss III R, Ingraham JL, Lin ECC, Low KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, Umbarger HE (eds) Escherichia coli and Salmonella: cellular and molecular biology, 2nd edn. American Society for Microbiology, Washington, DC, p 13
    • (1996) Escherichia Coli and Salmonella: Cellular and molecular biology , pp. 13
    • Neidhardt, F.C.1    Umbarger, H.E.2
  • 202
    • 0028728698 scopus 로고
    • Recent developments in transferred noe methods
    • Ni F (1994) Recent developments in transferred NOE methods. Prog Nucl Magn Reson Spectrosc 26:517-606
    • (1994) Prog Nucl Magn Reson Spectrosc , vol.26 , pp. 517-606
    • Ni, F.1
  • 203
    • 0003161755 scopus 로고
    • Effect of nonrectangular field gradient pulses in the stejskal and tanner (Diffusion) pulse sequence
    • Price WS, Kuchel PW (1991) Effect of nonrectangular field gradient pulses in the stejskal and tanner (diffusion) pulse sequence. J Magn Reson 94:133-139
    • (1991) J Magn Reson , vol.94 , pp. 133-139
    • Price, W.S.1    Kuchel, P.W.2
  • 204
    • 0029836953 scopus 로고    scopus 로고
    • Discovering high-affinity ligands for proteins: Sar by nmr
    • Shuker SB, Hajduk PJ, Meadows RP, Fesik SW (1996) Discovering high-affinity ligands for proteins: SAR by NMR. Science 274:1531-1534
    • (1996) Science , vol.274 , pp. 1531-1534
    • Shuker, S.B.1    Hajduk, P.J.2    Meadows, R.P.3    Fesik, S.W.4
  • 205
    • 0025098765 scopus 로고
    • Quantitation of muscle glycogen synthesis in normal subjects and subjects with non-insulin-dependent diabetes by 13c nuclear magnetic resonance spectroscopy
    • Shulman GI, Rothman DL, Jue T, Stein P, DeFronzo RA, Shulman RG (1990) Quantitation of muscle glycogen synthesis in normal subjects and subjects with non-insulin-dependent diabetes by 13C nuclear magnetic resonance spectroscopy. N Engl J Med 322:223-228
    • (1990) N Engl J Med , vol.322 , pp. 223-228
    • Shulman, G.I.1    Rothman, D.L.2    Jue, T.3    Stein, P.4    DeFronzo, R.A.5    Shulman, R.G.6
  • 207
    • 33646376290 scopus 로고
    • Spin diffusion measurements: Spin echoes in the presence of a time-dependent field gradient
    • Stejskal EO, Tanner JE (1965) Spin diffusion measurements: spin echoes in the presence of a time-dependent field gradient. J Chem Phys 42:288-292
    • (1965) J Chem Phys , vol.42 , pp. 288-292
    • Stejskal, E.O.1    Tanner, J.E.2
  • 208
    • 34047191652 scopus 로고
    • Fourier transform pulsed-gradient spin-echo studies of molecular diffusion
    • Stilbs P (1987) Fourier transform pulsed-gradient spin-echo studies of molecular diffusion. Prog Nucl Magn Reson Spectrosc 19:1-45
    • (1987) Prog Nucl Magn Reson Spectrosc , vol.19 , pp. 1-45
    • Stilbs, P.1
  • 209
    • 0026616869 scopus 로고
    • Validation of 13c nmr measurement of human skeletal muscle glycogen by direct biochemical assay of needle biopsy samples
    • Taylor R, Price TB, Rothman DL, Shulman RG, Shulman GI (1992) Validation of 13C NMR measurement of human skeletal muscle glycogen by direct biochemical assay of needle biopsy samples. Magn Reson Med 27:13-20
    • (1992) Magn Reson Med , vol.27 , pp. 13-20
    • Taylor, R.1    Price, T.B.2    Rothman, D.L.3    Shulman, R.G.4    Shulman, G.I.5
  • 210
    • 0030986445 scopus 로고    scopus 로고
    • Ribose biosynthesis and evidence for an alternative first step in the common aromatic amino acid pathway in methanococcus maripaludis
    • Tumbula DL, Teng Q, Bartlett MG, Whitman WB (1997) Ribose biosynthesis and evidence for an alternative first step in the common aromatic amino acid pathway in Methanococcus maripaludis. J Bacteriol 179:6010-6013
    • (1997) J Bacteriol , vol.179 , pp. 6010-6013
    • Tumbula, D.L.1    Teng, Q.2    Bartlett, M.G.3    Whitman, W.B.4
  • 211
    • 1842343256 scopus 로고
    • The distribution of c14 in the hexose phosphates and the effect of recycling in the pentose cycle
    • Wood HG, Katz J (1958) The distribution of C14 in the hexose phosphates and the effect of recycling in the pentose cycle. J Biol Chem 233:1279-1282
    • (1958) J Biol Chem , vol.233 , pp. 1279-1282
    • Wood, H.G.1    Katz, J.2
  • 212
    • 0028123664 scopus 로고
    • Pathway of glycogen metabolism in methanococcus maripaludis
    • Yu JP, Ladapo J, Whitman WB (1994) Pathway of glycogen metabolism in Methanococcus maripaludis. J Bacteriol 176:325-332
    • (1994) J Bacteriol , vol.176 , pp. 325-332
    • Yu, J.P.1    Ladapo, J.2    Whitman, W.B.3
  • 213
    • 0030808350 scopus 로고    scopus 로고
    • Methods for measurement of intermolecular noes by multinuclear nmr spectroscopy: Application to a bacteriophage 1 n-peptide/boxb rna complex
    • Zwahlen C, Legault P, Vincent SJF, Greenblatt J, Konrat R, Kay LE (1997) Methods for measurement of intermolecular NOEs by multinuclear NMR spectroscopy: application to a bacteriophage 1 N-peptide/boxB RNA complex. J Am Chem Soc 119:6711-6721
    • (1997) J am Chem Soc , vol.119 , pp. 6711-6721
    • Zwahlen, C.1    Legault, P.2    Vincent, S.3    Greenblatt, J.4    Konrat, R.5    Kay, L.E.6
  • 215
    • 0025339406 scopus 로고
    • Solution structure of phage.Lambda. Half-operator dna by use of nmr, restrained molecular dynamics, and noe-based refinement
    • Baleja JD, Pon RT, Sykes BD (1990) Solution structure of phage.lambda. Half-operator DNA by use of NMR, restrained molecular dynamics, and NOE-based refinement. Biochemistry 29:4828-4839
    • (1990) Biochemistry , vol.29 , pp. 4828-4839
    • Baleja, J.D.1    Pon, R.T.2    Sykes, B.D.3
  • 216
    • 0023339433 scopus 로고
    • Distance geometry and related methods for protein structure determination from nmr data
    • Braun W (1987) Distance geometry and related methods for protein structure determination from NMR data. Quart Rev Biophys 19:115-157
    • (1987) Quart Rev Biophys , vol.19 , pp. 115-157
    • Braun, W.1
  • 218
    • 0026597444 scopus 로고
    • Free r value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brlinger A (1992a) Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355:472-475
    • (1992) Nature , vol.355 , pp. 472-475
    • Brlinger, A.1
  • 221
    • 0031933143 scopus 로고    scopus 로고
    • Determining the structures of large proteins and protein complexes by nmr
    • Clore GM, Gronenborn AM (1998) Determining the structures of large proteins and protein complexes by NMR. Trends Biotech 16:22-34
    • (1998) Trends Biotech , vol.16 , pp. 22-34
    • Clore, G.M.1    Gronenborn, A.M.2
  • 222
    • 0023008905 scopus 로고
    • Application of molecular dynamics with interproton distance restraints to three-dimensional protein structure determination: A model study of crambin
    • Clore GM, Brlunger AT, Karplus M, Gronenborn AM (1986) Application of molecular dynamics with interproton distance restraints to three-dimensional protein structure determination: a model study of crambin. J Mol Biol 191:523-551
    • (1986) J Mol Biol , vol.191 , pp. 523-551
    • Clore, G.M.1    Brlunger, A.T.2    Karplus, M.3    Gronenborn, A.M.4
  • 224
    • 0037169646 scopus 로고    scopus 로고
    • Nmr dipolar couplings for the structure determination of biopolymers in solution
    • de Alba E, Tjandra N (2002) NMR dipolar couplings for the structure determination of biopolymers in solution. Prog Nucl Magn Reson Spectrosc 40:175-197
    • (2002) Prog Nucl Magn Reson Spectrosc , vol.40 , pp. 175-197
    • De Alba, E.1    Tjandra, N.2
  • 225
    • 0027308278 scopus 로고
    • Secondary and tertiary structural effects on protein nmr chemical shifts: An ab initio approach
    • de Dios AC, Pearson JG, Oldfield E (1993) Secondary and tertiary structural effects on protein NMR chemical shifts: an ab initio approach. Science 260:1491-1496
    • (1993) Science , vol.260 , pp. 1491-1496
    • De Dios, A.C.1    Pearson, J.G.2    Oldfield, E.3
  • 226
    • 0017805596 scopus 로고
    • Analysis of the 1h-nmr spectra of ferrichrome peptides. I. The non-amide protons
    • Demarco A, Llinas M, Wuthrich K (1978a) Analysis of the 1H-NMR spectra of ferrichrome peptides. I. The non-amide protons. Biopolymers 17:617-636
    • (1978) Biopolymers , vol.17 , pp. 617-636
    • Demarco, A.1    Llinas, M.2    Wuthrich, K.3
  • 227
    • 84985648219 scopus 로고
    • 1h-15n spin-spin couplings in alumichrome
    • Demarco A, Llinas M, Wuthrich K (1978b) 1H-15N Spin-spin couplings in alumichrome. Biopolymers 17:2727-2742
    • (1978) Biopolymers , vol.17 , pp. 2727-2742
    • Demarco, A.1    Llinas, M.2    Wuthrich, K.3
  • 228
    • 0026598960 scopus 로고
    • Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex
    • de Vos AM, Ultsch M, Kossiakoff AA (1992) Human growth hormone and extracellular domain of its receptor: crystal structure of the complex. Science 255:306-312
    • (1992) Science , vol.255 , pp. 306-312
    • De Vos, A.M.1    Ultsch, M.2    Kossiakoff, A.A.3
  • 229
    • 33847086368 scopus 로고
    • Torsion angles in the cystine bridge of oxytocin in aqueous solution. Measurements of circumjacent vicinal couplings between proton, carbon-13, and nitrogen-15
    • Fischman AJ, Live DH, Wyssbrod HR, Agosta WC, Cowbum D (1980) Torsion angles in the cystine bridge of oxytocin in aqueous solution. Measurements of circumjacent vicinal couplings between proton, carbon-13, and nitrogen-15. J Am Chem Soc 102:2533-2539
    • (1980) J am Chem Soc , vol.102 , pp. 2533-2539
    • Fischman, A.J.1    Live, D.H.2    Wyssbrod, H.R.3    Agosta, W.C.4    Cowbum, D.5
  • 230
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu G, Delagio F, Bax A (1999) Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J Biomol NMR 13:289-302, http://spin. Niddk.nih.gov/bax/software/TOLAS/info.html
    • (1999) J Biomol NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delagio, F.2    Bax, B.3
  • 231
    • 0025688812 scopus 로고
    • Solution structure studies of d(Ac)4.Cntdot.D(gt)4 via restrained molecular dynamics simulations with nmr constraints derived from two-dimensional noe and double-quantum-filtered cosy experiments
    • Gochin M, James TL (1990) Solution structure studies of d(AC)4.cntdot.d(GT)4 via restrained molecular dynamics simulations with NMR constraints derived from two-dimensional NOE and double-quantum-filtered COSY experiments. Biochemistry 29:11172-11180
    • (1990) Biochemistry , vol.29 , pp. 11172-11180
    • Gochin, M.1    James, T.L.2
  • 232
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for nmr structure calculation with the new program dyana
    • Giintert P, Mumenthaler C, Wuthrich K (1997) Torsion angle dynamics for NMR structure calculation with the new program Dyana. J Mol Biol 273:283-298
    • (1997) J Mol Biol , vol.273 , pp. 283-298
    • Giintert, P.1    Mumenthaler, C.2    Wuthrich, K.3
  • 233
    • 4344698912 scopus 로고    scopus 로고
    • Automated nmr protein structure calculation
    • Giintert P (2003) Automated NMR protein structure calculation. Prog Nucl Magn Reson Spectrosc 43:105-125
    • (2003) Prog Nucl Magn Reson Spectrosc , vol.43 , pp. 105-125
    • Giintert, P.1
  • 234
    • 0031714689 scopus 로고    scopus 로고
    • Structure calculation of biological macromolecules from nmr data
    • Guntert P (1998) Structure calculation of biological macromolecules from NMR data. Quart Rev Biophys 31:145-237
    • (1998) Quart Rev Biophys , vol.31 , pp. 145-237
    • Guntert, P.1
  • 235
    • 0026089657 scopus 로고
    • Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program diana and the supporting programs caliba, habas and glomsa
    • Guuntert P, Braun W, Wuthrich K (1991) Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA. J Mol Biol 217:517-530, http://www.mol.biol.ethz.ch/groups/wuthrich_group/software/
    • (1991) J Mol Biol , vol.217 , pp. 517-530
    • Guuntert, P.1    Braun, W.2    Wuthrich, K.3
  • 236
    • 0025932859 scopus 로고
    • An evaluation of computational strategies for use in the determination of protein structure from distance constraints obtained by nuclear magnetic resonance
    • Havel TF (1991) An evaluation of computational strategies for use in the determination of protein structure from distance constraints obtained by nuclear magnetic resonance. Prog Biophys Mol Biol 56:43-78
    • (1991) Prog Biophys Mol Biol , vol.56 , pp. 43-78
    • Havel, T.F.1
  • 238
    • 12244297937 scopus 로고
    • Vicinal proton coupling in nuclear magnetic resonance
    • Karplus K (1963) Vicinal proton coupling in nuclear magnetic resonance. J Am Chem Soc 85:2870-2871
    • (1963) J am Chem Soc , vol.85 , pp. 2870-2871
    • Karplus, K.1
  • 239
    • 33745356391 scopus 로고
    • Contact electron-spin interactions of nuclear magnetic moments
    • Karplus K (1959) Contact electron-spin interactions of nuclear magnetic moments. J Phys Chem 30:11-15
    • (1959) J Phys Chem , vol.30 , pp. 11-15
    • Karplus, K.1
  • 240
    • 0029314335 scopus 로고
    • The impact of direct refinement against proton chemical shifts on protein structure determination by nmr
    • Kuszewski J, Gronenborn AM, Clore GM (1995a) The impact of direct refinement against proton chemical shifts on protein structure determination by NMR. J Magn Reson B107:293-297
    • (1995) J Magn Reson , vol.B107 , pp. 293-297
    • Kuszewski, J.1    Gronenborn, A.M.2    Clore, G.M.3
  • 241
    • 0029202363 scopus 로고
    • The impact on direct refinement against 13ca and 13cb chemical shifts on protein structure determination by nmr
    • Kuszewski J, Qin J, Gronenborn AM, Clore GM (1995b) The impact on direct refinement against 13Ca and 13Cb chemical shifts on protein structure determination by NMR. J Magn Reson B106:92-96
    • (1995) J Magn Reson , vol.B106 , pp. 92-96
    • Kuszewski, J.1    Qin, J.2    Gronenborn, A.M.3    Clore, G.M.4
  • 242
    • 0030339738 scopus 로고    scopus 로고
    • Aqua and procheck-nmr: Programs for checking the quality of protein structures solved by nmr
    • Laskowski RA, Rullmann JAC, MacArthur MW, Kaptein R, Thornton JM (1996) AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J Biomol NMR 8:477-486
    • (1996) J Biomol NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmann, J.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 243
    • 0037316363 scopus 로고    scopus 로고
    • Aria: Automated noe assignment and nmr structure calculation
    • Linge JP, Habeck M, Rieping W, Nilges M (2003) ARIA: automated NOE assignment and NMR structure calculation. Bioinformatic 19:315-316
    • (2003) Bioinformatic , vol.19 , pp. 315-316
    • Linge, J.P.1    Habeck, M.2    Rieping, W.3    Nilges, M.4
  • 244
    • 0034919240 scopus 로고    scopus 로고
    • Automated assignment of ambiguous nuclear overhauser effects with aria
    • Linge JP, O’Donoghue SI, Nilges M (2001) Automated assignment of ambiguous nuclear overhauser effects with ARIA. Methods Enzymol 339:71-90
    • (2001) Methods Enzymol , vol.339 , pp. 71-90
    • Linge, J.P.1    O’Donoghue, S.I.2    Nilges, M.3
  • 245
  • 246
    • 0001455222 scopus 로고
    • Statistical basis for the use of 13ca chemical shifts in protein structure determination
    • Luginbuhl P, Szyperski T, Wuuthrich K (1995) Statistical basis for the use of 13Ca chemical shifts in protein structure determination. J Magn Reson B109:229-233
    • (1995) J Magn Reson , vol.B109 , pp. 229-233
    • Luginbuhl, P.1    Szyperski, T.2    Wuuthrich, K.3
  • 247
    • 0033610476 scopus 로고    scopus 로고
    • Identification by nmr spectroscopy of residues at contact surfaces in large, slowly exchanging macromolecular complexes
    • Mastsuo H, Walters KJ, Teruya K, Tanaka T, Gassner GT, Lippard SJ, Kyogoku Y, Wagner G (1999) Identification by NMR spectroscopy of residues at contact surfaces in large, slowly exchanging macromolecular complexes. J Am Chem Soc 121:9903-9904
    • (1999) J am Chem Soc , vol.121 , pp. 9903-9904
    • Mastsuo, H.1    Walters, K.J.2    Teruya, K.3    Tanaka, T.4    Gassner, G.T.5    Lippard, S.J.6    Kyogoku, Y.7    Wagner, G.8
  • 248
    • 0034713909 scopus 로고    scopus 로고
    • Nmr solution structure and receptor peptide binding of the cc chemokine eotaxin-2
    • Mayer KL, Stone MJ (2000) NMR solution structure and receptor peptide binding of the CC chemokine eotaxin-2. Biochemistry 39:8382-8395
    • (2000) Biochemistry , vol.39 , pp. 8382-8395
    • Mayer, K.L.1    Stone, M.J.2
  • 249
    • 0024435833 scopus 로고
    • Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the dna-binding domain of the 434 repressor by biosynthetically directed fractional carbon-13 labeling
    • Neri D, Szyperski T, Otting G, Senn H, Wuthrich K (1989) Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the DNA-binding domain of the 434 repressor by biosynthetically directed fractional carbon-13 labeling. Biochemistry 28:7510-7516
    • (1989) Biochemistry , vol.28 , pp. 7510-7516
    • Neri, D.1    Szyperski, T.2    Otting, G.3    Senn, H.4    Wuthrich, K.5
  • 251
    • 0347988396 scopus 로고    scopus 로고
    • Ambiguous noes and automated noe assignment
    • Nilges M, O’Donoghue SI (1998) Ambiguous NOEs and automated NOE assignment. Prog NMR Spectrosc 32:107-139
    • (1998) Prog NMR Spectrosc , vol.32 , pp. 107-139
    • Nilges, M.1    O’Donoghue, S.I.2
  • 252
    • 0025894164 scopus 로고
    • Relaxation matrix refinement of the solution structure of squash trypsin inhibitor
    • Nilges M, Habazettl J, Brunger A, Holak TA (1991) Relaxation matrix refinement of the solution structure of squash trypsin inhibitor. J Mol Biol 219:499-510
    • (1991) J Mol Biol , vol.219 , pp. 499-510
    • Nilges, M.1    Habazettl, J.2    Brunger, A.3    Holak, T.A.4
  • 253
    • 0031566434 scopus 로고    scopus 로고
    • Automated noesy interpretation with ambiguous distance restraints: The refined nmr solution structure of the pleckstrin homology domain from b-spectrin
    • Nilges M, Macias MJ, O’Donoghue SI, Oschkinat H (1997) Automated NOESY interpretation with ambiguous distance restraints: the refined NMR solution structure of the pleckstrin homology domain from b-spectrin. J Mol Biol 269:408-422
    • (1997) J Mol Biol , vol.269 , pp. 408-422
    • Nilges, M.1    Macias, M.J.2    O’Donoghue, S.I.3    Oschkinat, H.4
  • 255
    • 0000495503 scopus 로고
    • Three-dimensional triple-resonance nmr of 13c/15n-enriched proteins using constant-time evolution
    • Powers R, Gronenborn AM, Clore GM, Bax A (1991) Three-dimensional triple-resonance NMR of 13C/15N-enriched proteins using constant-time evolution. J Magn Reson 94:209-213
    • (1991) J Magn Reson , vol.94 , pp. 209-213
    • Powers, R.1    Gronenborn, A.M.2    Clore, G.M.3    Bax, A.4
  • 256
    • 0034480326 scopus 로고    scopus 로고
    • Nmr structures of biomolecules using field oriented media and residual dipolar couplings
    • Prestegard JH, Al-Hashimi HM, Tolman JR (2000) NMR structures of biomolecules using field oriented media and residual dipolar couplings. Quart Rev Biophys 33:371-424
    • (2000) Quart Rev Biophys , vol.33 , pp. 371-424
    • Prestegard, J.H.1    Al-Hashimi, H.M.2    Tolman, J.R.3
  • 257
    • 0034919312 scopus 로고    scopus 로고
    • Protein-protein interactions probed by nuclear magnetic resonance spectroscopy
    • Qin J, Vinogradova O, Gronenborn AM (2001) Protein-protein interactions probed by nuclear magnetic resonance spectroscopy. Meth Enzmol 339:377-389
    • (2001) Meth Enzmol , vol.339 , pp. 377-389
    • Qin, J.1    Vinogradova, O.2    Gronenborn, A.M.3
  • 258
    • 0001125521 scopus 로고
    • Stereospecific assignment of the methyl 1h nmr lines of valine and leucine in polypeptides by nonrandom 13c labelling
    • Senn H, Werner B, Messerle BA, Weber C, Traber R, Wuthrich K (1989) Stereospecific assignment of the methyl 1H NMR lines of valine and leucine in polypeptides by nonrandom 13C labelling. Febs Lett 249:113-118
    • (1989) FEBS Lett , vol.249 , pp. 113-118
    • Senn, H.1    Werner, B.2    Messerle, B.A.3    Weber, C.4    Traber, R.5    Wuthrich, K.6
  • 259
    • 0032467377 scopus 로고    scopus 로고
    • Nmr for the design of functional mimetics of protein-protein interactions: One key is in the building of bridges
    • Song J, Ni F (1998) NMR for the design of functional mimetics of protein-protein interactions: one key is in the building of bridges. Biochem Cell Biol 76:177-188
    • (1998) Biochem Cell Biol , vol.76 , pp. 177-188
    • Song, J.1    Ni, F.2
  • 260
    • 0347610773 scopus 로고
    • Empirical correlation between protein backbone conformation and c.Alpha. And c.Beta. 13C nuclear magnetic resonance chemical shifts
    • Spera S, Bax A (1991) Empirical correlation between protein backbone conformation and C.alpha. And C.beta. 13C nuclear magnetic resonance chemical shifts. J Am Chem Soc 113:5490-5492
    • (1991) J am Chem Soc , vol.113 , pp. 5490-5492
    • Spera, S.1    Bax, A.2
  • 261
    • 0034051065 scopus 로고    scopus 로고
    • A novel nmr method for determining the interfaces of large protein—protein complexes
    • Takahashi H, Nahanishi T, Kami K, Arata Y, Shimada I (2000) A novel NMR method for determining the interfaces of large protein—protein complexes. Nat Struct Biol 7:220-223
    • (2000) Nat Struct Biol , vol.7 , pp. 220-223
    • Takahashi, H.1    Nahanishi, T.2    Kami, K.3    Arata, Y.4    Shimada, I.5
  • 262
    • 0030722243 scopus 로고    scopus 로고
    • Direct measurement of distances and angles in biomolecules by nmr in a dilute liquid crystalline medium
    • Tjandra N, Bax A (1997) Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium. Science 278:1111-1114
    • (1997) Science , vol.278 , pp. 1111-1114
    • Tjandra, N.1    Bax, A.2
  • 263
    • 0030612335 scopus 로고    scopus 로고
    • Use of dipolar 1h—15n and 1h—13c couplings in the structure determination of magnetically oriented macromolecules in solution
    • Tjandra N, Omichinski JG, Gronenborn AM, Clore GM, Bax A (1997) Use of dipolar 1H—15N and 1H—13C couplings in the structure determination of magnetically oriented macromolecules in solution. Nature Struct Biol 4:732-738
    • (1997) Nature Struct Biol , vol.4 , pp. 732-738
    • Tjandra, N.1    Omichinski, J.G.2    Gronenborn, A.M.3    Clore, G.M.4    Bax, A.5
  • 265
    • 0027481669 scopus 로고
    • Molecular dynamics studies of proteins
    • van Gunsteren WF (1993) Molecular dynamics studies of proteins. Curr Opin Struct Biol 3:277-281
    • (1993) Curr Opin Struct Biol , vol.3 , pp. 277-281
    • Van Gunsteren, W.F.1
  • 266
    • 0037031551 scopus 로고    scopus 로고
    • A structural mechanism of integrin aiibp3 ‘inside-out’ activation as regulated by its cytoplasmic face
    • Vinogradova O, Velyvis A, Velyvience A, Hu B, Haas AT, Plow EF, Qin J (2002) A structural mechanism of integrin aIIbp3 ‘inside-out’ activation as regulated by its cytoplasmic face. Cell 110:587-597
    • (2002) Cell , vol.110 , pp. 587-597
    • Vinogradova, O.1    Velyvis, A.2    Velyvience, A.3    Hu, B.4    Haas, A.T.5    Plow, E.F.6    Qin, J.7
  • 267
    • 12044259775 scopus 로고
    • Quantitative j correlation: A new approach for measuring homonuclear three-bond j(hnh.Alpha.) coupling constants in 15n-enriched proteins
    • Vuister GW, Bax A (1993) Quantitative J correlation: a new approach for measuring homonuclear three-bond J(HNH.alpha.) coupling constants in 15N-enriched proteins. J Am Chem Soc 115:7772-7777
    • (1993) J am Chem Soc , vol.115 , pp. 7772-7777
    • Vuister, G.W.1    Bax, A.2
  • 268
    • 0001501991 scopus 로고
    • Reparametrization of the karplus relation for 3j(H.Alpha.-n) and 3j(hn-c’) in peptides from uniformly 13c/15n-enriched human ubiquitin
    • Wang AC, Bax A (1995) Reparametrization of the karplus relation for 3J(H.alpha.-N) and 3J(HN-C’) in peptides from uniformly 13C/15N-enriched human ubiquitin. J Am Chem Soc 117:1810-1813
    • (1995) J am Chem Soc , vol.117 , pp. 1810-1813
    • Wang, A.C.1    Bax, A.2
  • 269
    • 0029879363 scopus 로고    scopus 로고
    • Determination of the backbone dihedral angles j in human ubiquitin from reparametrized empirical karplus equations
    • Wang AC, Bax A (1996) Determination of the backbone dihedral angles j in human ubiquitin from reparametrized empirical Karplus equations. J Am Chem Soc 118:2483-2494
    • (1996) J am Chem Soc , vol.118 , pp. 2483-2494
    • Wang, A.C.1    Bax, A.2
  • 270
    • 0026597879 scopus 로고
    • The chemical shift index: A fast and simple method for the assignment of protein secondary structure through nmr spectroscopy
    • Wishart DS, Sykes BD, Richards FM (1992) The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry 31:1647-1651
    • (1992) Biochemistry , vol.31 , pp. 1647-1651
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 271
    • 0026410969 scopus 로고
    • Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
    • Wishart DS, Sykes BD, Richards FM (1991) Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J Mol Biol 222:311-333
    • (1991) J Mol Biol , vol.222 , pp. 311-333
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 273
    • 0000299865 scopus 로고
    • A new method for refinement of macro molecular structures based on nuclear overhauser effect spectra
    • Yip P, Case DA (1989) A new method for refinement of macro molecular structures based on nuclear overhauser effect spectra. J Magn Reson 83:643-648
    • (1989) J Magn Reson , vol.83 , pp. 643-648
    • Yip, P.1    Case, D.A.2
  • 274
    • 84910517192 scopus 로고    scopus 로고
    • University of Alberta
    • Zhang H (2001) M.Sc. Thesis, University of Alberta http://redpoll.pharmacy.ualberta.ca
    • (2001) M.Sc. Thesis
    • Zhang, H.1
  • 276
    • 0001144784 scopus 로고    scopus 로고
    • Monitoring macromolecular motions on microsecond to millisecond time scales by r1p—r1 constant relaxation time nmr spectroscopy
    • Akke M, Palmer G (1996) Monitoring macromolecular motions on microsecond to millisecond time scales by R1p—R1 constant relaxation time NMR spectroscopy. J Am Chem Soc 118:911-912
    • (1996) J am Chem Soc , vol.118 , pp. 911-912
    • Akke, M.1    Palmer, G.2
  • 277
    • 0029029566 scopus 로고
    • Long-range motional restrictions in a multidomain zinc-finger protein from anisotropic tumbling
    • Briischweiler R, Liao X, Wright PE (1995) Long-range motional restrictions in a multidomain zinc-finger protein from anisotropic tumbling. Science 268:886-889
    • (1995) Science , vol.268 , pp. 886-889
    • Briischweiler, R.1    Liao, X.2    Wright, P.E.3
  • 278
    • 0000174284 scopus 로고
    • Relaxation in the rotating frame in liquids
    • Bull TE (1992) Relaxation in the rotating frame in liquids. Prog Nucl Magn Reson Spectrosc 24:377-410
    • (1992) Prog Nucl Magn Reson Spectrosc , vol.24 , pp. 377-410
    • Bull, T.E.1
  • 279
    • 33847534249 scopus 로고
    • Effects of diffusion on free precession in nuclear magnetic resonance experiments
    • Carr HY, Purcell EM (1954) Effects of diffusion on free precession in nuclear magnetic resonance experiments. Phys Rev 94:630-638
    • (1954) Phys Rev , vol.94 , pp. 630-638
    • Carr, H.Y.1    Purcell, E.M.2
  • 280
    • 0025046144 scopus 로고
    • Deviations from the simple two-parameter model-free approach to the interpretation of nitrogen-15 nuclear magnetic relaxation of proteins
    • Clore GM, Szabo A, Bax A, Kay LE, Driscoll PC, Gronenborn AM (1990a) Deviations from the simple two-parameter model-free approach to the interpretation of nitrogen-15 nuclear magnetic relaxation of proteins. J Am Chem Soc 112:4989-4991
    • (1990) J am Chem Soc , vol.112 , pp. 4989-4991
    • Clore, G.M.1    Szabo, A.2    Bax, A.3    Kay, L.E.4    Driscoll, P.C.5    Gronenborn, A.M.6
  • 281
    • 0025063347 scopus 로고
    • Analysis of the backbone dynamics of interleukin-1.Beta. Using two-dimensional inverse detected heteronuclear nitrogen-15-proton nmr spectroscopy
    • Clore GM, Driscoll PC, Wingfield PT, Gronenborn AM (1990b) Analysis of the backbone dynamics of interleukin-1.beta. Using two-dimensional inverse detected heteronuclear nitrogen-15-proton NMR spectroscopy. Biochemistry 29:7387-7401
    • (1990) Biochemistry , vol.29 , pp. 7387-7401
    • Clore, G.M.1    Driscoll, P.C.2    Wingfield, P.T.3    Gronenborn, A.M.4
  • 282
    • 0030338305 scopus 로고    scopus 로고
    • Theory and practice of nuclear spin relaxation in proteins
    • Dayie KT, Wagner G, Lefevre JF (1996) Theory and practice of nuclear spin relaxation in proteins. Annu Rev Phys Chem 47:243-282
    • (1996) Annu Rev Phys Chem , vol.47 , pp. 243-282
    • Dayie, K.T.1    Wagner, G.2    Lefevre, J.F.3
  • 283
    • 0024402002 scopus 로고
    • Model-independent and model-dependent analysis of the global and internal dynamics of cyclosporin a
    • Dellwo MJ, Wand AJ (1989) Model-independent and model-dependent analysis of the global and internal dynamics of cyclosporin A. J Am Chem Soc 111:4571-4578
    • (1989) J am Chem Soc , vol.111 , pp. 4571-4578
    • Dellwo, M.J.1    Wand, A.J.2
  • 284
    • 0001238486 scopus 로고    scopus 로고
    • Study of dynamic processes in liquids using off-resonance rf irradiation
    • Desvaux H, Berthault P (1999) Study of dynamic processes in liquids using off-resonance rf irradiation. Prog Nucl Magn Reson Spectrosc 35:295-340
    • (1999) Prog Nucl Magn Reson Spectrosc , vol.35 , pp. 295-340
    • Desvaux, H.1    Berthault, P.2
  • 285
    • 0029367044 scopus 로고
    • Spectral density function mapping using 15n relaxation data exclusively
    • Farrow NA, Zhang O, Szabo A, Torchoia DA, Kay LE (1995) Spectral density function mapping using 15N relaxation data exclusively. J Biomol NMR 6:153-162
    • (1995) J Biomol NMR , vol.6 , pp. 153-162
    • Farrow, N.A.1    Zhang, O.2    Szabo, A.3    Torchoia, D.A.4    Kay, L.E.5
  • 287
    • 0035810993 scopus 로고    scopus 로고
    • Main chain and side chain dynamics of a heme protein: 15N and 2h nmr relaxation studies of r. Capsulatus ferrocytochrome c2
    • Flynn PF, Bieber Urbauer RJ, Zhang H, Lee AL, Wand AJ (2001) Main chain and side chain dynamics of a heme protein: 15N and 2H NMR relaxation studies of R. Capsulatus ferrocytochrome c2. Biochemistry 40:6559-6569
    • (2001) Biochemistry , vol.40 , pp. 6559-6569
    • Flynn, P.F.1    Bieber Urbauer, R.J.2    Zhang, H.3    Lee, A.L.4    Wand, A.J.5
  • 288
    • 48549112585 scopus 로고
    • Interference effects in the relaxation of a pair of unlike spin-1/2 nuclei
    • Goldman M (1984) Interference effects in the relaxation of a pair of unlike spin-1/2 nuclei. J Magn Reson 60:437-452
    • (1984) J Magn Reson , vol.60 , pp. 437-452
    • Goldman, M.1
  • 289
    • 0023914502 scopus 로고
    • Determination of 15n chemical shift tensor via 15n-2h dipolar coupling in boc-glycylglycyl[15n glycine]benzyl ester
    • Hiyama Y, Niu C, Silverton JV, Bavoso A, Torchia DA (1988) Determination of 15N chemical shift tensor via 15N-2H dipolar coupling in Boc-glycylglycyl[15N glycine]benzyl ester. J Am Chem Soc 110:2378-2383
    • (1988) J Am Chem Soc , vol.110 , pp. 2378-2383
    • Hiyama, Y.1    Niu, C.2    Silverton, J.V.3    Bavoso, A.4    Torchia, D.A.5
  • 291
    • 0028938022 scopus 로고
    • Protein backbone dynamics revealed by quasi spectral density function analysis of amide n-15 nuclei
    • Ishima R, Nagayama K (1995a) Protein backbone dynamics revealed by quasi spectral density function analysis of amide N-15 nuclei. Biochemistry 34:3162-3171
    • (1995) Biochemistry , vol.34 , pp. 3162-3171
    • Ishima, R.1    Nagayama, K.2
  • 292
    • 0003075383 scopus 로고
    • Quasi-spectral-density function analysis for nitrogen-15 nuclei in proteins
    • Ishima R, Nagayama K (1995b) Quasi-spectral-density function analysis for nitrogen-15 nuclei in proteins. J Magn Reson 108:73-76
    • (1995) J Magn Reson , vol.108 , pp. 73-76
    • Ishima, R.1    Nagayama, K.2
  • 293
    • 0024449503 scopus 로고
    • Backbone dynamics of proteins as studied by 15n inverse detected heteronuclear nmr spectroscopy: Application to staphylococcal nuclease
    • Kay LE, Torchia DA, Bax A (1989) Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease. Biochemistry 28:8972-8979
    • (1989) Biochemistry , vol.28 , pp. 8972-8979
    • Kay, L.E.1    Torchia, D.A.2    Bax, A.3
  • 294
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • Kay LE, Keifer P, Saarinen T (1992) Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J Am Chem Soc 114:10663-10665
    • (1992) J am Chem Soc , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 295
    • 0033520723 scopus 로고    scopus 로고
    • Variability of the 15n chemical shift anisotropy in escherichia coli ribonuclease h in solution
    • Kroenke CD, Rance M, Palmer AG III (1999) Variability of the 15N chemical shift anisotropy in Escherichia coli Ribonuclease H in solution. J Am Chem Soc 121:10119-10125
    • (1999) J am Chem Soc , vol.121 , pp. 10119-10125
    • Kroenke, C.D.1    Rance, M.2    Palmer, A.3
  • 296
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity
    • Lipari G, Szabo A (1982a) Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity. J Am Chem Soc 104:4546-4559
    • (1982) J am Chem Soc , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 297
    • 33845553743 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 2. Analysis of experimental results
    • Lipari G, Szabo A (1982b) Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 2. Analysis of experimental results. J Am Chem Soc 104:4559-4570
    • (1982) J am Chem Soc , vol.104 , pp. 4559-4570
    • Lipari, G.1    Szabo, A.2
  • 298
    • 0041080990 scopus 로고
    • Intramolecular dynamics of proteins and peptides as monitored by nuclear magnetic relaxation experiments
    • J.S. Cohen, Wiley, New York
    • London RE (1980) Intramolecular dynamics of proteins and peptides as monitored by nuclear magnetic relaxation experiments. In Magnetic Resonance in Biology, J.S. Cohen (ed.), Wiley, New York, pp. 1-69
    • (1980) Magnetic Resonance in Biology , pp. 1-69
    • London, R.E.1
  • 299
    • 0028941877 scopus 로고
    • Backbone dynamics of escherichia coli ribonuclease hi: Correlations with structure ad function in a active enzyme
    • Mandel AM, Akke M, Palmer AG (1995) Backbone dynamics of Escherichia coli ribonuclease HI: correlations with structure ad function in a active enzyme. J Mol Biol 246:144-163
    • (1995) J Mol Biol , vol.246 , pp. 144-163
    • Mandel, A.M.1    Akke, M.2    Palmer, A.G.3
  • 300
    • 0034264355 scopus 로고    scopus 로고
    • Peptide internal motions on nanosecond time scale derived from direct fitting of 13c and 15n nmr spectral density functions
    • Mayo KH, Daragan VA, Idiyatullin D, Nesmelova I (2000) Peptide internal motions on nanosecond time scale derived from direct fitting of 13C and 15N NMR spectral density functions. J MagnReson 146:188-195
    • (2000) J MagnReson , vol.146 , pp. 188-195
    • Mayo, K.H.1    Daragan, V.A.2    Idiyatullin, D.3    Nesmelova, I.4
  • 301
    • 0002899752 scopus 로고
    • Modified spin-echo method for measuring nuclear relaxation times
    • Meiboom S, Gill D (1958) Modified spin-echo method for measuring nuclear relaxation times. Rev Sci Instrum 29:688-691
    • (1958) Rev Sci Instrum , vol.29 , pp. 688-691
    • Meiboom, S.1    Gill, D.2
  • 302
    • 36849120169 scopus 로고
    • Nuclear magnetic resonance study of the proton transfer in water
    • Meiboom S (1961) Nuclear magnetic resonance study of the proton transfer in water. J Chem Phys 34:375-388
    • (1961) J Chem Phys , vol.34 , pp. 375-388
    • Meiboom, S.1
  • 303
    • 45249130688 scopus 로고
    • Solvent suppression using a spin lock in 2d and 3d nmr spectroscopy with h2o solutions
    • Messerlie BA, Wider G, Otting G, Weber C, Wuthrich K (1989) Solvent suppression using a spin lock in 2D and 3D NMR spectroscopy with H2O solutions. J Magn Reson 85:608-61
    • (1989) J Magn Reson , vol.85 , pp. 608-661
    • Messerlie, B.A.1    Wider, G.2    Otting, G.3    Weber, C.4    Wuthrich, K.5
  • 304
    • 0000987483 scopus 로고    scopus 로고
    • An off-resonance rotating frame relaxation experiment for the investigation of macromolecular dynamics using adiabatic rotations
    • Mulder FAA, de Graaf RA, Kaptein R, Boelens R (1998) An off-resonance rotating frame relaxation experiment for the investigation of macromolecular dynamics using adiabatic rotations. J Magn Reson 131:351-357
    • (1998) J Magn Reson , vol.131 , pp. 351-357
    • Mulder, F.1    De Graaf, R.A.2    Kaptein, R.3    Boelens, R.4
  • 305
    • 0026663387 scopus 로고
    • Dynamics of methyl groups in proteins as studied by proton-detected carbon-13 nmr spectroscopy. Application to the leucine residues of staphylococcal nuclease
    • Nicholson LK, Kay LE, Baldisseri DM, Arango J, Young PE, Torchia DA (1992) Dynamics of methyl groups in proteins as studied by proton-detected carbon-13 NMR spectroscopy. Application to the leucine residues of staphylococcal nuclease. Biochemistry 31:5253-5263
    • (1992) Biochemistry , vol.31 , pp. 5253-5263
    • Nicholson, L.K.1    Kay, L.E.2    Baldisseri, D.M.3    Arango, J.4    Young, P.E.5    Torchia, D.A.6
  • 306
    • 0034984208 scopus 로고    scopus 로고
    • Nmr probes of molecular dynamics: Overview and comparison with other techniques
    • Palmer AG (2001) NMR probes of molecular dynamics: overview and comparison with other techniques. Annu Rev Biophys Biomol Struct 30:129-155
    • (2001) Annu Rev Biophys Biomol Struct , vol.30 , pp. 129-155
    • Palmer, A.G.1
  • 307
    • 12044256620 scopus 로고
    • Intramolecular motions of a zinc finger dna-binding domain from xfin characterized by proton-detected natural abundance carbon-13 heteronuclear nmr spectroscopy
    • Palmer AG III, Rance M, Wright PE (1991) Intramolecular motions of a zinc finger DNA-binding domain from Xfin characterized by proton-detected natural abundance carbon-13 heteronuclear NMR spectroscopy. J Am Chem Soc 113:4371-4380
    • (1991) J am Chem Soc , vol.113 , pp. 4371-4380
    • Palmer, A.1    Rance, M.2    Wright, P.E.3
  • 309
    • 0029623152 scopus 로고
    • Frequency spectrum of nh bonds in eglin c from spectral density mapping at multiple fields
    • Peng JW, Wagner G (1995) Frequency spectrum of NH bonds in eglin c from spectral density mapping at multiple fields. Biochemistry 34:16733-16752
    • (1995) Biochemistry , vol.34 , pp. 16733-16752
    • Peng, J.W.1    Wagner, G.2
  • 310
    • 44949274459 scopus 로고
    • 2d heteronuclear nmr measurements of spin-lattice relaxation times in the rotating frame of x nuclei in heteronuclear hx spin systems
    • Peng JW, Thanabal V, Wagner G (1991) 2D heteronuclear NMR measurements of spin-lattice relaxation times in the rotating frame of X nuclei in heteronuclear HX spin systems. J Magn Reson 94:82-100
    • (1991) J Magn Reson , vol.94 , pp. 82-100
    • Peng, J.W.1    Thanabal, V.2    Wagner, G.3
  • 311
    • 0000808109 scopus 로고    scopus 로고
    • Dynamic studies of a fibronectin type i module pair at three frequencies: Anisotropic modelling and direct determination of conformational exchange
    • Phan IQ, Boyd J, Campbell ID (1996) Dynamic studies of a fibronectin type I module pair at three frequencies: anisotropic modelling and direct determination of conformational exchange. J Biomol NMR 8:369-378
    • (1996) J Biomol NMR , vol.8 , pp. 369-378
    • Phan, I.Q.1    Boyd, J.2    Campbell, I.D.3
  • 313
    • 0001030227 scopus 로고
    • Theory of nmr relaxation in macromolecules: Restricted diffusion and jump models for multiple internal rotations in amino acid side chains
    • Wittebort R, Szabo A (1978) Theory of NMR relaxation in macromolecules: restricted diffusion and jump models for multiple internal rotations in amino acid side chains. J Chem Phys 69:1722-1736
    • (1978) J Chem Phys , vol.69 , pp. 1722-1736
    • Wittebort, R.1    Szabo, A.2
  • 314
    • 0000733545 scopus 로고
    • Nmr experiments for the measurement of carbon relaxation properties in highly enriched, uniformly 13c, 15n-labeled proteins: Application to 13ca carbons
    • Yamazaki T, Muhandiram R, Kay LE (1994) NMR experiments for the measurement of carbon relaxation properties in highly enriched, uniformly 13C, 15N-labeled proteins: application to 13Ca carbons. J Am Chem Soc 116:8266-8278
    • (1994) J am Chem Soc , vol.116 , pp. 8266-8278
    • Yamazaki, T.1    Muhandiram, R.2    Kay, L.E.3
  • 315
    • 84989095338 scopus 로고
    • Carbon-13 chemical shift anisotropies of solid amino acids
    • Ye C, Fu R, Hu J, Hou L, Ding S (1993) Carbon-13 chemical shift anisotropies of solid amino acids. Magn Reson Chem 31:699-704
    • (1993) Magn Reson Chem , vol.31 , pp. 699-704
    • Ye, C.1    Fu, R.2    Hu, J.3    Hou, L.4    Ding, S.5
  • 316
    • 0000941586 scopus 로고    scopus 로고
    • Off-resonance rf fields in heteronuclear nmr: Application to the study of slow motions
    • Zinn-Justin S, Berthault P, Guenneuges M, Desvaux H (1997) Off-resonance rf fields in heteronuclear NMR: application to the study of slow motions. J Biomol NMR 10:363-372
    • (1997) J Biomol NMR , vol.10 , pp. 363-372
    • Zinn-Justin, S.1    Berthault, P.2    Guenneuges, M.3    Desvaux, H.4
  • 317
    • 0001133594 scopus 로고
    • Pituitary gland: Enzymic formation of methanol from s-adenosyl-methionine
    • Axelrod J, Daly J (1965) Pituitary gland: enzymic formation of methanol from S-adenosyl-methionine. Science 150:892-893
    • (1965) Science , vol.150 , pp. 892-893
    • Axelrod, J.1    Daly, J.2
  • 318
    • 21844507505 scopus 로고
    • Standardization and transformation in principal component analysis, with applications to archaeometry
    • Baxter MJ (1995) Standardization and transformation in principal component analysis, with applications to archaeometry. Appl Statist 44:513-527
    • (1995) Appl Statist , vol.44 , pp. 513-527
    • Baxter, M.J.1
  • 319
    • 74249109330 scopus 로고    scopus 로고
    • Metabolic assessment of the action of targeted cancer therapeutics using magnetic resonance spectroscopy
    • Beloueche-Babari M, Chung YL, Al-Saffar NM, Falck-Miniotis M, Leach MO (2010) Metabolic assessment of the action of targeted cancer therapeutics using magnetic resonance spectroscopy. Brj Canc 102:1-7
    • (2010) Brj Canc , vol.102 , pp. 1-7
    • Beloueche-Babari, M.1    Chung, Y.L.2    Al-Saffar, N.M.3    Falck-Miniotis, M.4    Leach, M.O.5
  • 320
    • 79958771235 scopus 로고    scopus 로고
    • Standard operating procedures for pre-analytical handling of blood and urine for metabolomic studies and biobanks
    • Bernini P, Bertini I, Luchinat C, Nincheri P, Staderini S, Turano P (2011) Standard operating procedures for pre-analytical handling of blood and urine for metabolomic studies and biobanks. J Biomol NMR 49:231-243
    • (2011) J Biomol NMR , vol.49 , pp. 231-243
    • Bernini, P.1    Bertini, I.2    Luchinat, C.3    Nincheri, P.4    Staderini, S.5    Turano, P.6
  • 322
    • 0032727651 scopus 로고    scopus 로고
    • Inhibition of human carcinoma cell growth and dna synthesis by silibinin, an active constituent of milk thistle: Comparison with silymarin
    • Bhatia N, Zhao J, Wolf DM, Agarwal R (1999) Inhibition of human carcinoma cell growth and DNA synthesis by silibinin, an active constituent of milk thistle: comparison with silymarin. Cancer Lett 147:77-84
    • (1999) Cancer Lett , vol.147 , pp. 77-84
    • Bhatia, N.1    Zhao, J.2    Wolf, D.M.3    Agarwal, R.4
  • 323
    • 0008617878 scopus 로고
    • The amino acid pool in escherichia coli
    • Britten RJ, McClure FT (1962) The amino acid pool in Escherichia coli. Bacteriol Rev 26:292-335
    • (1962) Bacteriol Rev , vol.26 , pp. 292-335
    • Britten, R.J.1    McClure, F.T.2
  • 324
    • 26844461245 scopus 로고    scopus 로고
    • Franklin rb (2005) ‘why do tumour cells glycolyse?’: From glycolysis through citrate to lipogenesis
    • Costello LC, Franklin RB (2005) ‘Why do tumour cells glycolyse?’: from glycolysis through citrate to lipogenesis. Mol Cell Biochem 280:1-8
    • Mol Cell Biochem , vol.280 , pp. 1-8
    • Costello, L.C.1
  • 325
    • 0033668356 scopus 로고    scopus 로고
    • The intermediary metabolism of the prostate: A key to understanding the pathogenesis and progression of prostate malignancy
    • Costello LC, Franklin RB (2000) The intermediary metabolism of the prostate: a key to understanding the pathogenesis and progression of prostate malignancy. Oncology 59:269-282
    • (2000) Oncology , vol.59 , pp. 269-282
    • Costello, L.C.1    Franklin, R.B.2
  • 326
    • 0041677489 scopus 로고    scopus 로고
    • Homocysteine and oxidized low density lipoprotein enhance platelet adhesion to endothelial cells under flow conditions: Distinct mechanisms of thrombogenic modulation
    • Dardik R, Varon D, Tamarin I, Zivelin A, Salomon O, Shenkman B, Savion N (2000) Homocysteine and oxidized low density lipoprotein enhance platelet adhesion to endothelial cells under flow conditions: distinct mechanisms of thrombogenic modulation. Thromb Haemost 83:338-344
    • (2000) Thromb Haemost , vol.83 , pp. 338-344
    • Dardik, R.1    Varon, D.2    Tamarin, I.3    Zivelin, A.4    Salomon, O.5    Shenkman, B.6    Savion, N.7
  • 328
    • 37449034854 scopus 로고    scopus 로고
    • Beyond aerobic glycolysis: Transformed cells can engage in glutamine metabolism that exceeds the requirement for protein and nucleotide synthesis
    • DeBerardinis RJ, Mancuso A, Daikhin E, Nissim I, Yudkoff M, Wehrli S, Thompson CB (2007) Beyond aerobic glycolysis: transformed cells can engage in glutamine metabolism that exceeds the requirement for protein and nucleotide synthesis. Pnas 104:19345-19350
    • (2007) PNAS , vol.104 , pp. 19345-19350
    • DeBerardinis, R.J.1    Mancuso, A.2    Daikhin, E.3    Nissim, I.4    Yudkoff, M.5    Wehrli, S.6    Thompson, C.B.7
  • 329
    • 0026715777 scopus 로고
    • A method for the determination of changes of glycolytic metabolites in yeast on a subsecond time scale using extraction at neutral ph
    • de Koning W, van Dam K (1992) A method for the determination of changes of glycolytic metabolites in yeast on a subsecond time scale using extraction at neutral pH. Anal Biochem 204:118-123
    • (1992) Anal Biochem , vol.204 , pp. 118-123
    • De Koning, W.1    Van Dam, K.2
  • 330
    • 0037038340 scopus 로고    scopus 로고
    • Optimisation of collection, storage and preparation of rat plasma for 1h nmr spectroscopic analysis in toxicology studies to determine inherent variation in biochemical profiles
    • Deprez S, Sweatman BC, Connor SC, Haselden JN, Waterfield CJ (2002) Optimisation of collection, storage and preparation of rat plasma for 1H NMR spectroscopic analysis in toxicology studies to determine inherent variation in biochemical profiles. J Pharm Biomed Anal 30:1297-1310
    • (2002) J Pharm Biomed Anal , vol.30 , pp. 1297-1310
    • Deprez, S.1    Sweatman, B.C.2    Connor, S.C.3    Haselden, J.N.4    Waterfield, C.J.5
  • 331
    • 38849184046 scopus 로고    scopus 로고
    • Cell lines: A tool for in vitro drug metabolism studies
    • Donato MT, Lahoz A, Castell JV, (2008) Cell lines: a tool for in vitro drug metabolism studies. Curr Drug Metab 9:1-11
    • (2008) Curr Drug Metab , vol.9 , pp. 1-11
    • Donato, M.T.1    Lahoz, A.2    Castell, J.V.3
  • 332
    • 44449134287 scopus 로고    scopus 로고
    • Investigating compensation and recovery of fathead minnow (Pimephales promelas) exposed to 17alpha-ethynylestradiol with metabolite profiling
    • Ekman DR, Teng Q, Villeneuve DL et al (2008) Investigating compensation and recovery of fathead minnow (Pimephales promelas) exposed to 17alpha-ethynylestradiol with metabolite profiling. Environ Sci Technol 42:4188-4194
    • (2008) Environ Sci Technol , vol.42 , pp. 4188-4194
    • Ekman, D.R.1    Teng, Q.2    Villeneuve, D.L.3
  • 334
    • 0001413420 scopus 로고    scopus 로고
    • Metabolite profiling by one- and two-dimensional nmr analysis of complex mixtures
    • Fan TWM (1996) Metabolite profiling by one- and two-dimensional NMR analysis of complex mixtures. Prog Nucl Magn Reson Spectr 28:161-219
    • (1996) Prog Nucl Magn Reson Spectr , vol.28 , pp. 161-219
    • Fan, T.1
  • 335
    • 0034959944 scopus 로고    scopus 로고
    • Combining genomics, metabolome analysis, and biochemical modelling to understand metabolic networks
    • Fiehn O (2001) Combining genomics, metabolome analysis, and biochemical modelling to understand metabolic networks. Comp Funct Genom 2:155-168
    • (2001) Comp Funct Genom , vol.2 , pp. 155-168
    • Fiehn, O.1
  • 338
    • 33749319703 scopus 로고    scopus 로고
    • Type, density, and location of immune cells within human colorectal tumors predict clinical outcome
    • Galon J, Costes A, Sanchez-Cabo F, Kirilovsky A, Mlecnik B, Lagorce-Pages C et al (2006) Type, density, and location of immune cells within human colorectal tumors predict clinical outcome. Science 313:1960-1964
    • (2006) Science , vol.313 , pp. 1960-1964
    • Galon, J.1    Costes, A.2    Sanchez-Cabo, F.3    Kirilovsky, A.4    Mlecnik, B.5    Lagorce-Pages, C.6
  • 339
    • 0017405353 scopus 로고
    • The synthesis of hippurate from benzoate and glycine by rat liver mitochondria
    • Biochem J
    • Gatley SJ, Sherratt HS (1977) The synthesis of hippurate from benzoate and glycine by rat liver mitochondria. Submitochondrial localization and kinetics. Biochem J 166:39-47
    • (1977) Submitochondrial Localization and Kinetics , vol.166 , pp. 39-47
    • Gatley, S.J.1    Sherratt, H.S.2
  • 340
    • 0018137689 scopus 로고
    • Quantitative metabolic profiling based on gas chromatography
    • Gates SC, Sweeley CC (1978) Quantitative metabolic profiling based on gas chromatography. Clin Chem 24:1663-1673
    • (1978) Clin Chem , vol.24 , pp. 1663-1673
    • Gates, S.C.1    Sweeley, C.C.2
  • 341
    • 33750435528 scopus 로고    scopus 로고
    • Therapeutic targets and biomarkers identified in cancer choline phospholipid metabolism
    • Glunde K, Serkova NJ (2006) Therapeutic targets and biomarkers identified in cancer choline phospholipid metabolism. Pharmacogenomics 7:1109-1123
    • (2006) Pharmacogenomics , vol.7 , pp. 1109-1123
    • Glunde, K.1    Serkova, N.J.2
  • 342
    • 33845383242 scopus 로고    scopus 로고
    • Choline metabolism in cancer: Implications for diagnosis and therapy
    • Glunde K, Jacobs MA, Bhujwalla ZM (2006) Choline metabolism in cancer: implications for diagnosis and therapy. Expert Rev Mol Diagn 6:821-829
    • (2006) Expert Rev Mol Diagn , vol.6 , pp. 821-829
    • Glunde, K.1    Jacobs, M.A.2    Bhujwalla, Z.M.3
  • 343
    • 22144487727 scopus 로고    scopus 로고
    • Metabolomics - the way forward
    • Goodacre R (2005) Metabolomics - the way forward. Metabolomics 1:1-2
    • (2005) Metabolomics , vol.1 , pp. 1-2
    • Goodacre, R.1
  • 345
    • 34548248572 scopus 로고    scopus 로고
    • Oestrogen-receptor-mediated transcription and the influence of cofactors and chromatin state
    • Green KA, Carroll JS (2007) Oestrogen-receptor-mediated transcription and the influence of cofactors and chromatin state. Nat Rev Cancer 7:713-722
    • (2007) Nat Rev Cancer , vol.7 , pp. 713-722
    • Green, K.A.1    Carroll, J.S.2
  • 346
    • 3042823722 scopus 로고    scopus 로고
    • Metabolic profiles of cancer cells
    • Griffin JL, Shockcor JP (2004) Metabolic profiles of cancer cells. Nat Rev Cancer 4:551-561
    • (2004) Nat Rev Cancer , vol.4 , pp. 551-561
    • Griffin, J.L.1    Shockcor, J.P.2
  • 347
    • 33847370301 scopus 로고    scopus 로고
    • Tumour metabolomics in animal models of human cancer
    • Griffin JL, Kauppinen RA (2007) Tumour metabolomics in animal models of human cancer. J Proteome Res 6:498-505
    • (2007) J Proteome Res , vol.6 , pp. 498-505
    • Griffin, J.L.1    Kauppinen, R.A.2
  • 348
    • 35248818831 scopus 로고    scopus 로고
    • Flavonoid, silibinin, inhibits proliferation and promotes cell-cycle arrest of human colon cancer
    • Hogan FS, Krishnegowda NK, Mikhailova M, Kahlenberg MS (2007) Flavonoid, silibinin, inhibits proliferation and promotes cell-cycle arrest of human colon cancer. J Surgical Res 143:58-65
    • (2007) J Surgical Res , vol.143 , pp. 58-65
    • Hogan, F.S.1    Krishnegowda, N.K.2    Mikhailova, M.3    Kahlenberg, M.S.4
  • 350
    • 0037164104 scopus 로고    scopus 로고
    • Homocysteine and risk of ischemic heart disease and stroke: A meta-analysis
    • Homocysteine Studies Collaboration (2002) Homocysteine and risk of ischemic heart disease and stroke: a meta-analysis. Jama 288:2015-2022
    • (2002) JAMA , vol.288 , pp. 2015-2022
  • 351
    • 0015111451 scopus 로고
    • Metabolic profiles: Gas-phase methods for analysis of metabolites
    • Horning EC, Horning MG (1971) Metabolic profiles: gas-phase methods for analysis of metabolites. Clin Chem 17:802-809
    • (1971) Clin Chem , vol.17 , pp. 802-809
    • Horning, E.C.1    Horning, M.G.2
  • 352
    • 0001038967 scopus 로고
    • The generalization of student’s ratio
    • Hotelling H (1931) The generalization of student’s ratio. Ann Math Stat 2:360-378
    • (1931) Ann Math Stat , vol.2 , pp. 360-378
    • Hotelling, H.1
  • 356
    • 1842714914 scopus 로고    scopus 로고
    • Accounting for poisson noise in the multivariate analysis of tof-sims spectrum images
    • Keenan MR, Kotula PG (2004) Accounting for poisson noise in the multivariate analysis of ToF-SIMS spectrum images. Surf Int Anal 36:203-212
    • (2004) Surf Int Anal , vol.36 , pp. 203-212
    • Keenan, M.R.1    Kotula, P.G.2
  • 357
    • 84955096888 scopus 로고    scopus 로고
    • Metabolomics
    • Al-Rubeai M, Fussenegger M, system, biology, Springer
    • Khoo SHG, Al-Rubeai M (2007) Metabolomics. Al-Rubeai M, Fussenegger M (eds) Cell engineering vol. 5. System biology. Springer
    • (2007) Cell Engineering , vol.5
    • Khoo, S.1    Al-Rubeai, M.2
  • 358
    • 5344244045 scopus 로고    scopus 로고
    • Experimental animal urine collection: A review
    • Kurien BT, Everds NE, Scofield RH (2004) Experimental animal urine collection: a review. Lab Anim. 38:333-361
    • (2004) Lab Anim , vol.38 , pp. 333-361
    • Kurien, B.T.1    Everds, N.E.2    Scofield, R.H.3
  • 359
    • 34249870845 scopus 로고    scopus 로고
    • Quantification and identification of isotopomer distributions of metabolites in crude cell extracts using 1h tocsy
    • Lane AN, Fan TWM (2007) Quantification and identification of isotopomer distributions of metabolites in crude cell extracts using 1H TOCSY. Metabolomics 3:79-86
    • (2007) Metabolomics , vol.3 , pp. 79-86
    • Lane, A.N.1    Fan, T.2
  • 362
    • 77950944945 scopus 로고    scopus 로고
    • Serum metabolome analysis by 1h-nmr reveals differences between chronic lymphocytic leukaemia molecular subgroups
    • MacIntyre DA, Jimenez B, Lewintre EJ, Martin CR, Schafer H, Ballesteros CG et al (2010) Serum metabolome analysis by 1H-NMR reveals differences between chronic lymphocytic leukaemia molecular subgroups. Leukemia 24:788-797
    • (2010) Leukemia , vol.24 , pp. 788-797
    • MacIntyre, D.A.1    Jimenez, B.2    Lewintre, E.J.3    Martin, C.R.4    Schafer, H.5    Ballesteros, C.G.6
  • 363
    • 0028220787 scopus 로고
    • Vitamin b-6 deficiency vs folate deficiency: Comparison of responses to methionine loading in rats
    • Miller JW, Nadeau MR, Smith D, Selhub J (1994) Vitamin B-6 deficiency vs folate deficiency: comparison of responses to methionine loading in rats. Am J Clin Nutr 59:1033-1039
    • (1994) Am J Clin Nutr , vol.59 , pp. 1033-1039
    • Miller, J.W.1    Nadeau, M.R.2    Smith, D.3    Selhub, J.4
  • 366
    • 0032694577 scopus 로고    scopus 로고
    • ’metabonomics’: Understanding the metabolic responses of living systems to pathophysiological stimuli via multivariate statistical analysis of biological nmr spectroscopic data
    • Nicholson JK, Lindon JC, Holmes E (1999) ’Metabonomics’: understanding the metabolic responses of living systems to pathophysiological stimuli via multivariate statistical analysis of biological NMR spectroscopic data. Xenobiotica 29:1181-1189
    • (1999) Xenobiotica , vol.29 , pp. 1181-1189
    • Nicholson, J.K.1    Lindon, J.C.2    Holmes, E.3
  • 370
    • 73349142719 scopus 로고    scopus 로고
    • In situ cytotoxic and memory t cells predict outcome in patients with early-stage colorectal cancer
    • Pages F, Kirilovsky A, Mlecnik B, Asslaber M, Tosolini M, Bindea G et al (2009) In situ cytotoxic and memory T cells predict outcome in patients with early-stage colorectal cancer. J Clin Oncol 27:5944-5951
    • (2009) J Clin Oncol , vol.27 , pp. 5944-5951
    • Pages, F.1    Kirilovsky, A.2    Mlecnik, B.3    Asslaber, M.4    Tosolini, M.5    Bindea, G.6
  • 371
    • 36849105803 scopus 로고
    • Water eliminated fourier transform nmr spectroscopy
    • Patt SL, Sykes BD (1972) Water eliminated Fourier transform NMR spectroscopy. Chem Phys 56:3182
    • (1972) Chem Phys , vol.56 , pp. 3182
    • Patt, S.L.1    Sykes, B.D.2
  • 372
    • 0000325341 scopus 로고
    • On lines and planes of closest fit to systems of points in space
    • Pearson K (1901) On lines and planes of closest fit to systems of points in space. Phil Mag 2:559-572
    • (1901) Phil Mag , vol.2 , pp. 559-572
    • Pearson, K.1
  • 373
    • 70149102858 scopus 로고    scopus 로고
    • Metabolic characterization of primary human colorectal cancers using high resolution magic angle spinning 1h magnetic resonance spectroscopy
    • Piotto M, Moussallieh FM, Dillman B, Imperiale A, Neuville A, Brigand C et al (2009) Metabolic characterization of primary human colorectal cancers using high resolution magic angle spinning 1H magnetic resonance spectroscopy. Metabolomics 5:292-301
    • (2009) Metabolomics , vol.5 , pp. 292-301
    • Piotto, M.1    Moussallieh, F.M.2    Dillman, B.3    Imperiale, A.4    Neuville, A.5    Brigand, C.6
  • 374
    • 36348976518 scopus 로고    scopus 로고
    • Dietary feeding of silibinin inhibits prostate tumor growth and progression in transgenic adenocarcinoma of the mouse prostate model
    • Raina K, Blouin MJ, Singh RP et al (2007) Dietary feeding of silibinin inhibits prostate tumor growth and progression in transgenic adenocarcinoma of the mouse prostate model. Cancer Res 67:11083-11091
    • (2007) Cancer Res , vol.67 , pp. 11083-11091
    • Raina, K.1    Blouin, M.J.2    Singh, R.P.3
  • 375
    • 65949108395 scopus 로고    scopus 로고
    • Silibinin feeding alters the metabolic profile in tramp prostatic tumors: 1H-nmrs-based metabolomics study
    • Raina K, Serkova NJ, Agarwal R (2009) Silibinin feeding alters the metabolic profile in TRAMP prostatic tumors: 1H-NMRS-based metabolomics study. Cancer Res 69:3731-3735
    • (2009) Cancer Res , vol.69 , pp. 3731-3735
    • Raina, K.1    Serkova, N.J.2    Agarwal, R.3
  • 376
    • 53049106036 scopus 로고    scopus 로고
    • Stage-speacific inhibitory effects and associated mechanisms of silibinin on tumor progression and metastasis in transgenic adenocarcinoma of the mouse prostate model
    • Raina K, Rajamanickam S, Singh RP et al (2008) Stage-speacific inhibitory effects and associated mechanisms of silibinin on tumor progression and metastasis in transgenic adenocarcinoma of the mouse prostate model. Cancer Res 68:6822-6830
    • (2008) Cancer Res , vol.68 , pp. 6822-6830
    • Raina, K.1    Rajamanickam, S.2    Singh, R.P.3
  • 377
    • 17844383964 scopus 로고    scopus 로고
    • Perturbational profiling of a cell-line model of tumorigenesis by using metabolic measurements
    • Ramanathan A, Wang C, Schreiber SL (2005) Perturbational profiling of a cell-line model of tumorigenesis by using metabolic measurements. Pnas 102:5992-5997
    • (2005) PNAS , vol.102 , pp. 5992-5997
    • Ramanathan, A.1    Wang, C.2    Schreiber, S.L.3
  • 379
    • 77949479965 scopus 로고    scopus 로고
    • Reduced levels of hydroxylated, polyunsaturated ultra long-chain fatty acids in the serum of colorectal cancer patients: Implications for early screening and detection
    • Ritchie SA, Ahiahonu PWK, Jayasinghe D, Heath D, Liu J, Lu YS et al (2010) Reduced levels of hydroxylated, polyunsaturated ultra long-chain fatty acids in the serum of colorectal cancer patients: implications for early screening and detection. Bmc Med 8:13-32
    • (2010) BMC Med , vol.8 , pp. 13-32
    • Ritchie, S.A.1    Ahiahonu, P.2    Jayasinghe, D.3    Heath, D.4    Liu, J.5    Lu, Y.S.6
  • 380
    • 36549000754 scopus 로고    scopus 로고
    • Nmr-based metabolomics: Translational application and treatment of cancer
    • Serkova NJ, Spratlin JL, Eckhardt SG (2007) NMR-based metabolomics: translational application and treatment of cancer. Curr Opin Mol Ther 9:572-585
    • (2007) Curr Opin Mol Ther , vol.9 , pp. 572-585
    • Serkova, N.J.1    Spratlin, J.L.2    Eckhardt, S.G.3
  • 381
    • 33749529146 scopus 로고    scopus 로고
    • Pattern recognition and biomarker validation using quantitative 1h-nmr-based metabolomics
    • Serkova NJ, Niemann CU (2006) Pattern recognition and biomarker validation using quantitative 1H-NMR-based metabolomics. Expert Rev Mol Diagn 6:717-731
    • (2006) Expert Rev Mol Diagn , vol.6 , pp. 717-731
    • Serkova, N.J.1    Niemann, C.U.2
  • 383
    • 21244439545 scopus 로고    scopus 로고
    • Purge nmr: Effective and easy solvent suppression
    • Simpson AJ, Brown SA (2005) Purge NMR: effective and easy solvent suppression. J Magn Reson 175:340-346
    • (2005) J Magn Reson , vol.175 , pp. 340-346
    • Simpson, A.J.1    Brown, S.A.2
  • 384
    • 0014197617 scopus 로고
    • Selective release of ribonuclease-inhibitor from bacillus subtilis cells by cold shock treatment
    • Smeaton JR, Elliott WH (1967) Selective release of ribonuclease-inhibitor from Bacillus subtilis cells by cold shock treatment. Biochem Biophys Res Commun 26:75-81
    • (1967) Biochem Biophys Res Commun , vol.26 , pp. 75-81
    • Smeaton, J.R.1    Elliott, W.H.2
  • 385
    • 84859357918 scopus 로고    scopus 로고
    • Push-through direct injection nmr: An optimized automation method applied to metabolomics
    • Teng Q, Ekman DR, Huang W, Collette TW (2012) Push-through direct injection NMR: an optimized automation method applied to metabolomics. Analyst 137:2226-2232
    • (2012) Analyst , vol.137 , pp. 2226-2232
    • Teng, Q.1    Ekman, D.R.2    Huang, W.3    Collette, T.W.4
  • 386
    • 67349235296 scopus 로고    scopus 로고
    • A direct cell quenching method for cell-culture based metabolomics
    • Teng Q, Huang W, Collette TW, Ekman DR, Tan C (2009) A direct cell quenching method for cell-culture based metabolomics. Metabolomics 5:199-208
    • (2009) Metabolomics , vol.5 , pp. 199-208
    • Teng, Q.1    Huang, W.2    Collette, T.W.3    Ekman, D.R.4    Tan, C.5
  • 387
    • 62549138339 scopus 로고    scopus 로고
    • Early stage diagnosis of oral cancer using 1h nmr-based metabolomics
    • Tiziani S, Lopes V, Gunther UL (2009) Early stage diagnosis of oral cancer using 1H NMR-based metabolomics. Neoplasia 11:269-276
    • (2009) Neoplasia , vol.11 , pp. 269-276
    • Tiziani, S.1    Lopes, V.2    Gunther, U.L.3
  • 388
    • 0032935018 scopus 로고    scopus 로고
    • Magnetic resonance spectroscopy of serum and acute-phase proteins revisited: A multiparametric statistical analysis of metabolite variations in inflammatory, infectious and miscellaneous diseases
    • Torri GM, Torri J, Gulian JM, Vion-Dury J, Viout P, Cozzone PJ (1999) Magnetic resonance spectroscopy of serum and acute-phase proteins revisited: a multiparametric statistical analysis of metabolite variations in inflammatory, infectious and miscellaneous diseases. Clin Chim Acta 279:77-96
    • (1999) Clin Chim Acta , vol.279 , pp. 77-96
    • Torri, G.M.1    Torri, J.2    Gulian, J.M.3    Vion-Dury, J.4    Viout, P.5    Cozzone, P.J.6
  • 390
    • 33747019547 scopus 로고    scopus 로고
    • Centering, scaling, and transformations: Improving the biological information content of metabolomics data
    • van den Berg RA, Hoefsloot HCJ, Westerhuis JA, Smilde AK, van der Werf MJ (2006) Centering, scaling, and transformations: improving the biological information content of metabolomics data. Genomics 7:142-156
    • (2006) Genomics , vol.7 , pp. 142-156
    • Van Den Berg, R.A.1    Hoefsloot, H.2    Westerhuis, J.A.3    Smilde, A.K.4    Van Der Werf, M.J.5
  • 391
    • 32444433438 scopus 로고    scopus 로고
    • Symbiosis of chemometrics and metabolomics: Past, present, and future
    • Van der Greef J, Smilde AK (2005) Symbiosis of chemometrics and metabolomics: past, present, and future. J Chemomet 19:376-386
    • (2005) J Chemomet , vol.19 , pp. 376-386
    • Van Der Greef, J.1    Smilde, A.K.2
  • 392
    • 0141757204 scopus 로고    scopus 로고
    • Improved methods for the acquisition and interpretation of nmr metabolomic data
    • Viant M (2003) Improved methods for the acquisition and interpretation of NMR metabolomic data. Biochem Biophys Res Commun 310:943-948
    • (2003) Biochem Biophys Res Commun , vol.310 , pp. 943-948
    • Viant, M.1
  • 393
    • 34548545724 scopus 로고    scopus 로고
    • Revealing the metabolome of animal tissues using 1h nuclear magnetic resonance spectroscopy
    • Methods in molecular biology, Weckwerth W, Clifton, NJ, Humana Press
    • Viant MR (2007) Revealing the metabolome of animal tissues using 1H nuclear magnetic resonance spectroscopy. In: Methods in molecular biology, Weckwerth W (ed). Clifton, NJ, Humana Press, 358:229-246
    • (2007) Methods in Molecular Biology , vol.358 , pp. 229-246
    • Viant, M.R.1
  • 395
    • 0000459772 scopus 로고
    • Biochem Z (German), (Reprinted in Warburg O. On metabolism of tumors. Constable, London)
    • Warburg O, Posener K, Negelei E (1924/1930) Ueber den Stoffwechsel der Tumoren. Biochem Z (German) 152:319-344 (Reprinted in Warburg O. On metabolism of tumors. Constable, London)
    • (1924) Ueber Den Stoffwechsel Der Tumoren , vol.152 , pp. 319-344
    • Warburg, O.1    Posener, K.2    Negelei, E.3
  • 396
    • 0001221508 scopus 로고
    • On respiratory impairment in cancer cells
    • Warburg O (1956) On respiratory impairment in cancer cells. Science 124:269-270
    • (1956) Science , vol.124 , pp. 269-270
    • Warburg, O.1
  • 398
    • 33846088138 scopus 로고    scopus 로고
    • Hmdb: The human metabolome database
    • Wishart DS, Tzur D, Knox C et al (2007) HMDB: the human metabolome database. Nucleic Acids Res 35:D521-D526
    • (2007) Nucleic Acids Res , vol.35 , pp. D521-D526
    • Wishart, D.S.1    Tzur, D.2    Knox, C.3
  • 399
    • 0001681052 scopus 로고
    • The colunearity problem in linear regression. The partial least squares (pls) approach to generalized inverses
    • Wold S, Ruhe A, Wold H, Dunn WJ III (1984) The colUnearity problem in linear regression. The partial least squares (PLS) approach to generalized inverses. Siam J Sci Stat Comput 5:735-743
    • (1984) SIAM J Sci Stat Comput , vol.5 , pp. 735-743
    • Wold, S.1    Ruhe, A.2    Wold, H.3    Dunn, W.4
  • 403
    • 34547171180 scopus 로고    scopus 로고
    • Metabonomic studies of human hepatocellular carcinoma using high-resolution magic-angle spinning 1h nmr spectroscopy in conjunction with multivariate data analysis
    • Yang YX, Li CL, Nie X, Feng X, Chen W, Yue Y et al (2007b) Metabonomic studies of human hepatocellular carcinoma using high-resolution magic-angle spinning 1H NMR spectroscopy in conjunction with multivariate data analysis. J Proteome Res 6:2605-2614
    • (2007) J Proteome Res , vol.6 , pp. 2605-2614
    • Yang, Y.X.1    Li, C.L.2    Nie, X.3    Feng, X.4    Chen, W.5    Yue, Y.6
  • 404
    • 5344244045 scopus 로고    scopus 로고
    • Experimental animal urine collection: A review
    • Kurien BT, Everds NE, Scofield RH (2004) Experimental animal urine collection: a review. Lab Anim 38:333-361
    • (2004) Lab Anim , vol.38 , pp. 333-361
    • Kurien, B.T.1    Everds, N.E.2    Scofield, R.H.3


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