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Volumn 8, Issue 5, 2013, Pages

BcL-xL Conformational Changes upon Fragment Binding Revealed by NMR

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN BCL XL;

EID: 84878164756     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0064400     Document Type: Article
Times cited : (8)

References (76)
  • 1
    • 84862659868 scopus 로고    scopus 로고
    • History of protein-protein interactions: from egg-white to complex networks
    • Braun P, Gingras AC, (2012) History of protein-protein interactions: from egg-white to complex networks. Proteomics 12: 1478-1498.
    • (2012) Proteomics , vol.12 , pp. 1478-1498
    • Braun, P.1    Gingras, A.C.2
  • 2
    • 84856389159 scopus 로고    scopus 로고
    • Structural biology and drug discovery of difficult targets: the limits of ligandability
    • Surade S, Blundell TL, (2012) Structural biology and drug discovery of difficult targets: the limits of ligandability. Chem Biol 19: 42-50.
    • (2012) Chem Biol , vol.19 , pp. 42-50
    • Surade, S.1    Blundell, T.L.2
  • 3
    • 84873433440 scopus 로고    scopus 로고
    • Using a fragment-based approach to target protein-protein interactions
    • Scott DE, Ehebauer MT, Pukala T, Marsh M, Blundell TL, et al. (2013) Using a fragment-based approach to target protein-protein interactions. Chembiochem 14: 332-342.
    • (2013) Chembiochem , vol.14 , pp. 332-342
    • Scott, D.E.1    Ehebauer, M.T.2    Pukala, T.3    Marsh, M.4    Blundell, T.L.5
  • 4
    • 79960990847 scopus 로고    scopus 로고
    • Chemical and structural lessons from recent successes in protein-protein interaction inhibition (2p2i)
    • Morelli X, Bourgeas R, Roche P, (2011) Chemical and structural lessons from recent successes in protein-protein interaction inhibition (2p2i). Curr Opin Chem Biol 15: 475-481.
    • (2011) Curr Opin Chem Biol , vol.15 , pp. 475-481
    • Morelli, X.1    Bourgeas, R.2    Roche, P.3
  • 7
    • 84866362396 scopus 로고    scopus 로고
    • Using fragment-based technologies to target protein-protein interac-tions
    • Bower JF, Pannifer A, (2012) Using fragment-based technologies to target protein-protein interac-tions. Curr Pharm Des 18: 4685-4696.
    • (2012) Curr Pharm Des , vol.18 , pp. 4685-4696
    • Bower, J.F.1    Pannifer, A.2
  • 8
    • 84868026890 scopus 로고    scopus 로고
    • Dissecting fragment-based lead discovery at the von hippel-lindau protein:hypoxia inducible factor 1alpha protein-protein interface
    • Molle IV, Thomann A, Buckley DL, So EC, Lang S, et al. (2012) Dissecting fragment-based lead discovery at the von hippel-lindau protein:hypoxia inducible factor 1alpha protein-protein interface. Chem Biol 19: 1300-1312.
    • (2012) Chem Biol , vol.19 , pp. 1300-1312
    • Molle, I.V.1    Thomann, A.2    Buckley, D.L.3    So, E.C.4    Lang, S.5
  • 10
    • 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
  • 11
    • 1942453243 scopus 로고    scopus 로고
    • Ligand efficiency: a useful metric for lead selection
    • Hopkins AL, Groom CR, Alex A, (2004) Ligand efficiency: a useful metric for lead selection. Drug Discov Today 9: 430-431.
    • (2004) Drug Discov Today , vol.9 , pp. 430-431
    • Hopkins, A.L.1    Groom, C.R.2    Alex, A.3
  • 14
    • 77958048793 scopus 로고    scopus 로고
    • Discovery of a potent and selective bcl-2 inhibitor using sar by nmr
    • Petros AM, Huth JR, Oost T, Park CM, Ding H, et al. (2010) Discovery of a potent and selective bcl-2 inhibitor using sar by nmr. Bioorg Med Chem Lett 20: 6587-6591.
    • (2010) Bioorg Med Chem Lett , vol.20 , pp. 6587-6591
    • Petros, A.M.1    Huth, J.R.2    Oost, T.3    Park, C.M.4    Ding, H.5
  • 15
    • 31544467109 scopus 로고    scopus 로고
    • Discovery of a potent inhibitor of the antiapoptotic protein bcl-xl from nmr and parallel synthesis
    • Petros AM, Dinges J, Augeri DJ, Baumeister SA, Betebenner DA, et al. (2006) Discovery of a potent inhibitor of the antiapoptotic protein bcl-xl from nmr and parallel synthesis. J Med Chem 49: 656-663.
    • (2006) J Med Chem , vol.49 , pp. 656-663
    • Petros, A.M.1    Dinges, J.2    Augeri, D.J.3    Baumeister, S.A.4    Betebenner, D.A.5
  • 16
    • 34548047900 scopus 로고    scopus 로고
    • Crystal structure of abt-737 complexed with bcl-xl: implications for selectivity of antagonists of the bcl-2 family
    • Lee EF, Czabotar PE, Smith BJ, Deshayes K, Zobel K, et al. (2007) Crystal structure of abt-737 complexed with bcl-xl: implications for selectivity of antagonists of the bcl-2 family. Cell Death Differ 14: 1711-1713.
    • (2007) Cell Death Differ , vol.14 , pp. 1711-1713
    • Lee, E.F.1    Czabotar, P.E.2    Smith, B.J.3    Deshayes, K.4    Zobel, K.5
  • 17
    • 84872301920 scopus 로고    scopus 로고
    • Discovery of potent myeloid cell leukemia 1 (mcl-1) inhibitors using fragment-based methods and structure-based design
    • Friberg A, Vigil D, Zhao B, Daniels RN, Burke JP, et al. (2013) Discovery of potent myeloid cell leukemia 1 (mcl-1) inhibitors using fragment-based methods and structure-based design. J Med Chem 56: 15-30.
    • (2013) J Med Chem , vol.56 , pp. 15-30
    • Friberg, A.1    Vigil, D.2    Zhao, B.3    Daniels, R.N.4    Burke, J.P.5
  • 18
    • 80052384557 scopus 로고    scopus 로고
    • Sar by interligand nuclear overhauser effects (iloes) based discovery of acylsulfonamide compounds active against bcl-x(l) and mcl-1
    • Rega MF, Wu B, Wei J, Zhang Z, Cellitti JF, et al. (2011) Sar by interligand nuclear overhauser effects (iloes) based discovery of acylsulfonamide compounds active against bcl-x(l) and mcl-1. J Med Chem 54: 6000-6013.
    • (2011) J Med Chem , vol.54 , pp. 6000-6013
    • Rega, M.F.1    Wu, B.2    Wei, J.3    Zhang, Z.4    Cellitti, J.F.5
  • 19
    • 0037414274 scopus 로고    scopus 로고
    • Discovery of a potent small molecule il-2 inhibitor through fragment assembly
    • Braisted AC, Oslob JD, Delano WL, Hyde J, McDowell RS, et al. (2003) Discovery of a potent small molecule il-2 inhibitor through fragment assembly. J Am Chem Soc 125: 3714-3715.
    • (2003) J Am Chem Soc , vol.125 , pp. 3714-3715
    • Braisted, A.C.1    Oslob, J.D.2    Delano, W.L.3    Hyde, J.4    McDowell, R.S.5
  • 20
    • 33750067690 scopus 로고    scopus 로고
    • Discovery of novel inhibitors of the zipa/ftsz complex by nmr fragment screening coupled with structure-based design
    • Tsao DHH, Sutherland AG, Jennings LD, Li Y, Rush TS, et al. (2006) Discovery of novel inhibitors of the zipa/ftsz complex by nmr fragment screening coupled with structure-based design. Bioorg Med Chem 14: 7953-7961.
    • (2006) Bioorg Med Chem , vol.14 , pp. 7953-7961
    • Tsao, D.H.H.1    Sutherland, A.G.2    Jennings, L.D.3    Li, Y.4    Rush, T.S.5
  • 21
    • 84862649997 scopus 로고    scopus 로고
    • Discovery of small molecules that bind to k-ras and inhibit sos-mediated activation
    • Sun Q, Burke JP, Phan J, Burns MC, Olejniczak ET, et al. (2012) Discovery of small molecules that bind to k-ras and inhibit sos-mediated activation. Angew Chem Int Ed Engl 51: 6140-6143.
    • (2012) Angew Chem Int Ed Engl , vol.51 , pp. 6140-6143
    • Sun, Q.1    Burke, J.P.2    Phan, J.3    Burns, M.C.4    Olejniczak, E.T.5
  • 22
    • 84859463451 scopus 로고    scopus 로고
    • Small-molecule ligands bind to a distinct pocket in ras and inhibit sos-mediated nucleotide exchange activity
    • Maurer T, Garrenton LS, Oh A, Pitts K, Anderson DJ, et al. (2012) Small-molecule ligands bind to a distinct pocket in ras and inhibit sos-mediated nucleotide exchange activity. Proc Natl Acad Sci U S A 109: 5299-5304.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 5299-5304
    • Maurer, T.1    Garrenton, L.S.2    Oh, A.3    Pitts, K.4    Anderson, D.J.5
  • 25
    • 33751076241 scopus 로고    scopus 로고
    • Deconstructing fragment-based inhibitor discovery
    • Babaoglu K, Shoichet BK, (2006) Deconstructing fragment-based inhibitor discovery. Nat Chem Biol 2: 720-723.
    • (2006) Nat Chem Biol , vol.2 , pp. 720-723
    • Babaoglu, K.1    Shoichet, B.K.2
  • 26
    • 38149105771 scopus 로고    scopus 로고
    • Fragment-based identification of determinants of conformational and spectroscopic change at the ricin active site
    • Carra JH, McHugh CA, Mulligan S, Machiesky LM, Soares AS, et al. (2007) Fragment-based identification of determinants of conformational and spectroscopic change at the ricin active site. BMC Struct Biol 7: 72.
    • (2007) BMC Struct Biol , vol.7 , pp. 72
    • Carra, J.H.1    McHugh, C.A.2    Mulligan, S.3    Machiesky, L.M.4    Soares, A.S.5
  • 27
    • 49249150528 scopus 로고
    • Ring current theories in nuclear magnetic resonance
    • Haigh C, Mallion R, (1979) Ring current theories in nuclear magnetic resonance. Prog Nucl Magn Reson Spectrosc 13: 303-344.
    • (1979) Prog Nucl Magn Reson Spectrosc , vol.13 , pp. 303-344
    • Haigh, C.1    Mallion, R.2
  • 28
    • 0038407231 scopus 로고    scopus 로고
    • Rapid and accurate calculation of protein 1 h, 13c and 15n chemical shifts
    • Neal S, Nip AM, Zhang H, Wishart DS, (2003) Rapid and accurate calculation of protein 1 h, 13c and 15n chemical shifts. J Biomol NMR 26: 215-240.
    • (2003) J Biomol NMR , vol.26 , pp. 215-240
    • Neal, S.1    Nip, A.M.2    Zhang, H.3    Wishart, D.S.4
  • 29
    • 0035544152 scopus 로고    scopus 로고
    • Automated prediction of 15n, 13calpha, 13cbeta and 13c′ chemical shifts in proteins using a density functional database
    • Xu XP, Case DA, (2001) Automated prediction of 15n, 13calpha, 13cbeta and 13c′ chemical shifts in proteins using a density functional database. J Biomol NMR 21: 321-333.
    • (2001) J Biomol NMR , vol.21 , pp. 321-333
    • Xu, X.P.1    Case, D.A.2
  • 30
    • 0033636878 scopus 로고    scopus 로고
    • Alignment of weakly interacting molecules to protein surfaces using simulations of chemical shift perturbations
    • McCoy MA, Wyss DF, (2000) Alignment of weakly interacting molecules to protein surfaces using simulations of chemical shift perturbations. J Biomol NMR 18: 189-198.
    • (2000) J Biomol NMR , vol.18 , pp. 189-198
    • McCoy, M.A.1    Wyss, D.F.2
  • 31
  • 32
    • 56249144184 scopus 로고    scopus 로고
    • Discovery of an orally bioavailable small molecule inhibitor of prosurvival b-cell lymphoma 2 proteins
    • Park CM, Bruncko M, Adickes J, Bauch J, Ding H, et al. (2008) Discovery of an orally bioavailable small molecule inhibitor of prosurvival b-cell lymphoma 2 proteins. J Med Chem 51: 6902-6915.
    • (2008) J Med Chem , vol.51 , pp. 6902-6915
    • Park, C.M.1    Bruncko, M.2    Adickes, J.3    Bauch, J.4    Ding, H.5
  • 34
    • 32644473650 scopus 로고    scopus 로고
    • How the bcl-2 family of proteins interact to regulate apoptosis
    • van Delft MF, Huang DCS, (2006) How the bcl-2 family of proteins interact to regulate apoptosis. Cell Res 16: 203-213.
    • (2006) Cell Res , vol.16 , pp. 203-213
    • van Delft, M.F.1    Huang, D.C.S.2
  • 35
    • 37549048249 scopus 로고    scopus 로고
    • The bcl-2 protein family: opposing activities that mediate cell death
    • Youle RJ, Strasser A, (2008) The bcl-2 protein family: opposing activities that mediate cell death. Nat Rev Mol Cell Biol 9: 47-59.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 47-59
    • Youle, R.J.1    Strasser, A.2
  • 36
    • 0030614915 scopus 로고    scopus 로고
    • Structure of bcl-xl-bak peptide complex: recognition between regulators of apoptosis
    • Sattler M, Liang H, Nettesheim D, Meadows RP, Harlan JE, et al. (1997) Structure of bcl-xl-bak peptide complex: recognition between regulators of apoptosis. Science 275: 983-986.
    • (1997) Science , vol.275 , pp. 983-986
    • Sattler, M.1    Liang, H.2    Nettesheim, D.3    Meadows, R.P.4    Harlan, J.E.5
  • 37
    • 17744396094 scopus 로고    scopus 로고
    • Rationale for bcl-xl/bad peptide complex formation from structure, mutagenesis, and biophysical studies
    • Petros AM, Nettesheim DG, Wang Y, Olejniczak ET, Meadows RP, et al. (2000) Rationale for bcl-xl/bad peptide complex formation from structure, mutagenesis, and biophysical studies. Protein Sci 9: 2528-2534.
    • (2000) Protein Sci , vol.9 , pp. 2528-2534
    • Petros, A.M.1    Nettesheim, D.G.2    Wang, Y.3    Olejniczak, E.T.4    Meadows, R.P.5
  • 38
    • 0042220409 scopus 로고    scopus 로고
    • The structure of a bcl-xl/bim fragment complex: implications for bim function
    • Liu X, Dai S, Zhu Y, Marrack P, Kappler JW, (2003) The structure of a bcl-xl/bim fragment complex: implications for bim function. Immunity 19: 341-352.
    • (2003) Immunity , vol.19 , pp. 341-352
    • Liu, X.1    Dai, S.2    Zhu, Y.3    Marrack, P.4    Kappler, J.W.5
  • 39
    • 34547689505 scopus 로고    scopus 로고
    • Molecular basis of bcl-xl's target recognition versatility revealed by the structure of bcl-xl in complex with the bh3 domain of beclin-1
    • Feng W, Huang S, Wu H, Zhang M, (2007) Molecular basis of bcl-xl's target recognition versatility revealed by the structure of bcl-xl in complex with the bh3 domain of beclin-1. J Mol Biol 372: 223-235.
    • (2007) J Mol Biol , vol.372 , pp. 223-235
    • Feng, W.1    Huang, S.2    Wu, H.3    Zhang, M.4
  • 40
    • 33847404358 scopus 로고    scopus 로고
    • Studies leading to potent, dual inhibitors of bcl-2 and bcl-xl
    • Bruncko M, Oost TK, Belli BA, Ding H, Joseph MK, et al. (2007) Studies leading to potent, dual inhibitors of bcl-2 and bcl-xl. J Med Chem 50: 641-662.
    • (2007) J Med Chem , vol.50 , pp. 641-662
    • Bruncko, M.1    Oost, T.K.2    Belli, B.A.3    Ding, H.4    Joseph, M.K.5
  • 41
    • 33744913530 scopus 로고    scopus 로고
    • Protein-ligand noe matching: a high-throughput method for binding pose evaluation that does not require protein nmr resonance assignments
    • Constantine KL, Davis ME, Metzler WJ, Mueller L, Claus BL, (2006) Protein-ligand noe matching: a high-throughput method for binding pose evaluation that does not require protein nmr resonance assignments. J Am Chem Soc 128: 7252-7263.
    • (2006) J Am Chem Soc , vol.128 , pp. 7252-7263
    • Constantine, K.L.1    Davis, M.E.2    Metzler, W.J.3    Mueller, L.4    Claus, B.L.5
  • 42
    • 70349394112 scopus 로고    scopus 로고
    • Application of protein-ligand NOE matching to the rapid evaluation of fragment binding poses
    • In: Zartler ER, Shapiro MJ, editors, Chichester: John Wiley and sons
    • Metzler WJ, Caus BL, McDonnell PA, Johnson SR, Goldfarb V, et al. (2008) Application of protein-ligand NOE matching to the rapid evaluation of fragment binding poses. In: Zartler ER, Shapiro MJ, editors. Fragment-Based Drug Discovery. Chichester: John Wiley and sons. pp. 99-133.
    • (2008) Fragment-Based Drug Discovery , pp. 99-133
    • Metzler, W.J.1    Caus, B.L.2    McDonnell, P.A.3    Johnson, S.R.4    Goldfarb, V.5
  • 43
    • 0035443893 scopus 로고    scopus 로고
    • Dipolar couplings as a probe of molecular dynamics and structure in solution
    • Tolman JR, (2001) Dipolar couplings as a probe of molecular dynamics and structure in solution. Curr Opin Struct Biol 11: 532-539.
    • (2001) Curr Opin Struct Biol , vol.11 , pp. 532-539
    • Tolman, J.R.1
  • 44
    • 33645936984 scopus 로고    scopus 로고
    • Residual dipolar couplings: Measurements and applications to biomolecular studies
    • In: Webb GA, editor, Academic Press, Annual Reports on NMR Spectroscopy
    • Hu W, Wang L (2006) Residual dipolar couplings: Measurements and applications to biomolecular studies. In: Webb GA, editor, Annual Reports on NMR Spectroscopy, Academic Press, volume 58 of Annual Reports on NMR Spectroscopy. pp. 231-303.
    • (2006) Annual Reports on NMR Spectroscopy , vol.58 , pp. 231-303
    • Hu, W.1    Wang, L.2
  • 45
    • 77449091505 scopus 로고    scopus 로고
    • Bclxl changes conformation upon binding to wild-type but not mutant p53 dna binding domain
    • Hagn F, Klein C, Demmer O, Marchenko N, Vaseva A, et al. (2010) Bclxl changes conformation upon binding to wild-type but not mutant p53 dna binding domain. J Biol Chem 285: 3439-3450.
    • (2010) J Biol Chem , vol.285 , pp. 3439-3450
    • Hagn, F.1    Klein, C.2    Demmer, O.3    Marchenko, N.4    Vaseva, A.5
  • 46
    • 39649120317 scopus 로고    scopus 로고
    • Affinity makes the difference: nonselective interaction of the uba domain of ubiquilin-1 with monomeric ubiquitin and polyubiquitin chains
    • Zhang D, Raasi S, Fushman D, (2008) Affinity makes the difference: nonselective interaction of the uba domain of ubiquilin-1 with monomeric ubiquitin and polyubiquitin chains. J Mol Biol 377: 162-180.
    • (2008) J Mol Biol , vol.377 , pp. 162-180
    • Zhang, D.1    Raasi, S.2    Fushman, D.3
  • 47
    • 0344838627 scopus 로고    scopus 로고
    • Conformational differences in liganded and unliganded states of galectin-3
    • Umemoto K, Leffler H, Venot A, Valafar H, Prestegard JH, (2003) Conformational differences in liganded and unliganded states of galectin-3. Biochemistry 42: 3688-3695.
    • (2003) Biochemistry , vol.42 , pp. 3688-3695
    • Umemoto, K.1    Leffler, H.2    Venot, A.3    Valafar, H.4    Prestegard, J.H.5
  • 48
    • 0035941534 scopus 로고    scopus 로고
    • Conformational analysis of a exible oligosaccharide using residual dipolar couplings
    • Tian F, Al-Hashimi HM, Craighead JL, Prestegard JH, (2001) Conformational analysis of a exible oligosaccharide using residual dipolar couplings. J Am Chem Soc 123: 485-492.
    • (2001) J Am Chem Soc , vol.123 , pp. 485-492
    • Tian, F.1    Al-Hashimi, H.M.2    Craighead, J.L.3    Prestegard, J.H.4
  • 50
    • 70349932423 scopus 로고    scopus 로고
    • Autodock4 and autodock-tools4: Automated docking with selective receptor exibility
    • Morris GM, Huey R, Lindstrom W, Sanner MF, Belew RK, et al. (2009) Autodock4 and autodock-tools4: Automated docking with selective receptor exibility. J Comput Chem 30: 2785-2791.
    • (2009) J Comput Chem , vol.30 , pp. 2785-2791
    • Morris, G.M.1    Huey, R.2    Lindstrom, W.3    Sanner, M.F.4    Belew, R.K.5
  • 51
    • 77249094569 scopus 로고    scopus 로고
    • Application of fragment-based nmr screening, x-ray crystallography, structure-based design, and focused chemical library design to identify novel microm leads for the development of nm bace-1 (beta-site app cleaving enzyme 1) inhibitors
    • Wang YS, Strickland C, Voigt JH, Kennedy ME, Beyer BM, et al. (2010) Application of fragment-based nmr screening, x-ray crystallography, structure-based design, and focused chemical library design to identify novel microm leads for the development of nm bace-1 (beta-site app cleaving enzyme 1) inhibitors. J Med Chem 53: 942-950.
    • (2010) J Med Chem , vol.53 , pp. 942-950
    • Wang, Y.S.1    Strickland, C.2    Voigt, J.H.3    Kennedy, M.E.4    Beyer, B.M.5
  • 52
    • 58049204429 scopus 로고    scopus 로고
    • Role of protein exibility in the design of bcl-x(l) targeting agents: insight from molecular dynamics
    • Novak W, Wang H, Krilov G, (2009) Role of protein exibility in the design of bcl-x(l) targeting agents: insight from molecular dynamics. J Comput Aided Mol Des 23: 49-61.
    • (2009) J Comput Aided Mol Des , vol.23 , pp. 49-61
    • Novak, W.1    Wang, H.2    Krilov, G.3
  • 53
    • 84859783234 scopus 로고    scopus 로고
    • Analysis of exibility and hotspots in bcl-xl and mcl-1 proteins for the design of selective small-molecule inhibitors
    • Yang CY, Wang S, (2012) Analysis of exibility and hotspots in bcl-xl and mcl-1 proteins for the design of selective small-molecule inhibitors. ACS Medicinal Chemistry Letters 3: 308-312.
    • (2012) ACS Medicinal Chemistry Letters , vol.3 , pp. 308-312
    • Yang, C.Y.1    Wang, S.2
  • 54
    • 0037009985 scopus 로고    scopus 로고
    • Spatial localization of ligand binding sites from electron current density surfaces calculated from nmr chemical shift perturbations
    • McCoy MA, Wyss DF, (2002) Spatial localization of ligand binding sites from electron current density surfaces calculated from nmr chemical shift perturbations. J Am Chem Soc 124: 11758-11763.
    • (2002) J Am Chem Soc , vol.124 , pp. 11758-11763
    • McCoy, M.A.1    Wyss, D.F.2
  • 55
    • 70350508200 scopus 로고    scopus 로고
    • Steering protein-ligand docking with quantitative nmr chemical shift perturbations
    • Gonzlez-Ruiz D, Gohlke H, (2009) Steering protein-ligand docking with quantitative nmr chemical shift perturbations. J Chem Inf Model 49: 2260-2271.
    • (2009) J Chem Inf Model , vol.49 , pp. 2260-2271
    • Gonzlez-Ruiz, D.1    Gohlke, H.2
  • 56
    • 0034923356 scopus 로고    scopus 로고
    • Use of chemical shifts in macromolecular structure determination
    • Wishart DS, Case DA, (2001) Use of chemical shifts in macromolecular structure determination. Methods Enzymol 338: 3-34.
    • (2001) Methods Enzymol , vol.338 , pp. 3-34
    • Wishart, D.S.1    Case, D.A.2
  • 57
    • 33746645192 scopus 로고    scopus 로고
    • Cooperative hydrogen bonding effects are key determinants of backbone amide proton chemical shifts in proteins
    • Parker LL, Houk AR, Jensen JH, (2006) Cooperative hydrogen bonding effects are key determinants of backbone amide proton chemical shifts in proteins. J Am Chem Soc 128: 9863-9872.
    • (2006) J Am Chem Soc , vol.128 , pp. 9863-9872
    • Parker, L.L.1    Houk, A.R.2    Jensen, J.H.3
  • 58
    • 34249098127 scopus 로고    scopus 로고
    • A new model for chemical shifts of amide hydrogens in proteins
    • Moon S, Case DA, (2007) A new model for chemical shifts of amide hydrogens in proteins. J Biomol NMR 38: 139-150.
    • (2007) J Biomol NMR , vol.38 , pp. 139-150
    • Moon, S.1    Case, D.A.2
  • 59
    • 2342652311 scopus 로고    scopus 로고
    • Non-peptidic small-molecule inhibitors of the single-chain hepatitis c virus ns3 protease/ns4a cofactor complex discov-ered by structure-based nmr screening
    • Wyss DF, Arasappan A, Senior MM, Wang YS, Beyer BM, et al. (2004) Non-peptidic small-molecule inhibitors of the single-chain hepatitis c virus ns3 protease/ns4a cofactor complex discov-ered by structure-based nmr screening. J Med Chem 47: 2486-2498.
    • (2004) J Med Chem , vol.47 , pp. 2486-2498
    • Wyss, D.F.1    Arasappan, A.2    Senior, M.M.3    Wang, Y.S.4    Beyer, B.M.5
  • 60
    • 43049083331 scopus 로고    scopus 로고
    • Determination of protein-ligand binding modes using complexation-induced changes in (1)h nmr chemical shift
    • Cioffi M, Hunter CA, Packer MJ, Spitaleri A, (2008) Determination of protein-ligand binding modes using complexation-induced changes in (1)h nmr chemical shift. J Med Chem 51: 2512-2517.
    • (2008) J Med Chem , vol.51 , pp. 2512-2517
    • Cioffi, M.1    Hunter, C.A.2    Packer, M.J.3    Spitaleri, A.4
  • 61
    • 57549112574 scopus 로고    scopus 로고
    • Use of quantitative (1)h nmr chemical shift changes for ligand docking into barnase
    • Cioffi M, Hunter CA, Packer MJ, Pandya MJ, Williamson MP, (2009) Use of quantitative (1)h nmr chemical shift changes for ligand docking into barnase. J Biomol NMR 43: 11-19.
    • (2009) J Biomol NMR , vol.43 , pp. 11-19
    • Cioffi, M.1    Hunter, C.A.2    Packer, M.J.3    Pandya, M.J.4    Williamson, M.P.5
  • 62
    • 0029400480 scopus 로고
    • Nmrpipe: a multidimensional spectral processing system based on unix pipes
    • Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, et al. (1995) Nmrpipe: a multidimensional spectral processing system based on unix pipes. J Biomol NMR 6: 277-293.
    • (1995) J Biomol NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5
  • 63
    • 34249765651 scopus 로고
    • Nmr view: A computer program for the visualization and analysis of nmr data
    • Johnson BA, Blevins RA, (1994) Nmr view: A computer program for the visualization and analysis of nmr data. J Biomol NMR 4: 603-614.
    • (1994) J Biomol NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 64
    • 0004757060 scopus 로고    scopus 로고
    • University of California, San Fransisco, CA
    • Goddard TD, Kneller DG (2004) Sparky 3. University of California, San Fransisco, CA.
    • (2004) Sparky , vol.3
    • Goddard, T.D.1    Kneller, D.G.2
  • 65
    • 35848958773 scopus 로고    scopus 로고
    • Combined chemical shift changes and amino acid specific chemical shift mapping of protein-protein interactions
    • Schumann FH, Riepl H, Maurer T, Gronwald W, Neidig KP, et al. (2007) Combined chemical shift changes and amino acid specific chemical shift mapping of protein-protein interactions. J Biomol NMR 39: 275-289.
    • (2007) J Biomol NMR , vol.39 , pp. 275-289
    • Schumann, F.H.1    Riepl, H.2    Maurer, T.3    Gronwald, W.4    Neidig, K.P.5
  • 66
    • 0032976814 scopus 로고    scopus 로고
    • Complexation-induced changes in 1 h nmr chemical shift for supramolecular structure determination
    • Hunter CA, Packer MJ, (1999) Complexation-induced changes in 1 h nmr chemical shift for supramolecular structure determination. Chem Eur J 5: 1891-1897.
    • (1999) Chem Eur J , vol.5 , pp. 1891-1897
    • Hunter, C.A.1    Packer, M.J.2
  • 67
  • 68
    • 34547179849 scopus 로고    scopus 로고
    • Protein backbone chemical shifts predicted from searching a database for torsion angle and sequence homology
    • Shen Y, Bax A, (2007) Protein backbone chemical shifts predicted from searching a database for torsion angle and sequence homology. J Biomol NMR 38: 289-302.
    • (2007) J Biomol NMR , vol.38 , pp. 289-302
    • Shen, Y.1    Bax, A.2
  • 69
    • 79960264767 scopus 로고    scopus 로고
    • Definitive benchmark study of ring current effects on amide proton chemical shifts
    • Christensen AS, Sauer SPA, Jensen JH, (2011) Definitive benchmark study of ring current effects on amide proton chemical shifts. J Chem Theory Comput 7: 2078-2084.
    • (2011) J Chem Theory Comput , vol.7 , pp. 2078-2084
    • Christensen, A.S.1    Sauer, S.P.A.2    Jensen, J.H.3
  • 70
    • 0032042263 scopus 로고    scopus 로고
    • Measurement of j and dipolar couplings from simplified two-dimensional nmr spectra
    • Ottiger M, Delaglio F, Bax A, (1998) Measurement of j and dipolar couplings from simplified two-dimensional 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
  • 71
    • 0036922992 scopus 로고    scopus 로고
    • Structural properties of polyubiquitin chains in solution
    • Varadan R, Walker O, Pickart C, Fushman D, (2002) Structural properties of polyubiquitin chains in solution. J Mol Biol 324: 637-647.
    • (2002) J Mol Biol , vol.324 , pp. 637-647
    • Varadan, R.1    Walker, O.2    Pickart, C.3    Fushman, D.4
  • 72
    • 0033145058 scopus 로고    scopus 로고
    • Order matrix analysis of residual dipolar couplings using singular value decomposition
    • Losonczi JA, Andrec M, Fischer MW, Prestegard JH, (1999) Order matrix analysis of residual dipolar couplings using singular value decomposition. J Magn Reson 138: 334-342.
    • (1999) J Magn Reson , vol.138 , pp. 334-342
    • Losonczi, J.A.1    Andrec, M.2    Fischer, M.W.3    Prestegard, J.H.4
  • 73
    • 0032879507 scopus 로고    scopus 로고
    • R-factor, free r, and complete cross-validation for dipolar coupling refinement of nmr structures
    • Clore GM, Garrett DS, (1999) R-factor, free r, and complete cross-validation for dipolar coupling refinement of nmr structures. J Am Chem Soc 121: 9008-9012.
    • (1999) J Am Chem Soc , vol.121 , pp. 9008-9012
    • Clore, G.M.1    Garrett, D.S.2
  • 74
    • 80054911951 scopus 로고    scopus 로고
    • Ligplot+: multiple ligand-protein interaction diagrams for drug discovery
    • Laskowski RA, Swindells MB, (2011) Ligplot+: multiple ligand-protein interaction diagrams for drug discovery. J Chem Inf Model 51: 2778-2786.
    • (2011) J Chem Inf Model , vol.51 , pp. 2778-2786
    • Laskowski, R.A.1    Swindells, M.B.2
  • 76
    • 5244224827 scopus 로고    scopus 로고
    • X-ray and nmr structure of human bcl-xl, an inhibitor of programmed cell death
    • Muchmore SW, Sattler M, Liang H, Meadows RP, Harlan JE, et al. (1996) X-ray and nmr structure of human bcl-xl, an inhibitor of programmed cell death. Nature 381: 335-341.
    • (1996) Nature , vol.381 , pp. 335-341
    • Muchmore, S.W.1    Sattler, M.2    Liang, H.3    Meadows, R.P.4    Harlan, J.E.5


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