메뉴 건너뛰기




Volumn 110, Issue 47, 2013, Pages

NMR reveals the allosteric opening and closing of Abelson tyrosine kinase by ATP-site and myristoyl pocket inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEIN; BCR ABL PROTEIN; GNF 5 PROTEIN; IMATINIB; PROTEIN SH2; PROTEIN SH3; PROTEIN TYROSINE KINASE INHIBITOR; UNCLASSIFIED DRUG;

EID: 84888104464     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1314712110     Document Type: Article
Times cited : (103)

References (58)
  • 2
    • 0037169351 scopus 로고    scopus 로고
    • Autoinhibition of c-Abl
    • Pluk H, Dorey K, Superti-Furga G (2002) Autoinhibition of c-Abl. Cell 108(2-247-259
    • (2002) Cell , vol.108 , Issue.2 , pp. 247-259
    • Pluk, H.1    Dorey, K.2    Superti-Furga, G.3
  • 3
    • 0344626926 scopus 로고    scopus 로고
    • Structural basis for the autoinhibition of c-Abl tyrosine kinase
    • Nagar B, et al. (2003) Structural basis for the autoinhibition of c-Abl tyrosine kinase. Cell 112(6-859-871
    • (2003) Cell , vol.112 , Issue.6 , pp. 859-871
    • Nagar, B.1
  • 4
    • 0344626925 scopus 로고    scopus 로고
    • A myristoyl/phosphotyrosine switch regulates c-Abl
    • Hantschel O, et al. (2003) A myristoyl/phosphotyrosine switch regulates c-Abl. Cell 112(6-845-857
    • (2003) Cell , vol.112 , Issue.6 , pp. 845-857
    • Hantschel, O.1
  • 5
    • 33644871166 scopus 로고    scopus 로고
    • Organization of the SH3-SH2 unit in active and inactive forms of the c-Abl tyrosine kinase
    • Nagar B, et al. (2006) Organization of the SH3-SH2 unit in active and inactive forms of the c-Abl tyrosine kinase. Mol Cell 21(6-787-798
    • (2006) Mol Cell , vol.21 , Issue.6 , pp. 787-798
    • Nagar, B.1
  • 6
    • 0025117392 scopus 로고
    • Induction of chronic myelogenous leukemia in mice by the P210bcr/abl gene of the Philadelphia chromosome
    • Daley GQ, Van Etten RA, Baltimore D (1990) Induction of chronic myelogenous leukemia in mice by the P210bcr/abl gene of the Philadelphia chromosome. Science 247(4944-824-830
    • (1990) Science , vol.247 , Issue.4944 , pp. 824-830
    • Daley, G.Q.1    Van Etten, R.A.2    Baltimore, D.3
  • 7
    • 0033614446 scopus 로고    scopus 로고
    • Chronic myeloid leukemia
    • Sawyers CL (1999) Chronic myeloid leukemia. N Engl J Med 340(17-1330-1340
    • (1999) N Engl J Med , vol.340 , Issue.17 , pp. 1330-1340
    • Sawyers, C.L.1
  • 8
    • 0029947186 scopus 로고    scopus 로고
    • Effects of a selective inhibitor of the Abl tyrosine kinase on the growth of Bcr-Abl positive cells
    • Druker BJ, et al. (1996) Effects of a selective inhibitor of the Abl tyrosine kinase on the growth of Bcr-Abl positive cells. Nat Med 2(5-561-566
    • (1996) Nat Med , vol.2 , Issue.5 , pp. 561-566
    • Druker, B.J.1
  • 9
    • 0034665713 scopus 로고    scopus 로고
    • Structural mechanism for STI-571 inhibition of abelson tyrosine kinase
    • Schindler T, et al. (2000) Structural mechanism for STI-571 inhibition of abelson tyrosine kinase. Science 289(5486-1938-1942
    • (2000) Science , vol.289 , Issue.5486 , pp. 1938-1942
    • Schindler, T.1
  • 10
    • 3142676436 scopus 로고    scopus 로고
    • Overriding imatinib resistance with a novel ABL kinase inhibitor
    • Shah NP, et al. (2004) Overriding imatinib resistance with a novel ABL kinase inhibitor. Science 305(5682-399-401
    • (2004) Science , vol.305 , Issue.5682 , pp. 399-401
    • Shah, N.P.1
  • 11
    • 13844251975 scopus 로고    scopus 로고
    • Characterization of AMN107, a selective inhibitor of native and mutant Bcr-Abl
    • Weisberg E, et al. (2005) Characterization of AMN107, a selective inhibitor of native and mutant Bcr-Abl. Cancer Cell 7(2-129-141
    • (2005) Cancer Cell , vol.7 , Issue.2 , pp. 129-141
    • Weisberg, E.1
  • 12
    • 0035800507 scopus 로고    scopus 로고
    • Clinical resistance to STI-571 cancer therapy caused by BCR-ABL gene mutation or amplification
    • Gorre ME, et al. (2001) Clinical resistance to STI-571 cancer therapy caused by BCR-ABL gene mutation or amplification. Science 293(5531-876-880
    • (2001) Science , vol.293 , Issue.5531 , pp. 876-880
    • Gorre, M.E.1
  • 13
    • 34548825795 scopus 로고    scopus 로고
    • Bcr-Abl kinase domain mutations, drug resistance, and the road to a cure for chronic myeloid leukemia
    • O'Hare T, Eide CA, Deininger MWN (2007) Bcr-Abl kinase domain mutations, drug resistance, and the road to a cure for chronic myeloid leukemia. Blood 110(7- 2242-2249
    • (2007) Blood , vol.110 , Issue.7 , pp. 2242-2249
    • O'Hare, T.1    Eide, C.A.2    Mwn, D.3
  • 14
    • 34848911943 scopus 로고    scopus 로고
    • Sequential ABL kinase inhibitor therapy selects for compound drug-resistant BCR-ABL mutations with altered oncogenic potency
    • Shah NP, et al. (2007) Sequential ABL kinase inhibitor therapy selects for compound drug-resistant BCR-ABL mutations with altered oncogenic potency. J Clin Invest 117(9-2562-2569
    • (2007) J Clin Invest , vol.117 , Issue.9 , pp. 2562-2569
    • Shah, N.P.1
  • 15
    • 70350507997 scopus 로고    scopus 로고
    • AP24534, a pan-BCR-ABL inhibitor for chronic myeloid leukemia, potently inhibits the T315I mutant and overcomes mutation-based resistance
    • O'Hare T, et al. (2009) AP24534, a pan-BCR-ABL inhibitor for chronic myeloid leukemia, potently inhibits the T315I mutant and overcomes mutation-based resistance. Cancer Cell 16(5-401-412
    • (2009) Cancer Cell , vol.16 , Issue.5 , pp. 401-412
    • O'Hare, T.1
  • 16
    • 79953765304 scopus 로고    scopus 로고
    • Conformational control inhibition of the BCR-ABL1 tyrosine kinase, including the gatekeeper T315I mutant, by the switch-control inhibitor DCC- 2036
    • Chan WW, et al. (2011) Conformational control inhibition of the BCR-ABL1 tyrosine kinase, including the gatekeeper T315I mutant, by the switch-control inhibitor DCC- 2036. Cancer Cell 19(4-556-568
    • (2011) Cancer Cell , vol.19 , Issue.4 , pp. 556-568
    • Chan, W.W.1
  • 17
    • 79957857223 scopus 로고    scopus 로고
    • Discovery of 5-(arenethynyl) hetero-monocyclic derivatives as potent inhibitors of BCR-ABL including the T315I gatekeeper mutant
    • Thomas M, et al. (2011) Discovery of 5-(arenethynyl) hetero-monocyclic derivatives as potent inhibitors of BCR-ABL including the T315I gatekeeper mutant. Bioorg Med Chem Lett 21(12-3743-3748
    • (2011) Bioorg Med Chem Lett , vol.21 , Issue.12 , pp. 3743-3748
    • Thomas, M.1
  • 18
    • 33644889108 scopus 로고    scopus 로고
    • Allosteric inhibitors of Bcr-abl-dependent cell proliferation
    • Adrián FJ, et al. (2006) Allosteric inhibitors of Bcr-abl-dependent cell proliferation. Nat Chem Biol 2(2-95-102
    • (2006) Nat Chem Biol , vol.2 , Issue.2 , pp. 95-102
    • Adrián, F.J.1
  • 19
    • 75349104148 scopus 로고    scopus 로고
    • Inhibitors of the Abl kinase directed at either the ATP- or myristate-binding site
    • Fabbro D, et al. (2010) Inhibitors of the Abl kinase directed at either the ATP- or myristate-binding site. Biochim Biophys Acta 1804(3-454-462
    • (2010) Biochim Biophys Acta , vol.3 , pp. 454-462
    • Fabbro, D.1
  • 20
    • 75749146563 scopus 로고    scopus 로고
    • Targeting Bcr-Abl by combining allosteric with ATP-binding-site inhibitors
    • Zhang J, et al. (2010) Targeting Bcr-Abl by combining allosteric with ATP-binding-site inhibitors. Nature 463(7280-501-506
    • (2010) Nature , vol.463 , Issue.7280 , pp. 501-506
    • Zhang, J.1
  • 21
    • 77952575338 scopus 로고    scopus 로고
    • Binding or bending: Distinction of allosteric Abl kinase agonists from antagonists by an NMR-based conformational assay
    • Jahnke W, et al. (2010) Binding or bending: Distinction of allosteric Abl kinase agonists from antagonists by an NMR-based conformational assay. J Am Chem Soc 132(20-7043-7048
    • (2010) J Am Chem Soc , vol.132 , Issue.20 , pp. 7043-7048
    • Jahnke, W.1
  • 22
    • 79951816826 scopus 로고    scopus 로고
    • Discovery and characterization of a cell-permeable, small-molecule c-Abl kinase activator that binds to the myristoyl binding site
    • Yang J, et al. (2011) Discovery and characterization of a cell-permeable, small-molecule c-Abl kinase activator that binds to the myristoyl binding site. Chem Biol 18(2- 177-186
    • (2011) Chem Biol , vol.18 , Issue.2 , pp. 177-186
    • Yang, J.1
  • 23
    • 50249132542 scopus 로고    scopus 로고
    • Structural coupling of SH2-kinase domains links Fes and Abl substrate recognition and kinase activation
    • Filippakopoulos P, et al. (2008) Structural coupling of SH2-kinase domains links Fes and Abl substrate recognition and kinase activation. Cell 134(5-793-803
    • (2008) Cell , vol.134 , Issue.5 , pp. 793-803
    • Filippakopoulos, P.1
  • 24
    • 70649096122 scopus 로고    scopus 로고
    • SH2 domains: Modulators of nonreceptor tyrosine kinase activity
    • Filippakopoulos P, Müller S, Knapp S (2009) SH2 domains: Modulators of nonreceptor tyrosine kinase activity. Curr Opin Struct Biol 19(6-643-649
    • (2009) Curr Opin Struct Biol , vol.19 , Issue.6 , pp. 643-649
    • Filippakopoulos, P.1    Müller, S.2    Knapp, S.3
  • 25
    • 80054690374 scopus 로고    scopus 로고
    • Targeting the SH2-kinase interface in Bcr-Abl inhibits leukemogenesis
    • Grebien F, et al. (2011) Targeting the SH2-kinase interface in Bcr-Abl inhibits leukemogenesis. Cell 147(2-306-319
    • (2011) Cell , vol.147 , Issue.2 , pp. 306-319
    • Grebien, F.1
  • 26
    • 70349856159 scopus 로고    scopus 로고
    • From biomolecular structure to functional understanding: New NMR developments narrow the gap
    • Grzesiek S, Sass H-J (2009) From biomolecular structure to functional understanding: New NMR developments narrow the gap. Curr Opin Struct Biol 19(5-585-595
    • (2009) Curr Opin Struct Biol , vol.19 , Issue.5 , pp. 585-595
    • Grzesiek, S.1    Sass, H.-J.2
  • 27
    • 79955558165 scopus 로고    scopus 로고
    • Dynamically committed, uncommitted, and quenched states encoded in protein kinase A revealed by NMR spectroscopy
    • Masterson LR, et al. (2011) Dynamically committed, uncommitted, and quenched states encoded in protein kinase A revealed by NMR spectroscopy. Proc Natl Acad Sci USA 108(17-6969-6974
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.17 , pp. 6969-6974
    • Masterson, L.R.1
  • 28
    • 84883397614 scopus 로고    scopus 로고
    • Signaling through dynamic linkers as revealed by PKA
    • Akimoto M, et al. (2013) Signaling through dynamic linkers as revealed by PKA. Proc Natl Acad Sci USA 110(35-14231-14236
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.35 , pp. 14231-14236
    • Akimoto, M.1
  • 29
    • 32044462537 scopus 로고    scopus 로고
    • NMR characterization of kinase p38 dynamics in free and ligand-bound forms
    • Vogtherr M, et al. (2006) NMR characterization of kinase p38 dynamics in free and ligand-bound forms. Angew Chem Int Ed Engl 45(6-993-997
    • (2006) Angew Chem Int Ed Engl , vol.45 , Issue.6 , pp. 993-997
    • Vogtherr, M.1
  • 30
    • 44049100186 scopus 로고    scopus 로고
    • Dynamics in the p38alpha MAP kinase-SB203580 complex observed by liquid-state NMR spectroscopy
    • Honndorf VS, Coudevylle N, Laufer S, Becker S, Griesinger C (2008) Dynamics in the p38alpha MAP kinase-SB203580 complex observed by liquid-state NMR spectroscopy. Angew Chem Int Ed Engl 47(19-3548-3551
    • (2008) Angew Chem Int Ed Engl , vol.47 , Issue.19 , pp. 3548-3551
    • Honndorf, V.S.1    Coudevylle, N.2    Laufer, S.3    Becker, S.4    Griesinger, C.5
  • 31
    • 33749346713 scopus 로고    scopus 로고
    • A change in conformational dynamics underlies the activation of Eph receptor tyrosine kinases
    • Wiesner S, et al. (2006) A change in conformational dynamics underlies the activation of Eph receptor tyrosine kinases. EMBO J 25(19-4686-4696
    • (2006) EMBO J , vol.25 , Issue.19 , pp. 4686-4696
    • Wiesner, S.1
  • 32
    • 49649108911 scopus 로고    scopus 로고
    • Solution conformations and dynamics of ABL kinase-inhibitor complexes determined by NMR substantiate the different binding modes of imatinib/nilotinib and dasatinib
    • Vajpai N, et al. (2008) Solution conformations and dynamics of ABL kinase-inhibitor complexes determined by NMR substantiate the different binding modes of imatinib/nilotinib and dasatinib. J Biol Chem 283(26-18292-18302
    • (2008) J Biol Chem , vol.283 , Issue.26 , pp. 18292-18302
    • Vajpai, N.1
  • 33
    • 25844506708 scopus 로고    scopus 로고
    • Weak alignment NMR: A hawk-eyed view of biomolecular structure
    • Bax A, Grishaev A (2005) Weak alignment NMR: A hawk-eyed view of biomolecular structure. Curr Opin Struct Biol 15(5-563-570
    • (2005) Curr Opin Struct Biol , vol.15 , Issue.5 , pp. 563-570
    • Bax, A.1    Grishaev, A.2
  • 34
    • 0034327162 scopus 로고    scopus 로고
    • The effect of finite sampling on the determination of orientational properties: A theoretical treatment with application to interatomic vectors in proteins
    • Fushman D, Ghose R, Cowburn D (2000) The effect of finite sampling on the determination of orientational properties: A theoretical treatment with application to interatomic vectors in proteins. J Am Chem Soc 122(43-10640-10649
    • (2000) J Am Chem Soc , vol.122 , Issue.43 , pp. 10640-10649
    • Fushman, D.1    Ghose, R.2    Cowburn, D.3
  • 35
    • 0033577274 scopus 로고    scopus 로고
    • Purple membrane induced alignment of biological macromolecules in the magnetic field
    • Sass J, et al. (1999) Purple membrane induced alignment of biological macromolecules in the magnetic field. J Am Chem Soc 121(10-2047-2055
    • (1999) J Am Chem Soc , vol.121 , Issue.10 , pp. 2047-2055
    • Sass, J.1
  • 37
    • 28444453002 scopus 로고    scopus 로고
    • Refinement of multidomain protein structures by combination of solution small-angle X-ray scattering and NMR data
    • Grishaev A, Wu J, Trewhella J, Bax A (2005) Refinement of multidomain protein structures by combination of solution small-angle X-ray scattering and NMR data. J Am Chem Soc 127(47-16621-16628
    • (2005) J Am Chem Soc , vol.127 , Issue.47 , pp. 16621-16628
    • Grishaev, A.1    Wu, J.2    Trewhella, J.3    Bax, A.4
  • 38
    • 77956641793 scopus 로고    scopus 로고
    • Solution structure of the 128 kDa enzyme i dimer from Escherichia coli and its 146 kDa complex with HPr using residual dipolar couplings and small- and wide-angle X-ray scattering
    • Schwieters CD, et al. (2010) Solution structure of the 128 kDa enzyme I dimer from Escherichia coli and its 146 kDa complex with HPr using residual dipolar couplings and small- and wide-angle X-ray scattering. J Am Chem Soc 132(37-13026-13045
    • (2010) J Am Chem Soc , vol.132 , Issue.37 , pp. 13026-13045
    • Schwieters, C.D.1
  • 39
    • 0036682301 scopus 로고    scopus 로고
    • Crystal structures of the kinase domain of c-Abl in complex with the small molecule inhibitors PD173955 and imatinib (STI-571)
    • Nagar B, et al. (2002) Crystal structures of the kinase domain of c-Abl in complex with the small molecule inhibitors PD173955 and imatinib (STI-571). Cancer Res 62(15- 4236-4243
    • (2002) Cancer Res , vol.62 , Issue.15 , pp. 4236-4243
    • Nagar, B.1
  • 40
  • 41
    • 0347132269 scopus 로고    scopus 로고
    • Regulation of the c-Abl and Bcr-Abl tyrosine kinases
    • Hantschel O, Superti-Furga G (2004) Regulation of the c-Abl and Bcr-Abl tyrosine kinases. Nat Rev Mol Cell Biol 5(1-33-44
    • (2004) Nat Rev Mol Cell Biol , vol.5 , Issue.1 , pp. 33-44
    • Hantschel, O.1    Superti-Furga, G.2
  • 42
    • 0034634597 scopus 로고    scopus 로고
    • C-Abl has high intrinsic tyrosine kinase activity that is stimulated by mutation of the Src homology 3 domain and by autophosphorylation at two distinct regulatory tyrosines
    • Brasher BB, Van Etten RA (2000) c-Abl has high intrinsic tyrosine kinase activity that is stimulated by mutation of the Src homology 3 domain and by autophosphorylation at two distinct regulatory tyrosines. J Biol Chem 275(45-35631-35637
    • (2000) J Biol Chem , vol.275 , Issue.45 , pp. 35631-35637
    • Brasher, B.B.1    Van Etten, R.A.2
  • 43
    • 84874326369 scopus 로고    scopus 로고
    • Enhanced SH3/linker interaction overcomes Abl kinase activation by gatekeeper and myristic acid binding pocket mutations and increases sensitivity to small molecule inhibitors
    • Panjarian S, et al. (2013) Enhanced SH3/linker interaction overcomes Abl kinase activation by gatekeeper and myristic acid binding pocket mutations and increases sensitivity to small molecule inhibitors. J Biol Chem 288(9-6116-6129
    • (2013) J Biol Chem , vol.288 , Issue.9 , pp. 6116-6129
    • Panjarian, S.1
  • 44
    • 0027422977 scopus 로고
    • A coiled-coil oligomerization domain of Bcr is essential for the transforming function of Bcr-Abl oncoproteins
    • McWhirter JR, Galasso DL, Wang JY (1993) A coiled-coil oligomerization domain of Bcr is essential for the transforming function of Bcr-Abl oncoproteins. Mol Cell Biol 13(12-7587-7595
    • (1993) Mol Cell Biol , vol.13 , Issue.12 , pp. 7587-7595
    • McWhirter, J.R.1    Galasso, D.L.2    Wang, J.Y.3
  • 45
    • 14644425319 scopus 로고    scopus 로고
    • Mechanisms of BCR-ABL in the pathogenesis of chronic myelogenous leukaemia
    • Ren R (2005) Mechanisms of BCR-ABL in the pathogenesis of chronic myelogenous leukaemia. Nat Rev Cancer 5(3-172-183
    • (2005) Nat Rev Cancer , vol.5 , Issue.3 , pp. 172-183
    • Ren, R.1
  • 46
    • 0031882251 scopus 로고    scopus 로고
    • An intramolecular SH3-domain interaction regulates c-Abl activity
    • Barilá D, Superti-Furga G (1998) An intramolecular SH3-domain interaction regulates c-Abl activity. Nat Genet 18(3-280-282
    • (1998) Nat Genet , vol.18 , Issue.3 , pp. 280-282
    • Barilá, D.1    Superti-Furga, G.2
  • 47
    • 0037459344 scopus 로고    scopus 로고
    • Mechanisms of autoinhibition and STI-571/imatinib resistance revealed by mutagenesis of BCR-ABL
    • Azam M, Latek RR, Daley GQ (2003) Mechanisms of autoinhibition and STI-571/imatinib resistance revealed by mutagenesis of BCR-ABL. Cell 112(6-831-843
    • (2003) Cell , vol.112 , Issue.6 , pp. 831-843
    • Azam, M.1    Latek, R.R.2    Daley, G.Q.3
  • 48
    • 77956908206 scopus 로고    scopus 로고
    • BCR-ABL SH3-SH2 domain mutations in chronic myeloid leukemia patients on imatinib
    • Sherbenou DW, et al. (2010) BCR-ABL SH3-SH2 domain mutations in chronic myeloid leukemia patients on imatinib. Blood 116(17-3278-3285
    • (2010) Blood , vol.116 , Issue.17 , pp. 3278-3285
    • Sherbenou, D.W.1
  • 49
    • 0033518575 scopus 로고    scopus 로고
    • TROSY-type tripleresonance experiments for sequential NMR assignments of large proteins
    • Salzmann M, Wider G, Pervushin K, Senn H, Wuthrich K (1999) TROSY-type tripleresonance experiments for sequential NMR assignments of large proteins. J Am Chem Soc 121(4-844-848
    • (1999) J Am Chem Soc , vol.121 , Issue.4 , pp. 844-848
    • Salzmann, M.1    Wider, G.2    Pervushin, K.3    Senn, H.4    Wuthrich, K.5
  • 50
    • 69149089155 scopus 로고    scopus 로고
    • Backbone NMR resonance assignment of the Abelson kinase domain in complex with imatinib
    • Vajpai N, et al. (2008) Backbone NMR resonance assignment of the Abelson kinase domain in complex with imatinib. Biomol NMR Assign 2(1-41-42
    • (2008) Biomol NMR Assign , vol.2 , Issue.1 , pp. 41-42
    • Vajpai, N.1
  • 51
    • 0033143790 scopus 로고    scopus 로고
    • Triple resonance-based assignment for Abl SH(32) and its complex with a consolidated ligand
    • Xu R, Cahill S, Cowburn D (1999) Triple resonance-based assignment for Abl SH(32) and its complex with a consolidated ligand. J Biomol NMR 14(2-187-188
    • (1999) J Biomol NMR , vol.14 , Issue.2 , pp. 187-188
    • Xu, R.1    Cahill, S.2    Cowburn, D.3
  • 52
    • 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(23-8972-8979
    • (1989) Biochemistry , vol.28 , Issue.23 , pp. 8972-8979
    • Kay, L.E.1    Torchia, D.A.2    Bax, A.3
  • 53
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio F, et al. (1995) NMRPipe: A multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6(3-277-293
    • (1995) J Biomol NMR , vol.6 , Issue.3 , pp. 277-293
    • Delaglio, F.1
  • 54
    • 84871444338 scopus 로고    scopus 로고
    • Univ of California, San Francisco
    • Goddard T, Kneller D (2008) SPARKY 3 (Univ of California, San Francisco).
    • (2008) SPARKY 3
    • Goddard, T.1    Kneller, D.2
  • 55
    • 78149362336 scopus 로고    scopus 로고
    • Facile measurement of residual dipolar couplings in larger perdeuterated proteins
    • Fitzkee NC, Bax A (2010) Facile measurement of H-5N residual dipolar couplings in larger perdeuterated proteins. J Biomol NMR 48(2-65-70
    • (2010) J Biomol NMR , vol.48 , Issue.2 , pp. 65-70
    • Fitzkee, N.C.1    Bax, A.2
  • 56
  • 57
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun DI (1992) Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J Appl Crystallogr 25(4-495-503
    • (1992) J Appl Crystallogr , vol.25 , Issue.4 , pp. 495-503
    • Svergun, D.I.1
  • 58
    • 77953872197 scopus 로고    scopus 로고
    • Rational design of T315I BCR-Abl inhibitors for the treatment of drug-resistant chronic myelogenous leukemia (CML- BGG463
    • Manley PW, et al. (2008) Rational design of T315I BCR-Abl inhibitors for the treatment of drug-resistant chronic myelogenous leukemia (CML- BGG463. Chimia (Aarau) 62(7-8-579.
    • (2008) Chimia (Aarau , vol.62 , Issue.7-8 , pp. 579
    • Manley, P.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.