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Volumn 392, Issue 3, 2009, Pages 630-644

Structural Basis for Bivalent Smac-Mimetics Recognition in the IAP Protein Family

Author keywords

cIAP; inhibition of apoptosis; pro apoptotic drugs; Smac DIABLO; XIAP

Indexed keywords

ANTINEOPLASTIC AGENT; CASPASE 3; CASPASE 7; CASPASE 9; INHIBITOR OF APOPTOSIS PROTEIN 1; INHIBITOR OF APOPTOSIS PROTEIN 2; SECOND MITOCHONDRIAL ACTIVATOR OF CASPASE; SECOND MITOCHONDRIAL ACTIVATOR OF CASPASE ACTIVATOR; UNCLASSIFIED DRUG; X LINKED INHIBITOR OF APOPTOSIS;

EID: 69349104331     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.04.033     Document Type: Article
Times cited : (42)

References (58)
  • 1
    • 0028929328 scopus 로고
    • Mechanisms and genes of cellular suicide
    • Steller H. Mechanisms and genes of cellular suicide. Science 267 (1995) 1445-1449
    • (1995) Science , vol.267 , pp. 1445-1449
    • Steller, H.1
  • 2
    • 0028943734 scopus 로고
    • Apoptosis in the pathogenesis and treatment of disease
    • Thompson C.B. Apoptosis in the pathogenesis and treatment of disease. Science 267 (1995) 1456-1462
    • (1995) Science , vol.267 , pp. 1456-1462
    • Thompson, C.B.1
  • 3
    • 2442547741 scopus 로고    scopus 로고
    • Cell death and cancer: an introduction
    • Salvesen G.S., and Abrams J.M. Cell death and cancer: an introduction. Oncogene 23 (2004) 2774-2784
    • (2004) Oncogene , vol.23 , pp. 2774-2784
    • Salvesen, G.S.1    Abrams, J.M.2
  • 4
    • 0033082995 scopus 로고    scopus 로고
    • IAP family proteins: suppressors of apoptosis
    • Deveraux Q.L., and Reed T.C. IAP family proteins: suppressors of apoptosis. Gene Dev. 13 (1999) 239-252
    • (1999) Gene Dev. , vol.13 , pp. 239-252
    • Deveraux, Q.L.1    Reed, T.C.2
  • 5
    • 0034641932 scopus 로고    scopus 로고
    • From bench to clinic with apoptosis-based therapeutic agents
    • Nicholson D.W. From bench to clinic with apoptosis-based therapeutic agents. Nature 407 (2000) 810-816
    • (2000) Nature , vol.407 , pp. 810-816
    • Nicholson, D.W.1
  • 7
    • 0035902166 scopus 로고    scopus 로고
    • Cancer genetics
    • Ponder B.A. Cancer genetics. Nature 411 (2001) 336-341
    • (2001) Nature , vol.411 , pp. 336-341
    • Ponder, B.A.1
  • 8
    • 0346880501 scopus 로고    scopus 로고
    • The inhibitors of apoptosis: there is more to life than Bcl2
    • Liston P., Fong W.G., and Korneluk R.G. The inhibitors of apoptosis: there is more to life than Bcl2. Oncogene 22 (2003) 8568-8580
    • (2003) Oncogene , vol.22 , pp. 8568-8580
    • Liston, P.1    Fong, W.G.2    Korneluk, R.G.3
  • 11
    • 0030954209 scopus 로고    scopus 로고
    • The CARD domain: a new apoptotic signalling motif
    • Hofmann K., Bucher P., and Tschopp J. The CARD domain: a new apoptotic signalling motif. Trends Biochem. Sci. 22 (1997) 155-156
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 155-156
    • Hofmann, K.1    Bucher, P.2    Tschopp, J.3
  • 12
    • 0030447483 scopus 로고    scopus 로고
    • The tumor necrosis factor receptor 2 signal transducers TRAF2 and c-IAP1 are components of the tumor necrosis factor receptor 1 signaling complex
    • Shu H.B., Takeuchi M., and Goeddel D.V. The tumor necrosis factor receptor 2 signal transducers TRAF2 and c-IAP1 are components of the tumor necrosis factor receptor 1 signaling complex. Proc. Natl Acad. Sci. USA 93 (1996) 13973-13978
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 13973-13978
    • Shu, H.B.1    Takeuchi, M.2    Goeddel, D.V.3
  • 13
    • 0032508414 scopus 로고    scopus 로고
    • NF-kappaB antiapoptosis: induction of TRAF1 and TRAF2 and c-IAP1 and c-IAP2 to suppress caspase-8 activation
    • Wang C.Y., Mayo M.W., Korneluk R.G., Goeddel D.V., and Baldwin Jr. A.S. NF-kappaB antiapoptosis: induction of TRAF1 and TRAF2 and c-IAP1 and c-IAP2 to suppress caspase-8 activation. Science 281 (1998) 1680-1683
    • (1998) Science , vol.281 , pp. 1680-1683
    • Wang, C.Y.1    Mayo, M.W.2    Korneluk, R.G.3    Goeddel, D.V.4    Baldwin Jr., A.S.5
  • 14
    • 0029595282 scopus 로고
    • The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins
    • Rothe M., Pan M.G., Henzel W.J., Ayres T.M., and Goeddel D.V. The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins. Cell 83 (1995) 1243-1252
    • (1995) Cell , vol.83 , pp. 1243-1252
    • Rothe, M.1    Pan, M.G.2    Henzel, W.J.3    Ayres, T.M.4    Goeddel, D.V.5
  • 15
    • 33644853217 scopus 로고    scopus 로고
    • Distinct BIR domains of cIAP1 mediate binding to and ubiquitination of tumor necrosis factor receptor-associated factor 2 and second mitochondrial activator of caspases
    • Samuel T., Welsh K., Lober T., Togo S.H., Zapata J.M., and Reed J.C. Distinct BIR domains of cIAP1 mediate binding to and ubiquitination of tumor necrosis factor receptor-associated factor 2 and second mitochondrial activator of caspases. J. Biol. Chem. 281 (2006) 1080-1090
    • (2006) J. Biol. Chem. , vol.281 , pp. 1080-1090
    • Samuel, T.1    Welsh, K.2    Lober, T.3    Togo, S.H.4    Zapata, J.M.5    Reed, J.C.6
  • 16
    • 36048999753 scopus 로고    scopus 로고
    • IAP antagonists induce autoubiquitination of c-IAPs, NF-kappaB activation, and TNFalpha-dependent apoptosis
    • Varfolomeev E., Blankenship J.W., Wayson S.M., Fedorova A.V., Kayagaki N., Garg P., et al. IAP antagonists induce autoubiquitination of c-IAPs, NF-kappaB activation, and TNFalpha-dependent apoptosis. Cell 131 (2007) 669-681
    • (2007) Cell , vol.131 , pp. 669-681
    • Varfolomeev, E.1    Blankenship, J.W.2    Wayson, S.M.3    Fedorova, A.V.4    Kayagaki, N.5    Garg, P.6
  • 17
    • 17144438370 scopus 로고    scopus 로고
    • Expression and prognostic significance of IAP-family genes in human cancers and myeloid leukemias
    • Tamm I., Kornblau S.M., Segall H., Krajewski S., Welsh K., Kitada S., et al. Expression and prognostic significance of IAP-family genes in human cancers and myeloid leukemias. Clin. Cancer Res. 6 (2000) 1796-1803
    • (2000) Clin. Cancer Res. , vol.6 , pp. 1796-1803
    • Tamm, I.1    Kornblau, S.M.2    Segall, H.3    Krajewski, S.4    Welsh, K.5    Kitada, S.6
  • 21
    • 0035831022 scopus 로고    scopus 로고
    • Structural basis of caspase inhibition by XIAP: differential roles of the linker versus the BIR domain
    • Huang Y., Park Y.C., Rich R.L., Segal D., Myszka D.G., and Wu H. Structural basis of caspase inhibition by XIAP: differential roles of the linker versus the BIR domain. Cell 104 (2001) 781-790
    • (2001) Cell , vol.104 , pp. 781-790
    • Huang, Y.1    Park, Y.C.2    Rich, R.L.3    Segal, D.4    Myszka, D.G.5    Wu, H.6
  • 22
    • 0034616945 scopus 로고    scopus 로고
    • Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition
    • Du C., Fang M., Li Y., Li L., and Wang X. Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell 102 (2000) 33-42
    • (2000) Cell , vol.102 , pp. 33-42
    • Du, C.1    Fang, M.2    Li, Y.3    Li, L.4    Wang, X.5
  • 23
    • 0034616942 scopus 로고    scopus 로고
    • Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins
    • Verhagen A.M., Ekert P.G., Pakusch M., Silke J., Connolly L.M., Reid G.E., et al. Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins. Cell 102 (2000) 43-53
    • (2000) Cell , vol.102 , pp. 43-53
    • Verhagen, A.M.1    Ekert, P.G.2    Pakusch, M.3    Silke, J.4    Connolly, L.M.5    Reid, G.E.6
  • 24
    • 0034700491 scopus 로고    scopus 로고
    • Structural basis of IAP recognition by Smac/DIABLO
    • Wu G., Chai J., Suber T.L., Wu J.W., Du C., Wang X., and Shi Y. Structural basis of IAP recognition by Smac/DIABLO. Nature 408 (2000) 1008-1012
    • (2000) Nature , vol.408 , pp. 1008-1012
    • Wu, G.1    Chai, J.2    Suber, T.L.3    Wu, J.W.4    Du, C.5    Wang, X.6    Shi, Y.7
  • 25
    • 19944426570 scopus 로고    scopus 로고
    • Structure-based design of potent, conformationally constrained Smac mimetics
    • Sun H., Nikolovska-Coleska Z., Yang C.Y., Xu L., Liu M., Tomita Y., et al. Structure-based design of potent, conformationally constrained Smac mimetics. J. Am. Chem. Soc. 126 (2004) 16686-16687
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 16686-16687
    • Sun, H.1    Nikolovska-Coleska, Z.2    Yang, C.Y.3    Xu, L.4    Liu, M.5    Tomita, Y.6
  • 26
    • 33947160238 scopus 로고    scopus 로고
    • Structure-activity based study of the Smac-binding pocket within the BIR3 domain of XIAP
    • Wist A.D., Gu L., Riedl S.J., Shi Y., and McLendon G.L. Structure-activity based study of the Smac-binding pocket within the BIR3 domain of XIAP. Bioorg. Med. Chem. 15 (2007) 2935-2943
    • (2007) Bioorg. Med. Chem. , vol.15 , pp. 2935-2943
    • Wist, A.D.1    Gu, L.2    Riedl, S.J.3    Shi, Y.4    McLendon, G.L.5
  • 27
    • 4444243683 scopus 로고    scopus 로고
    • A small molecule Smac mimic potentiates TRAIL- and TNFalpha-mediated cell death
    • Li L., Thomas R.M., Suzuki H., De Brabander J.K., Wang X., and Harran P.G. A small molecule Smac mimic potentiates TRAIL- and TNFalpha-mediated cell death. Science 305 (2004) 1471-1474
    • (2004) Science , vol.305 , pp. 1471-1474
    • Li, L.1    Thomas, R.M.2    Suzuki, H.3    De Brabander, J.K.4    Wang, X.5    Harran, P.G.6
  • 28
    • 37049019494 scopus 로고    scopus 로고
    • Design, synthesis, and characterization of a potent, nonpeptide, cell-permeable, bivalent Smac mimetic that concurrently targets both the BIR2 and BIR3 domains in XIAP
    • Sun H., Nikolovska-Coleska Z., Lu J., Meagher J.L., Yang C.Y., Qiu S., et al. Design, synthesis, and characterization of a potent, nonpeptide, cell-permeable, bivalent Smac mimetic that concurrently targets both the BIR2 and BIR3 domains in XIAP. J. Am. Chem. Soc. 129 (2007) 15279-15294
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 15279-15294
    • Sun, H.1    Nikolovska-Coleska, Z.2    Lu, J.3    Meagher, J.L.4    Yang, C.Y.5    Qiu, S.6
  • 29
    • 35948994157 scopus 로고    scopus 로고
    • Autocrine TNFalpha signaling renders human cancer cells susceptible to Smac-mimetic-induced apoptosis
    • Petersen S.L., Wang L., Yalcin-Chin A., Li L., Peyton M., Minna J., et al. Autocrine TNFalpha signaling renders human cancer cells susceptible to Smac-mimetic-induced apoptosis. Cancer Cell 12 (2007) 445-456
    • (2007) Cancer Cell , vol.12 , pp. 445-456
    • Petersen, S.L.1    Wang, L.2    Yalcin-Chin, A.3    Li, L.4    Peyton, M.5    Minna, J.6
  • 31
    • 55149126196 scopus 로고    scopus 로고
    • Targeting the X-linked inhibitor of apoptosis protein through 4-substituted azabicyclo[5.3.0]alkane smac mimetics. Structure, activity, and recognition principles
    • Mastrangelo E., Cossu F., Milani M., Sorrentino G., Lecis D., Delia D., et al. Targeting the X-linked inhibitor of apoptosis protein through 4-substituted azabicyclo[5.3.0]alkane smac mimetics. Structure, activity, and recognition principles. J. Mol. Biol. 384 (2008) 673-689
    • (2008) J. Mol. Biol. , vol.384 , pp. 673-689
    • Mastrangelo, E.1    Cossu, F.2    Milani, M.3    Sorrentino, G.4    Lecis, D.5    Delia, D.6
  • 32
    • 56749160346 scopus 로고    scopus 로고
    • Structure-based design, synthesis, evaluation, and crystallographic studies of conformationally constrained Smac mimetics as inhibitors of the X-linked inhibitor of apoptosis protein (XIAP)
    • Sun H., Stuckey J.A., Nikolovska-Coleska Z., Qin D., Meagher J.L., Qiu S., et al. Structure-based design, synthesis, evaluation, and crystallographic studies of conformationally constrained Smac mimetics as inhibitors of the X-linked inhibitor of apoptosis protein (XIAP). J. Med. Chem. 51 (2008) 7169-7180
    • (2008) J. Med. Chem. , vol.51 , pp. 7169-7180
    • Sun, H.1    Stuckey, J.A.2    Nikolovska-Coleska, Z.3    Qin, D.4    Meagher, J.L.5    Qiu, S.6
  • 33
    • 51849137433 scopus 로고    scopus 로고
    • Interaction of a cyclic, bivalent smac mimetic with the x-linked inhibitor of apoptosis protein
    • Nikolovska-Coleska Z., Meagher J.L., Jiang S., Yang C.Y., Qiu S., Roller P.P., et al. Interaction of a cyclic, bivalent smac mimetic with the x-linked inhibitor of apoptosis protein. Biochemistry 47 (2008) 9811-9824
    • (2008) Biochemistry , vol.47 , pp. 9811-9824
    • Nikolovska-Coleska, Z.1    Meagher, J.L.2    Jiang, S.3    Yang, C.Y.4    Qiu, S.5    Roller, P.P.6
  • 34
    • 38349131701 scopus 로고    scopus 로고
    • Design and characterization of bivalent Smac-based peptides as antagonists of XIAP and development and validation of a fluorescence polarization assay for XIAP containing both BIR2 and BIR3 domains
    • Nikolovska-Coleska Z., Meagher J.L., Jiang S., Kawamoto S.A., Gao W., Yi H., et al. Design and characterization of bivalent Smac-based peptides as antagonists of XIAP and development and validation of a fluorescence polarization assay for XIAP containing both BIR2 and BIR3 domains. Anal. Biochem. 374 (2008) 87-98
    • (2008) Anal. Biochem. , vol.374 , pp. 87-98
    • Nikolovska-Coleska, Z.1    Meagher, J.L.2    Jiang, S.3    Kawamoto, S.A.4    Gao, W.5    Yi, H.6
  • 35
    • 7444262377 scopus 로고    scopus 로고
    • Development and optimization of a binding assay for the XIAP BIR3 domain using fluorescence polarization
    • Nikolovska-Coleska Z., Wang R., Fang X., Pan H., Tomita Y., Li P., et al. Development and optimization of a binding assay for the XIAP BIR3 domain using fluorescence polarization. Anal. Biochem. 332 (2004) 261-273
    • (2004) Anal. Biochem. , vol.332 , pp. 261-273
    • Nikolovska-Coleska, Z.1    Wang, R.2    Fang, X.3    Pan, H.4    Tomita, Y.5    Li, P.6
  • 36
    • 0003751511 scopus 로고
    • The behavior of biological macromolecules
    • Freeman, W. H. & Co, San Francisco, CA
    • Cantor, C. R. & Schimmel, P. R. (1980). The behavior of biological macromolecules. In Biophysical Chemistry, part III, pp. 850-852, Freeman, W. H. & Co, San Francisco, CA.
    • (1980) Biophysical Chemistry , Issue.PART III , pp. 850-852
    • Cantor, C.R.1    Schimmel, P.R.2
  • 38
  • 39
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • Svergun D.I. Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys. J. 76 (1999) 2879-2886
    • (1999) Biophys. J. , vol.76 , pp. 2879-2886
    • Svergun, D.I.1
  • 40
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure proteins from X-ray solution scattering
    • Svergun D.I., Petoukhov M.V., and Koch M.H. Determination of domain structure proteins from X-ray solution scattering. Biophys. J. 80 (2001) 2946-2953
    • (2001) Biophys. J. , vol.80 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.3
  • 41
    • 36148954336 scopus 로고    scopus 로고
    • IAP antagonists target cIAP1 to induce TNFalpha-dependent apoptosis
    • Vince J.E., Wong W.W., Khan N., Feltham R., Chau D., Ahmed A.U., et al. IAP antagonists target cIAP1 to induce TNFalpha-dependent apoptosis. Cell 131 (2007) 682-693
    • (2007) Cell , vol.131 , pp. 682-693
    • Vince, J.E.1    Wong, W.W.2    Khan, N.3    Feltham, R.4    Chau, D.5    Ahmed, A.U.6
  • 42
    • 58549094527 scopus 로고    scopus 로고
    • The crystal structure of the BIR3 domain from cIAP1 in complex with the N-terminal peptide of SMAC and Caspase-9
    • Kulathila R., Vash B., Sage D., Cornell-Kennon S., Wright K., Koehn J., et al. The crystal structure of the BIR3 domain from cIAP1 in complex with the N-terminal peptide of SMAC and Caspase-9. Acta Cryst. D 65 (2009) 58-66
    • (2009) Acta Cryst. D , vol.65 , pp. 58-66
    • Kulathila, R.1    Vash, B.2    Sage, D.3    Cornell-Kennon, S.4    Wright, K.5    Koehn, J.6
  • 43
    • 43049152912 scopus 로고    scopus 로고
    • TNF-alpha induces two distinct caspase-8 activation pathways
    • Wang L., Du F., and Wang X. TNF-alpha induces two distinct caspase-8 activation pathways. Cell 133 (2008) 693-703
    • (2008) Cell , vol.133 , pp. 693-703
    • Wang, L.1    Du, F.2    Wang, X.3
  • 44
    • 0000614826 scopus 로고    scopus 로고
    • An algorithm for automatic indexing of oscillation images using Fourier analysis
    • Steller I., Bolotovsky R., and MG R. An algorithm for automatic indexing of oscillation images using Fourier analysis. J. Appl. Crystallogr. 30 (1997) 1036-1040
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1036-1040
    • Steller, I.1    Bolotovsky, R.2    MG, R.3
  • 45
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallog. D 50 (1994) 760-763
    • (1994) Acta Crystallog. D , vol.50 , pp. 760-763
  • 47
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • Winn M.D., Isupov M.N., and Murshudov G.N. Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallogr. D 57 (2001) 122-133
    • (2001) Acta Crystallogr. D , vol.57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 48
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60 (2004) 2126-2132
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 49
    • 0033776369 scopus 로고    scopus 로고
    • Modelling prior distributions of atoms for Macromolecular Refinement and Completion
    • Roversi P., Blanc E., Vonrhein C., Evans G., and Bricogne G. Modelling prior distributions of atoms for Macromolecular Refinement and Completion. Acta Crystallogr. D 56 (2000) 1313-1323
    • (2000) Acta Crystallogr. D , vol.56 , pp. 1313-1323
    • Roversi, P.1    Blanc, E.2    Vonrhein, C.3    Evans, G.4    Bricogne, G.5
  • 50
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR
    • Laskowski R.A., Rullmannn J.A., MacArthur M.W., Kaptein R., and Thornton J.M. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8 (1996) 477-486
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 51
    • 4143121255 scopus 로고    scopus 로고
    • Evaluation of fluorescence-based thermal shift assays for hit identification in drug discovery
    • Lo M.C., Aulabaugh A., Jin G., Cowling R., Bard J., Malamas M., and Ellestad G. Evaluation of fluorescence-based thermal shift assays for hit identification in drug discovery. Anal. Biochem. 332 (2004) 153-159
    • (2004) Anal. Biochem. , vol.332 , pp. 153-159
    • Lo, M.C.1    Aulabaugh, A.2    Jin, G.3    Cowling, R.4    Bard, J.5    Malamas, M.6    Ellestad, G.7
  • 53
    • 0001498978 scopus 로고
    • Diffraction of X-rays of very small angles - application to the study of ultramicroscopic phenomenon
    • Guinier A. Diffraction of X-rays of very small angles - application to the study of ultramicroscopic phenomenon. Ann. Phys. 12 (1939) 161-237
    • (1939) Ann. Phys. , vol.12 , pp. 161-237
    • Guinier, A.1
  • 54
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun D.I. Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J. Appl. Crystallogr. 25 (1992) 495-503
    • (1992) J. Appl. Crystallogr. , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 55
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • Volkov V.V., and Svergun D.I. Uniqueness of ab initio shape determination in small-angle scattering. J. Appl. Crystallogr. 36 (2003) 860-864
    • (2003) J. Appl. Crystallogr. , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 56
    • 0035124442 scopus 로고    scopus 로고
    • Automated matching of high- and low- resolution structural models
    • Kozin M.B., and Svergun D.I. Automated matching of high- and low- resolution structural models. J. Appl. Crystallogr. 34 (2001) 33-41
    • (2001) J. Appl. Crystallogr. , vol.34 , pp. 33-41
    • Kozin, M.B.1    Svergun, D.I.2


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