메뉴 건너뛰기




Volumn 6, Issue , 2015, Pages

Crystal structure of a mirror-image L-RNA aptamer (Spiegelmer) in complex with the natural L-protein target CCL2

Author keywords

[No Author keywords available]

Indexed keywords

APTAMER; DIHYDROLIPOAMIDE DEHYDROGENASE; EMAPTICAP PEGOL; EOTAXIN; MONOCYTE CHEMOTACTIC PROTEIN 1; MONOCYTE CHEMOTACTIC PROTEIN 4; RNA; SELENIUM; NOX-E36 APTAMER; RECOMBINANT PROTEIN;

EID: 84928789604     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms7923     Document Type: Article
Times cited : (80)

References (60)
  • 2
    • 34247855761 scopus 로고    scopus 로고
    • Chemokine: Receptor structure, interactions, and antagonism
    • Allen, S. J., Crown, S. E. & Handel, T. M. Chemokine: receptor structure, interactions, and antagonism. Annu. Rev. Immunol. 25, 787-820 (2007).
    • (2007) Annu. Rev. Immunol. , vol.25 , pp. 787-820
    • Allen, S.J.1    Crown, S.E.2    Handel, T.M.3
  • 4
    • 0037452728 scopus 로고    scopus 로고
    • Glycosaminoglycan binding and oligomerization are essential for the in vivo activity of certain chemokines
    • Proudfoot, A. E. et al. Glycosaminoglycan binding and oligomerization are essential for the in vivo activity of certain chemokines. Proc. Natl Acad. Sci. USA 100, 1885-1890 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 1885-1890
    • Proudfoot, A.E.1
  • 5
    • 0037317834 scopus 로고    scopus 로고
    • Targeting monocyte chemoattractant protein-1 signalling in disease
    • Dawson, J., Miltz, W., Mir, A. K. & Wiessner, C. Targeting monocyte chemoattractant protein-1 signalling in disease. Expert. Opin. Ther. Targets 7, 35-48 (2003).
    • (2003) Expert. Opin. Ther. Targets , vol.7 , pp. 35-48
    • Dawson, J.1    Miltz, W.2    Mir, A.K.3    Wiessner, C.4
  • 6
    • 0035260881 scopus 로고    scopus 로고
    • Chemokines and disease
    • Gerard, C. & Rollins, B. J. Chemokines and disease. Nat. Immunol. 2, 108-115 (2001).
    • (2001) Nat. Immunol. , vol.2 , pp. 108-115
    • Gerard, C.1    Rollins, B.J.2
  • 7
    • 79955784400 scopus 로고    scopus 로고
    • MCP-1: Chemoattractant with a role beyond immunity: A review
    • Yadav, A., Saini, V. & Arora, S. MCP-1: chemoattractant with a role beyond immunity: a review. Clin. Chim. Acta 411, 1570-1579 (2010).
    • (2010) Clin. Chim. Acta , vol.411 , pp. 1570-1579
    • Yadav, A.1    Saini, V.2    Arora, S.3
  • 9
    • 84889300061 scopus 로고    scopus 로고
    • Spiegelmers for therapeutic applications - Use of chiral principles in evolutionary selection techniques
    • ed. Klussmann, S.) (Wiley-VCH, Weinheim,).
    • Eulberg, D., Jarosch, F., Vonhoff, S. & Klussmann, S. Spiegelmers for therapeutic applications - use of chiral principles in evolutionary selection techniques. in The Aptamer Handbook (ed. Klussmann, S.) 417-442 (Wiley-VCH, Weinheim, 2006).
    • (2006) The Aptamer Handbook , pp. 417-442
    • Eulberg, D.1    Jarosch, F.2    Vonhoff, S.3    Klussmann, S.4
  • 10
    • 0025194307 scopus 로고
    • Systematic evolution of ligands by exponential enrichment: RNA ligands to bacteriophage T4 DNA polymerase
    • Tuerk, C. & Gold, L. Systematic evolution of ligands by exponential enrichment: RNA ligands to bacteriophage T4 DNA polymerase. Science 249, 505-510 (1990).
    • (1990) Science , vol.249 , pp. 505-510
    • Tuerk, C.1    Gold, L.2
  • 11
    • 84857055199 scopus 로고    scopus 로고
    • Pharmacological inhibition of the chemokine CCL2 (MCP-1) diminishes liver macrophage infiltration and steatohepatitis in chronic hepatic injury
    • Baeck, C. et al. Pharmacological inhibition of the chemokine CCL2 (MCP-1) diminishes liver macrophage infiltration and steatohepatitis in chronic hepatic injury. Gut 61, 416-426 (2012).
    • (2012) Gut , vol.61 , pp. 416-426
    • Baeck, C.1
  • 12
    • 34547645572 scopus 로고    scopus 로고
    • Spiegelmer inhibition of CCL2/MCP-1 ameliorates lupus nephritis in MRL-(Fas)lpr mice
    • Kulkarni, O. et al. Spiegelmer inhibition of CCL2/MCP-1 ameliorates lupus nephritis in MRL-(Fas)lpr mice. J. Am. Soc. Nephrol. 18, 2350-2358 (2007).
    • (2007) J. Am. Soc. Nephrol. , vol.18 , pp. 2350-2358
    • Kulkarni, O.1
  • 13
    • 40449140901 scopus 로고    scopus 로고
    • Late onset of Ccl2 blockade with the Spiegelmer mNOX-E36-3'PEG prevents glomerulosclerosis and improves glomerular filtration rate in db/db mice
    • Ninichuk, V. et al. Late onset of Ccl2 blockade with the Spiegelmer mNOX-E36-3'PEG prevents glomerulosclerosis and improves glomerular filtration rate in db/db mice. Am. J. Pathol. 172, 628-637 (2008).
    • (2008) Am. J. Pathol. , vol.172 , pp. 628-637
    • Ninichuk, V.1
  • 14
    • 84922453363 scopus 로고    scopus 로고
    • CCL2 inhibition with emapticap pegol (NOX-E36) in type 2 diabetic patients with albuminuria
    • Amsterdam
    • Haller, H. G., Baumann, M. & Eulberg, D. CCL2 Inhibition with Emapticap Pegol (NOX-E36) in Type 2 Diabetic Patients with Albuminuria. in 51st ERA-EDTA Congress (Amsterdam, 2014).
    • (2014) 51st ERA-EDTA Congress
    • Haller, H.G.1    Baumann, M.2    Eulberg, D.3
  • 15
    • 84928780593 scopus 로고    scopus 로고
    • Structural basis for the targeting of complement anaphylatoxin C5a using a mixed L-RNA/L-DNA aptamer
    • Yatime, L. et al. Structural basis for the targeting of complement anaphylatoxin C5a using a mixed L-RNA/L-DNA aptamer. Nat. Commun. 6, 6481 (2015).
    • (2015) Nat. Commun. , vol.6 , pp. 6481
    • Yatime, L.1
  • 16
    • 41649093743 scopus 로고    scopus 로고
    • Selenium derivatization of nucleic acids for phase and structure determination in nucleic acid X-ray crystallography
    • Sheng, J. & Huang, Z. Selenium derivatization of nucleic acids for phase and structure determination in nucleic acid X-ray crystallography. Int. J. Mol. Sci. 9, 258-271 (2008).
    • (2008) Int. J. Mol. Sci. , vol.9 , pp. 258-271
    • Sheng, J.1    Huang, Z.2
  • 17
    • 0019450355 scopus 로고
    • Structure of the hydrophobic protein crambin determined directly from the anomalous scattering of sulphur
    • Hendrickson, W. A. & Teeter, M. M. Structure of the hydrophobic protein crambin determined directly from the anomalous scattering of sulphur. Nature 290, 107-113 (1981).
    • (1981) Nature , vol.290 , pp. 107-113
    • Hendrickson, W.A.1    Teeter, M.M.2
  • 18
    • 0031026207 scopus 로고    scopus 로고
    • The structure of MCP-1 in two crystal forms provides a rare example of variable quaternary interactions
    • Lubkowski, J. et al. The structure of MCP-1 in two crystal forms provides a rare example of variable quaternary interactions. Nat. Struct. Biol. 4, 64-69 (1997).
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 64-69
    • Lubkowski, J.1
  • 19
    • 0029665212 scopus 로고    scopus 로고
    • Heteronuclear (1H, 13C, 15N) NMR assignments and solution structure of the monocyte chemoattractant protein-1 (MCP-1) dimer
    • Handel, T. M. & Domaille, P. J. Heteronuclear (1H, 13C, 15N) NMR assignments and solution structure of the monocyte chemoattractant protein-1 (MCP-1) dimer. Biochemistry 35, 6569-6584 (1996).
    • (1996) Biochemistry , vol.35 , pp. 6569-6584
    • Handel, T.M.1    Domaille, P.J.2
  • 20
    • 0042121256 scopus 로고    scopus 로고
    • Mfold web server for nucleic acid folding and hybridization prediction
    • Zuker, M. Mfold web server for nucleic acid folding and hybridization prediction. Nucleic Acids Res. 31, 3406-3415 (2003).
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3406-3415
    • Zuker, M.1
  • 21
    • 35648969956 scopus 로고    scopus 로고
    • Hydrogen bonds in the crystal structure of strontium hydroxide octahydrate Sr(OH)2 8H2O
    • Reuter, H., Kamaha, S. & Zerzouf, O. Hydrogen bonds in the crystal structure of strontium hydroxide octahydrate Sr(OH)2 8H2O. Z. Naturforsch. 62b, 215-219 (2007).
    • (2007) Z. Naturforsch. , vol.62 B , pp. 215-219
    • Reuter, H.1    Kamaha, S.2    Zerzouf, O.3
  • 22
    • 2442681690 scopus 로고    scopus 로고
    • Structure of the hydrated and dimethyl sulfoxide solvated rubidium ions in solution
    • D'Angelo, P. & Persson, I. Structure of the hydrated and dimethyl sulfoxide solvated rubidium ions in solution. Inorg. Chem. 43, 3543-3549 (2004).
    • (2004) Inorg. Chem. , vol.43 , pp. 3543-3549
    • D'angelo, P.1    Persson, I.2
  • 24
    • 84891668860 scopus 로고    scopus 로고
    • Validation of metal-binding sites in macromolecular structures with the CheckMyMetal web server
    • Zheng, H. et al. Validation of metal-binding sites in macromolecular structures with the CheckMyMetal web server. Nat. Protoc. 9, 156-170 (2014).
    • (2014) Nat. Protoc. , vol.9 , pp. 156-170
    • Zheng, H.1
  • 25
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel, E. & Henrick, K. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372, 774-797 (2007).
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 26
    • 0032833999 scopus 로고    scopus 로고
    • Identification of residues in the monocyte chemotactic protein-1 that contact the MCP-1 receptor, CCR2
    • Hemmerich, S. et al. Identification of residues in the monocyte chemotactic protein-1 that contact the MCP-1 receptor, CCR2. Biochemistry 38, 13013-13025 (1999).
    • (1999) Biochemistry , vol.38 , pp. 13013-13025
    • Hemmerich, S.1
  • 27
    • 0033534151 scopus 로고    scopus 로고
    • Identification of surface residues of the monocyte chemotactic protein 1 that affect signaling through the receptor CCR2
    • Jarnagin, K. et al. Identification of surface residues of the monocyte chemotactic protein 1 that affect signaling through the receptor CCR2. Biochemistry 38, 16167-16177 (1999).
    • (1999) Biochemistry , vol.38 , pp. 16167-16177
    • Jarnagin, K.1
  • 28
    • 0032491615 scopus 로고    scopus 로고
    • Lysine 58 and histidine 66 at the C-terminal a-helix of monocyte chemoattractant protein-1 are essential for glycosaminoglycan binding
    • Chakravarty, L., Rogers, L., Quach, T., Breckenridge, S. & Kolattukudy, P. E. Lysine 58 and histidine 66 at the C-terminal a-helix of monocyte chemoattractant protein-1 are essential for glycosaminoglycan binding. J. Biol. Chem. 273, 29641-29647 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 29641-29647
    • Chakravarty, L.1    Rogers, L.2    Quach, T.3    Breckenridge, S.4    Kolattukudy, P.E.5
  • 29
    • 2542498611 scopus 로고    scopus 로고
    • Identification of the glycosaminoglycan binding site of the CC chemokine, MCP-1: Implications for structure and function in vivo
    • Lau, E. K. et al. Identification of the glycosaminoglycan binding site of the CC chemokine, MCP-1: implications for structure and function in vivo. J. Biol. Chem. 279, 22294-22305 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 22294-22305
    • Lau, E.K.1
  • 30
    • 0034700312 scopus 로고    scopus 로고
    • Complete crystal structure of monocyte chemotactic protein-2, a CC chemokine that interacts with multiple receptors
    • Blaszczyk, J. et al. Complete crystal structure of monocyte chemotactic protein-2, a CC chemokine that interacts with multiple receptors. Biochemistry 39, 14075-14081 (2000).
    • (2000) Biochemistry , vol.39 , pp. 14075-14081
    • Blaszczyk, J.1
  • 31
    • 0032575660 scopus 로고    scopus 로고
    • Solution structure of eotaxin, a chemokine that selectively recruits eosinophils in allergic inflammation
    • Crump, M. P., Rajarathnam, K., Kim, K. S., Clark-Lewis, I. & Sykes, B. D. Solution structure of eotaxin, a chemokine that selectively recruits eosinophils in allergic inflammation. J. Biol. Chem. 273, 22471-22479 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 22471-22479
    • Crump, M.P.1    Rajarathnam, K.2    Kim, K.S.3    Clark-Lewis, I.4    Sykes, B.D.5
  • 33
    • 0030597050 scopus 로고    scopus 로고
    • Structural characterization of a monomeric chemokine: Monocyte chemoattractant protein-3
    • Kim, K. S., Rajarathnam, K., Clark-Lewis, I. & Sykes, B. D. Structural characterization of a monomeric chemokine: monocyte chemoattractant protein-3. FEBS Lett. 395, 277-282 (1996).
    • (1996) FEBS Lett. , vol.395 , pp. 277-282
    • Kim, K.S.1    Rajarathnam, K.2    Clark-Lewis, I.3    Sykes, B.D.4
  • 34
    • 84922437365 scopus 로고    scopus 로고
    • Pharmacokinetics, pharmacodynamics, safety and tolerability of the CCL2 antagonist NOX-E36, a novel agent being investigated for treatment of diabetic nephropathy [Abstract]
    • Landgraf, G. et al. Pharmacokinetics, pharmacodynamics, safety and tolerability of the CCL2 antagonist NOX-E36, a novel agent being investigated for treatment of diabetic nephropathy [Abstract]. J. Am. Soc. Nephrol. 23, 960A (2012).
    • (2012) J. Am. Soc. Nephrol. , vol.23 , pp. 960A
    • Landgraf, G.1
  • 35
    • 84896528539 scopus 로고    scopus 로고
    • An RNA aptamer possessing a novel monovalent cationmediated fold inhibits lysozyme catalysis by inhibiting the binding of long natural substrates
    • Padlan, C. S. et al. An RNA aptamer possessing a novel monovalent cationmediated fold inhibits lysozyme catalysis by inhibiting the binding of long natural substrates. RNA 20, 447-461 (2014).
    • (2014) RNA , vol.20 , pp. 447-461
    • Padlan, C.S.1
  • 36
    • 33750997616 scopus 로고    scopus 로고
    • Protein-RNA interactions: Exploring binding patterns with a three-dimensional superposition analysis of high resolution structures
    • Morozova, N., Allers, J., Myers, J. & Shamoo, Y. Protein-RNA interactions: exploring binding patterns with a three-dimensional superposition analysis of high resolution structures. Bioinformatics 22, 2746-2752 (2006).
    • (2006) Bioinformatics , vol.22 , pp. 2746-2752
    • Morozova, N.1    Allers, J.2    Myers, J.3    Shamoo, Y.4
  • 37
    • 0036308878 scopus 로고    scopus 로고
    • Cation-pi/H-bond stair motifs at protein-DNA interfaces
    • Rooman, M., Lievin, J., Buisine, E. & Wintjens, R. Cation-pi/H-bond stair motifs at protein-DNA interfaces. J. Mol. Biol. 319, 67-76 (2002).
    • (2002) J. Mol. Biol. , vol.319 , pp. 67-76
    • Rooman, M.1    Lievin, J.2    Buisine, E.3    Wintjens, R.4
  • 38
    • 0034665865 scopus 로고    scopus 로고
    • Contribution of cation-pi interactions to the stability of protein-DNA complexes
    • Wintjens, R., Lievin, J., Rooman, M. & Buisine, E. Contribution of cation-pi interactions to the stability of protein-DNA complexes. J. Mol. Biol. 302, 395-410 (2000).
    • (2000) J. Mol. Biol. , vol.302 , pp. 395-410
    • Wintjens, R.1    Lievin, J.2    Rooman, M.3    Buisine, E.4
  • 40
    • 84860378596 scopus 로고    scopus 로고
    • Structural basis for high selectivity of anti-CCL2 neutralizing antibody CNTO 888
    • Obmolova, G. et al. Structural basis for high selectivity of anti-CCL2 neutralizing antibody CNTO 888. Mol. Immunol. 51, 227-233 (2012).
    • (2012) Mol. Immunol. , vol.51 , pp. 227-233
    • Obmolova, G.1
  • 41
    • 33745712854 scopus 로고    scopus 로고
    • Structure activity relationships of monocyte chemoattractant proteins in complex with a blocking antibody
    • Reid, C. et al. Structure activity relationships of monocyte chemoattractant proteins in complex with a blocking antibody. Protein Eng. Des. Sel. 19, 317-324 (2006).
    • (2006) Protein Eng. Des. Sel. , vol.19 , pp. 317-324
    • Reid, C.1
  • 42
    • 84879085632 scopus 로고    scopus 로고
    • Phase 2 study of carlumab (CNTO 888), a human monoclonal antibody against CC-chemokine ligand 2 (CCL2), in metastatic castrationresistant prostate cancer
    • Pienta, K. J. et al. Phase 2 study of carlumab (CNTO 888), a human monoclonal antibody against CC-chemokine ligand 2 (CCL2), in metastatic castrationresistant prostate cancer. Invest. New Drugs 31, 760-768 (2013).
    • (2013) Invest. New Drugs , vol.31 , pp. 760-768
    • Pienta, K.J.1
  • 43
    • 84878849941 scopus 로고    scopus 로고
    • A first-in-human, first-in-class, phase i study of carlumab (CNTO 888), a human monoclonal antibody against CC-chemokine ligand 2 in patients with solid tumors
    • Sandhu, S. K. et al. A first-in-human, first-in-class, phase I study of carlumab (CNTO 888), a human monoclonal antibody against CC-chemokine ligand 2 in patients with solid tumors. Cancer Chemother. Pharmacol. 71, 1041-1050 (2013).
    • (2013) Cancer Chemother. Pharmacol. , vol.71 , pp. 1041-1050
    • Sandhu, S.K.1
  • 44
    • 84857576006 scopus 로고    scopus 로고
    • RNA aptamers and spiegelmers: Synthesis, purification, and post-synthetic PEG conjugation
    • Unit 4.46
    • Hoffmann, S., Hoos, J., Klussmann, S. & Vonhoff, S. RNA aptamers and spiegelmers: synthesis, purification, and post-synthetic PEG conjugation. Curr. Protoc. Nucleic Acid Chem. Chapter 4, Unit 4.46.1-30 (2011).
    • (2011) Curr. Protoc. Nucleic Acid Chem. Chapter , vol.4 , pp. 1-30
    • Hoffmann, S.1    Hoos, J.2    Klussmann, S.3    Vonhoff, S.4
  • 45
    • 76449106188 scopus 로고    scopus 로고
    • Integration, scaling, space-group assignment and post-refinement
    • Kabsch, W. Integration, scaling, space-group assignment and post-refinement. Acta Crystallogr. D 66, 133-144 (2010).
    • (2010) Acta Crystallogr. D , vol.66 , pp. 133-144
    • Kabsch, W.1
  • 47
    • 79953737180 scopus 로고    scopus 로고
    • Overview of the CCP4 suite and current developments
    • Winn, M. D. et al. Overview of the CCP4 suite and current developments. Acta Crystallogr. D 67, 235-242 (2011).
    • (2011) Acta Crystallogr. D , vol.67 , pp. 235-242
    • Winn, M.D.1
  • 49
    • 66249112826 scopus 로고    scopus 로고
    • Decision-making in structure solution using Bayesian estimates of map quality: The PHENIX AutoSol wizard
    • Terwilliger, T. C. et al. Decision-making in structure solution using Bayesian estimates of map quality: the PHENIX AutoSol wizard. Acta Crystallogr. D Biol. Crystallogr. 65, 582-601 (2009).
    • (2009) Acta Crystallogr. D Biol. Crystallogr. , vol.65 , pp. 582-601
    • Terwilliger, T.C.1
  • 50
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of Macromolecular Structures by the Maximum-Likelihood method
    • Murshudov, G. N., Vagin, A. A. & Dodson., E. J. Refinement of Macromolecular Structures by the Maximum-Likelihood method. Acta Cryst. D 53, 1285-1294 (1997).
    • (1997) Acta Cryst. D , vol.53 , pp. 1285-1294
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 51
    • 79953763877 scopus 로고    scopus 로고
    • REFMAC5 for the refinement of macromolecular crystal structures
    • Murshudov, G. N. et al. REFMAC5 for the refinement of macromolecular crystal structures. Acta Crystallogr. D Biol. Crystallogr. 67, 355-367 (2011).
    • (2011) Acta Crystallogr. D Biol. Crystallogr. , vol.67 , pp. 355-367
    • Murshudov, G.N.1
  • 52
    • 0035094475 scopus 로고    scopus 로고
    • Geometry of metal-ligand interactions in proteins
    • Harding, M. M. Geometry of metal-ligand interactions in proteins. Acta Crystallogr. D Biol. Crystallogr. 57, 401-411 (2001).
    • (2001) Acta Crystallogr. D Biol. Crystallogr. , vol.57 , pp. 401-411
    • Harding, M.M.1
  • 53
    • 84860273177 scopus 로고    scopus 로고
    • Towards automated crystallographic structure refinement with phenix.refine
    • Afonine, P. V. et al. Towards automated crystallographic structure refinement with phenix.refine. Acta Crystallogr. D Biol. Crystallogr. 68, 352-367 (2012).
    • (2012) Acta Crystallogr. D Biol. Crystallogr. , vol.68 , pp. 352-367
    • Afonine, P.V.1
  • 54
    • 48849104435 scopus 로고    scopus 로고
    • Data mining of metal ion environments present in protein structures
    • Zheng, H., Chruszcz, M., Lasota, P., Lebioda, L. & Minor, W. Data mining of metal ion environments present in protein structures. J. Inorg. Biochem. 102, 1765-1776 (2008).
    • (2008) J. Inorg. Biochem. , vol.102 , pp. 1765-1776
    • Zheng, H.1    Chruszcz, M.2    Lasota, P.3    Lebioda, L.4    Minor, W.5
  • 55
    • 0001752768 scopus 로고    scopus 로고
    • The Cambridge Structural Database: A quarter of a million crystal structures and rising
    • Allen, F. H. The Cambridge Structural Database: a quarter of a million crystal structures and rising. Acta Crystallogr.B Struct. Sci. 58, 380-388 (2002).
    • (2002) Acta Crystallogr.B Struct. Sci. , vol.58 , pp. 380-388
    • Allen, F.H.1
  • 58
    • 4444221565 scopus 로고    scopus 로고
    • Chimera - A visualization system for exploratory research and analysis
    • Pettersen, E. F. et al. Chimera - A visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605-1612 (2004).
    • (2004) J. Comput. Chem. , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1
  • 59
    • 80054911951 scopus 로고    scopus 로고
    • LigPlot+: Multiple ligand-protein interaction diagrams for drug discovery
    • Laskowski, R. A. & Swindells, M. B. LigPlot+: multiple ligand-protein interaction diagrams for drug discovery. J. Chem. Inf. Model 51, 2778-2786 (2011).
    • (2011) J. Chem. Inf. Model , vol.51 , pp. 2778-2786
    • Laskowski, R.A.1    Swindells, M.B.2
  • 60
    • 50349085962 scopus 로고    scopus 로고
    • 3DNA: A versatile, integrated software system for the analysis, rebuilding and visualization of three-dimensional nucleic-acid structures
    • Lu, X. J. & Olson, W. K. 3DNA: a versatile, integrated software system for the analysis, rebuilding and visualization of three-dimensional nucleic-acid structures. Nat. Protoc. 3, 1213-1227 (2008).
    • (2008) Nat. Protoc. , vol.3 , pp. 1213-1227
    • Lu, X.J.1    Olson, W.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.