메뉴 건너뛰기




Volumn 54, Issue 12, 2011, Pages 3989-4005

How well can fragments explore accessed chemical space? A case study from heat shock protein 90

Author keywords

[No Author keywords available]

Indexed keywords

5 (2,4 DIHYDROXY 5 ISOPROPYLPHENYL) 4 (4 MORPHOLINOMETHYLPHENYL) 3 ISOXAZOLECARBOXYLIC ACID ETHYLAMIDE; ALVESPIMYCIN; AT 13387; BENZAMIDE DERIVATIVE; CNF 1010; CUDC 305; GELDANAMYCIN; HEAT SHOCK PROTEIN 90; HEAT SHOCK PROTEIN 90 INHIBITOR; IPI 493; NVP BEP 800; RESORCINOL; RETASPIMYCIN; SNX 2112; SNX 5422; TANESPIMYCIN; UNCLASSIFIED DRUG;

EID: 79959407930     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm200350g     Document Type: Review
Times cited : (69)

References (83)
  • 1
    • 1942453243 scopus 로고    scopus 로고
    • Ligand efficiency: A useful metric for lead selection
    • DOI 10.1016/S1359-6446(04)03069-7, PII S1359644604030697
    • Hopkins, A. L.; Groom, C. R.; Alex, A. Ligand efficiency: a useful metric for lead selection Drug Discovery Today 2004, 9, 430-431 (Pubitemid 38510559)
    • (2004) Drug Discovery Today , vol.9 , Issue.10 , pp. 430-431
    • Hopkins, A.L.1    Groom, C.R.2    Alex, A.3
  • 2
    • 33845364148 scopus 로고    scopus 로고
    • Fragment-based drug design: How big is too big?
    • DOI 10.1021/jm060511h
    • Hajduk, P. J. Fragment-based drug design: how big is too big? J. Med. Chem. 2006, 49, 6972-6976 (Pubitemid 44885985)
    • (2006) Journal of Medicinal Chemistry , vol.49 , Issue.24 , pp. 6972-6976
    • Hajduk, P.J.1
  • 4
    • 67649341990 scopus 로고    scopus 로고
    • From fragment to clinical candidate - A historical perspective
    • Chessari, G.; Woodhead, A. J. From fragment to clinical candidate - a historical perspective Drug Discovery Today 2009, 14, 668-675
    • (2009) Drug Discovery Today , vol.14 , pp. 668-675
    • Chessari, G.1    Woodhead, A.J.2
  • 5
    • 70349425790 scopus 로고    scopus 로고
    • Recent progress in fragment-based lead discovery
    • Schulz, M. N.; Hubbard, R. E. Recent progress in fragment-based lead discovery Curr. Opin. Pharmacol. 2009, 9, 615-621
    • (2009) Curr. Opin. Pharmacol. , vol.9 , pp. 615-621
    • Schulz, M.N.1    Hubbard, R.E.2
  • 7
    • 67650999672 scopus 로고    scopus 로고
    • Lessons for fragment library design: Analysis of output from multiple screening campaigns
    • Chen, I. J.; Hubbard, R. E. Lessons for fragment library design: analysis of output from multiple screening campaigns J. Comput.-Aided Mol. Des. 2009, 23, 603-620
    • (2009) J. Comput.-Aided Mol. Des. , vol.23 , pp. 603-620
    • Chen, I.J.1    Hubbard, R.E.2
  • 10
    • 77955982439 scopus 로고    scopus 로고
    • Structural biology in fragment-based drug design
    • Murray, C. W.; Blundell, T. L. Structural biology in fragment-based drug design Curr. Opin. Struct. Biol. 2010, 20, 497-507
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 497-507
    • Murray, C.W.1    Blundell, T.L.2
  • 11
    • 79952429629 scopus 로고    scopus 로고
    • Experiences in fragment-based lead discovery
    • Hubbard, R.; Murray, J. B. Experiences in fragment-based lead discovery Methods Enzymol. 2011, 493, 509-531
    • (2011) Methods Enzymol. , vol.493 , pp. 509-531
    • Hubbard, R.1    Murray, J.B.2
  • 12
    • 33751204422 scopus 로고    scopus 로고
    • Fragment-based lead discovery: A chemical update
    • DOI 10.1016/j.copbio.2006.10.007, PII S0958166906001510
    • Erlanson, D. A. Fragment-based lead discovery: a chemical update Curr. Opin. Biotechnol. 2006, 17, 643-652 (Pubitemid 44791912)
    • (2006) Current Opinion in Biotechnology , vol.17 , Issue.6 , pp. 643-652
    • Erlanson, D.A.1
  • 13
    • 0029836953 scopus 로고    scopus 로고
    • Discovering high-affinity ligands for proteins: SAR by NMR
    • DOI 10.1126/science.274.5292.1531
    • Shuker, S. B.; Hajduk, P. J.; Meadows, R. P.; Fesik, S. W. Discovering high-affinity ligands for proteins: SAR by NMR Science 1996, 274, 1531-1534 (Pubitemid 26403929)
    • (1996) Science , vol.274 , Issue.5292 , pp. 1531-1534
    • Shuker, S.B.1    Hajduk, P.J.2    Meadows, R.P.3    Fesik, S.W.4
  • 14
    • 33749659675 scopus 로고    scopus 로고
    • SAR by NMA: Putting the pieces together
    • DOI 10.1124/mi.6.5.8
    • Hajduk, P. J. SAR by NMR: putting the pieces together Mol. Interventions 2006, 6, 266-272 (Pubitemid 44556047)
    • (2006) Molecular Interventions , vol.6 , Issue.5 , pp. 266-272
    • Hajduk, P.J.1
  • 20
    • 42449142359 scopus 로고    scopus 로고
    • Fragment approaches in structure-based drug discovery
    • DOI 10.1107/S090904950705666X, PII S090904950705666X
    • Hubbard, R. E. Fragment approaches in structure-based drug discovery J. Synchrotron Radiat. 2008, 15, 227-230 (Pubitemid 351571008)
    • (2008) Journal of Synchrotron Radiation , vol.15 , Issue.3 , pp. 227-230
    • Hubbard, R.E.1
  • 22
    • 34247194965 scopus 로고    scopus 로고
    • Virtual exploration of the chemical universe up to 11 atoms of C, N, O, F: Assembly of 26.4 million structures (110.9 million stereoisomers) and analysis for new ring systems, stereochemistry, physicochemical properties, compound classes, and drug discovery
    • DOI 10.1021/ci600423u
    • Fink, T.; Reymond, J. L. Virtual exploration of the chemical universe up to 11 atoms of C, N, O, F: assembly of 26.4 million structures (110.9 million stereoisomers) and analysis for new ring systems, stereochemistry, physicochemical properties, compound classes, and drug discovery J. Chem. Inf. Model. 2007, 47, 342-353 (Pubitemid 46615939)
    • (2007) Journal of Chemical Information and Modeling , vol.47 , Issue.2 , pp. 342-353
    • Fink, T.1    Raymond, J.-L.2
  • 24
    • 77952544010 scopus 로고    scopus 로고
    • ATPase inhibitors of heat-shock protein 90, second season
    • Janin, Y. L. ATPase inhibitors of heat-shock protein 90, second season Drug Discovery Today 2010, 15, 342-353
    • (2010) Drug Discovery Today , vol.15 , pp. 342-353
    • Janin, Y.L.1
  • 25
    • 33746364784 scopus 로고    scopus 로고
    • Structure and mechanism of the Hsp90 molecular chaperone machinery
    • DOI 10.1146/annurev.biochem.75.103004.142738
    • Pearl, L. H.; Prodromou, C. Structure and mechanism of the Hsp90 molecular chaperone machinery Annu. Rev. Biochem. 2006, 75, 271-294 (Pubitemid 44118034)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 271-294
    • Pearl, L.H.1    Prodromou, C.2
  • 26
    • 0033985080 scopus 로고    scopus 로고
    • GHKL, an emergent ATPase/kinase superfamily
    • DOI 10.1016/S0968-0004(99)01503-0, PII S0968000499015030
    • Dutta, R.; Inouye, M. GHKL, an emergent ATPase/kinase superfamily Trends Biochem. Sci. 2000, 25, 24-28 (Pubitemid 30060426)
    • (2000) Trends in Biochemical Sciences , vol.25 , Issue.1 , pp. 24-28
    • Dutta, R.1    Inouye, M.2
  • 27
    • 0035071607 scopus 로고    scopus 로고
    • A small molecule designed to bind to the adenine nucleotide pocket of Hsp90 causes Her2 degradation and the growth arrest and differentiation of breast cancer cells
    • DOI 10.1016/S1074-5521(01)00015-1, PII S1074552101000151
    • Chiosis, G.; Timaul, M. N.; Lucas, B.; Munster, P. N.; Zheng, F. F.; Sepp-Lorenzino, L.; Rosen, N. A small molecule designed to bind to the adenine nucleotide pocket of Hsp90 causes Her2 degradation and the growth arrest and differentiation of breast cancer cells Chem. Biol. 2001, 8, 289-299 (Pubitemid 32296118)
    • (2001) Chemistry and Biology , vol.8 , Issue.3 , pp. 289-299
    • Chiosis, G.1    Timaul, M.N.2    Lucas, B.3    Munster, P.N.4    Zheng, F.F.5    Sepp-Lorenzino, L.6    Rosen, N.7
  • 28
    • 77749270556 scopus 로고    scopus 로고
    • Hsp90 inhibitors: Clinical development and future opportunities in oncology therapy
    • Gao, Z.; Garcia-Echeverria, C.; Jensen, M. R. Hsp90 inhibitors: clinical development and future opportunities in oncology therapy Curr. Opin. Drug Discovery Dev. 2010, 13, 193-202
    • (2010) Curr. Opin. Drug Discovery Dev. , vol.13 , pp. 193-202
    • Gao, Z.1    Garcia-Echeverria, C.2    Jensen, M.R.3
  • 29
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan, D.; Weinberg, R. A. The hallmarks of cancer Cell 2000, 100, 57-70 (Pubitemid 30046295)
    • (2000) Cell , vol.100 , Issue.1 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 30
    • 0031005361 scopus 로고    scopus 로고
    • Crystal structure of an Hsp90-geldanamycin complex: Targeting of a protein chaperone by an antitumor agent
    • Stebbins, C. E.; Russo, A. A.; Schneider, C.; Rosen, N.; Hartl, F. U.; Pavletich, N. P. Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent Cell 1997, 89, 239-250 (Pubitemid 27199896)
    • (1997) Cell , vol.89 , Issue.2 , pp. 239-250
    • Stebbins, C.E.1    Russo, A.A.2    Schneider, C.3    Rosen, N.4    Hartl, F.U.5    Pavletich, N.P.6
  • 33
    • 51449093764 scopus 로고    scopus 로고
    • Targeting Hsp90: Small-molecule inhibitors and their clinical development
    • Taldone, T.; Gozman, A.; Maharaj, R.; Chiosis, G. Targeting Hsp90: small-molecule inhibitors and their clinical development Curr. Opin. Pharmacol. 2008, 8, 370-374
    • (2008) Curr. Opin. Pharmacol. , vol.8 , pp. 370-374
    • Taldone, T.1    Gozman, A.2    Maharaj, R.3    Chiosis, G.4
  • 37
    • 79952752856 scopus 로고    scopus 로고
    • STA-9090, a small-molecule Hsp90 inhibitor for the potential treatment of cancer
    • Wang, Y.; Trepel, J. B.; Neckers, L. M.; Giaccone, G. STA-9090, a small-molecule Hsp90 inhibitor for the potential treatment of cancer Curr. Opin. Invest. Drugs 2010, 11, 1466-1476
    • (2010) Curr. Opin. Invest. Drugs , vol.11 , pp. 1466-1476
    • Wang, Y.1    Trepel, J.B.2    Neckers, L.M.3    Giaccone, G.4
  • 40
    • 0033553844 scopus 로고    scopus 로고
    • Characterization of ligand binding by saturation transfer difference NMR spectroscopy
    • DOI 10.1002/(SICI)1521-3773(19990614)38:12<1784::AID-ANIE1784>3.0. CO;2-Q
    • Mayer, M.; Meyer, B. Characterization of ligand binding by saturation transfer difference NMR spectroscopy Angew. Chem., Int. Ed. 1999, 38, 1784-1788 (Pubitemid 29290947)
    • (1999) Angewandte Chemie - International Edition , vol.38 , Issue.12 , pp. 1784-1788
    • Mayer, M.1    Meyer, B.2
  • 41
    • 0141485327 scopus 로고    scopus 로고
    • Development of purine-scaffold small molecule inhibitors of Hsp90
    • DOI 10.2174/1568009033481778
    • Chiosis, G.; Lucas, B.; Huezo, H.; Solit, D.; Basso, A.; Rosen, N. Development of purine-scaffold small molecule inhibitors of Hsp90 Curr. Cancer Drug Targets 2003, 3, 371-376 (Pubitemid 37128323)
    • (2003) Current Cancer Drug Targets , vol.3 , Issue.5 , pp. 371-376
    • Chiosis, G.1    Lucas, B.2    Huezo, H.3    Solit, D.4    Basso, A.5    Rosen, N.6
  • 42
    • 36248956723 scopus 로고    scopus 로고
    • The SeeDs approach: Integrating fragments into drug discovery
    • DOI 10.2174/156802607782341109
    • Hubbard, R. E.; Davis, B.; Chen, I.; Drysdale, M. J. The SeeDs approach: integrating fragments into drug discovery Curr. Top. Med. Chem. 2007, 7, 1568-1581 (Pubitemid 350131015)
    • (2007) Current Topics in Medicinal Chemistry , vol.7 , Issue.16 , pp. 1568-1581
    • Hubbard, R.E.1    Davis, B.2    Chen, I.3    Drysdale, M.J.4
  • 43
    • 0033789206 scopus 로고    scopus 로고
    • Identification of compounds with binding affinity to proteins via magnetization transfer from bulk water
    • Dalvit, C.; Pevarello, P.; Tatò, M.; Veronesi, M.; Vulpetti, A.; Sundström, M. Identification of compounds with binding affinity to proteins via magnetization transfer from bulk water J. Biomol. NMR 2000, 18, 65-68
    • (2000) J. Biomol. NMR , vol.18 , pp. 65-68
    • Dalvit, C.1    Pevarello, P.2    Tatò, M.3    Veronesi, M.4    Vulpetti, A.5    Sundström, M.6
  • 44
    • 0002899752 scopus 로고
    • Modified spin-echo method for measuring nuclear relaxation times
    • Meiboom, S.; Gill, D. Modified spin-echo method for measuring nuclear relaxation times Rev. Sci. Instrum. 1958, 29, 688-691
    • (1958) Rev. Sci. Instrum. , vol.29 , pp. 688-691
    • Meiboom, S.1    Gill, D.2
  • 48
    • 70350548428 scopus 로고    scopus 로고
    • 17 AAG for HSP90 inhibition in cancer - From bench to bedside
    • Usmani, S. Z.; Bona, R.; Li, Z. 17 AAG for HSP90 inhibition in cancer - from bench to bedside Curr. Mol. Med. 2009, 9, 654-664
    • (2009) Curr. Mol. Med. , vol.9 , pp. 654-664
    • Usmani, S.Z.1    Bona, R.2    Li, Z.3
  • 49
    • 68849101479 scopus 로고    scopus 로고
    • Retaspimycin hydrochloride (IPI-504): A novel heat shock protein inhibitor as an anticancer agent
    • Hanson, B. E.; Vesole, D. H. Retaspimycin hydrochloride (IPI-504): a novel heat shock protein inhibitor as an anticancer agent Expert Opin. Invest. Drugs 2009, 18, 1375-1383
    • (2009) Expert Opin. Invest. Drugs , vol.18 , pp. 1375-1383
    • Hanson, B.E.1    Vesole, D.H.2
  • 50
    • 62149135294 scopus 로고    scopus 로고
    • Discovery and development of heat shock protein 90 inhibitors
    • Taldone, T.; Sun, W.; Chiosis, G. Discovery and development of heat shock protein 90 inhibitors Bioorg. Med. Chem. 2009, 17, 2225-2235
    • (2009) Bioorg. Med. Chem. , vol.17 , pp. 2225-2235
    • Taldone, T.1    Sun, W.2    Chiosis, G.3
  • 56
    • 1642288258 scopus 로고    scopus 로고
    • Novel inhibitors of DNA gyrase: 3D structure based biased needle screening, hit validation by biophysical methods, and 3D guided optimization. A promising alternative to random screening
    • DOI 10.1021/jm000017s
    • Boehm, H. J.; Boehringer, M.; Bur, D.; Gmuender, H.; Huber, W.; Klaus, W.; Kostrewa, D.; Kuehne, H.; Luebbers, T.; Meunier-Keller, N.; Mueller, F. Novel inhibitors of DNA gyrase: 3D structure based biased needle screening, hit validation by biophysical methods, and 3D guided optimization. A promising alternative to random screening J. Med. Chem. 2000, 43, 2664-2674 (Pubitemid 30463915)
    • (2000) Journal of Medicinal Chemistry , vol.43 , Issue.14 , pp. 2664-2674
    • Boehm, H.-J.1    Boehringer, M.2    Bur, D.3    Gmuender, H.4    Huber, W.5    Klaus, W.6    Kostrewa, D.7    Kuehne, H.8    Luebbers, T.9    Meunier-Keller, N.10    Mueller, F.11
  • 63
    • 33746914732 scopus 로고    scopus 로고
    • Structural and quantum chemical studies of 8-aryl-sulfanyl adenine class Hsp90 inhibitors
    • DOI 10.1021/jm060297x
    • Immormino, R. M.; Kang, Y.; Chiosis, G.; Gewirth, D. T. Structural and quantum chemical studies of 8-aryl-sulfanyl adenine class Hsp90 inhibitors J. Med. Chem. 2006, 49, 4953-4960 (Pubitemid 44201053)
    • (2006) Journal of Medicinal Chemistry , vol.49 , Issue.16 , pp. 4953-4960
    • Immormino, R.M.1    Kang, Y.2    Chiosis, G.3    Gewirth, D.T.4
  • 64
    • 33645412367 scopus 로고    scopus 로고
    • Kinase patent space visualization using chemical replacements
    • Southall, N. T.; Ajay Kinase patent space visualization using chemical replacements J. Med. Chem. 2006, 49, 2103-2109
    • (2006) J. Med. Chem. , vol.49 , pp. 2103-2109
    • Southall, N.T.1    Ajay2
  • 65
    • 78649496901 scopus 로고    scopus 로고
    • Nitrile-containing pharmaceuticals: Efficacious roles of the nitrile pharmacophore
    • Fleming, F. F.; Yao, L.; Ravikumar, P. C.; Funk, L.; Shook, B. C. Nitrile-containing pharmaceuticals: efficacious roles of the nitrile pharmacophore J. Med. Chem. 2010, 53, 7902-7917
    • (2010) J. Med. Chem. , vol.53 , pp. 7902-7917
    • Fleming, F.F.1    Yao, L.2    Ravikumar, P.C.3    Funk, L.4    Shook, B.C.5
  • 70
    • 0014428697 scopus 로고
    • Alpha-[(t -Butylamino)methyl]-4-hydroxy- m -xylene-alpha 1,alpha 3-diol (AH.3365): A selective beta-adrenergic stimulant
    • Brittain, R. T.; Farmer, J. B.; Jack, D.; Martin, L. E.; Simpson, W. T. Alpha-[(t -Butylamino)methyl]-4-hydroxy- m -xylene-alpha 1,alpha 3-diol (AH.3365): a selective beta-adrenergic stimulant Nature 1968, 219, 862-863
    • (1968) Nature , vol.219 , pp. 862-863
    • Brittain, R.T.1    Farmer, J.B.2    Jack, D.3    Martin, L.E.4    Simpson, W.T.5
  • 71
    • 77949799227 scopus 로고    scopus 로고
    • Intramolecular hydrogen bonding in medicinal chemistry
    • Kuhn, B.; Mohr, P.; Stahl, M. Intramolecular hydrogen bonding in medicinal chemistry J. Med. Chem. 2010, 53, 2601-2611
    • (2010) J. Med. Chem. , vol.53 , pp. 2601-2611
    • Kuhn, B.1    Mohr, P.2    Stahl, M.3
  • 72
    • 33746206247 scopus 로고    scopus 로고
    • Dual-acting agents that possess free radical scavenging and antithrombotic activities: Design, synthesis, and evaluation of phenolic tetrahydro-β-carboline RGD peptide conjugates
    • DOI 10.1016/j.bmcl.2006.06.024, PII S0960894X06006822
    • Bi, W.; Bi, L.; Cai, J.; Liu, S.; Peng, S.; Fischer, N. O.; Tok, J. B. H.; Wang, G. Dual-acting agents that possess free radical scavenging and antithrombotic activities: design, synthesis, and evaluation of phenolic tetrahydro-[beta]-carboline RGD peptide conjugates Bioorg. Med. Chem. Lett. 2006, 16, 4523-4527 (Pubitemid 44094081)
    • (2006) Bioorganic and Medicinal Chemistry Letters , vol.16 , Issue.17 , pp. 4523-4527
    • Bi, W.1    Bi, L.2    Cai, J.3    Liu, S.4    Peng, S.5    Fischer, N.O.6    Tok, J.B.-H.7    Wang, G.8
  • 73
    • 33846154262 scopus 로고    scopus 로고
    • A new approach to N-3 functionalized 3,4-dihydropyrimidine-2(1H)-ones with 1,2,4-oxadiazole group as amide isostere via ionic liquid-phase technology
    • DOI 10.1016/j.tetlet.2006.11.148, PII S0040403906023860
    • Legeay, J. C.; Vanden Eynde, J. J.; Bazureau, J. P. A new approach to N-3 functionalized 3,4-dihydropyrimidine-2(1 H)-ones with 1,2,4-oxadiazole group as amide isostere via ionic liquid-phase technology Tetrahedron Lett. 2007, 48, 1063-1068 (Pubitemid 46075223)
    • (2007) Tetrahedron Letters , vol.48 , Issue.6 , pp. 1063-1068
    • Legeay, J.C.1    Vanden Eynde, J.J.2    Bazureau, J.P.3
  • 74
    • 77957889281 scopus 로고    scopus 로고
    • Surface plasmon resonance biosensor based fragment screening using acetylcholine binding protein identifies ligand efficiency hot spots (LE hot spots) by deconstruction of nicotinic acetylcholine receptor α7 ligands
    • de Kloe, G. E.; Retra, K.; Geitmann, M.; Kallblad, P.; Nahar, T.; van Elk, R.; Smit, A. B.; van Muijlwijk-Koezen, J. E.; Leurs, R.; Irth, H.; Danielson, U. H.; de Esch, I. J. P. Surface plasmon resonance biosensor based fragment screening using acetylcholine binding protein identifies ligand efficiency hot spots (LE hot spots) by deconstruction of nicotinic acetylcholine receptor α7 ligands J. Med. Chem. 2010, 53, 7192-7201
    • (2010) J. Med. Chem. , vol.53 , pp. 7192-7201
    • De Kloe, G.E.1    Retra, K.2    Geitmann, M.3    Kallblad, P.4    Nahar, T.5    Van Elk, R.6    Smit, A.B.7    Van Muijlwijk-Koezen, J.E.8    Leurs, R.9    Irth, H.10    Danielson, U.H.11    De Esch, I.J.P.12
  • 77
    • 79952430797 scopus 로고    scopus 로고
    • Designing a diverse high-quality library for crystallography-based FBDD screening
    • Tounge, B. A.; Parker, M. H. Designing a diverse high-quality library for crystallography-based FBDD screening Methods Enzymol. 2011, 493, 3-20
    • (2011) Methods Enzymol. , vol.493 , pp. 3-20
    • Tounge, B.A.1    Parker, M.H.2
  • 79
    • 78549234304 scopus 로고    scopus 로고
    • A novel class of specific Hsp90 small molecule inhibitors demonstrate in vitro and in vivo anti-tumor activity in human melanoma cells
    • Mehta, P. P.; Kung, P.-P.; Yamazaki, S.; Walls, M.; Shen, A.; Nguyen, L.; Gehring, M. R.; Los, G.; Smeal, T.; Yin, M.-J. A novel class of specific Hsp90 small molecule inhibitors demonstrate in vitro and in vivo anti-tumor activity in human melanoma cells Cancer Lett. 2011, 300, 30-39
    • (2011) Cancer Lett. , vol.300 , pp. 30-39
    • Mehta, P.P.1    Kung, P.-P.2    Yamazaki, S.3    Walls, M.4    Shen, A.5    Nguyen, L.6    Gehring, M.R.7    Los, G.8    Smeal, T.9    Yin, M.-J.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.