메뉴 건너뛰기




Volumn 7, Issue 12, 2012, Pages

Binding Modes of Peptidomimetics Designed to Inhibit STAT3

Author keywords

[No Author keywords available]

Indexed keywords

PEPTIDOMIMETIC AGENT; PHOSPHOTYROSINE; PROTEIN SH2; STAT3 PROTEIN;

EID: 84871207124     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0051603     Document Type: Article
Times cited : (27)

References (87)
  • 1
    • 0036782884 scopus 로고    scopus 로고
    • Telomerase: A target for cancer therapeutics
    • Shay JW, Wright WE, (2002) Telomerase: A target for cancer therapeutics. Cancer Cell 2: 257-265.
    • (2002) Cancer Cell , vol.2 , pp. 257-265
    • Shay, J.W.1    Wright, W.E.2
  • 2
    • 0043288724 scopus 로고    scopus 로고
    • Heat shock protein 90 as a molecular target for cancer therapeutics
    • Isaccs JS, Xu W, Neckers L, (2003) Heat shock protein 90 as a molecular target for cancer therapeutics. Cancer Cell 3: 213-217.
    • (2003) Cancer Cell , vol.3 , pp. 213-217
    • Isaccs, J.S.1    Xu, W.2    Neckers, L.3
  • 5
    • 34547922452 scopus 로고    scopus 로고
    • Targeting the function of the her2 oncogene in human cancer therapeutics
    • Moasser MM, (2007) Targeting the function of the her2 oncogene in human cancer therapeutics. Oncogene 26: 6577-6592.
    • (2007) Oncogene , vol.26 , pp. 6577-6592
    • Moasser, M.M.1
  • 8
    • 84871237741 scopus 로고    scopus 로고
    • Why is big pharma getting out of antibacterial drug discovery?
    • Projan SJ, (2007) Why is big pharma getting out of antibacterial drug discovery? Nature Reviews Drug Discovery 6: 115-120.
    • (2007) Nature Reviews Drug Discovery , vol.6 , pp. 115-120
    • Projan, S.J.1
  • 11
    • 0141676629 scopus 로고    scopus 로고
    • The process of structure-based drug design
    • Anderson AC, (2003) The process of structure-based drug design. Chemistry & Biology 10: 787-797.
    • (2003) Chemistry & Biology , vol.10 , pp. 787-797
    • Anderson, A.C.1
  • 12
    • 0026730489 scopus 로고
    • Structure-based strategies for drug design and discovery
    • Kuntz IW, (1992) Structure-based strategies for drug design and discovery. Science 257: 1078-1082.
    • (1992) Science , vol.257 , pp. 1078-1082
    • Kuntz, I.W.1
  • 13
    • 34447275949 scopus 로고    scopus 로고
    • Ligand docking and structure-based virtual screening in drug discovery
    • Cavasotto CN, W Orry AJ, (2007) Ligand docking and structure-based virtual screening in drug discovery. Current Topics in Medicinal Chemistry 7: 1006-1014.
    • (2007) Current Topics in Medicinal Chemistry , vol.7 , pp. 1006-1014
    • Cavasotto, C.N.1    Orry, W.A.J.2
  • 15
    • 79952254027 scopus 로고    scopus 로고
    • Discovery of potent inhibitors of soluble epoxide hydrolase by combinatorial library design and structure-based virtual screening
    • Xing L, McDonald JJ, Kolodziej SA, Kurumbail RG, Williams JM, et al. (2011) Discovery of potent inhibitors of soluble epoxide hydrolase by combinatorial library design and structure-based virtual screening. Journal of Medicinal Chemistry 54: 1211-1222.
    • (2011) Journal of Medicinal Chemistry , vol.54 , pp. 1211-1222
    • Xing, L.1    McDonald, J.J.2    Kolodziej, S.A.3    Kurumbail, R.G.4    Williams, J.M.5
  • 17
    • 8844263008 scopus 로고    scopus 로고
    • Docking and scoring in virtual screening for drug discovery: methods and applications
    • Kitchen DB, Decornez H, Furr JR, Bajorathe J, (2004) Docking and scoring in virtual screening for drug discovery: methods and applications. Nature Reviews Drug Discovery 3: 935-949.
    • (2004) Nature Reviews Drug Discovery , vol.3 , pp. 935-949
    • Kitchen, D.B.1    Decornez, H.2    Furr, J.R.3    Bajorathe, J.4
  • 19
    • 0036725277 scopus 로고    scopus 로고
    • Molecular dynamics simulations of biomolecules
    • Karplus M, McCammon A, (2002) Molecular dynamics simulations of biomolecules. Nature Structural Biology 9: 646-652.
    • (2002) Nature Structural Biology , vol.9 , pp. 646-652
    • Karplus, M.1    McCammon, A.2
  • 21
    • 84889844714 scopus 로고    scopus 로고
    • Hoboken, NJ: John Wiley & Sons, Inc. 377-424. doi:10.1002/0470037237.ch16
    • Kubinyi H (2006) Success Stories of Computer-Aided Design. Hoboken, NJ: John Wiley & Sons, Inc. 377-424. doi:10.1002/0470037237.ch16.
    • (2006) Success Stories of Computer-Aided Design
    • Kubinyi, H.1
  • 22
    • 77950503976 scopus 로고    scopus 로고
    • Virtual screening: an endless staircase?
    • Schneider G, (2010) Virtual screening: an endless staircase? Nature Reviews Drug Discovery 9: 273-276.
    • (2010) Nature Reviews Drug Discovery , vol.9 , pp. 273-276
    • Schneider, G.1
  • 23
    • 27144475507 scopus 로고    scopus 로고
    • Investigation of the binding determinants of phosphopeptides targeted to the SRC homology 2 domain of the signal transducer and activator of transcription 3. Development of a high-affinity peptide inhibitor
    • Coleman DR, Ren Z, Mandal PK, Cameron AG, Dyer GA, et al. (2005) Investigation of the binding determinants of phosphopeptides targeted to the SRC homology 2 domain of the signal transducer and activator of transcription 3. Development of a high-affinity peptide inhibitor. Journal of medicinal chemistry 48: 6661-6670.
    • (2005) Journal of Medicinal Chemistry , vol.48 , pp. 6661-6670
    • Coleman, D.R.1    Ren, Z.2    Mandal, P.K.3    Cameron, A.G.4    Dyer, G.A.5
  • 24
    • 65249166871 scopus 로고    scopus 로고
    • Conformationally constrained peptidomimetic inhibitors of signal transducer and activator of transcription 3: Evaluation and molecular modeling
    • Mandal PK, Limbrick D, Coleman DR, Dyer GA, Ren Z, et al. (2009) Conformationally constrained peptidomimetic inhibitors of signal transducer and activator of transcription 3: Evaluation and molecular modeling. Journal of medicinal chemistry 52: 2429-2442.
    • (2009) Journal of Medicinal Chemistry , vol.52 , pp. 2429-2442
    • Mandal, P.K.1    Limbrick, D.2    Coleman, D.R.3    Dyer, G.A.4    Ren, Z.5
  • 25
    • 70349651657 scopus 로고    scopus 로고
    • Structure-affnity relationships of glutamine mimics incorporated into phosphopeptides targeted to the SH2 domain of signal transducer and activator of transcription 3
    • Mandal PK, Ren Z, Chen X, Xiong C, McMurray JS, (2009) Structure-affnity relationships of glutamine mimics incorporated into phosphopeptides targeted to the SH2 domain of signal transducer and activator of transcription 3. Journal of medicinal chemistry 52: 6126-6141.
    • (2009) Journal of Medicinal Chemistry , vol.52 , pp. 6126-6141
    • Mandal, P.K.1    Ren, Z.2    Chen, X.3    Xiong, C.4    McMurray, J.S.5
  • 26
    • 79957742210 scopus 로고    scopus 로고
    • Potent and selective phosphopeptide mimetic prodrugs targeted to the Src homology 2 (SH2) domain of signal transducer and activator of transcription 3
    • Mandal PK, Gao F, Lu Z, Ren Z, Ramesh R, et al. (2011) Potent and selective phosphopeptide mimetic prodrugs targeted to the Src homology 2 (SH2) domain of signal transducer and activator of transcription 3. Journal of medicinal chemistry 54: 3549-63.
    • (2011) Journal of Medicinal Chemistry , vol.54 , pp. 3549-3563
    • Mandal, P.K.1    Gao, F.2    Lu, Z.3    Ren, Z.4    Ramesh, R.5
  • 27
    • 0032499801 scopus 로고    scopus 로고
    • Three-dimensional structure of the Stat3β homodimer bound to DNA
    • Becker S, Groner B, Müller CW, (1998) Three-dimensional structure of the Stat3β homodimer bound to DNA. Nature 394: 145-51.
    • (1998) Nature , vol.394 , pp. 145-151
    • Becker, S.1    Groner, B.2    Müller, C.W.3
  • 29
    • 0036554816 scopus 로고    scopus 로고
    • Activated stat signaling in human tumors provides novel molecular targets for therapeutic intervention
    • Buettner R, Mora LB, Jove R, (2002) Activated stat signaling in human tumors provides novel molecular targets for therapeutic intervention. Clinical Cancer Resesarch 8: 945-954.
    • (2002) Clinical Cancer Resesarch , vol.8 , pp. 945-954
    • Buettner, R.1    Mora, L.B.2    Jove, R.3
  • 30
    • 1042302005 scopus 로고    scopus 로고
    • The stats of cancer-new molecular targets come of age
    • Hua Y, Jove R, (2004) The stats of cancer-new molecular targets come of age. Nature Reviews Cancer 4: 97-105.
    • (2004) Nature Reviews Cancer , vol.4 , pp. 97-105
    • Hua, Y.1    Jove, R.2
  • 31
    • 0028234529 scopus 로고
    • Jak-stat pathways and transcriptional activation in response to ifns and other extracellular signaling proteins
    • Darnell J, Kerr I, Stark G, (1994) Jak-stat pathways and transcriptional activation in response to ifns and other extracellular signaling proteins. Science 264: 1415-1421.
    • (1994) Science , vol.264 , pp. 1415-1421
    • Darnell, J.1    Kerr, I.2    Stark, G.3
  • 33
    • 0033773937 scopus 로고    scopus 로고
    • Fluorescence polarization and anisotropy in high throughput screening: perspectives and primer
    • Owicki JC, (2000) Fluorescence polarization and anisotropy in high throughput screening: perspectives and primer. Journal of Biomolecular Engineering 5: 297-306.
    • (2000) Journal of Biomolecular Engineering , vol.5 , pp. 297-306
    • Owicki, J.C.1
  • 34
    • 0343851682 scopus 로고    scopus 로고
    • Automated docking and molecular dynamics simulations of nimesulide in the cyclooxygenase active site of human prostaglandin-endoperoxide synthase-2 (cox-2)
    • García-Nieto R, Pérez C, Gago F, (2000) Automated docking and molecular dynamics simulations of nimesulide in the cyclooxygenase active site of human prostaglandin-endoperoxide synthase-2 (cox-2). Journal of Computer-Aided Molecular Design 14: 147-160.
    • (2000) Journal of Computer-Aided Molecular Design , vol.14 , pp. 147-160
    • García-Nieto, R.1    Pérez, C.2    Gago, F.3
  • 35
    • 73349093728 scopus 로고    scopus 로고
    • High-performance drug discovery: Computational screening by combining docking and molecular dynamics simulations
    • Okimoto N, Futatsugi N, Fuji H, Suenaga A, Morimoto G, et al. (2009) High-performance drug discovery: Computational screening by combining docking and molecular dynamics simulations. PLoS Computational Biology 5: e1000528.
    • (2009) PLoS Computational Biology , vol.5
    • Okimoto, N.1    Futatsugi, N.2    Fuji, H.3    Suenaga, A.4    Morimoto, G.5
  • 36
    • 62849104063 scopus 로고    scopus 로고
    • Chemical probes that competitively and selectively inhibit stat3 activation
    • Xu X, Kasembeli MM, Jiang X, Tweardy BJ, Tweardy DJ, (2009) Chemical probes that competitively and selectively inhibit stat3 activation. PLoS ONE 4: e4783.
    • (2009) PLoS ONE , vol.4
    • Xu, X.1    Kasembeli, M.M.2    Jiang, X.3    Tweardy, B.J.4    Tweardy, D.J.5
  • 37
    • 81755171903 scopus 로고    scopus 로고
    • Structural analysis of prolyl oligopeptidases using molecular docking and dynamics: insights into conformational changes and ligand binding
    • Kaushik S, Sowdhamini R, (2011) Structural analysis of prolyl oligopeptidases using molecular docking and dynamics: insights into conformational changes and ligand binding. PLoS ONE 6: e26251.
    • (2011) PLoS ONE , vol.6
    • Kaushik, S.1    Sowdhamini, R.2
  • 38
    • 79952176419 scopus 로고    scopus 로고
    • Characterization of molecular recognition of STAT3 SH2 domain inhibitors through molecular simulation
    • Park I, Li C, (2011) Characterization of molecular recognition of STAT3 SH2 domain inhibitors through molecular simulation. Journal of Molecular Recognition 24: 254-265.
    • (2011) Journal of Molecular Recognition , vol.24 , pp. 254-265
    • Park, I.1    Li, C.2
  • 39
    • 79955716232 scopus 로고    scopus 로고
    • Rosetta FlexPepDock ab-initio: simultaneous folding, docking and refinenement of peptides onto their Receptors
    • Raveh B, London N, Zimmerman L, Schueler-Furman O, (2011) Rosetta FlexPepDock ab-initio: simultaneous folding, docking and refinenement of peptides onto their Receptors. PLoS ONE 6: e18934.
    • (2011) PLoS ONE , vol.6
    • Raveh, B.1    London, N.2    Zimmerman, L.3    Schueler-Furman, O.4
  • 40
    • 0020491251 scopus 로고
    • A geometric approach to macromolecule-ligand interactions
    • Kuntz I, (1982) A geometric approach to macromolecule-ligand interactions. Journal of Molecular Biology 161: 269-288.
    • (1982) Journal of Molecular Biology , vol.161 , pp. 269-288
    • Kuntz, I.1
  • 41
    • 84986522918 scopus 로고
    • ICM-a new method for protein modeling and design: applications to docking and structure prediction from the distorted native conformation
    • Abagyan R, Totrov M, Kuznetsov D, (1994) ICM-a new method for protein modeling and design: applications to docking and structure prediction from the distorted native conformation. Journal of Computational Chemistry 15: 488-506.
    • (1994) Journal of Computational Chemistry , vol.15 , pp. 488-506
    • Abagyan, R.1    Totrov, M.2    Kuznetsov, D.3
  • 42
    • 0028854034 scopus 로고
    • Molecular recognition of receptor sites using a genetic algorithm with a description of desolvation
    • Jones G, Willett P, Glen RC, (1995) Molecular recognition of receptor sites using a genetic algorithm with a description of desolvation. Journal of Molecular Biology 245: 43-53.
    • (1995) Journal of Molecular Biology , vol.245 , pp. 43-53
    • Jones, G.1    Willett, P.2    Glen, R.C.3
  • 43
    • 0030599010 scopus 로고    scopus 로고
    • A fast exible docking method using an incremental construction algorithm
    • Rarey M, Kramer B, Lengauer T, Klebe G, (1996) A fast exible docking method using an incremental construction algorithm. Journal of Molecular Biology 261: 470-489.
    • (1996) Journal of Molecular Biology , vol.261 , pp. 470-489
    • Rarey, M.1    Kramer, B.2    Lengauer, T.3    Klebe, G.4
  • 44
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function
    • Morris GM, Goodsell DS, Halliday RS, Huey R, Hart WE, et al. (1998) Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function. Journal of Computational Chemistry 19: 1639-1662.
    • (1998) Journal of Computational Chemistry , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5
  • 45
    • 0033969620 scopus 로고    scopus 로고
    • Morphological similarity: a 3D molecular similarity method correlated with proteinligand recognition
    • Jain AN, (2000) Morphological similarity: a 3D molecular similarity method correlated with proteinligand recognition. Journal of Computer-aided Molecular Design 14: 199-213.
    • (2000) Journal of Computer-Aided Molecular Design , vol.14 , pp. 199-213
    • Jain, A.N.1
  • 46
    • 12144289984 scopus 로고    scopus 로고
    • Glide: a new approach for rapid, accurate docking and scoring. 1. Method and assessment of docking accuracy
    • Friesner RA, Banks JL, Murphy RB, Halgren TA, Klicic JJ, et al. (2004) Glide: a new approach for rapid, accurate docking and scoring. 1. Method and assessment of docking accuracy. Journal of Medicinal Chemistry 47: 1739-1749.
    • (2004) Journal of Medicinal Chemistry , vol.47 , pp. 1739-1749
    • Friesner, R.A.1    Banks, J.L.2    Murphy, R.B.3    Halgren, T.A.4    Klicic, J.J.5
  • 47
    • 84871225647 scopus 로고    scopus 로고
    • VoteDock: consensus docking method for prediction of protein-ligand interactions
    • Plewczynski D, (2010) VoteDock: consensus docking method for prediction of protein-ligand interactions. Journal of Computational Chemistry 32: 1-14.
    • (2010) Journal of Computational Chemistry , vol.32 , pp. 1-14
    • Plewczynski, D.1
  • 48
    • 76149120388 scopus 로고    scopus 로고
    • AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading
    • Trott O, Olson AJ, (2010) AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. Journal of Computational Chemistry 31: 455-461.
    • (2010) Journal of Computational Chemistry , vol.31 , pp. 455-461
    • Trott, O.1    Olson, A.J.2
  • 50
    • 34250827919 scopus 로고    scopus 로고
    • Analysis of hiv wild-type and mutant structures via in silico docking against diverse ligand libraries
    • Chang MW, Lindstrom W, Olson AJ, Belew RK, (2007) Analysis of hiv wild-type and mutant structures via in silico docking against diverse ligand libraries. Journal of Chemical Information and Modeling 47: 1258-1262.
    • (2007) Journal of Chemical Information and Modeling , vol.47 , pp. 1258-1262
    • Chang, M.W.1    Lindstrom, W.2    Olson, A.J.3    Belew, R.K.4
  • 54
    • 77957820654 scopus 로고    scopus 로고
    • Virtual screening for HIV protease inhibitors: a comparison of AutoDock 4 and Vina
    • Chang MW, Ayeni C, Breuer S, Torbett BE, (2010) Virtual screening for HIV protease inhibitors: a comparison of AutoDock 4 and Vina. PloS ONE 5: e10926.
    • (2010) PloS ONE , vol.5
    • Chang, M.W.1    Ayeni, C.2    Breuer, S.3    Torbett, B.E.4
  • 55
    • 77954274507 scopus 로고    scopus 로고
    • Evaluation of the performance of four molecular docking programs on a diverse set of protein-ligand complexes
    • Li X, Li Y, Cheng T, Liu Z, Wang R, (2010) Evaluation of the performance of four molecular docking programs on a diverse set of protein-ligand complexes. Journal of Computational Chemistry 31: 2109-2125.
    • (2010) Journal of Computational Chemistry , vol.31 , pp. 2109-2125
    • Li, X.1    Li, Y.2    Cheng, T.3    Liu, Z.4    Wang, R.5
  • 56
    • 77956332699 scopus 로고    scopus 로고
    • Discovery of selective inhibitors against EBNA1 via high throughput in silico virtual screening
    • Li N, Thompson S, Schultz DC, Zhu W, Jiang H, et al. (2010) Discovery of selective inhibitors against EBNA1 via high throughput in silico virtual screening. PloS ONE 5: e10126.
    • (2010) PloS ONE , vol.5
    • Li, N.1    Thompson, S.2    Schultz, D.C.3    Zhu, W.4    Jiang, H.5
  • 58
    • 0035966871 scopus 로고    scopus 로고
    • Detailed analysis of scoring functions for virtual screening
    • Stahl M, Rarey M, (2001) Detailed analysis of scoring functions for virtual screening. Journal of Medicinal Chemistry 44: 1035-1042.
    • (2001) Journal of Medicinal Chemistry , vol.44 , pp. 1035-1042
    • Stahl, M.1    Rarey, M.2
  • 61
    • 1442351132 scopus 로고    scopus 로고
    • Protein exibility in ligand docking and virtual screening to protein kinases
    • Cavasotto CN, Abagyan RA, (2004) Protein exibility in ligand docking and virtual screening to protein kinases. Journal of Molecular Biology 337: 209-225.
    • (2004) Journal of Molecular Biology , vol.337 , pp. 209-225
    • Cavasotto, C.N.1    Abagyan, R.A.2
  • 62
    • 0347361642 scopus 로고    scopus 로고
    • Lessons in molecular recognition: The effects of ligand and protein exibility on molecular docking accuracy
    • Erickson JA, Jalaie M, Robertson DH, Lewis RA, Vieth M, (2004) Lessons in molecular recognition: The effects of ligand and protein exibility on molecular docking accuracy. Journal of Medicinal Chemistry 47: 45-55.
    • (2004) Journal of Medicinal Chemistry , vol.47 , pp. 45-55
    • Erickson, J.A.1    Jalaie, M.2    Robertson, D.H.3    Lewis, R.A.4    Vieth, M.5
  • 63
    • 0036084259 scopus 로고    scopus 로고
    • Efficient docking of peptides to proteins without prior knowledge of the binding site
    • Hetényi C, van der Spoel D, (2002) Efficient docking of peptides to proteins without prior knowledge of the binding site. Protein Science 11: 1729-1737.
    • (2002) Protein Science , vol.11 , pp. 1729-1737
    • Hetényi, C.1    van der Spoel, D.2
  • 67
    • 0034084991 scopus 로고    scopus 로고
    • Combined molecular mechanical and continuum solvent approach (mm-pbsa/gbsa) to predict ligand binding
    • Massova I, Kollman P, (2000) Combined molecular mechanical and continuum solvent approach (mm-pbsa/gbsa) to predict ligand binding. Perspectives in Drug Discovery and Design 18: 113-135.
    • (2000) Perspectives in Drug Discovery and Design , vol.18 , pp. 113-135
    • Massova, I.1    Kollman, P.2
  • 69
    • 39149090322 scopus 로고    scopus 로고
    • Structural basis for the binding of high affnity phosphopetides to stat3
    • McMurray JS, (2007) Structural basis for the binding of high affnity phosphopetides to stat3. Biopolymers 90: 69-79.
    • (2007) Biopolymers , vol.90 , pp. 69-79
    • McMurray, J.S.1
  • 71
    • 84871218921 scopus 로고    scopus 로고
    • Maestro website, Available, Accessed 2012 Nov 11
    • Maestro website. Available: http://www.schrodinger.com/products/14/12/. Accessed 2012 Nov 11.
  • 74
    • 84871194043 scopus 로고    scopus 로고
    • AmberTools website. Available, Accessed 2012 Nov 11
    • AmberTools website. Available: http://ambermd.org/. Accessed 2012 Nov 11.
  • 76
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An Nlog(N) method for Ewald sums in large systems
    • Darden T, York D, Pedersen L, (1993) Particle mesh Ewald: An Nlog(N) method for Ewald sums in large systems. The Journal of Chemical Physics 98: 10089-10092.
    • (1993) The Journal of Chemical Physics , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 78
    • 0034521981 scopus 로고    scopus 로고
    • Calculating structures and free energies of complex molecules: Combining molecular mechanics and continuum models
    • Kollman PA, Massova I, Reyes C, Kuhn B, Huo S, et al. (2000) Calculating structures and free energies of complex molecules: Combining molecular mechanics and continuum models. Accounts of Chemical Research 33: 889-897.
    • (2000) Accounts of Chemical Research , vol.33 , pp. 889-897
    • Kollman, P.A.1    Massova, I.2    Reyes, C.3    Kuhn, B.4    Huo, S.5
  • 80
    • 0024588901 scopus 로고
    • Structural origins of high-affinity biotin binding to streptavidin
    • Weber P, Ohlendorf D, Wendoloski J, Salemme F, (1989) Structural origins of high-affinity biotin binding to streptavidin. Science 243: 85-88.
    • (1989) Science , vol.243 , pp. 85-88
    • Weber, P.1    Ohlendorf, D.2    Wendoloski, J.3    Salemme, F.4
  • 81
    • 0027510004 scopus 로고
    • Further development of hydrogen bond functions for use in determining energetically favorable binding sites on molecules of known structure. 2. ligand probe groups with the ability to form more than two hydrogen bonds
    • Wade RC, Goodford PJ, (1993) Further development of hydrogen bond functions for use in determining energetically favorable binding sites on molecules of known structure. 2. ligand probe groups with the ability to form more than two hydrogen bonds. Journal of Medicinal Chemistry 36: 148-156.
    • (1993) Journal of Medicinal Chemistry , vol.36 , pp. 148-156
    • Wade, R.C.1    Goodford, P.J.2
  • 85
    • 0015861774 scopus 로고
    • Relationship between the inhibition constant (Ki) and the concentration of inhibitor which causes 50 per cent inhibition (IC50) of an enzymatic reaction
    • Cheng Y, Prusoff WH, (1973) Relationship between the inhibition constant (Ki) and the concentration of inhibitor which causes 50 per cent inhibition (IC50) of an enzymatic reaction. Biochemical Pharmacology 22: 3099-3108.
    • (1973) Biochemical Pharmacology , vol.22 , pp. 3099-3108
    • Cheng, Y.1    Prusoff, W.H.2
  • 86
    • 2942579547 scopus 로고    scopus 로고
    • A high-throughput uorescence polarization assay for signal transducer and activator of transcription 3
    • Schust J, Berg T, (2004) A high-throughput uorescence polarization assay for signal transducer and activator of transcription 3. Analytical Biochemistry 330: 114-118.
    • (2004) Analytical Biochemistry , vol.330 , pp. 114-118
    • Schust, J.1    Berg, T.2
  • 87
    • 20144376462 scopus 로고    scopus 로고
    • Structural bases of unphosphorylated stat1 association and receptor binding
    • Mao X, Ren Z, Parker GN, Sondermann H, Pastorello MA, et al. (2005) Structural bases of unphosphorylated stat1 association and receptor binding. Molecular Cell 17: 761-771.
    • (2005) Molecular Cell , vol.17 , pp. 761-771
    • Mao, X.1    Ren, Z.2    Parker, G.N.3    Sondermann, H.4    Pastorello, M.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.