메뉴 건너뛰기




Volumn 6, Issue 7, 2011, Pages 724-732

Screening of protein-protein interaction modulators via Sulfo-Click kinetic target-guided synthesis

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ASPARTIC ACID; AZIDE; PHENYLALANINE; SULFONAMIDE;

EID: 79960550248     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb200085q     Document Type: Article
Times cited : (44)

References (60)
  • 1
    • 37249004920 scopus 로고    scopus 로고
    • Reaching for high-hanging fruit in drug discovery at protein-protein interfaces
    • DOI 10.1038/nature06526, PII NATURE06526
    • Wells, J. A. and McClendon, C. L. (2007) Reaching for high-hanging fruit in drug discovery at protein-protein interfaces Nature (London, U. K.) 450, 1001-1009 (Pubitemid 350273630)
    • (2007) Nature , vol.450 , Issue.7172 , pp. 1001-1009
    • Wells, J.A.1    McClendon, C.L.2
  • 2
    • 20444376940 scopus 로고    scopus 로고
    • Protein-protein interactions and cancer: Small molecules going in for the kill
    • DOI 10.1016/j.cbpa.2005.03.001, PII S1367593105000487, Combinatorial Chemistry
    • Arkin, M. (2005) Protein-protein interactions and cancer: small molecules going in for the kill Curr. Opin. Chem. Biol. 9, 317-324 (Pubitemid 40804556)
    • (2005) Current Opinion in Chemical Biology , vol.9 , Issue.3 , pp. 317-324
    • Arkin, M.1
  • 3
    • 3142781225 scopus 로고    scopus 로고
    • Small-molecule inhibitors of protein-protein interactions: Progressing towards the dream
    • Arkin, M. R. and Wells, J. A. (2004) Small-molecule inhibitors of protein-protein interactions: Progressing towards the dream Nat. Rev. Drug Discovery 3, 301-317 (Pubitemid 38499758)
    • (2004) Nature Reviews Drug Discovery , vol.3 , Issue.4 , pp. 301-317
    • Arkin, M.R.1    Wells, J.A.2
  • 4
    • 0037860938 scopus 로고    scopus 로고
    • Modulation of protein-protein interactions with small organic molecules
    • DOI 10.1002/anie.200200558
    • Berg, T. (2003) Modulation of protein-protein interactions with small organic molecules Angew. Chem., Int. Ed. 42, 2462-2481 (Pubitemid 36753413)
    • (2003) Angewandte Chemie - International Edition , vol.42 , Issue.22 , pp. 2462-2481
    • Berg, T.1
  • 5
    • 0032540856 scopus 로고    scopus 로고
    • Dictionary of interfaces in proteins (DIP). Data bank of complementary molecular surface patches
    • DOI 10.1006/jmbi.1998.1878
    • Preissner, R., Goede, A., and Frommel, C. (1998) Dictionary of interfaces in proteins (DIP). Data bank of complementary molecular surface patches J. Mol. Biol. 280, 535-550 (Pubitemid 28327289)
    • (1998) Journal of Molecular Biology , vol.280 , Issue.3 , pp. 535-550
    • Preissner, R.1    Goede, A.2    Frommel, C.3
  • 6
    • 0031547966 scopus 로고    scopus 로고
    • Electrostatic complementarity at protein/protein interfaces
    • DOI 10.1006/jmbi.1997.0987
    • McCoy, A. J., Epa, V. C., and Colman, P. M. (1997) Electrostatic complementarity at protein/protein interfaces J. Mol. Biol. 268, 570-584 (Pubitemid 27208075)
    • (1997) Journal of Molecular Biology , vol.268 , Issue.2 , pp. 570-584
    • McCoy, A.J.1    Chandana Epa, V.2    Colman, P.M.3
  • 7
    • 0034681465 scopus 로고    scopus 로고
    • Convergent solutions to binding at a protein-protein interface
    • DOI 10.1126/science.287.5456.1279
    • DeLano, W. L., Ultsch, M. H., de Vos, A. M., and Wells, J. A. (2000) Convergent solutions to binding at a protein-protein interface Science 287, 1279-1283 (Pubitemid 30112152)
    • (2000) Science , vol.287 , Issue.5456 , pp. 1279-1283
    • DeLano, W.L.1    Ultsch, M.H.2    De Vos, A.M.3    Wells, J.A.4
  • 9
    • 0037474541 scopus 로고    scopus 로고
    • Structural characterisation and functional significance of transient protein-protein interactions
    • DOI 10.1016/S0022-2836(02)01281-0
    • Nooren, I. M. A. and Thornton, J. M. (2003) Structural characterisation and functional significance of transient protein-protein interactions J. Mol. Biol. 325, 991-1018 (Pubitemid 36263408)
    • (2003) Journal of Molecular Biology , vol.325 , Issue.5 , pp. 991-1018
    • Nooren, I.M.A.1    Thornton, J.M.2
  • 10
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein-protein recognition sites
    • DOI 10.1006/jmbi.1998.2439
    • Lo Conte, L., Chothia, C., and Janin, J. (1999) The atomic structure of protein-protein recognition sites J. Mol. Biol. 285, 2177-2198 (Pubitemid 29078179)
    • (1999) Journal of Molecular Biology , vol.285 , Issue.5 , pp. 2177-2198
    • Conte, L.L.1    Chothia, C.2    Janin, J.3
  • 11
    • 0041312697 scopus 로고    scopus 로고
    • Diversity of protein-protein interactions
    • DOI 10.1093/emboj/cdg359
    • Nooren, I. M. A. and Thornton, J. M. (2003) Diversity of protein-protein interactions EMBO J. 22, 3486-3492 (Pubitemid 36898326)
    • (2003) EMBO Journal , vol.22 , Issue.14 , pp. 3486-3492
    • Nooren, I.M.A.1    Thornton, J.M.2
  • 12
    • 0028916599 scopus 로고
    • A hot-spot of binding-energy in a hormone-receptor interface
    • Clackson, T. and Wells, J. A. (1995) A hot-spot of binding-energy in a hormone-receptor interface Science 267, 383-386
    • (1995) Science , vol.267 , pp. 383-386
    • Clackson, T.1    Wells, J.A.2
  • 13
    • 0032479179 scopus 로고    scopus 로고
    • Anatomy of hot spots in protein interfaces
    • DOI 10.1006/jmbi.1998.1843
    • Bogan, A. A. and Thorn, K. S. (1998) Anatomy of hot spots in protein interfaces J. Mol. Biol. 280, 1-9 (Pubitemid 28312802)
    • (1998) Journal of Molecular Biology , vol.280 , Issue.1 , pp. 1-9
    • Bogan, A.A.1    Thorn, K.S.2
  • 14
    • 0036469060 scopus 로고    scopus 로고
    • Unraveling hot spots in binding interfaces: Progress and challenges
    • DeLano, W. L. (2002) Unraveling hot spots in binding interfaces: progress and challenges Curr. Opin. Struct. Biol. 12, 14-20
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 14-20
    • Delano, W.L.1
  • 15
    • 0032705432 scopus 로고    scopus 로고
    • Designed molecules that fold to mimic protein secondary structures
    • Stigers, K. D., Soth, M. J., and Nowick, J. S. (1999) Designed molecules that fold to mimic protein secondary structures Curr. Opin. Chem. Biol. 3, 714-723
    • (1999) Curr. Opin. Chem. Biol. , vol.3 , pp. 714-723
    • Stigers, K.D.1    Soth, M.J.2    Nowick, J.S.3
  • 16
    • 77949858836 scopus 로고    scopus 로고
    • Kinetic target-guided synthesis
    • Hu, X. D. and Manetsch, R. (2010) Kinetic target-guided synthesis Chem. Soc. Rev. 39, 1316-1324
    • (2010) Chem. Soc. Rev. , vol.39 , pp. 1316-1324
    • Hu, X.D.1    Manetsch, R.2
  • 17
    • 77949786732 scopus 로고    scopus 로고
    • In situ click chemistry: Probing the binding landscapes of biological molecules
    • Mamidyala, S. K. and Finn, M. G. (2010) In situ click chemistry: probing the binding landscapes of biological molecules Chem. Soc. Rev. 39, 1252-1261
    • (2010) Chem. Soc. Rev. , vol.39 , pp. 1252-1261
    • Mamidyala, S.K.1    Finn, M.G.2
  • 18
    • 34447562439 scopus 로고    scopus 로고
    • In situ click chemistry: A powerful means for lead discovery
    • Sharpless, K. B. and Manetsch, R. (2006) In situ click chemistry: a powerful means for lead discovery Exp. Opin. Drug Discovery 1, 525-538
    • (2006) Exp. Opin. Drug Discovery , vol.1 , pp. 525-538
    • Sharpless, K.B.1    Manetsch, R.2
  • 20
    • 54249167081 scopus 로고    scopus 로고
    • Bcl-XL-templated assembly of its own protein-protein interaction modulator from fragments decorated with thio acids and sulfonyl azides
    • Hu, X., Sun, J., Wang, H.-G., and Manetsch, R. (2008) Bcl-XL-templated assembly of its own protein-protein interaction modulator from fragments decorated with thio acids and sulfonyl azides J. Am. Chem. Soc. 130, 13820-13821
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 13820-13821
    • Hu, X.1    Sun, J.2    Wang, H.-G.3    Manetsch, R.4
  • 21
    • 0038788894 scopus 로고    scopus 로고
    • The reaction of thio acids with azides: A new mechanism and new synthetic applications
    • DOI 10.1021/ja0294919
    • Shangguan, N., Katukojvala, S., Greenburg, R., and Williams, L. J. (2003) The reaction of thio acids with azides: A new mechanism and new synthetic applications J. Am. Chem. Soc. 125, 7754-7755 (Pubitemid 36789754)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.26 , pp. 7754-7755
    • Shangguan, N.1    Katukojvala, S.2    Greenberg, R.3    Williams, L.J.4
  • 23
    • 74749090341 scopus 로고    scopus 로고
    • "Sulfo-click" for ligation as well as for site-specific conjugation with peptides, fluorophores, and metal chelators
    • Rijkers, D. T. S., Merkx, R., Yim, C.-B., Brouwer, A. J., and Liskamp, R. M. J. (2010) "Sulfo-click" for ligation as well as for site-specific conjugation with peptides, fluorophores, and metal chelators, J. Pept. Sci. 16, 1-5.
    • (2010) J. Pept. Sci. , vol.16 , pp. 1-5
    • Rijkers, D.T.S.1    Merkx, R.2    Yim, C.-B.3    Brouwer, A.J.4    Liskamp, R.M.J.5
  • 24
    • 0842281645 scopus 로고    scopus 로고
    • Cell Death: Critical Control Points
    • DOI 10.1016/S0092-8674(04)00046-7
    • Danial, N. N. and Korsmeyer, S. J. (2004) Cell death: Critical control points Cell 116, 205-219 (Pubitemid 38167313)
    • (2004) Cell , vol.116 , Issue.2 , pp. 205-219
    • Danial, N.N.1    Korsmeyer, S.J.2
  • 25
    • 0036463405 scopus 로고    scopus 로고
    • A matter of life and death
    • DOI 10.1016/S1535-6108(02)00024-7
    • Green, D. R. and Evan, G. I. (2002) A matter of life and death Cancer Cell 1, 19-30 (Pubitemid 41039172)
    • (2002) Cancer Cell , vol.1 , Issue.1 , pp. 19-30
    • Green, D.R.1    Evan, G.I.2
  • 26
    • 0034953632 scopus 로고    scopus 로고
    • Apoptosis-regulating proteins as targets for drug discovery
    • DOI 10.1016/S1471-4914(01)02026-3, PII S1471491401020263
    • Reed, J. C. (2001) Apoptosis-regulating proteins as targets for drug discovery Trends Mol. Med. 7, 314-319 (Pubitemid 32606571)
    • (2001) Trends in Molecular Medicine , vol.7 , Issue.7 , pp. 314-319
    • Reed, J.C.1
  • 28
    • 0030634474 scopus 로고    scopus 로고
    • Bcl-2 family proteins: Strategies for overcoming chemoresistance in cancer
    • Reed, J. C. (1997) Bcl-2 family proteins: strategies for overcoming chemoresistance in cancer Adv. Pharmacol. (San Diego) 41, 501-532
    • (1997) Adv. Pharmacol. (San Diego) , vol.41 , pp. 501-532
    • Reed, J.C.1
  • 29
    • 33646380068 scopus 로고    scopus 로고
    • At the gates of death
    • DOI 10.1016/j.ccr.2006.05.004, PII S153561080600122X
    • Green, D. R. (2006) At the gates of death Cancer Cell 9, 328-330 (Pubitemid 43668728)
    • (2006) Cancer Cell , vol.9 , Issue.5 , pp. 328-330
    • Green, D.R.1
  • 30
    • 37549048249 scopus 로고    scopus 로고
    • The BCL-2 protein family: Opposing activities that mediate cell death
    • Youle, R. J. and Strasser, A. (2008) The BCL-2 protein family: opposing activities that mediate cell death Nat. Rev. Mol. Cell Biol. 9, 47-59
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 47-59
    • Youle, R.J.1    Strasser, A.2
  • 36
    • 33846931348 scopus 로고    scopus 로고
    • Efficient amidation from carboxylic acids and azides via selenocarboxylates: Application to the coupling of amino acids and peptides with azides
    • Wu, X. H. and Hu, L. Q. (2007) Efficient amidation from carboxylic acids and azides via selenocarboxylates: Application to the coupling of amino acids and peptides with azides J. Org. Chem. 72, 765-774
    • (2007) J. Org. Chem. , vol.72 , pp. 765-774
    • Wu, X.H.1    Hu, L.Q.2
  • 38
    • 0036830438 scopus 로고    scopus 로고
    • Bcl-XL protects BimEL-induced Bax conformational change and cytochrome c release independent of interacting with Bax or BimEL
    • DOI 10.1074/jbc.M207516200
    • Yamaguchi, H. and Wang, H.-G. (2002) Bcl-XL protects BimEL-induced Bax conformational change and cytochrome c release independent of interacting with Bax or BimEL J. Biol. Chem. 277, 41604-41612 (Pubitemid 35257465)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.44 , pp. 41604-41612
    • Yamaguchi, H.1    Wang, H.-G.2
  • 40
    • 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. (2006) Fragment-based lead discovery: a chemical update Curr. Opin. Biotechnol. 17, 643-652 (Pubitemid 44791912)
    • (2006) Current Opinion in Biotechnology , vol.17 , Issue.6 , pp. 643-652
    • Erlanson, D.A.1
  • 41
    • 22044441118 scopus 로고    scopus 로고
    • Fragment-based lead discovery: Leads by design
    • DOI 10.1016/S1359-6446(05)03511-7, PII S1359644605035117
    • Carr, R. A. E., Congreve, M., Murray, C. W., and Rees, D. C. (2005) Fragment-based lead discovery: leads by design Drug Discovery Today 10, 987-992 (Pubitemid 40967047)
    • (2005) Drug Discovery Today , vol.10 , Issue.14 , pp. 987-992
    • Carr, R.A.E.1    Congreve, M.2    Murray, C.W.3    Rees, D.C.4
  • 42
    • 33645852593 scopus 로고    scopus 로고
    • Fragment-based drug discovery of carbonic anhydrase II inhibitors by dynamic combinatorial chemistry utilizing alkene cross metathesis
    • Poulsen, S. A. and Bornaghi, L. F. (2006) Fragment-based drug discovery of carbonic anhydrase II inhibitors by dynamic combinatorial chemistry utilizing alkene cross metathesis Bioorg. Med. Chem. 14, 3275-3284
    • (2006) Bioorg. Med. Chem. , vol.14 , pp. 3275-3284
    • Poulsen, S.A.1    Bornaghi, L.F.2
  • 43
    • 70349425790 scopus 로고    scopus 로고
    • Recent progress in fragment-based lead discovery
    • Schulz, M. N. and Hubbard, R. E. (2009) Recent progress in fragment-based lead discovery Curr. Opin. Pharmacol. 9, 615-621
    • (2009) Curr. Opin. Pharmacol. , vol.9 , pp. 615-621
    • Schulz, M.N.1    Hubbard, R.E.2
  • 45
    • 67849113794 scopus 로고    scopus 로고
    • The rise of fragment-based drug discovery
    • Murray, C. W. and Rees, D. C. (2009) The rise of fragment-based drug discovery Nat. Chem. 1, 187-192
    • (2009) Nat. Chem. , vol.1 , pp. 187-192
    • Murray, C.W.1    Rees, D.C.2
  • 46
    • 33845364148 scopus 로고    scopus 로고
    • Fragment-based drug design: How big is too big?
    • DOI 10.1021/jm060511h
    • Hajduk, P. J. (2006) Fragment-based drug design: How big is too big? J. Med. Chem. 49, 6972-6976 (Pubitemid 44885985)
    • (2006) Journal of Medicinal Chemistry , vol.49 , Issue.24 , pp. 6972-6976
    • Hajduk, P.J.1
  • 47
    • 0035805266 scopus 로고    scopus 로고
    • Using an enzyme's active site to template inhibitors
    • DOI 10.1002/1521-3773(20010504)40:9<1774::AID-ANIE17740>3.0.CO;2-G
    • Nguyen, R. and Huc, I. (2001) Using an enzyme's active site to template inhibitors Angew. Chem., Int. Ed. 40, 1774-1776 (Pubitemid 32441108)
    • (2001) Angewandte Chemie - International Edition , vol.40 , Issue.9 , pp. 1774-1776
    • Nguyen, R.1    Huc, I.2
  • 49
    • 18644384979 scopus 로고    scopus 로고
    • In situ selection of lead compounds by click chemistry: Target-guided optimization of acetylcholinesterase inhibitors
    • DOI 10.1021/ja043031t
    • Krasinski, A., Radic, Z., Manetsch, R., Raushel, J., Taylor, P., Sharpless, K. B., and Kolb, H. C. (2005) In situ selection of lead compounds by click chemistry: Target-guided optimization of acetylcholinesterase inhibitors J. Am. Chem. Soc. 127, 6686-6692 (Pubitemid 40664175)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.18 , pp. 6686-6692
    • Krasinski, A.1    Radic, Z.2    Manetsch, R.3    Raushel, J.4    Taylor, P.5    Sharpless, K.B.6    Kolb, H.C.7
  • 55
    • 0019407381 scopus 로고
    • On the attribution and additivity of binding-energies
    • Jencks, W. P. (1981) On the attribution and additivity of binding-energies Proc. Natl. Acad. Sci. U. S. A. 78, 4046-4050
    • (1981) Proc. Natl. Acad. Sci. U. S. A. , vol.78 , pp. 4046-4050
    • Jencks, W.P.1
  • 57
    • 28744444023 scopus 로고    scopus 로고
    • Structural insights into conformational flexibility at the peripheral site and within the active center gorge of AChE
    • DOI 10.1016/j.cbi.2005.10.018, PII S0009279705002590
    • Bourne, Y., Radic, Z., Kolb, H. C., Sharpless, K. B., Taylor, P., and Marchot, P. (2005) Structural insights into conformational flexibility at the peripheral site and within the active center gorge of AChE Chem.-Biol. Interact. 157, 159-165 (Pubitemid 41757646)
    • (2005) Chemico-Biological Interactions , vol.157-158 , pp. 159-165
    • Bourne, Y.1    Radic, Z.2    Kolb, H.C.3    Sharpless, K.B.4    Taylor, P.5    Marchot, P.6
  • 59
    • 0030039619 scopus 로고    scopus 로고
    • The art and practice of structure-based drug design: A molecular modeling perspective
    • DOI 10.1002/(SICI)1098-1128(199601)16:1<3::AID-MED1>3.0.CO;2-6
    • Bohacek, R. S., McMartin, C., and Guida, W. C. (1996) The art and practice of structure-based drug design: a molecular modeling perspective Med. Res. Rev. 16, 3-50 (Pubitemid 26037075)
    • (1996) Medicinal Research Reviews , vol.16 , Issue.1 , pp. 3-50
    • Bohacek, R.S.1    McMartin, C.2    Guida, W.C.3
  • 60
    • 0032476812 scopus 로고    scopus 로고
    • Polyvalent interactions in biological systems: Implications for design and use of multivalent ligands and inhibitors
    • Mammen, M., Choi, S. K., and Whitesides, G. M. (1998) Polyvalent interactions in biological systems: Implications for design and use of multivalent ligands and inhibitors Angew. Chem., Int. Ed. 37, 2755-2794
    • (1998) Angew. Chem., Int. Ed. , vol.37 , pp. 2755-2794
    • Mammen, M.1    Choi, S.K.2    Whitesides, G.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.