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Volumn 9, Issue 18, 2009, Pages 1705-1717

Fragment-based discovery of inhibitors of protein kinase B

Author keywords

[No Author keywords available]

Indexed keywords

AZAINDOLE DERIVATIVE; CCT 128930; CYCLIC AMP DEPENDENT PROTEIN KINASE; INDOLE DERIVATIVE; PROTEIN KINASE B; PROTEIN KINASE B INHIBITOR; PYRAZOLE DERIVATIVE; UNCLASSIFIED DRUG; ENZYME INHIBITOR; PROTEIN BINDING;

EID: 74249105250     PISSN: 15680266     EISSN: None     Source Type: Journal    
DOI: 10.2174/156802609790102419     Document Type: Article
Times cited : (12)

References (66)
  • 1
    • 61749102616 scopus 로고    scopus 로고
    • Targeted small-molecule inhibitors of protein kinase B as anticancer agents
    • Collins, I. Targeted small-molecule inhibitors of protein kinase B as anticancer agents. Anti-Cancer Agents Med. Chem. 2009, 9, 32-50.
    • (2009) Anti-Cancer Agents Med. Chem , vol.9 , pp. 32-50
    • Collins, I.1
  • 3
    • 0037162293 scopus 로고    scopus 로고
    • High-resolution structure of the pleckstrin homology domain of protein kinase B/Akt bound to phosphatidylinositol 3,4,5-triphosphate
    • Thomas, C. C.; Deak, M.; Alessi, D. R.; Van Aalten, D. M. F. High-resolution structure of the pleckstrin homology domain of protein kinase B/Akt bound to phosphatidylinositol 3,4,5-triphosphate. Curr. Biol. 2002, 12, 1256-1262.
    • (2002) Curr. Biol , vol.12 , pp. 1256-1262
    • Thomas, C.C.1    Deak, M.2    Alessi, D.R.3    Van Aalten, D.M.F.4
  • 4
    • 0242468741 scopus 로고    scopus 로고
    • Binding of phosphatidylinositol 3,4,5-triphosphate to the pleckstrin homology domain of protein kinase B induces a conformational change
    • Milburn, C. C.; Deak, M.; Kelly, S. M.; Price, N. C.; Alessi, D. R.; Van Aalten, D. M. F. Binding of phosphatidylinositol 3,4,5-triphosphate to the pleckstrin homology domain of protein kinase B induces a conformational change. Biochem. J. 2003, 375, 531-538.
    • (2003) Biochem. J , vol.375 , pp. 531-538
    • Milburn, C.C.1    Deak, M.2    Kelly, S.M.3    Price, N.C.4    Alessi, D.R.5    Van Aalten, D.M.F.6
  • 5
    • 13844312400 scopus 로고    scopus 로고
    • Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex
    • Sarbassov, D. D.; Guertin, D. A.; Ali, S. M.; Sabatini, D. M. Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex. Science 2005, 307, 1098-1101.
    • (2005) Science , vol.307 , pp. 1098-1101
    • Sarbassov, D.D.1    Guertin, D.A.2    Ali, S.M.3    Sabatini, D.M.4
  • 6
    • 18744373865 scopus 로고    scopus 로고
    • Crystal structure of an activated Akt/protein kinase B ternary complex with GSK3β-peptide and AMP-PNP
    • Yang, J.; Cron, P.; Good, V. M.; Thompson, V.; Hemmings, B. A.; Barford, D. Crystal structure of an activated Akt/protein kinase B ternary complex with GSK3β-peptide and AMP-PNP. Nat. Struct. Biol. 2002, 9, 940-944.
    • (2002) Nat. Struct. Biol , vol.9 , pp. 940-944
    • Yang, J.1    Cron, P.2    Good, V.M.3    Thompson, V.4    Hemmings, B.A.5    Barford, D.6
  • 8
    • 27844598284 scopus 로고    scopus 로고
    • The Akt/PKB pathway: Molecular target for cancer drug discovery
    • Cheng, J. Q.; Lindsley, C. W.; Cheng, G. Z.; Yang, H.; Nicosia, S. V. The Akt/PKB pathway: molecular target for cancer drug discovery. Oncogene 2005, 24, 7842-7492.
    • (2005) Oncogene , vol.24 , pp. 7842-7492
    • Cheng, J.Q.1    Lindsley, C.W.2    Cheng, G.Z.3    Yang, H.4    Nicosia, S.V.5
  • 10
    • 28844448182 scopus 로고    scopus 로고
    • Oncogenic PI3K deregulates transcription and translation
    • Bader, A. G.; Khang, S.; Zhao, L.; Vogt, P. K. Oncogenic PI3K deregulates transcription and translation. Nat. Rev. Cancer 2005, 5, 921-929.
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 921-929
    • Bader, A.G.1    Khang, S.2    Zhao, L.3    Vogt, P.K.4
  • 11
    • 33644513730 scopus 로고    scopus 로고
    • Beyond PTEN mutations: The PI3K pathway as an integrator of multiple inputs during tumorigenesis
    • Cully, M.; You, H.; Levine, A. J.; Mak, T. W. Beyond PTEN mutations: the PI3K pathway as an integrator of multiple inputs during tumorigenesis. Nat. Rev. Cancer 2006, 6, 184-192.
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 184-192
    • Cully, M.1    You, H.2    Levine, A.J.3    Mak, T.W.4
  • 12
    • 4344684649 scopus 로고    scopus 로고
    • PTEN function: How normal cells control it and tumour cells lose it
    • Leslie, N. R.; Downes, C.P. PTEN function: how normal cells control it and tumour cells lose it. Biochem. J. 2004, 382, 1-11.
    • (2004) Biochem. J , vol.382 , pp. 1-11
    • Leslie, N.R.1    Downes, C.P.2
  • 13
    • 0035949699 scopus 로고    scopus 로고
    • AKT plays a central role in tumorigenesis
    • Testa, J. R.; Bellacosa, A. AKT plays a central role in tumorigenesis. Proc. Natl. Acad. Sci. USA 2001, 98, 10983-10985.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 10983-10985
    • Testa, J.R.1    Bellacosa, A.2
  • 15
    • 17144392548 scopus 로고    scopus 로고
    • The Akt/PKB family of protein kinases: A review of small molecule inhibitors and progress towards target validation
    • Barnett, S. F.; Bilodeau, M. T.; Lindsley, C. W. The Akt/PKB family of protein kinases: a review of small molecule inhibitors and progress towards target validation. Curr. Top. Med. Chem. 2005, 5, 109-125.
    • (2005) Curr. Top. Med. Chem , vol.5 , pp. 109-125
    • Barnett, S.F.1    Bilodeau, M.T.2    Lindsley, C.W.3
  • 16
    • 34548844487 scopus 로고    scopus 로고
    • Recent progress in the development of ATP-competitive and allosteric Akt kinase inhibitors
    • Lindsley, C. W.; Barnett, S. F.; Yaroschak, M.; Bilodeau, M. T.; Layton, M. E. Recent progress in the development of ATP-competitive and allosteric Akt kinase inhibitors. Curr. Top. Med. Chem. 2007, 7, 1349-1363.
    • (2007) Curr. Top. Med. Chem , vol.7 , pp. 1349-1363
    • Lindsley, C.W.1    Barnett, S.F.2    Yaroschak, M.3    Bilodeau, M.T.4    Layton, M.E.5
  • 17
    • 35748952229 scopus 로고    scopus 로고
    • Small molecule inhibitors of AKT/PKB kinase as a strategy for treating cancer
    • Heerding, D. A.; Safonov, I. G.; Verma, S. K. Small molecule inhibitors of AKT/PKB kinase as a strategy for treating cancer. Ann. Rep. Med. Chem. 2007, 42, 365-376.
    • (2007) Ann. Rep. Med. Chem , vol.42 , pp. 365-376
    • Heerding, D.A.1    Safonov, I.G.2    Verma, S.K.3
  • 18
    • 35349005202 scopus 로고    scopus 로고
    • Recent progress in the discovery of Akt inhibitors as anticancer agents
    • Li, Q. Recent progress in the discovery of Akt inhibitors as anticancer agents. Expert Opin. Ther. Pat. 2007, 17, 1077-1130.
    • (2007) Expert Opin. Ther. Pat , vol.17 , pp. 1077-1130
    • Li, Q.1
  • 26
    • 33144478148 scopus 로고    scopus 로고
    • Li, Q.; Woods, K. W.; Thomas, S.; Zhu, G.; Packard, G.; Fisher, J.; Li, T.; Gong, J.; Dinges, J.; Song, X.; Abrams, J.; Luo, Y.; Johnson, E. F.; Shi, Y.; Liu, X.; Klinghofer, V.; Des Jong, R.; Oltersdorf, T.; Stoll, V. S.; Jakob, C. G.; Rosenberg, S. H.; Giranda, V. L. Synthesis and structure-activity relationship of 3,4′-bispyridinylethylenes: discovery of a potent 3-isoquinolinylpyridine inhibitor of protein kinase B (PKB/Akt) for the treatment of cancer. Bioorg. Med. Chem. Lett. 2006, 16, 2000-2007.
    • Li, Q.; Woods, K. W.; Thomas, S.; Zhu, G.; Packard, G.; Fisher, J.; Li, T.; Gong, J.; Dinges, J.; Song, X.; Abrams, J.; Luo, Y.; Johnson, E. F.; Shi, Y.; Liu, X.; Klinghofer, V.; Des Jong, R.; Oltersdorf, T.; Stoll, V. S.; Jakob, C. G.; Rosenberg, S. H.; Giranda, V. L. Synthesis and structure-activity relationship of 3,4′-bispyridinylethylenes: discovery of a potent 3-isoquinolinylpyridine inhibitor of protein kinase B (PKB/Akt) for the treatment of cancer. Bioorg. Med. Chem. Lett. 2006, 16, 2000-2007.
  • 27
    • 20344384859 scopus 로고    scopus 로고
    • Luo, Y.; Shoemaker, A. R.; Liu, X.; Woods, K. W.; Thomas, S. A.; de Jong, R.; Kan, E. H.; Li, T.; Stoll, V. S.; Powlas, J. A.; Oleksijew, A.; Mitten, M. J.; Shi, Y.; Guan, R.; McGonigal, T. P.; Klinghofer, V.; Johnson, E. F.; Leverson, J. D.; Bouska, J. J.; Mamo, M.; Smith, R. A.; Gramling-Evans, E. E.; Zinker, B. A.; Mika, A. K.; Nguyen, P. T.; Oltersdorf, T.; Rosenberg, S. H.; Li, Q.; Giranda, V. L. Potent and selective inhibitors of Akt kinases slow the progress of tumours in vivo. Mol. Cancer Ther. 2005, 4, 977-986.
    • Luo, Y.; Shoemaker, A. R.; Liu, X.; Woods, K. W.; Thomas, S. A.; de Jong, R.; Kan, E. H.; Li, T.; Stoll, V. S.; Powlas, J. A.; Oleksijew, A.; Mitten, M. J.; Shi, Y.; Guan, R.; McGonigal, T. P.; Klinghofer, V.; Johnson, E. F.; Leverson, J. D.; Bouska, J. J.; Mamo, M.; Smith, R. A.; Gramling-Evans, E. E.; Zinker, B. A.; Mika, A. K.; Nguyen, P. T.; Oltersdorf, T.; Rosenberg, S. H.; Li, Q.; Giranda, V. L. Potent and selective inhibitors of Akt kinases slow the progress of tumours in vivo. Mol. Cancer Ther. 2005, 4, 977-986.
  • 30
    • 3543117821 scopus 로고    scopus 로고
    • The development of phosphatidylinositol etther lipid analogues as inhibitors of the serine/threonine kinase, Akt
    • Gills, J. J.; Dennis, P. A. The development of phosphatidylinositol etther lipid analogues as inhibitors of the serine/threonine kinase, Akt. Expert Opin. Investig. Drugs 2004, 13, 787-797.
    • (2004) Expert Opin. Investig. Drugs , vol.13 , pp. 787-797
    • Gills, J.J.1    Dennis, P.A.2
  • 31
    • 0032572649 scopus 로고    scopus 로고
    • 3-Deoxy-D-myoinositol 1-phosphate, 1-phosphonate, and ether lipid analogues as inhibitors of phosphatidylinositol-3-kinase signalling and cancer cell growth
    • Qiao, L.; Nan, F.; Kunkel, M.; Gallegos, A.; Powis, G.; Kozikowski, A. P. 3-Deoxy-D-myoinositol 1-phosphate, 1-phosphonate, and ether lipid analogues as inhibitors of phosphatidylinositol-3-kinase signalling and cancer cell growth. J. Med. Chem. 1998, 41, 3303-3306.
    • (1998) J. Med. Chem , vol.41 , pp. 3303-3306
    • Qiao, L.1    Nan, F.2    Kunkel, M.3    Gallegos, A.4    Powis, G.5    Kozikowski, A.P.6
  • 32
    • 0034632791 scopus 로고    scopus 로고
    • 3-(Hydroxymethyl)-bearing phosphatidylinositol ether lipid analogues and carbonate surrogates block PI3-K, Akt, and cancer cell growth
    • Hu, Y.; Qiao, L.; Wang, S.; Rong, S.; Meuillet, E. J.; Bergren, M.; Gallegos, A.; Powis, G.; Kozikowski, A. P. 3-(Hydroxymethyl)-bearing phosphatidylinositol ether lipid analogues and carbonate surrogates block PI3-K, Akt, and cancer cell growth. J. Med. Chem. 2000, 43, 3045-3051.
    • (2000) J. Med. Chem , vol.43 , pp. 3045-3051
    • Hu, Y.1    Qiao, L.2    Wang, S.3    Rong, S.4    Meuillet, E.J.5    Bergren, M.6    Gallegos, A.7    Powis, G.8    Kozikowski, A.P.9
  • 33
    • 0037419785 scopus 로고    scopus 로고
    • Novel PI analogues selectively block activation of the pro-survival serine/threonine kinase Akt
    • Kozikowski, A. P.; Sun, H.; Brognard, J.; Dennis, P. A. Novel PI analogues selectively block activation of the pro-survival serine/threonine kinase Akt. J. Am. Chem. Soc. 2003, 125, 1144-1145.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 1144-1145
    • Kozikowski, A.P.1    Sun, H.2    Brognard, J.3    Dennis, P.A.4
  • 35
    • 34248549518 scopus 로고    scopus 로고
    • Novel inositol phospholipid head-group surrogate crystallised in the pleckstrin homology domain of protein kinase Balpha
    • Mill, S. J.; Komander, D.; Trusselle, M. N.; Safrany, S. T.; van Aalten, D. M. F.; Potter, B. V. L. Novel inositol phospholipid head-group surrogate crystallised in the pleckstrin homology domain of protein kinase Balpha. Chem. Biol. 2007, 2, 242-246.
    • (2007) Chem. Biol , vol.2 , Issue.242 , pp. 246
    • Mill, S.J.1    Komander, D.2    Trusselle, M.N.3    Safrany, S.T.4    van Aalten, D.M.F.5    Potter, B.V.L.6
  • 40
    • 58849120491 scopus 로고    scopus 로고
    • Calleja, V.; Laguerre, M.; Parker, P. J.; Larijani, B. Role of a novel PH-kinase domain interface in PKB/Akt regulation: structural mechanism for allosteric inhibition. PLoS Biol. 2009, 7, e1000017.
    • Calleja, V.; Laguerre, M.; Parker, P. J.; Larijani, B. Role of a novel PH-kinase domain interface in PKB/Akt regulation: structural mechanism for allosteric inhibition. PLoS Biol. 2009, 7, e1000017.
  • 44
    • 0141726877 scopus 로고    scopus 로고
    • A 'rule of three' for fragment-based lead discovery?
    • Congreve, M.; Carr, R.; Murray. C.; Jhoti, H. A 'rule of three' for fragment-based lead discovery? Drug Discov. Today 2003, 8, 876-877.
    • (2003) Drug Discov. Today , vol.8 , pp. 876-877
    • Congreve, M.1    Carr, R.2    Murray, C.3    Jhoti, H.4
  • 46
    • 1942453243 scopus 로고    scopus 로고
    • Ligand efficiency: A useful metric for lead selection
    • Hopkins, A. L.; Groom, C. R.; Alex, A. Ligand efficiency: a useful metric for lead selection. Drug Discov. Today, 2004, 9, 430-431.
    • (2004) Drug Discov. Today , vol.9 , pp. 430-431
    • Hopkins, A.L.1    Groom, C.R.2    Alex, A.3
  • 50
    • 0029829066 scopus 로고    scopus 로고
    • Unravelling the principles of lead discovery: From frustrated energy landscapes to novel molecular anchors
    • Rejto, P. A.; Verkhiver, G. M. Unravelling the principles of lead discovery: from frustrated energy landscapes to novel molecular anchors. Proc. Natl. Acad. Sci. USA 1996, 93, 8945-8950.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8945-8950
    • Rejto, P.A.1    Verkhiver, G.M.2
  • 51
    • 33751076241 scopus 로고    scopus 로고
    • Deconstructing fragment-based inhibitor discovery
    • Babaoglu, K.; Shoichet, B. K. Deconstructing fragment-based inhibitor discovery. Nat. Chem. Biol. 2006, 2, 720-723.
    • (2006) Nat. Chem. Biol , vol.2 , pp. 720-723
    • Babaoglu, K.1    Shoichet, B.K.2
  • 52
    • 54449102045 scopus 로고    scopus 로고
    • Group efficiency: A guideline for hits-to-leads chemistry
    • Verdonk, M. L.; Rees, D. C. Group efficiency: a guideline for hits-to-leads chemistry. ChemMedChem. 2008, 3, 1179-1180.
    • (2008) ChemMedChem , vol.3 , pp. 1179-1180
    • Verdonk, M.L.1    Rees, D.C.2
  • 53
    • 33846610077 scopus 로고    scopus 로고
    • Synthesis of 4-(cyclic dialkylamino)-7-azaindoles by microwave heating of 4-halo-7-azaindoles and cyclic secondary amines
    • Caldwell, J. J.; Cheung, K.-M.; Collins, I. Synthesis of 4-(cyclic dialkylamino)-7-azaindoles by microwave heating of 4-halo-7-azaindoles and cyclic secondary amines. Tetrahedron Lett. 2007, 48, 1527-1529.
    • (2007) Tetrahedron Lett , vol.48 , pp. 1527-1529
    • Caldwell, J.J.1    Cheung, K.-M.2    Collins, I.3
  • 58
    • 9444247656 scopus 로고    scopus 로고
    • Minireview: PRKAR1A: normal and abnormal functions
    • Bossi, I.; Stratakis, C. A. Minireview: PRKAR1A: normal and abnormal functions. Endocrinology 2004, 145, 5452-5458.
    • (2004) Endocrinology , vol.145 , pp. 5452-5458
    • Bossi, I.1    Stratakis, C.A.2
  • 61
    • 34547933680 scopus 로고    scopus 로고
    • Akt inhibitor A-443654 induces rapid Akt Ser-473 phophorylation independent of mTORC1 inhibition
    • Han, E. K.; Leverson, J. D.; McGonigal, T.; Shah, O. J.; Woods, K. W.; Hunter, T.; Giranda, V. L.; Luo, Y. Akt inhibitor A-443654 induces rapid Akt Ser-473 phophorylation independent of mTORC1 inhibition. Oncogene 2007, 26, 5655-5661.
    • (2007) Oncogene , vol.26 , pp. 5655-5661
    • Han, E.K.1    Leverson, J.D.2    McGonigal, T.3    Shah, O.J.4    Woods, K.W.5    Hunter, T.6    Giranda, V.L.7    Luo, Y.8
  • 64
    • 0028143584 scopus 로고
    • Physiological concentrations of purines and pyrimidines
    • Traut, T. W. Physiological concentrations of purines and pyrimidines. Mol. Cell. Biochem. 1994, 140, 1-22.
    • (1994) Mol. Cell. Biochem , vol.140 , pp. 1-22
    • Traut, T.W.1
  • 65
    • 24944497371 scopus 로고    scopus 로고
    • Features of selective kinase inhibitors
    • Knight, Z. A.; Shokat, K. M. Features of selective kinase inhibitors. Chem. Biol. 2005, 12, 621-637.
    • (2005) Chem. Biol , vol.12 , pp. 621-637
    • Knight, Z.A.1    Shokat, K.M.2
  • 66
    • 68949147006 scopus 로고    scopus 로고
    • Measuring and interpreting the selectivity of protein kinase inhibitors
    • Smyth, L. A.; Collins, I. Measuring and interpreting the selectivity of protein kinase inhibitors. J. Chem. Biol. 2009, 2, 131-151.
    • (2009) J. Chem. Biol , vol.2 , pp. 131-151
    • Smyth, L.A.1    Collins, I.2


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