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Volumn 58, Issue 1, 2015, Pages 111-129

Inhibitors of p21-activated kinases (PAKs)

Author keywords

[No Author keywords available]

Indexed keywords

ANTINEOPLASTIC AGENT; BENZIMIDAZOLE DERIVATIVE; BIARYL KETONE AZAINDOLE DERIVATIVE; DIBENZODIAZEPINE DERIVATIVE; MALEIMIDE; OXINDOLE; P21 ACTIVATED KINASE 1; P21 ACTIVATED KINASE 2; P21 ACTIVATED KINASE 3; P21 ACTIVATED KINASE 4; P21 ACTIVATED KINASE 5; P21 ACTIVATED KINASE 6; PROTEIN SERINE THREONINE KINASE; PROTEIN SERINE THREONINE KINASE INHIBITOR; PYRAZOLE DERIVATIVE; PYRIDO[2,3 D ]PYRIMIDINE 7 ONE DERIVATIVE; UNCLASSIFIED DRUG; ISOENZYME; ISOPROTEIN; P21 ACTIVATED KINASE; PROTEIN BINDING; PROTEIN KINASE INHIBITOR;

EID: 84928427103     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm501613q     Document Type: Article
Times cited : (101)

References (97)
  • 1
    • 84890946972 scopus 로고    scopus 로고
    • PAK signalling during the development and progression of cancer
    • Radu, M.; Semenova, G.; Kosoff, R.; Chernoff, J. PAK signalling during the development and progression of cancer Nat. Rev. Cancer 2014, 14 (1) 13-25
    • (2014) Nat. Rev. Cancer , vol.14 , Issue.1 , pp. 13-25
    • Radu, M.1    Semenova, G.2    Kosoff, R.3    Chernoff, J.4
  • 3
    • 84879101332 scopus 로고    scopus 로고
    • PAK family kinases: Physiological roles and regulation
    • Zhao, Z. S.; Manser, E. PAK family kinases: physiological roles and regulation Cell. Logistics 2012, 2 (2) 59-68
    • (2012) Cell. Logistics , vol.2 , Issue.2 , pp. 59-68
    • Zhao, Z.S.1    Manser, E.2
  • 4
    • 84876011758 scopus 로고    scopus 로고
    • PAK signaling in cancer
    • Ye, D. Z.; Field, J. PAK signaling in cancer Cell. Logistics 2012, 2 (2) 105-116
    • (2012) Cell. Logistics , vol.2 , Issue.2 , pp. 105-116
    • Ye, D.Z.1    Field, J.2
  • 6
    • 84900544389 scopus 로고    scopus 로고
    • P21-Activated protein kinases and their emerging roles in glucose homeostasis
    • Chiang, Y. T.; Jin, T. p21-Activated protein kinases and their emerging roles in glucose homeostasis Am. J. Physiol.: Endocrinol. Metab. 2014, 306 (7) E707-E722
    • (2014) Am. J. Physiol.: Endocrinol. Metab. , vol.306 , Issue.7 , pp. 707-E722
    • Chiang, Y.T.1    Jin, T.2
  • 7
  • 9
    • 0028879613 scopus 로고
    • Fission yeast pak1+ encodes a protein kinase that interacts with Cdc42p and is involved in the control of cell polarity and mating
    • Ottilie, S.; Miller, P. J.; Johnson, D. I.; Creasy, C. L.; Sells, M. A.; Bagrodia, S.; Forsburg, S. L.; Chernoff, J. Fission yeast pak1+ encodes a protein kinase that interacts with Cdc42p and is involved in the control of cell polarity and mating EMBO J. 1995, 14 (23) 5908-59019
    • (1995) EMBO J. , vol.14 , Issue.23 , pp. 5908-59019
    • Ottilie, S.1    Miller, P.J.2    Johnson, D.I.3    Creasy, C.L.4    Sells, M.A.5    Bagrodia, S.6    Forsburg, S.L.7    Chernoff, J.8
  • 10
    • 84883313334 scopus 로고    scopus 로고
    • Mouse models of PAK function
    • Kelly, M. L.; Chernoff, J. Mouse models of PAK function Cell. Logistics 2012, 2 (2) 84-88
    • (2012) Cell. Logistics , vol.2 , Issue.2 , pp. 84-88
    • Kelly, M.L.1    Chernoff, J.2
  • 11
    • 22244449230 scopus 로고    scopus 로고
    • Abnormal long-lasting synaptic plasticity and cognition in mice lacking the mental retardation gene Pak3
    • Meng, J.; Meng, Y.; Hanna, A.; Janus, C.; Jia, Z. Abnormal long-lasting synaptic plasticity and cognition in mice lacking the mental retardation gene Pak3 J. Neurosci. 2005, 25 (28) 6641-6650
    • (2005) J. Neurosci. , vol.25 , Issue.28 , pp. 6641-6650
    • Meng, J.1    Meng, Y.2    Hanna, A.3    Janus, C.4    Jia, Z.5
  • 12
    • 78751518773 scopus 로고    scopus 로고
    • P21-Activated kinases 1 and 3 control brain size through coordinating neuronal complexity and synaptic properties
    • Huang, W.; Zhou, Z.; Asrar, S.; Henkelman, M.; Xie, W.; Jia, Z. p21-Activated kinases 1 and 3 control brain size through coordinating neuronal complexity and synaptic properties Mol. Cell. Biol. 2011, 31 (3) 388-403
    • (2011) Mol. Cell. Biol. , vol.31 , Issue.3 , pp. 388-403
    • Huang, W.1    Zhou, Z.2    Asrar, S.3    Henkelman, M.4    Xie, W.5    Jia, Z.6
  • 13
    • 68449101709 scopus 로고    scopus 로고
    • Essential role for the Pak4 protein kinase in extraembryonic tissue development and vessel formation
    • Tian, Y.; Lei, L.; Cammarano, M.; Nekrasova, T.; Minden, A. Essential role for the Pak4 protein kinase in extraembryonic tissue development and vessel formation Mech. Dev. 2009, 126 (8-9) 710-720
    • (2009) Mech. Dev. , vol.126 , Issue.89 , pp. 710-720
    • Tian, Y.1    Lei, L.2    Cammarano, M.3    Nekrasova, T.4    Minden, A.5
  • 14
    • 79955011361 scopus 로고    scopus 로고
    • A key role for Pak4 in proliferation and differentiation of neural progenitor cells
    • Tian, Y.; Lei, L.; Minden, A. A key role for Pak4 in proliferation and differentiation of neural progenitor cells Dev. Biol. 2011, 353 (2) 206-216
    • (2011) Dev. Biol. , vol.353 , Issue.2 , pp. 206-216
    • Tian, Y.1    Lei, L.2    Minden, A.3
  • 15
    • 52249101375 scopus 로고    scopus 로고
    • Targeted disruption of the Pak5 and Pak6 genes in mice leads to deficits in learning and locomotion
    • Nekrasova, T.; Jobes, M. L.; Ting, J. H.; Wagner, G. C.; Minden, A. Targeted disruption of the Pak5 and Pak6 genes in mice leads to deficits in learning and locomotion Dev. Biol. 2008, 322 (1) 95-108
    • (2008) Dev. Biol. , vol.322 , Issue.1 , pp. 95-108
    • Nekrasova, T.1    Jobes, M.L.2    Ting, J.H.3    Wagner, G.C.4    Minden, A.5
  • 16
    • 84879252044 scopus 로고    scopus 로고
    • PAK4-6 in cancer and neuronal development
    • Minden, A. PAK4-6 in cancer and neuronal development Cell. Logistics 2012, 2 (2) 95-104
    • (2012) Cell. Logistics , vol.2 , Issue.2 , pp. 95-104
    • Minden, A.1
  • 17
    • 84937126913 scopus 로고    scopus 로고
    • GeneCards. (accessed October, 1).
    • GeneCards. http://www.genecards.org (accessed October, 1, 2014).
    • (2014)
  • 22
    • 54249093368 scopus 로고    scopus 로고
    • MicroRNA-7, a homeobox D10 target, inhibits p21-activated kinase 1 and regulates its functions
    • Reddy, S. D.; Ohshiro, K.; Rayala, S. K.; Kumar, R. MicroRNA-7, a homeobox D10 target, inhibits p21-activated kinase 1 and regulates its functions Cancer Res. 2008, 68 (20) 8195-200
    • (2008) Cancer Res. , vol.68 , Issue.20 , pp. 8195-8200
    • Reddy, S.D.1    Ohshiro, K.2    Rayala, S.K.3    Kumar, R.4
  • 23
    • 33646940460 scopus 로고    scopus 로고
    • Association between Pak1 expression and subcellular localization and tamoxifen resistance in breast cancer patients
    • Holm, C.; Rayala, S.; Jirström, K.; Stål, O.; Kumar, R.; Landberg, G. Association between Pak1 expression and subcellular localization and tamoxifen resistance in breast cancer patients J. Natl. Cancer Inst. 2006, 98 (10) 671-680
    • (2006) J. Natl. Cancer Inst. , vol.98 , Issue.10 , pp. 671-680
    • Holm, C.1    Rayala, S.2    Jirström, K.3    Stål, O.4    Kumar, R.5    Landberg, G.6
  • 24
    • 33646682385 scopus 로고    scopus 로고
    • PAK1 hyperactivation is sufficient for mammary gland tumor formation
    • Wang, R. A.; Zhang, H.; Balasenthil, S.; Medina, D.; Kumar, R. PAK1 hyperactivation is sufficient for mammary gland tumor formation Oncogene 2006, 25 (20) 2931-2936
    • (2006) Oncogene , vol.25 , Issue.20 , pp. 2931-2936
    • Wang, R.A.1    Zhang, H.2    Balasenthil, S.3    Medina, D.4    Kumar, R.5
  • 25
    • 84879101353 scopus 로고    scopus 로고
    • PAK1 kinase links ErbB2 to β-catenin in transformation of breast epithelial cells
    • Arias-Romero, L. E.; Villamar-Cruz, O.; Huang, M.; Hoeflich, K. P.; Chernoff, J. PAK1 kinase links ErbB2 to β-catenin in transformation of breast epithelial cells Cancer Res. 2013, 73, 3671-3682
    • (2013) Cancer Res. , vol.73 , pp. 3671-3682
    • Arias-Romero, L.E.1    Villamar-Cruz, O.2    Huang, M.3    Hoeflich, K.P.4    Chernoff, J.5
  • 31
    • 84937124393 scopus 로고    scopus 로고
    • Data from COSMIC database: (accessed August, 2).
    • Data from COSMIC database: http://cancer.sanger.ac.uk (accessed August, 2, 2014).
    • (2014)
  • 32
    • 0028903247 scopus 로고
    • An essential role for Rac in Ras transformation
    • Qiu, R. G.; Chen, J.; Kirn, D.; McCormick, F.; Symons, M. An essential role for Rac in Ras transformation Nature 1995, 374 (6521) 457-459
    • (1995) Nature , vol.374 , Issue.6521 , pp. 457-459
    • Qiu, R.G.1    Chen, J.2    Kirn, D.3    McCormick, F.4    Symons, M.5
  • 33
    • 84862490151 scopus 로고    scopus 로고
    • Essential role of Cdc42 in Ras-induced transformation revealed by gene targeting
    • Stengel, K. R.; Zheng, Y. Essential role of Cdc42 in Ras-induced transformation revealed by gene targeting PLoS One 2012, 7 (6) e37317
    • (2012) PLoS One , vol.7 , Issue.6 , pp. 37317
    • Stengel, K.R.1    Zheng, Y.2
  • 36
    • 51649119414 scopus 로고    scopus 로고
    • The pak4 protein kinase plays a key role in cell survival and tumorigenesis in athymic mice
    • Liu, Y.; Xiao, H.; Tian, Y.; Nekrasova, T.; Hao, X.; Lee, H. J.; Suh, N.; Yang, C. S.; Minden, A. The pak4 protein kinase plays a key role in cell survival and tumorigenesis in athymic mice Mol. Cancer Res. 2008, 6 (7) 1215-1224
    • (2008) Mol. Cancer Res. , vol.6 , Issue.7 , pp. 1215-1224
    • Liu, Y.1    Xiao, H.2    Tian, Y.3    Nekrasova, T.4    Hao, X.5    Lee, H.J.6    Suh, N.7    Yang, C.S.8    Minden, A.9
  • 38
    • 84883243907 scopus 로고    scopus 로고
    • PAK in Alzheimer disease, Huntington disease and X-linked mental retardation
    • Ma, Q. L.; Yang, F.; Frautschy, S. A.; Cole, G. M. PAK in Alzheimer disease, Huntington disease and X-linked mental retardation Cell. Logistics 2012, 2 (2) 117-125
    • (2012) Cell. Logistics , vol.2 , Issue.2 , pp. 117-125
    • Ma, Q.L.1    Yang, F.2    Frautschy, S.A.3    Cole, G.M.4
  • 40
    • 38449120482 scopus 로고    scopus 로고
    • Signal transduction in Alzheimer disease: P21-activated kinase signaling requires C-terminal cleavage of APP at Asp664
    • Nguyen, T. V.; Galvan, V.; Huang, W.; Banwait, S.; Tang, H.; Zhang, J.; Bredesen, D. E. Signal transduction in Alzheimer disease: p21-activated kinase signaling requires C-terminal cleavage of APP at Asp664 J. Neurochem. 2008, 104 (4) 1065-1080
    • (2008) J. Neurochem. , vol.104 , Issue.4 , pp. 1065-1080
    • Nguyen, T.V.1    Galvan, V.2    Huang, W.3    Banwait, S.4    Tang, H.5    Zhang, J.6    Bredesen, D.E.7
  • 42
    • 77955914539 scopus 로고    scopus 로고
    • Physiological activation of synaptic Rac>PAK (p-21 activated kinase) signaling is defective in a mouse model of fragile X syndrome
    • Chen, L. Y.; Rex, C. S.; Babayan, A. H.; Kramár, E. A.; Lynch, G.; Gall, C. M.; Lauterborn, J. C. Physiological activation of synaptic Rac>PAK (p-21 activated kinase) signaling is defective in a mouse model of fragile X syndrome J. Neurosci. 2010, 30 (33) 10977-10984
    • (2010) J. Neurosci. , vol.30 , Issue.33 , pp. 10977-10984
    • Chen, L.Y.1    Rex, C.S.2    Babayan, A.H.3    Kramár, E.A.4    Lynch, G.5    Gall, C.M.6    Lauterborn, J.C.7
  • 43
    • 77950875820 scopus 로고    scopus 로고
    • A functional requirement for PAK1 binding to the KH(2) domain of the fragile X protein-related FXR1
    • Say, E.; Tay, H. G.; Zhao, Z. S.; Baskaran, Y.; Li, R.; Lim, L.; Manser, E. A functional requirement for PAK1 binding to the KH(2) domain of the fragile X protein-related FXR1 Mol. Cell 2010, 38 (2) 236-249
    • (2010) Mol. Cell , vol.38 , Issue.2 , pp. 236-249
    • Say, E.1    Tay, H.G.2    Zhao, Z.S.3    Baskaran, Y.4    Li, R.5    Lim, L.6    Manser, E.7
  • 44
    • 0035004343 scopus 로고    scopus 로고
    • Pathogenicity island-dependent activation of Rho GTPases Rac1 and Cdc42 in Helicobacter pylori infection
    • Churin, Y.; Kardalinou, E.; Meyer, T. F.; Naumann, M. Pathogenicity island-dependent activation of Rho GTPases Rac1 and Cdc42 in Helicobacter pylori infection Mol. Microbiol. 2001, 40 (4) 815-823
    • (2001) Mol. Microbiol. , vol.40 , Issue.4 , pp. 815-823
    • Churin, Y.1    Kardalinou, E.2    Meyer, T.F.3    Naumann, M.4
  • 45
    • 0033579479 scopus 로고    scopus 로고
    • The N-terminal domain of Pseudomonas aeruginosa exoenzyme S is a GTPase-activating protein for Rho GTPases
    • Goehring, U. M.; Schmidt, G.; Pederson, K. J.; Aktories, K.; Barbieri, J. T. The N-terminal domain of Pseudomonas aeruginosa exoenzyme S is a GTPase-activating protein for Rho GTPases J. Biol. Chem. 1999, 274 (51) 36369-36372
    • (1999) J. Biol. Chem. , vol.274 , Issue.51 , pp. 36369-36372
    • Goehring, U.M.1    Schmidt, G.2    Pederson, K.J.3    Aktories, K.4    Barbieri, J.T.5
  • 46
    • 42949162611 scopus 로고    scopus 로고
    • RNAi screen reveals an Abl kinase-dependent host cell pathway involved in Pseudomonas aeruginosa internalization
    • Pielage, J. F.; Powell, K. R.; Kalman, D.; Engel, J. N. RNAi screen reveals an Abl kinase-dependent host cell pathway involved in Pseudomonas aeruginosa internalization PLoS Pathog. 2008, 4 (3) e1000031
    • (2008) PLoS Pathog. , vol.4 , Issue.3 , pp. 1000031
    • Pielage, J.F.1    Powell, K.R.2    Kalman, D.3    Engel, J.N.4
  • 47
  • 48
    • 0035173735 scopus 로고    scopus 로고
    • HIV-1 Nef associated PAK and PI3-kinases stimulate Akt-independent Bad-phosphorylation to induce anti-apoptotic signals
    • Wolf, D.; Witte, V.; Laffert, B.; Blume, K.; Stromer, E.; Trapp, S.; d'Aloja, P.; Schürmann, A.; Baur, A. S. HIV-1 Nef associated PAK and PI3-kinases stimulate Akt-independent Bad-phosphorylation to induce anti-apoptotic signals Nat. Med. 2001, 7 (11) 1217-1224
    • (2001) Nat. Med. , vol.7 , Issue.11 , pp. 1217-1224
    • Wolf, D.1    Witte, V.2    Laffert, B.3    Blume, K.4    Stromer, E.5    Trapp, S.6    D'Aloja, P.7    Schürmann, A.8    Baur, A.S.9
  • 49
    • 33645960667 scopus 로고    scopus 로고
    • "unPAKing" human immunodeficiency virus (HIV) replication: Using small interfering RNA screening to identify novel cofactors and elucidate the role of group i PAKs in HIV infection
    • Nguyen, D. G.; Wolff, K. C.; Yin, H.; Caldwell, J. S.; Kuhen, K. L. "UnPAKing" human immunodeficiency virus (HIV) replication: using small interfering RNA screening to identify novel cofactors and elucidate the role of group I PAKs in HIV infection J. Virol 2006, 80 (1) 130-137
    • (2006) J. Virol , vol.80 , Issue.1 , pp. 130-137
    • Nguyen, D.G.1    Wolff, K.C.2    Yin, H.3    Caldwell, J.S.4    Kuhen, K.L.5
  • 51
    • 84880140682 scopus 로고    scopus 로고
    • 3D structure analysis of PAKs: A clue to the rational design for affinity reagents and blockers
    • Jha, R. K.; Strauss, C. E. 3D structure analysis of PAKs: a clue to the rational design for affinity reagents and blockers Cell. Logistics 2012, 2 (2) 69-77
    • (2012) Cell. Logistics , vol.2 , Issue.2 , pp. 69-77
    • Jha, R.K.1    Strauss, C.E.2
  • 52
    • 0034604338 scopus 로고    scopus 로고
    • Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switch
    • Lei, M.; Lu, W.; Meng, W.; Parrini, M. C.; Eck, M. J.; Mayer, B. J.; Harrison, S. C. Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switch Cell 2000, 102 (3) 387-397
    • (2000) Cell , vol.102 , Issue.3 , pp. 387-397
    • Lei, M.1    Lu, W.2    Meng, W.3    Parrini, M.C.4    Eck, M.J.5    Mayer, B.J.6    Harrison, S.C.7
  • 53
    • 0036158988 scopus 로고    scopus 로고
    • Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1
    • Parrini, M. C.; Lei, M.; Harrison, S. C.; Mayer, B. J. Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1 Mol. Cell 2002, 9 (1) 73-83
    • (2002) Mol. Cell , vol.9 , Issue.1 , pp. 73-83
    • Parrini, M.C.1    Lei, M.2    Harrison, S.C.3    Mayer, B.J.4
  • 54
    • 84863299837 scopus 로고    scopus 로고
    • Group i and II mammalian PAKs have different modes of activation by Cdc42
    • Baskaran, Y.; Ng, Y. W.; Selamat, W.; Ling, F. T.; Manser, E. Group I and II mammalian PAKs have different modes of activation by Cdc42 EMBO Rep. 2012, 13, 653-659
    • (2012) EMBO Rep. , vol.13 , pp. 653-659
    • Baskaran, Y.1    Ng, Y.W.2    Selamat, W.3    Ling, F.T.4    Manser, E.5
  • 58
    • 0024394417 scopus 로고
    • Staurosporine, K-252 and UCN-01: Potent but nonspecific inhibitors of protein kinases
    • Rüegg, U. T.; Burgess, G. M. Staurosporine, K-252 and UCN-01: potent but nonspecific inhibitors of protein kinases Trends Pharmacol. Sci. 1989, 10 (6) 218-220
    • (1989) Trends Pharmacol. Sci. , vol.10 , Issue.6 , pp. 218-220
    • Rüegg, U.T.1    Burgess, G.M.2
  • 60
    • 56749178863 scopus 로고    scopus 로고
    • Targeting large kinase active site with rigid, bulky octahedral ruthenium complexes
    • Maksimoska, J.; Feng, L.; Harms, K.; Yi, C.; Kissil, J.; Marmorstein, R.; Meggers, E. Targeting large kinase active site with rigid, bulky octahedral ruthenium complexes J. Am. Chem. Soc. 2008, 130 (47) 15764-15765
    • (2008) J. Am. Chem. Soc. , vol.130 , Issue.47 , pp. 15764-15765
    • Maksimoska, J.1    Feng, L.2    Harms, K.3    Yi, C.4    Kissil, J.5    Marmorstein, R.6    Meggers, E.7
  • 68
    • 84937146632 scopus 로고    scopus 로고
    • Abstract A177.
    • Mol. Cancer Ther. 2011, 10 (Suppl. 11), Abstract A177.
    • (2011) Mol. Cancer Ther. , vol.10
  • 70
    • 84937159390 scopus 로고    scopus 로고
    • Genentech, unpublished results.
    • Genentech, unpublished results.
  • 72
    • 84874424655 scopus 로고    scopus 로고
    • Knockdown of PAK4 or PAK1 inhibits the proliferation of mutant KRAS colon cancer cells independently of RAF/MEK/ERK and PI3K/AKT signaling
    • Tabusa, H.; Brooks, T.; Massey, A. J. Knockdown of PAK4 or PAK1 inhibits the proliferation of mutant KRAS colon cancer cells independently of RAF/MEK/ERK and PI3K/AKT signaling Mol. Cancer Res. 2013, 11 (2) 109-121
    • (2013) Mol. Cancer Res. , vol.11 , Issue.2 , pp. 109-121
    • Tabusa, H.1    Brooks, T.2    Massey, A.J.3
  • 76
    • 84908058944 scopus 로고    scopus 로고
    • PAK1: A therapeutic target for cancer treatment
    • Abdel-Magid, A. F. PAK1: A therapeutic target for cancer treatment ACS Med. Chem. Lett. 2013, 4 (5) 431-432
    • (2013) ACS Med. Chem. Lett. , vol.4 , Issue.5 , pp. 431-432
    • Abdel-Magid, A.F.1
  • 77
    • 17044403086 scopus 로고    scopus 로고
    • Ligand efficiency indices as guideposts for drug discovery
    • Abad-Zapatero, C.; Metz, J. T. Ligand efficiency indices as guideposts for drug discovery Drug Discov Today 2005, 10 (7) 464-469
    • (2005) Drug Discov Today , vol.10 , Issue.7 , pp. 464-469
    • Abad-Zapatero, C.1    Metz, J.T.2
  • 80
    • 33745676300 scopus 로고    scopus 로고
    • Toward understanding the structural basis of cyclin-dependent kinase 6 specific inhibition
    • Lu, H.; Schulze-Gahmen, U. Toward understanding the structural basis of cyclin-dependent kinase 6 specific inhibition J. Med. Chem. 2006, 49 (13) 3826-3831
    • (2006) J. Med. Chem. , vol.49 , Issue.13 , pp. 3826-3831
    • Lu, H.1    Schulze-Gahmen, U.2
  • 84
    • 33846899405 scopus 로고    scopus 로고
    • Molecular recognition of protein kinase binding pockets for design of potent and selective kinase inhibitors
    • Liao, J. J. Molecular recognition of protein kinase binding pockets for design of potent and selective kinase inhibitors J. Med. Chem. 2007, 50 (3) 409-424
    • (2007) J. Med. Chem. , vol.50 , Issue.3 , pp. 409-424
    • Liao, J.J.1
  • 89
    • 77950573400 scopus 로고    scopus 로고
    • Through the "gatekeeper door": Exploiting the active kinase conformation
    • Zuccotto, F.; Ardini, E.; Casale, E.; Angiolini, M. Through the "gatekeeper door": exploiting the active kinase conformation J. Med. Chem. 2010, 53 (7) 2681-94
    • (2010) J. Med. Chem. , vol.53 , Issue.7 , pp. 2681-2694
    • Zuccotto, F.1    Ardini, E.2    Casale, E.3    Angiolini, M.4
  • 90
    • 79953247066 scopus 로고    scopus 로고
    • Targeting the DFG-in kinase conformation: A new trend emerging from a patent analysis
    • Angiolini, M. Targeting the DFG-in kinase conformation: a new trend emerging from a patent analysis Future Med. Chem. 2011, 3 (3) 309-337
    • (2011) Future Med. Chem. , vol.3 , Issue.3 , pp. 309-337
    • Angiolini, M.1
  • 92
    • 84879909485 scopus 로고    scopus 로고
    • The Pak4 protein kinase is required for oncogenic transformation of MDA-MB-231 breast cancer cells
    • Wong, L. E.; Chen, N.; Karantza, V.; Minden, A. The Pak4 protein kinase is required for oncogenic transformation of MDA-MB-231 breast cancer cells Oncogenesis 2013, 2, e50
    • (2013) Oncogenesis , vol.2 , pp. 50
    • Wong, L.E.1    Chen, N.2    Karantza, V.3    Minden, A.4
  • 94
    • 84880362714 scopus 로고    scopus 로고
    • Classics in chemical neuroscience: Clozapine
    • Wenthur, C. J.; Lindsley, C. W. Classics in chemical neuroscience: clozapine ACS Chem. Neurosci. 2013, 4 (7) 1018-1025
    • (2013) ACS Chem. Neurosci. , vol.4 , Issue.7 , pp. 1018-1025
    • Wenthur, C.J.1    Lindsley, C.W.2
  • 95
    • 41949100602 scopus 로고    scopus 로고
    • An isoform-selective, small-molecule inhibitor targets the autoregulatory mechanism of p21-activated kinase
    • Deacon, S. W.; Beeser, A.; Fukui, J. A.; Rennefahrt, U. E.; Myers, C.; Chernoff, J.; Peterson, J. R. An isoform-selective, small-molecule inhibitor targets the autoregulatory mechanism of p21-activated kinase Chem. Biol. 2008, 15 (4) 322-331
    • (2008) Chem. Biol. , vol.15 , Issue.4 , pp. 322-331
    • Deacon, S.W.1    Beeser, A.2    Fukui, J.A.3    Rennefahrt, U.E.4    Myers, C.5    Chernoff, J.6    Peterson, J.R.7
  • 96
    • 70349484472 scopus 로고    scopus 로고
    • An allosteric kinase inhibitor binds the p21-activated kinase autoregulatory domain covalently
    • Viaud, J.; Peterson, J. R. An allosteric kinase inhibitor binds the p21-activated kinase autoregulatory domain covalently Mol. Cancer Ther 2009, 8 (9) 2559-2565
    • (2009) Mol. Cancer Ther , vol.8 , Issue.9 , pp. 2559-2565
    • Viaud, J.1    Peterson, J.R.2


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