메뉴 건너뛰기




Volumn 6, Issue 5, 2014, Pages 541-561

Novel approaches for targeting kinases: Allosteric inhibition, allosteric activation and pseudokinases

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN KINASE; PROTEIN KINASE INHIBITOR;

EID: 84896920166     PISSN: 17568919     EISSN: 17568927     Source Type: Journal    
DOI: 10.4155/fmc.13.216     Document Type: Review
Times cited : (84)

References (174)
  • 6
    • 0036682301 scopus 로고    scopus 로고
    • Crystal structures of the kinase domain of c-Abl in complex with the small molecule inhibitors PD173955 and imatinib (STI-571)
    • Nagar B, Bornmann WG, Pellicena P et al. Crystal structures of the kinase domain of c-Abl in complex with the small molecule inhibitors PD173955 and imatinib (STI-571). Cancer Res. 62(15), 4236-4243 (2002).
    • (2002) Cancer Res , vol.62 , Issue.15 , pp. 4236-4243
    • Nagar, B.1    Bornmann, W.G.2    Pellicena, P.3
  • 7
    • 13844251975 scopus 로고    scopus 로고
    • Characterization of AMN107, a selective inhibitor of native and mutant Bcr-Abl
    • Weisberg E, Manley PW, Breitenstein W et al. Characterization of AMN107, a selective inhibitor of native and mutant Bcr-Abl. Cancer Cell 7(2), 129-141 (2005).
    • (2005) Cancer Cell , vol.7 , Issue.2 , pp. 129-141
    • Weisberg, E.1    Manley, P.W.2    Breitenstein, W.3
  • 8
    • 0036769168 scopus 로고    scopus 로고
    • Imatinib: A selective tyrosine kinase inhibitor
    • Manley PW, Cowan-Jacob SW, Buchdunger E et al. Imatinib: a selective tyrosine kinase inhibitor. Eur. J. Cancer 38(Suppl. 5), S19-S27 (2002).
    • (2002) Eur. J. Cancer , vol.38 , Issue.SUPPL. 5
    • Manley, P.W.1    Cowan-Jacob, S.W.2    Buchdunger, E.3
  • 9
    • 80755125575 scopus 로고    scopus 로고
    • Comprehensive analysis of kinase inhibitor selectivity
    • Davis MI, Hunt JP, Herrgard S et al. Comprehensive analysis of kinase inhibitor selectivity. Nat. Biotechnol. 29(11), 1046-1051 (2011).
    • (2011) Nat. Biotechnol. , vol.29 , Issue.11 , pp. 1046-1051
    • Davis, M.I.1    Hunt, J.P.2    Herrgard, S.3
  • 10
    • 33749238553 scopus 로고    scopus 로고
    • Discovery and development of sorafenib: A multikinase inhibitor for treating cancer
    • Wilhelm S, Carter C, Lynch M et al. Discovery and development of sorafenib: a multikinase inhibitor for treating cancer. Nature Rev. Drug Discov. 5(10), 835-844 (2006).
    • (2006) Nature Rev. Drug Discov. , vol.5 , Issue.10 , pp. 835-844
    • Wilhelm, S.1    Carter, C.2    Lynch, M.3
  • 11
    • 84880307149 scopus 로고    scopus 로고
    • Chaperones as thermodynamic sensors of drug-target interactions reveal kinase inhibitor specificities in living cells
    • Taipale M, Krykbaeva I, Whitesell L et al. Chaperones as thermodynamic sensors of drug-target interactions reveal kinase inhibitor specificities in living cells. Nat. Biotechnol. 31, 630-637 (2013).
    • (2013) Nat. Biotechnol. , vol.31 , pp. 630-637
    • Taipale, M.1    Krykbaeva, I.2    Whitesell, L.3
  • 12
    • 34147108049 scopus 로고    scopus 로고
    • Structurebased design, synthesis, and biological evaluation of potent and selective macrocyclic checkpoint kinase 1 inhibitors
    • Tao ZF, Wang L, Stewart KD et al. Structurebased design, synthesis, and biological evaluation of potent and selective macrocyclic checkpoint kinase 1 inhibitors. J. Med. Chem. 50(7), 1514-1527 (2007).
    • (2007) J. Med. Chem. , vol.50 , Issue.7 , pp. 1514-1527
    • Tao, Z.F.1    Wang, L.2    Stewart, K.D.3
  • 13
    • 84874301754 scopus 로고    scopus 로고
    • Developing irreversible inhibitors of the protein kinase cysteinome
    • Liu Q, Sabnis Y, Zhao Z et al. Developing irreversible inhibitors of the protein kinase cysteinome. Chem. Biol. 20(2), 146-159 (2013).
    • (2013) Chem. Biol. , vol.20 , Issue.2 , pp. 146-159
    • Liu, Q.1    Sabnis, Y.2    Zhao, Z.3
  • 14
    • 34249789860 scopus 로고    scopus 로고
    • Exploring chemical space with organometallics: Ruthenium complexes as protein kinase inhibitors
    • Meggers E, Atilla-Gokcumen GE, Bregman H et al. Exploring chemical space with organometallics: ruthenium complexes as protein kinase inhibitors. SYNLETT 8, 1177-1189 (2007).
    • (2007) SYNLETT , vol.8 , pp. 1177-1189
    • Meggers, E.1    Atilla-Gokcumen, G.E.2    Bregman, H.3
  • 15
    • 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. 53(7), 2681-2694 (2010).
    • (2010) J. Med. Chem. , vol.53 , Issue.7 , pp. 2681-2694
    • Zuccotto, F.1    Ardini, E.2    Casale, E.3    Angiolini, M.4
  • 16
    • 84858631510 scopus 로고    scopus 로고
    • Targeting diverse signaling interaction sites allows the rapid generation of bivalent kinase inhibitors
    • Hill ZB, Perera BG, Andrews SS, Maly DJ. Targeting diverse signaling interaction sites allows the rapid generation of bivalent kinase inhibitors. ACS Chem. Biol. 7(3), 487-495 (2012).
    • (2012) ACS Chem. Biol. , vol.7 , Issue.3 , pp. 487-495
    • Hill, Z.B.1    Perera, B.G.2    Andrews, S.S.3    Maly, D.J.4
  • 17
    • 84874658250 scopus 로고    scopus 로고
    • Structure-based discovery of cellular-active allosteric inhibitors of FAK
    • Tomita N, Hayashi Y, Suzuki S et al. Structure-based discovery of cellular-active allosteric inhibitors of FAK. Bioorg. Med. Chem. Lett. 23(6), 1779-1785 (2013).
    • (2013) Bioorg. Med. Chem. Lett. , vol.23 , Issue.6 , pp. 1779-1785
    • Tomita, N.1    Hayashi, Y.2    Suzuki, S.3
  • 19
    • 84863634917 scopus 로고    scopus 로고
    • Fluorophore labeled kinase detects ligands that bind within the MAPK insert of p38alpha kinase
    • Getlik M, Simard JR, Termathe M et al. Fluorophore labeled kinase detects ligands that bind within the MAPK insert of p38alpha kinase. PLoS ONE 7(7), e39713 (2012).
    • (2012) PLoS ONE , vol.7 , Issue.7
    • Getlik, M.1    Simard, J.R.2    Termathe, M.3
  • 20
    • 84860851057 scopus 로고    scopus 로고
    • A guide to picking the most selective kinase inhibitor tool compounds for pharmacological validation of drug targets
    • Uitdehaag JC, Verkaar F, Alwan H, De Man J, Buijsman RC, Zaman GJ. A guide to picking the most selective kinase inhibitor tool compounds for pharmacological validation of drug targets. Br. J. Pharmacol. 166(3), 858-876 (2012).
    • (2012) Br. J. Pharmacol. , vol.166 , Issue.3 , pp. 858-876
    • Uitdehaag, J.C.1    Verkaar, F.2    Alwan, H.3    De Man, J.4    Buijsman, R.C.5    Zaman, G.J.6
  • 21
    • 84872511666 scopus 로고    scopus 로고
    • Strategies for the selective regulation of kinases with allosteric modulators: Exploiting exclusive structural features
    • Fang ZZ, Grutter C, Rauh D. Strategies for the selective regulation of kinases with allosteric modulators: exploiting exclusive structural features. ACS Chem. Biol. 8(1), 58-70 (2013).
    • (2013) ACS Chem. Biol. , vol.8 , Issue.1 , pp. 58-70
    • Fang, Z.Z.1    Grutter, C.2    Rauh, D.3
  • 22
    • 33644889108 scopus 로고    scopus 로고
    • Allosteric inhibitors of Bcr-abl-dependent cell proliferation
    • Adrian FJ, Ding Q, Sim T et al. Allosteric inhibitors of Bcr-abl-dependent cell proliferation. Nat. Chem. Biol. 2(2), 95-102 (2006).
    • (2006) Nat. Chem. Biol. , vol.2 , Issue.2 , pp. 95-102
    • Adrian, F.J.1    Ding, Q.2    Sim, T.3
  • 23
    • 75749146563 scopus 로고    scopus 로고
    • Targeting Bcr-Abl by combining allosteric with ATP-binding-site inhibitors
    • Zhang J, Adrian FJ, Jahnke W et al. Targeting Bcr-Abl by combining allosteric with ATP-binding-site inhibitors. Nature 463(7280), 501-506 (2010).
    • (2010) Nature , vol.463 , Issue.7280 , pp. 501-506
    • Zhang, J.1    Adrian, F.J.2    Jahnke, W.3
  • 24
    • 84874938176 scopus 로고    scopus 로고
    • Discovery and characterization of novel allosteric FAK inhibitors
    • Iwatani M, Iwata H, Okabe A et al. Discovery and characterization of novel allosteric FAK inhibitors. Eur. J. Med. Chem. 61, 49-60 (2013).
    • (2013) Eur. J. Med. Chem. , vol.61 , pp. 49-60
    • Iwatani, M.1    Iwata, H.2    Okabe, A.3
  • 25
    • 70350074904 scopus 로고    scopus 로고
    • Characterization of the CHK1 allosteric inhibitor binding site
    • Vanderpool D, Johnson TO, Ping C et al. Characterization of the CHK1 allosteric inhibitor binding site. Biochemistry 48(41), 9823-9830 (2009).
    • (2009) Biochemistry , vol.48 , Issue.41 , pp. 9823-9830
    • Vanderpool, D.1    Johnson, T.O.2    Ping, C.3
  • 26
    • 70349484472 scopus 로고    scopus 로고
    • An allosteric kinase inhibitor binds the p21-activated kinase autoregulatory domain covalently
    • Viaud J, Peterson JR. An allosteric kinase inhibitor binds the p21-activated kinase autoregulatory domain covalently. Mol. Cancer Ther. 8(9), 2559-2565 (2009).
    • (2009) Mol. Cancer Ther. , vol.8 , Issue.9 , pp. 2559-2565
    • Viaud, J.1    Peterson, J.R.2
  • 27
    • 41949100602 scopus 로고    scopus 로고
    • An isoform-selective, small-molecule inhibitor targets the autoregulatory mechanism of p21-activated kinase
    • Deacon SW, Beeser A, Fukui JA et al. An isoform-selective, small-molecule inhibitor targets the autoregulatory mechanism of p21-activated kinase. Chem. Biol. 15(4), 322-331 (2008).
    • (2008) Chem. Biol. , vol.15 , Issue.4 , pp. 322-331
    • Deacon, S.W.1    Beeser, A.2    Fukui, J.A.3
  • 28
    • 19944431003 scopus 로고    scopus 로고
    • Allosteric Akt (PKB) inhibitors: Discovery and SAR of isozyme selective inhibitors
    • Lindsley CW, Zhao Z, Leister WH et al. Allosteric Akt (PKB) inhibitors: discovery and SAR of isozyme selective inhibitors. Bioorg. Med. Chem. Lett. 15(3), 761-764 (2005).
    • (2005) Bioorg. Med. Chem. Lett. , vol.15 , Issue.3 , pp. 761-764
    • Lindsley, C.W.1    Zhao, Z.2    Leister, W.H.3
  • 29
    • 84896953965 scopus 로고    scopus 로고
    • Discovery of novel and highly selective allosteric inhibitors of PAK1
    • IN, USA 8-12 September
    • Lindvall M, Karpov A, Bellamacina C et al. Discovery of novel and highly selective allosteric inhibitors of PAK1. Presented at: 246th ACS National Meeting and Exposition. IN, USA, 8-12 September 2013.
    • (2013) 246th ACS National Meeting and Exposition
    • Lindvall, M.1    Karpov, A.2    Bellamacina, C.3
  • 30
    • 84859743432 scopus 로고    scopus 로고
    • A back-tofront fragment-based drug design search strategy targeting the DFG-out pocket of protein tyrosine kinases
    • Iwata H, Oki H, Okada K et al. A back-tofront fragment-based drug design search strategy targeting the DFG-out pocket of protein tyrosine kinases. ACS Med. Chem. Lett. 3, 342-346 (2012).
    • (2012) ACS Med. Chem. Lett. , vol.3 , pp. 342-346
    • Iwata, H.1    Oki, H.2    Okada, K.3
  • 31
    • 18344395134 scopus 로고    scopus 로고
    • Inhibition of p38 MAP kinase by utilizing a novel allosteric binding site
    • Pargellis C, Tong L, Churchill L et al. Inhibition of p38 MAP kinase by utilizing a novel allosteric binding site. Nat. Struct. Biol. 9(4), 268-272 (2002).
    • (2002) Nat. Struct. Biol. , vol.9 , Issue.4 , pp. 268-272
    • Pargellis, C.1    Tong, L.2    Churchill, L.3
  • 32
    • 15744380263 scopus 로고    scopus 로고
    • Structures of human MAP kinase kinase 1 (MEK1) and MEK2 describe novel noncompetitive kinase inhibition
    • Ohren JF, Chen H, Pavlovsky A et al. Structures of human MAP kinase kinase 1 (MEK1) and MEK2 describe novel noncompetitive kinase inhibition. Nat. Struct. Mol. Biol. 11(12), 1192-1197 (2004).
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , Issue.12 , pp. 1192-1197
    • Ohren, J.F.1    Chen, H.2    Pavlovsky, A.3
  • 33
    • 67349094019 scopus 로고    scopus 로고
    • A new screening assay for allosteric inhibitors of cSrc
    • Simard JR, Kluter S, Grutter C et al. A new screening assay for allosteric inhibitors of cSrc. Nat. Chem. Biol. 5(6), 394-396 (2009).
    • (2009) Nat. Chem. Biol. , vol.5 , Issue.6 , pp. 394-396
    • Simard, J.R.1    Kluter, S.2    Grutter, C.3
  • 34
    • 84861854598 scopus 로고    scopus 로고
    • Direct binding assay for the detection of type IV allosteric inhibitors of Abl
    • Schneider R, Becker C, Simard JR et al. Direct binding assay for the detection of type IV allosteric inhibitors of Abl. J. Am. Chem. Soc. 134(22), 9138-9141 (2012).
    • (2012) J. Am. Chem. Soc. , vol.134 , Issue.22 , pp. 9138-9141
    • Schneider, R.1    Becker, C.2    Simard, J.R.3
  • 35
    • 79957497448 scopus 로고    scopus 로고
    • Discovery of a potential allosteric ligand binding site in CDK2
    • Betzi S, Alam R, Martin M et al. Discovery of a potential allosteric ligand binding site in CDK2. ACS Chem. Biol. 6(5), 492-501 (2011).
    • (2011) ACS Chem. Biol. , vol.6 , Issue.5 , pp. 492-501
    • Betzi, S.1    Alam, R.2    Martin, M.3
  • 37
    • 77952575338 scopus 로고    scopus 로고
    • Binding or bending: Distinction of allosteric Abl kinase agonists from antagonists by an NMR-based conformational assay
    • Jahnke W, Grotzfeld RM, Pelle X et al. Binding or bending: distinction of allosteric Abl kinase agonists from antagonists by an NMR-based conformational assay. J. Am. Chem. Soc. 132(20), 7043-7048 (2010).
    • (2010) J. Am. Chem. Soc. , vol.132 , Issue.20 , pp. 7043-7048
    • Jahnke, W.1    Grotzfeld, R.M.2    Pelle, X.3
  • 38
    • 9944263528 scopus 로고    scopus 로고
    • Searching for new allosteric sites in enzymes
    • Hardy JA, Wells JA. Searching for new allosteric sites in enzymes. Curr. Opin. Struct. Biol. 14(6), 706-715 (2004).
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , Issue.6 , pp. 706-715
    • Hardy, J.A.1    Wells, J.A.2
  • 40
    • 0034732235 scopus 로고    scopus 로고
    • Peptide exosite inhibitors of factor VIIa as anticoagulants
    • Dennis MS, Eigenbrot C, Skelton NJ et al. Peptide exosite inhibitors of factor VIIa as anticoagulants. Nature 404, 465-470 (2000).
    • (2000) Nature , vol.404 , pp. 465-470
    • Dennis, M.S.1    Eigenbrot, C.2    Skelton, N.J.3
  • 41
    • 84856298523 scopus 로고    scopus 로고
    • Biosensor-based approach to the identification of protein kinase ligands with dual-site modes of action
    • Navratilova I, Macdonald G, Robinson C et al. Biosensor-based approach to the identification of protein kinase ligands with dual-site modes of action. J. Biomol. Screen. 17(2), 183-193 (2012).
    • (2012) J. Biomol. Screen. , vol.17 , Issue.2 , pp. 183-193
    • Navratilova, I.1    Macdonald, G.2    Robinson, C.3
  • 42
    • 79955617610 scopus 로고    scopus 로고
    • Discovery and characterization of non-ATP site inhibitors of the mitogen activated protein (MAP) kinases
    • Comess KM, Sun C, Abad-Zapatero C et al. Discovery and characterization of non-ATP site inhibitors of the mitogen activated protein (MAP) kinases. ACS Chem. Biol. 6(3), 234-244 (2011).
    • (2011) ACS Chem. Biol. , vol.6 , Issue.3 , pp. 234-244
    • Comess, K.M.1    Sun, C.2    Abad-Zapatero, C.3
  • 43
    • 84862282122 scopus 로고    scopus 로고
    • Discovery and optimization of a series of 3-(3-phenyl-3H-imidazo[4,5-b] pyridin-2-yl) pyridin-2-amines: Orally bioavailable, selective, and potent ATP-independent Akt inhibitors
    • Ashwell MA, Lapierre JM, Brassard C et al. Discovery and optimization of a series of 3-(3-phenyl-3H-imidazo[4,5-b]pyridin-2-yl) pyridin-2-amines: orally bioavailable, selective, and potent ATP-independent Akt inhibitors. J. Med. Chem. 55(11), 5291-5310 (2012).
    • (2012) J. Med. Chem. , vol.55 , Issue.11 , pp. 5291-5310
    • Ma, A.1    Lapierre, J.M.2    Brassard, C.3
  • 44
    • 4644289313 scopus 로고    scopus 로고
    • A unique structure for epidermal growth factor receptor bound to GW572016 (Lapatinib): Relationships among protein conformation, inhibitor off-rate, and receptor activity in tumor cells
    • Wood ER, Truesdale AT, McDonald OB et al. A unique structure for epidermal growth factor receptor bound to GW572016 (Lapatinib): relationships among protein conformation, inhibitor off-rate, and receptor activity in tumor cells. Cancer Res. 64(18), 6652-6659 (2004).
    • (2004) Cancer Res. , vol.64 , Issue.18 , pp. 6652-6659
    • Wood, E.R.1    Truesdale, A.T.2    McDonald, O.B.3
  • 45
    • 58849093668 scopus 로고    scopus 로고
    • Identification of allosteric PIF-pocket ligands for PDK1 using NMR-based fragment screening and 1H-15N TROSY experiments
    • Stockman BJ, Kothe M, Kohls D et al. Identification of allosteric PIF-pocket ligands for PDK1 using NMR-based fragment screening and 1H-15N TROSY experiments. Chem. Biol. Drug Design 73(2), 179-188 (2009).
    • (2009) Chem. Biol. Drug Design , vol.73 , Issue.2 , pp. 179-188
    • Stockman, B.J.1    Kothe, M.2    Kohls, D.3
  • 46
    • 84870401411 scopus 로고    scopus 로고
    • Fragment based drug design: From experimental to computational approaches
    • Kumar A, Voet A, Zhang KYJ. Fragment based drug design: from experimental to computational approaches. Curr. Med. Chem. 19, 5128-5147 (2012).
    • (2012) Curr. Med. Chem. , vol.19 , pp. 5128-5147
    • Kumar, A.1    Voet, A.2    Kyj, Z.3
  • 48
    • 24744449809 scopus 로고    scopus 로고
    • Strategies for the NMR-based identification and optimization of allosteric protein kinase inhibitors
    • Jahnke W, Blommers MJJ, Fernandez C, Zwingelstein C, Amstutz R. Strategies for the NMR-based identification and optimization of allosteric protein kinase inhibitors. ChemBioChem 6, 1607-1610 (2005).
    • (2005) ChemBioChem , vol.6 , pp. 1607-1610
    • Jahnke, W.1    Mjj, B.2    Fernandez, C.3    Zwingelstein, C.4    Amstutz, R.5
  • 49
    • 20444412386 scopus 로고    scopus 로고
    • Screening of protein kinases by ATP-STD NMR spectroscopy
    • McCoy MA, Senior MM, Wyss DF. Screening of protein kinases by ATP-STD NMR spectroscopy. J. Am. Chem. Soc. 127(22), 7978-7979 (2005).
    • (2005) J. Am. Chem. Soc. , vol.127 , Issue.22 , pp. 7978-7979
    • Ma, M.1    Senior, M.M.2    Wyss, D.F.3
  • 50
    • 45749113037 scopus 로고    scopus 로고
    • Development of paramagnetic probes for molecular recognition studies in protein kinases
    • Vazquez J, De SK, Chen L-H et al. Development of paramagnetic probes for molecular recognition studies in protein kinases. J. Med. Chem. 51, 3460-3465 (2008).
    • (2008) J. Med. Chem. , vol.51 , pp. 3460-3465
    • Vazquez, J.1    De Sk Chen, L.-H.2
  • 51
    • 77249174321 scopus 로고    scopus 로고
    • Novel synthesis and structural characterization of a high-affinity paramagnetic kinase probe for the identification of non-ATP site binders by nuclear magnetic resonance
    • Moy FJ, Lee A, Gavrin LK et al. Novel synthesis and structural characterization of a high-affinity paramagnetic kinase probe for the identification of non-ATP site binders by nuclear magnetic resonance. J. Med. Chem. 53, 1238-1249 (2010).
    • (2010) J. Med. Chem. , vol.53 , pp. 1238-1249
    • Moy, F.J.1    Lee, A.2    Gavrin, L.K.3
  • 52
    • 55949100580 scopus 로고    scopus 로고
    • Identification of a new JNK inhibitor targeting the JNK-JIP interaction site
    • Stebbins JL, De SK, Machleidt T et al. Identification of a new JNK inhibitor targeting the JNK-JIP interaction site. Proc. Natl Acad. Sci. USA. 105, 16809-16813 (2008).
    • (2008) Proc. Natl Acad. Sci. USA. , vol.105 , pp. 16809-16813
    • Stebbins, J.L.1    De Sk Machleidt, T.2
  • 53
    • 33751583820 scopus 로고    scopus 로고
    • Allosteric activation of the protein kinase PDK1 with low molecular weight compounds
    • Engel M, Hindie V, Lopez-Garcia LA et al. Allosteric activation of the protein kinase PDK1 with low molecular weight compounds. EMBO J. 25(23), 5469-5480 (2006).
    • (2006) EMBO J. , vol.25 , Issue.23 , pp. 5469-5480
    • Engel, M.1    Hindie, V.2    Lopez-Garcia, L.A.3
  • 54
    • 77954316554 scopus 로고    scopus 로고
    • Design and synthesis of benzoazepin-2-one analogs as allosteric binders targeting the PIF pocket of PDK1
    • Wei L, Gao X, Warne R et al. Design and synthesis of benzoazepin-2-one analogs as allosteric binders targeting the PIF pocket of PDK1. Bioorg. Med. Chem. Lett. 20(13), 3897-3902 (2010).
    • (2010) Bioorg. Med. Chem. Lett. , vol.20 , Issue.13 , pp. 3897-3902
    • Wei, L.1    Gao, X.2    Warne, R.3
  • 55
    • 84870011168 scopus 로고    scopus 로고
    • 2-(3-oxo-1,3-diphenylpropyl)malonic acids as potent allosteric ligands of the PIF pocket of phosphoinositide-dependent kinase-1: Development and prodrug concept
    • Wilhelm A, Lopez-Garcia LA, Busschots K et al. 2-(3-oxo-1,3- diphenylpropyl)malonic acids as potent allosteric ligands of the PIF pocket of phosphoinositide-dependent kinase-1: development and prodrug concept. J. Med. Chem. 55, 9817-9830 (2012).
    • (2012) J. Med. Chem. , vol.55 , pp. 9817-9830
    • Wilhelm, A.1    Lopez-Garcia, L.A.2    Busschots, K.3
  • 56
    • 80053931055 scopus 로고    scopus 로고
    • 4-benzimidazolyl-3-phenylbutanoic acids as novel PIF-pocket-targeting allosteric inhibitors of protein kinase PKCzeta
    • Frohner W, Lopez-Garcia LA, Neimanis S et al. 4-benzimidazolyl-3- phenylbutanoic acids as novel PIF-pocket-targeting allosteric inhibitors of protein kinase PKCzeta. J. Med. Chem. 54(19), 6714-6723 (2011).
    • (2011) J. Med. Chem. , vol.54 , Issue.19 , pp. 6714-6723
    • Frohner, W.1    Lopez-Garcia, L.A.2    Neimanis, S.3
  • 57
    • 80053904856 scopus 로고    scopus 로고
    • Allosteric regulation of protein kinase PKCzeta by the N-terminal C1 domain and small compounds to the PIF-pocket
    • Lopez-Garcia LA, Schulze JO, Frohner W et al. Allosteric regulation of protein kinase PKCzeta by the N-terminal C1 domain and small compounds to the PIF-pocket. Chem. Biol. 18(11), 1463-1473 (2011).
    • (2011) Chem. Biol. , vol.18 , Issue.11 , pp. 1463-1473
    • Lopez-Garcia, L.A.1    Schulze, J.O.2    Frohner, W.3
  • 58
    • 0344626926 scopus 로고    scopus 로고
    • Structural basis for the autoinhibition of c-Abl tyrosine kinase
    • Nagar B, Hantschel O, Young MA et al. Structural basis for the autoinhibition of c-Abl tyrosine kinase. Cell 112(6), 859-871 (2003).
    • (2003) Cell , vol.112 , Issue.6 , pp. 859-871
    • Nagar, B.1    Hantschel, O.2    Ma, Y.3
  • 59
    • 20444399897 scopus 로고    scopus 로고
    • The crystal structure of a c-Src complex in an active conformation suggests possible steps in c-Src activation
    • Cowan-Jacob SW, Fendrich G, Manley PW et al. The crystal structure of a c-Src complex in an active conformation suggests possible steps in c-Src activation. Structure 13(6), 861-871 (2005).
    • (2005) Structure , vol.13 , Issue.6 , pp. 861-871
    • Cowan-Jacob, S.W.1    Fendrich, G.2    Manley, P.W.3
  • 61
    • 84055217601 scopus 로고    scopus 로고
    • Exploring the binding sites of glycogen synthase kinase 3. Identification and characterization of allosteric modulation cavities
    • Palomo V, Soteras I, Perez DI et al. Exploring the binding sites of glycogen synthase kinase 3. Identification and characterization of allosteric modulation cavities. J. Med. Chem. 54(24), 8461-8470 (2011).
    • (2011) J. Med. Chem. , vol.54 , Issue.24 , pp. 8461-8470
    • Palomo, V.1    Soteras, I.2    Perez, D.I.3
  • 62
    • 84891778690 scopus 로고    scopus 로고
    • ASD v2.0: Updated content and novel features focusing on allosteric regulation
    • Huang Z, Mou L, Shen Q et al. ASD v2.0: updated content and novel features focusing on allosteric regulation. Nucleic acids Res. 42(1), D510-D516 (2013).
    • (2013) Nucleic Acids Res. , vol.42 , Issue.1
    • Huang, Z.1    Mou, L.2    Shen, Q.3
  • 63
    • 84883468084 scopus 로고    scopus 로고
    • Allosite: A method for predicting allosteric sites
    • Huang W, Lu S, Huang Z et al. Allosite: a method for predicting allosteric sites. Bioinformatics 29(18), 2357-2359 (2013).
    • (2013) Bioinformatics , vol.29 , Issue.18 , pp. 2357-2359
    • Huang, W.1    Lu, S.2    Huang, Z.3
  • 64
    • 84867744642 scopus 로고    scopus 로고
    • Exploiting protein flexibility to predict the location of allosteric sites
    • Panjkovich A, Daura X. Exploiting protein flexibility to predict the location of allosteric sites. BMC Bioinform. 13, 273 (2012).
    • (2012) BMC Bioinform. , vol.13 , pp. 273
    • Panjkovich, A.1    Daura, X.2
  • 65
    • 58849102947 scopus 로고    scopus 로고
    • Allosteric inhibitors of Akt1 and Akt2: Discovery of [1, 2,4] triazolo[3,4-f ][1,6]naphthyridines with potent and balanced activity
    • Li Y, Liang J, Siu T et al. Allosteric inhibitors of Akt1 and Akt2: discovery of [1,2,4] triazolo[3,4-f ][1,6]naphthyridines with potent and balanced activity. Bioorg. Med. Chem. Lett. 19(3), 834-836 (2009).
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , Issue.3 , pp. 834-836
    • Li, Y.1    Liang, J.2    Siu, T.3
  • 66
    • 37549000580 scopus 로고    scopus 로고
    • Development of potent, allosteric dual Akt1 and Akt2 inhibitors with improved physical properties and cell activity
    • Zhao Z, Robinson RG, Barnett SF et al. Development of potent, allosteric dual Akt1 and Akt2 inhibitors with improved physical properties and cell activity. Bioorg. Med. Chem. Lett. 18(1), 49-53 (2008).
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , Issue.1 , pp. 49-53
    • Zhao, Z.1    Robinson, R.G.2    Barnett, S.F.3
  • 67
    • 59649092904 scopus 로고    scopus 로고
    • Development of thioquinazolinones, allosteric Chk1 kinase inhibitors
    • Converso A, Hartingh T, Garbaccio RM et al. Development of thioquinazolinones, allosteric Chk1 kinase inhibitors. Bioorg. Med. Chem. Lett. 19(4), 1240-1244 (2009).
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , Issue.4 , pp. 1240-1244
    • Converso, A.1    Hartingh, T.2    Garbaccio, R.M.3
  • 68
    • 33750826362 scopus 로고    scopus 로고
    • Characterization of ATP-independent ERK inhibitors identified through in silico analysis of the active ERK2 structure
    • Chen F, Hancock CN, Macias AT et al. Characterization of ATP-independent ERK inhibitors identified through in silico analysis of the active ERK2 structure. Bioorg. Med. Chem. Lett. 16(24), 6281-6287 (2006).
    • (2006) Bioorg. Med. Chem. Lett. , vol.16 , Issue.24 , pp. 6281-6287
    • Chen, F.1    Hancock, C.N.2    Macias, A.T.3
  • 69
    • 84884127318 scopus 로고    scopus 로고
    • Mechanism of MEK inhibition determines efficacy in mutant KRAS- versus BRAFdriven cancers
    • Hatzivassiliou G, Haling JR, Chen H et al. Mechanism of MEK inhibition determines efficacy in mutant KRAS- versus BRAFdriven cancers. Nature 501(7466), 232-236 (2013).
    • (2013) Nature , vol.501 , Issue.7466 , pp. 232-236
    • Hatzivassiliou, G.1    Haling, J.R.2    Chen, H.3
  • 70
    • 83255162603 scopus 로고    scopus 로고
    • First-in-man clinical trial of the oral pan-AKT inhibitor MK-2206 in patients with advanced solid tumors
    • Yap TA, Yan L, Patnaik A et al. First-in-man clinical trial of the oral pan-AKT inhibitor MK-2206 in patients with advanced solid tumors. J. Clin. Oncol. 29 , 4688-4695 (2011).
    • (2011) J. Clin. Oncol. , vol.29 , pp. 4688-4695
    • Yap, T.A.1    Yan, L.2    Patnaik, A.3
  • 71
    • 67651083303 scopus 로고    scopus 로고
    • P38alpha MAP kinase C-terminal domain binding pocket characterized by crystallographic and computational analyses
    • Perry JJ, Harris RM, Moiani D, Olson AJ, Tainer JA. p38alpha MAP kinase C-terminal domain binding pocket characterized by crystallographic and computational analyses. J. Mol. Biol. 391(1), 1-11 (2009).
    • (2009) J. Mol. Biol. , vol.391 , Issue.1 , pp. 1-11
    • Perry, J.J.1    Harris, R.M.2    Moiani, D.3    Olson, A.J.4    Tainer, J.A.5
  • 72
    • 84858227014 scopus 로고    scopus 로고
    • RAS/RAF/ MEK inhibitors in oncology
    • Rusconi P, Caiola E, Broggini M. RAS/RAF/ MEK inhibitors in oncology. Curr. Med. Chem. 19(8), 1164-1176 (2012).
    • (2012) Curr. Med. Chem. , vol.19 , Issue.8 , pp. 1164-1176
    • Rusconi, P.1    Caiola, E.2    Broggini, M.3
  • 73
    • 70149122987 scopus 로고    scopus 로고
    • Direct small-molecule kinase activation: Novel approaches for a new era of drug discovery
    • Simpson GL, Hughes JA, Washio Y, Bertrand SM. Direct small-molecule kinase activation: Novel approaches for a new era of drug discovery. Curr. Opin. Drug Discov. Devel. 12(5), 585-596 (2009).
    • (2009) Curr. Opin. Drug Discov. Devel. , vol.12 , Issue.5 , pp. 585-596
    • Simpson, G.L.1    Hughes, J.A.2    Washio, Y.3    Bertrand, S.M.4
  • 74
    • 79953658137 scopus 로고    scopus 로고
    • Drug discovery and the human kinome: Recent trends
    • Eglen R, Reisine T. Drug discovery and the human kinome: recent trends. Pharmacol. Ther. 130(2), 144-156 (2011).
    • (2011) Pharmacol. Ther. , vol.130 , Issue.2 , pp. 144-156
    • Eglen, R.1    Reisine, T.2
  • 75
    • 77958509195 scopus 로고    scopus 로고
    • Akt inhibitors in clinical development for the treatment of cancer
    • Pal SK, Reckamp K, Yu H, Figlin RA. Akt inhibitors in clinical development for the treatment of cancer. Expert Opin. Investig. Drugs 19(11), 1355-1366 (2010).
    • (2010) Expert Opin. Investig. Drugs , vol.19 , Issue.11 , pp. 1355-1366
    • Pal, S.K.1    Reckamp, K.2    Yu, H.3    Figlin, R.A.4
  • 76
    • 79951816826 scopus 로고    scopus 로고
    • Discovery and characterization of a cellpermeable, small-molecule c-Abl kinase activator that binds to the myristoyl binding site
    • Yang J, Campobasso N, Biju MP et al. Discovery and characterization of a cellpermeable, small-molecule c-Abl kinase activator that binds to the myristoyl binding site. Chem. Biol. 18(2), 177-186 (2011).
    • (2011) Chem. Biol. , vol.18 , Issue.2 , pp. 177-186
    • Yang, J.1    Campobasso, N.2    Biju, M.P.3
  • 77
    • 15744398903 scopus 로고    scopus 로고
    • C-Abl tyrosine kinase regulates caspase-9 autocleavage in the apoptotic response to DNA damage
    • Raina D, Pandey P, Ahmad R et al. c-Abl tyrosine kinase regulates caspase-9 autocleavage in the apoptotic response to DNA damage. J. Biol. Chem. 280(12), 11147-11151 (2005).
    • (2005) J. Biol. Chem. , vol.280 , Issue.12 , pp. 11147-11151
    • Raina, D.1    Pandey, P.2    Ahmad, R.3
  • 79
    • 0028858170 scopus 로고
    • Oligodeoxynucleotides antisense to c-abl specifically inhibit entry into S-phase of CD34+ hematopoietic cells and their differentiation to granulocyte-macrophage progenitors
    • Rosti V, Bergamaschi G, Lucotti C et al. Oligodeoxynucleotides antisense to c-abl specifically inhibit entry into S-phase of CD34+ hematopoietic cells and their differentiation to granulocyte-macrophage progenitors. Blood 86(9), 3387-3393 (1995).
    • (1995) Blood , vol.86 , Issue.9 , pp. 3387-3393
    • Rosti, V.1    Bergamaschi, G.2    Lucotti, C.3
  • 80
    • 72749120841 scopus 로고    scopus 로고
    • Activated Abl kinase inhibits oncogenic transforming growth factor-beta signaling and tumorigenesis in mammary tumors
    • Allington TM, Galliher-Beckley AJ, Schiemann WP. Activated Abl kinase inhibits oncogenic transforming growth factor-beta signaling and tumorigenesis in mammary tumors. FASEB J. 23(12), 4231-4243 (2009).
    • (2009) FASEB J. , vol.23 , Issue.12 , pp. 4231-4243
    • Allington, T.M.1    Galliher-Beckley, A.J.2    Schiemann, W.P.3
  • 81
    • 70349305603 scopus 로고    scopus 로고
    • Structure and allosteric effects of low-molecular-weight activators on the protein kinase PDK1
    • Hindie V, Stroba A, Zhang H et al. Structure and allosteric effects of low-molecular-weight activators on the protein kinase PDK1. Nat. Chem. Biol. 5(10), 758-764 (2009).
    • (2009) Nat. Chem. Biol. , vol.5 , Issue.10 , pp. 758-764
    • Hindie, V.1    Stroba, A.2    Zhang, H.3
  • 82
    • 84866652604 scopus 로고    scopus 로고
    • Substrate-selective inhibition of protein kinase PDK1 by small compounds that bind to the PIF-pocket allosteric docking site
    • Busschots K, Lopez-Garcia LA, Lammi C et al. Substrate-selective inhibition of protein kinase PDK1 by small compounds that bind to the PIF-pocket allosteric docking site. Chem. Biol. 19(9), 1152-1163 (2012).
    • (2012) Chem. Biol. , vol.19 , Issue.9 , pp. 1152-1163
    • Busschots, K.1    Lopez-Garcia, L.A.2    Lammi, C.3
  • 83
    • 77953305214 scopus 로고    scopus 로고
    • Discovery of PDK1 kinase inhibitors with a novel mechanism of action by ultrahigh throughput screening
    • Bobkova EV, Weber MJ, Xu Z et al. Discovery of PDK1 kinase inhibitors with a novel mechanism of action by ultrahigh throughput screening. J. Biol. Chem. 285(24), 18838-18846 (2010).
    • (2010) J. Biol. Chem. , vol.285 , Issue.24 , pp. 18838-18846
    • Bobkova, E.V.1    Weber, M.J.2    Xu, Z.3
  • 84
    • 0038168241 scopus 로고    scopus 로고
    • Structural and biochemical evidence for an autoinhibitory role for tyrosine 984 in the juxtamembrane region of the insulin receptor
    • Li S, Covino ND, Stein EG, Till JH, Hubbard SR. Structural and biochemical evidence for an autoinhibitory role for tyrosine 984 in the juxtamembrane region of the insulin receptor. J. Biol. Chem. 278(28), 26007-26014 (2003).
    • (2003) J. Biol. Chem. , vol.278 , Issue.28 , pp. 26007-26014
    • Li, S.1    Covino, N.D.2    Stein, E.G.3    Till, J.H.4    Hubbard, S.R.5
  • 85
    • 0034699358 scopus 로고    scopus 로고
    • Discovery of a potent, highly selective, and orally efficacious small-molecule activator of the insulin receptor
    • Liu K, Xu L, Szalkowski D et al. Discovery of a potent, highly selective, and orally efficacious small-molecule activator of the insulin receptor. J. Med. Chem. 43(19), 3487-3494 (2000).
    • (2000) J. Med. Chem. , vol.43 , Issue.19 , pp. 3487-3494
    • Liu, K.1    Xu, L.2    Szalkowski, D.3
  • 86
    • 80655125020 scopus 로고    scopus 로고
    • Targeting energy metabolic and oncogenic signaling pathways in triple-negative breast cancer by a novel adenosine monophosphate-activated protein kinase (AMPK) Activator
    • Lee KH, Hsu EC, Guh JH et al. Targeting energy metabolic and oncogenic signaling pathways in triple-negative breast cancer by a novel adenosine monophosphate-activated protein kinase (AMPK) Activator. J. Biol. Chem. 286(45), 39247-39258 (2011).
    • (2011) J. Biol. Chem. , vol.286 , Issue.45 , pp. 39247-39258
    • Lee, K.H.1    Hsu, E.C.2    Guh, J.H.3
  • 87
    • 84863700565 scopus 로고    scopus 로고
    • Exploiting the antiinflammatory effects of AMP-activated protein kinase activation
    • Salt IP, Palmer TM. Exploiting the antiinflammatory effects of AMP-activated protein kinase activation. Expert Opin. Investig. Drugs 21(8), 1155-1167 (2012).
    • (2012) Expert Opin. Investig. Drugs , vol.21 , Issue.8 , pp. 1155-1167
    • Salt, I.P.1    Palmer, T.M.2
  • 88
    • 84869837353 scopus 로고    scopus 로고
    • Direct AMPactivated protein kinase activators: A review of evidence from the patent literature
    • Giordanetto F, Karis D. Direct AMPactivated protein kinase activators: a review of evidence from the patent literature. Expert Opin. Ther. Pat. 22(12), 1467-1477 (2012).
    • (2012) Expert Opin. Ther. Pat. , vol.22 , Issue.12 , pp. 1467-1477
    • Giordanetto, F.1    Karis, D.2
  • 90
    • 84862503641 scopus 로고    scopus 로고
    • MLR-1023 is a potent and selective allosteric activator of LYN kinase in vitro that improves glucose tolerance in vivo
    • Saporito MS, Ochman AR, Lipinski CA, Handler JA, Reaume AG. MLR-1023 is a potent and selective allosteric activator of LYN kinase in vitro that improves glucose tolerance in vivo. J. Pharmacol. Exp. Ther. 342(1), 15-22 (2012).
    • (2012) J. Pharmacol. Exp. Ther. , vol.342 , Issue.1 , pp. 15-22
    • Saporito, M.S.1    Ochman, A.R.2    Lipinski, C.A.3    Handler, J.A.4    Reaume, A.G.5
  • 91
    • 17944387219 scopus 로고    scopus 로고
    • Cross talk of pp125(FAK) and pp59(LYN) non-receptor tyrosine kinases to insulin-mimetic signaling in adipocytes
    • Muller G, Wied S, Frick W. Cross talk of pp125(FAK) and pp59(LYN) non-receptor tyrosine kinases to insulin-mimetic signaling in adipocytes. Mol. Cell. Biol. 20(13), 4708-4723 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , Issue.13 , pp. 4708-4723
    • Muller, G.1    Wied, S.2    Frick, W.3
  • 92
    • 77951855933 scopus 로고    scopus 로고
    • Small molecule BDNF mimetics activate TrkB signaling and prevent neuronal degeneration in rodents
    • Massa SM, Yang T, Xie Y et al. Small molecule BDNF mimetics activate TrkB signaling and prevent neuronal degeneration in rodents. J. Clin. Invest. 120(5), 1774-1785 (2010).
    • (2010) J. Clin. Invest. , vol.120 , Issue.5 , pp. 1774-1785
    • Massa, S.M.1    Yang, T.2    Xie, Y.3
  • 93
    • 77249164281 scopus 로고    scopus 로고
    • The (un) targeted cancer kinome
    • Fedorov O, Muller S, Knapp S. The (un) targeted cancer kinome. Nat. Chem. Biol. 6(3), 166-169 (2010).
    • (2010) Nat. Chem. Biol. , vol.6 , Issue.3 , pp. 166-169
    • Fedorov, O.1    Muller, S.2    Knapp, S.3
  • 94
    • 79251579303 scopus 로고    scopus 로고
    • Specific CLK inhibitors from a novel chemotype for regulation of alternative splicing
    • Fedorov O, Huber K, Eisenreich A et al. Specific CLK inhibitors from a novel chemotype for regulation of alternative splicing. Chem. Biol. 18(1), 67-76 (2011).
    • (2011) Chem. Biol. , vol.18 , Issue.1 , pp. 67-76
    • Fedorov, O.1    Huber, K.2    Eisenreich, A.3
  • 95
    • 79959406830 scopus 로고    scopus 로고
    • Leucettines, a class of potent inhibitors of cdc2-like kinases and dual specificity, tyrosine phosphorylation regulated kinases derived from the marine sponge leucettamine B. Modulation of alternative pre-RNA splicing
    • Debdab M, Carreaux F, Renault S et al. Leucettines, a class of potent inhibitors of cdc2-like kinases and dual specificity, tyrosine phosphorylation regulated kinases derived from the marine sponge leucettamine B. modulation of alternative pre-RNA splicing. J. Med. Chem. 54(12), 4172-4186 (2011).
    • (2011) J. Med. Chem. , vol.54 , Issue.12 , pp. 4172-4186
    • Debdab, M.1    Carreaux, F.2    Renault, S.3
  • 96
    • 84883642880 scopus 로고    scopus 로고
    • Topical Antiangiogenic SRPK1 inhibitors reduce choroidal neovascularization in rodent models of exudative AMD
    • Gammons MV, Fedorov O, Ivison D et al. Topical Antiangiogenic SRPK1 inhibitors reduce choroidal neovascularization in rodent models of exudative AMD. Invest Ophthalmol. Vis. Sci. 54(9), 6052-6062 (2013).
    • (2013) Invest Ophthalmol. Vis. Sci. , vol.54 , Issue.9 , pp. 6052-6062
    • Gammons, M.V.1    Fedorov, O.2    Ivison, D.3
  • 98
    • 84857132849 scopus 로고    scopus 로고
    • A novel protein kinase-like domain in a selenoprotein, widespread in the tree of life
    • Dudkiewicz M, Szczepinska T, Grynberg M, Pawlowski K. A novel protein kinase-like domain in a selenoprotein, widespread in the tree of life. PLoS ONE 7(2), e32138 (2012).
    • (2012) PLoS ONE , vol.7 , Issue.2
    • Dudkiewicz, M.1    Szczepinska, T.2    Grynberg, M.3    Pawlowski, K.4
  • 99
    • 67651027850 scopus 로고    scopus 로고
    • FAM20B is a kinase that phosphorylates xylose in the glycosaminoglycan- protein linkage region
    • Koike T, Izumikawa T, Tamura J, Kitagawa H. FAM20B is a kinase that phosphorylates xylose in the glycosaminoglycan-protein linkage region. Biochem. J. 421(2), 157-162 (2009).
    • (2009) Biochem. J. , vol.421 , Issue.2 , pp. 157-162
    • Koike, T.1    Izumikawa, T.2    Tamura, J.3    Kitagawa, H.4
  • 100
    • 47749093500 scopus 로고    scopus 로고
    • Four-jointed is a Golgi kinase that phosphorylates a subset of cadherin domains
    • Ishikawa HO, Takeuchi H, Haltiwanger RS, Irvine KD. Four-jointed is a Golgi kinase that phosphorylates a subset of cadherin domains. Science 321(5887), 401-404 (2008).
    • (2008) Science , vol.321 , Issue.5887 , pp. 401-404
    • Ishikawa, H.O.1    Takeuchi, H.2    Haltiwanger, R.S.3    Irvine, K.D.4
  • 101
    • 84865021971 scopus 로고    scopus 로고
    • The Raine syndrome protein FAM20C is a Golgi kinase that phosphorylates bio-mineralization proteins
    • Ishikawa HO, Xu A, Ogura E, Manning G, Irvine KD. The Raine syndrome protein FAM20C is a Golgi kinase that phosphorylates bio-mineralization proteins. PLoS ONE 7(8), e42988 (2012).
    • (2012) PLoS ONE , vol.7 , Issue.8
    • Ishikawa, H.O.1    Xu, A.2    Ogura, E.3    Manning, G.4    Irvine, K.D.5
  • 102
    • 84861658918 scopus 로고    scopus 로고
    • Secreted kinase phosphorylates extracellular proteins that regulate biomineralization
    • Tagliabracci VS, Engel JL, Wen J et al. Secreted kinase phosphorylates extracellular proteins that regulate biomineralization. Science 336(6085), 1150-1153 (2012).
    • (2012) Science , vol.336 , Issue.6085 , pp. 1150-1153
    • Tagliabracci, V.S.1    Engel, J.L.2    Wen, J.3
  • 104
    • 41949128173 scopus 로고    scopus 로고
    • CASK Functions as a Mg2+-independent neurexin kinase
    • Mukherjee K, Sharma M, Urlaub H et al. CASK Functions as a Mg2+-independent neurexin kinase. Cell 133(2), 328-339 (2008).
    • (2008) Cell , vol.133 , Issue.2 , pp. 328-339
    • Mukherjee, K.1    Sharma, M.2    Urlaub, H.3
  • 105
    • 58149204174 scopus 로고    scopus 로고
    • Structure of the pseudokinase VRK3 reveals a degraded catalytic site, a highly conserved kinase fold, and a putative regulatory binding site
    • Scheeff ED, Eswaran J, Bunkoczi G, Knapp S, Manning G. Structure of the pseudokinase VRK3 reveals a degraded catalytic site, a highly conserved kinase fold, and a putative regulatory binding site. Structure 17(1), 128-138 (2009).
    • (2009) Structure , vol.17 , Issue.1 , pp. 128-138
    • Scheeff, E.D.1    Eswaran, J.2    Bunkoczi, G.3    Knapp, S.4    Manning, G.5
  • 106
    • 58249138122 scopus 로고    scopus 로고
    • Large-scale structural analysis of the classical human protein tyrosine phosphatome
    • Barr AJ, Ugochukwu E, Lee WH et al. Large-scale structural analysis of the classical human protein tyrosine phosphatome. Cell 136(2), 352-363 (2009).
    • (2009) Cell , vol.136 , Issue.2 , pp. 352-363
    • Barr, A.J.1    Ugochukwu, E.2    Lee, W.H.3
  • 108
    • 0034595634 scopus 로고    scopus 로고
    • WNK1, a novel mammalian serine/threonine protein kinase lacking the catalytic lysine in subdomain II
    • Xu B, English JM, Wilsbacher JL, Stippec S, Goldsmith EJ, Cobb MH. WNK1, a novel mammalian serine/threonine protein kinase lacking the catalytic lysine in subdomain II. J. Biol. Chem. 275(22), 16795-16801 (2000).
    • (2000) J. Biol. Chem. , vol.275 , Issue.22 , pp. 16795-16801
    • Xu, B.1    English, J.M.2    Wilsbacher, J.L.3    Stippec, S.4    Goldsmith, E.J.5    Cobb, M.H.6
  • 109
    • 3142600709 scopus 로고    scopus 로고
    • Crystal structure of the kinase domain of WNK1, a kinase that causes a hereditary form of hypertension
    • Min X, Lee BH, Cobb MH, Goldsmith EJ. Crystal structure of the kinase domain of WNK1, a kinase that causes a hereditary form of hypertension. Structure 12(7), 1303-1311 (2004).
    • (2004) Structure , vol.12 , Issue.7 , pp. 1303-1311
    • Min, X.1    Lee, B.H.2    Cobb, M.H.3    Goldsmith, E.J.4
  • 110
    • 70350513073 scopus 로고    scopus 로고
    • Kinetic mechanism and inhibitor characterization of WNK1 kinase
    • Yagi YI, Abe K, Ikebukuro K, Sode K. Kinetic mechanism and inhibitor characterization of WNK1 kinase. Biochemistry 48(43), 10255-10266 (2009).
    • (2009) Biochemistry , vol.48 , Issue.43 , pp. 10255-10266
    • Yagi, Y.I.1    Abe, K.2    Ikebukuro, K.3    Sode, K.4
  • 111
    • 0035941268 scopus 로고    scopus 로고
    • Cloning and characterization of a p53-related protein kinase expressed in interleukin-2-activated cytotoxic T-cells, epithelial tumor cell lines, and the testes
    • Abe Y, Matsumoto S, Wei S et al. Cloning and characterization of a p53-related protein kinase expressed in interleukin-2-activated cytotoxic T-cells, epithelial tumor cell lines, and the testes. J. Biol. Chem. 276(47), 44003-44011 (2001).
    • (2001) J. Biol. Chem. , vol.276 , Issue.47 , pp. 44003-44011
    • Abe, Y.1    Matsumoto, S.2    Wei, S.3
  • 112
    • 0027504169 scopus 로고
    • Divalent metal ions influence catalysis and active-site accessibility in the cAMP-dependent protein kinase
    • Adams JA, Taylor SS. Divalent metal ions influence catalysis and active-site accessibility in the cAMP-dependent protein kinase. Protein Sci. 2(12), 2177-2186 (1993).
    • (1993) Protein Sci. , vol.2 , Issue.12 , pp. 2177-2186
    • Adams, J.A.1    Taylor, S.S.2
  • 113
    • 0037452906 scopus 로고    scopus 로고
    • Physiological concentrations of divalent magnesium ion activate the serine/threonine specific protein kinase ERK2
    • Waas WF, Dalby KN. Physiological concentrations of divalent magnesium ion activate the serine/threonine specific protein kinase ERK2. Biochemistry 42(10), 2960-2970 (2003).
    • (2003) Biochemistry , vol.42 , Issue.10 , pp. 2960-2970
    • Waas, W.F.1    Dalby, K.N.2
  • 114
    • 84865048047 scopus 로고    scopus 로고
    • CASK aberrations in male patients with Ohtahara syndrome and cerebellar hypoplasia
    • Saitsu H, Kato M, Osaka H et al. CASK aberrations in male patients with Ohtahara syndrome and cerebellar hypoplasia. Epilepsia 53(8), 1441-1449 (2012).
    • (2012) Epilepsia , vol.53 , Issue.8 , pp. 1441-1449
    • Saitsu, H.1    Kato, M.2    Osaka, H.3
  • 115
    • 84870248621 scopus 로고    scopus 로고
    • Clinical and radiological features of Japanese patients with a severe phenotype due to CASK mutations
    • Takanashi J, Okamoto N, Yamamoto Y et al. Clinical and radiological features of Japanese patients with a severe phenotype due to CASK mutations. Am. J. Med. Genet. A 158A(12), 3112-3118 (2012).
    • (2012) Am. J. Med. Genet. A , vol.158 , Issue.12 , pp. 3112-3118
    • Takanashi, J.1    Okamoto, N.2    Yamamoto, Y.3
  • 116
    • 81055126966 scopus 로고    scopus 로고
    • Phenotypic spectrum associated with CASK loss-of-function mutations
    • Moog U, Kutsche K, Kortum F et al. Phenotypic spectrum associated with CASK loss-of-function mutations. J. Med. Genet. 48(11), 741-751 (2011).
    • (2011) J. Med. Genet. , vol.48 , Issue.11 , pp. 741-751
    • Moog, U.1    Kutsche, K.2    Kortum, F.3
  • 117
    • 66749148353 scopus 로고    scopus 로고
    • A systematic, large-scale resequencing screen of X-chromosome coding exons in mental retardation
    • Tarpey PS, Smith R, Pleasance E et al. A systematic, large-scale resequencing screen of X-chromosome coding exons in mental retardation. Nat. Genet. 41(5), 535-543 (2009).
    • (2009) Nat. Genet. , vol.41 , Issue.5 , pp. 535-543
    • Tarpey, P.S.1    Smith, R.2    Pleasance, E.3
  • 118
    • 62649108006 scopus 로고    scopus 로고
    • A missense mutation in CASK causes FG syndrome in an Italian family
    • Piluso G, Damico F, Saccone V et al. A missense mutation in CASK causes FG syndrome in an Italian family. Am. J. Hum. Genet. 84(2), 162-177 (2009).
    • (2009) Am. J. Hum. Genet. , vol.84 , Issue.2 , pp. 162-177
    • Piluso, G.1    Damico, F.2    Saccone, V.3
  • 119
    • 76049128717 scopus 로고    scopus 로고
    • Structural analysis of the catalytically inactive kinase domain of the human EGF receptor 3
    • Jura N, Shan Y, Cao X, Shaw DE, Kuriyan J. Structural analysis of the catalytically inactive kinase domain of the human EGF receptor 3. Proc. Natl Acad. Sci. USA 106(51), 21608-21613 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , Issue.51 , pp. 21608-21613
    • Jura, N.1    Shan, Y.2    Cao, X.3    De, S.4    Kuriyan, J.5
  • 120
    • 77952338791 scopus 로고    scopus 로고
    • ErbB3/HER3 intracellular domain is competent to bind ATP and catalyze autophosphorylation
    • Shi F, Telesco SE, Liu Y, Radhakrishnan R, Lemmon MA. ErbB3/HER3 intracellular domain is competent to bind ATP and catalyze autophosphorylation. Proc. Natl Acad. Sci. USA 107(17), 7692-7697 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , Issue.17 , pp. 7692-7697
    • Shi, F.1    Telesco, S.E.2    Liu, Y.3    Radhakrishnan, R.4    Ma, L.5
  • 121
    • 84877839648 scopus 로고    scopus 로고
    • Oncogenic ERBB3 mutations in human cancers
    • Jaiswal BS, Kljavin NM, Stawiski EW et al. Oncogenic ERBB3 mutations in human cancers. Cancer Cell 23(5), 603-617 (2013).
    • (2013) Cancer Cell , vol.23 , Issue.5 , pp. 603-617
    • Jaiswal, B.S.1    Kljavin, N.M.2    Stawiski, E.W.3
  • 122
    • 78649642175 scopus 로고    scopus 로고
    • Pseudokinasesremnants of evolution or key allosteric regulators?
    • Zeqiraj E, Van Aalten DM. Pseudokinasesremnants of evolution or key allosteric regulators? Curr. Opin. Struct. Biol. 20(6), 772-781 (2010).
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , Issue.6 , pp. 772-781
    • Zeqiraj, E.1    Van Aalten, D.M.2
  • 123
    • 84867885462 scopus 로고    scopus 로고
    • ILK: A pseudokinase in the center stage of cell-matrix adhesion and signaling
    • Qin J, Wu C. ILK: a pseudokinase in the center stage of cell-matrix adhesion and signaling. Curr. Opin. Cell. Biol. 24(5), 607-613 (2012).
    • (2012) Curr. Opin. Cell. Biol. , vol.24 , Issue.5 , pp. 607-613
    • Qin, J.1    Wu, C.2
  • 124
    • 84871712311 scopus 로고    scopus 로고
    • An integrin-ILKmicrotubule network orients cell polarity and lumen formation in glandular epithelium
    • Akhtar N, Streuli CH. An integrin-ILKmicrotubule network orients cell polarity and lumen formation in glandular epithelium. Nat. Cell. Biol. 15(1), 17-27 (2013).
    • (2013) Nat. Cell. Biol. , vol.15 , Issue.1 , pp. 17-27
    • Akhtar, N.1    Ch, S.2
  • 125
    • 47749087950 scopus 로고    scopus 로고
    • Integrin-linked kinase-essential roles in physiology and cancer biology
    • McDonald PC, Fielding AB, Dedhar S. Integrin-linked kinase-essential roles in physiology and cancer biology. J. Cell. Sci. 121(Pt 19), 3121-3132 (2008).
    • (2008) J. Cell. Sci. , vol.121 , Issue.PART 19 , pp. 3121-3132
    • McDonald, P.C.1    Fielding, A.B.2    Dedhar, S.3
  • 126
    • 84879884856 scopus 로고    scopus 로고
    • Small interfering RNA targeting ILK inhibits metastasis in human tongue cancer cells through repression of epithelial-tomesenchymal transition
    • Xing Y, Qi J, Deng S, Wang C, Zhang L, Chen J. Small interfering RNA targeting ILK inhibits metastasis in human tongue cancer cells through repression of epithelial-tomesenchymal transition. Exp. Cell. Res. 319(13), 2058-2072 (2013).
    • (2013) Exp. Cell. Res. , vol.319 , Issue.13 , pp. 2058-2072
    • Xing, Y.1    Qi, J.2    Deng, S.3    Wang, C.4    Zhang, L.5    Chen, J.6
  • 127
    • 84878558950 scopus 로고    scopus 로고
    • Overexpression of integrin-linked kinase (ILK) is associated with tumor progression and an unfavorable prognosis in patients with colorectal cancer
    • Li R, Liu B, Yin H, Sun W, Yin J, Su Q. Overexpression of integrin-linked kinase (ILK) is associated with tumor progression and an unfavorable prognosis in patients with colorectal cancer. J. Mol. Histol. 44(2), 183-189 (2013).
    • (2013) J. Mol. Histol. , vol.44 , Issue.2 , pp. 183-189
    • Li, R.1    Liu, B.2    Yin, H.3    Sun, W.4    Yin, J.5    Su, Q.6
  • 128
    • 84872809562 scopus 로고    scopus 로고
    • ILK and PRDX1 are prognostic markers in squamous cell/ adenosquamous carcinomas and adenocarcinoma of gallbladder
    • Li J, Yang ZL, Ren X et al. ILK and PRDX1 are prognostic markers in squamous cell/ adenosquamous carcinomas and adenocarcinoma of gallbladder. Tumour Biol. 34(1), 359-368 (2013).
    • (2013) Tumour Biol. , vol.34 , Issue.1 , pp. 359-368
    • Li, J.1    Yang, Z.L.2    Ren, X.3
  • 129
    • 84867875608 scopus 로고    scopus 로고
    • Targeting ILK and beta4 integrin abrogates the invasive potential of ovarian cancer
    • Choi YP, Kim BG, Gao MQ, Kang S, Cho NH. Targeting ILK and beta4 integrin abrogates the invasive potential of ovarian cancer. Biochem. Biophys. Res. Commun. 427(3), 642-648 (2012).
    • (2012) Biochem. Biophys. Res. Commun. , vol.427 , Issue.3 , pp. 642-648
    • Choi, Y.P.1    Kim, B.G.2    Gao, M.Q.3    Kang, S.4    Cho, N.H.5
  • 130
    • 71149097258 scopus 로고    scopus 로고
    • The pseudoactive site of ILK is essential for its binding to alpha-Parvin and localization to focal adhesions
    • Fukuda K, Gupta S, Chen K, Wu C, Qin J. The pseudoactive site of ILK is essential for its binding to alpha-Parvin and localization to focal adhesions. Mol. Cell. 36(5), 819-830 (2009).
    • (2009) Mol. Cell. , vol.36 , Issue.5 , pp. 819-830
    • Fukuda, K.1    Gupta, S.2    Chen, K.3    Wu, C.4    Qin, J.5
  • 131
    • 84878346308 scopus 로고    scopus 로고
    • Selective bisubstrate inhibitors with sub-nanomolar affinity for protein kinase Pim-1
    • Ekambaram R, Enkvist E, Vaasa A et al. Selective bisubstrate inhibitors with sub-nanomolar affinity for protein kinase Pim-1. ChemMedChem 8(6), 909-913 (2013).
    • (2013) ChemMedChem , vol.8 , Issue.6 , pp. 909-913
    • Ekambaram, R.1    Enkvist, E.2    Vaasa, A.3
  • 132
    • 74849120037 scopus 로고    scopus 로고
    • Bisubstrate inhibitors of protein kinases: From principle to practical applications
    • Lavogina D, Enkvist E, Uri A. Bisubstrate inhibitors of protein kinases: from principle to practical applications. ChemMedChem 5(1), 23-34 (2010).
    • (2010) ChemMedChem , vol.5 , Issue.1 , pp. 23-34
    • Lavogina, D.1    Enkvist, E.2    Uri, A.3
  • 133
    • 0033637113 scopus 로고    scopus 로고
    • The level of C/ EBP protein is critical for cell migration during Drosophila oogenesis and is tightly controlled by regulated degradation
    • Rorth P, Szabo K, Texido G. The level of C/ EBP protein is critical for cell migration during Drosophila oogenesis and is tightly controlled by regulated degradation. Mol. Cell. 6(1), 23-30 (2000).
    • (2000) Mol. Cell. , vol.6 , Issue.1 , pp. 23-30
    • Rorth, P.1    Szabo, K.2    Texido, G.3
  • 134
    • 84886461020 scopus 로고    scopus 로고
    • COP1 targets C/EBPalpha for degradation and induces acute myeloid leukemia via Trib1
    • Yoshida A, Kato JY, Nakamae I, Yoneda-Kato N. COP1 targets C/EBPalpha for degradation and induces acute myeloid leukemia via Trib1. Blood 122(10), 1750-1760 (2013).
    • (2013) Blood , vol.122 , Issue.10 , pp. 1750-1760
    • Yoshida, A.1    Kato, J.Y.2    Nakamae, I.3    Yoneda-Kato, N.4
  • 135
    • 84880408795 scopus 로고    scopus 로고
    • Tribbles in acute leukemia
    • Liang KL, Rishi L, Keeshan K. Tribbles in acute leukemia. Blood 121(21), 4265-4270 (2013).
    • (2013) Blood , vol.121 , Issue.21 , pp. 4265-4270
    • Liang, K.L.1    Rishi, L.2    Keeshan, K.3
  • 136
    • 84875611758 scopus 로고    scopus 로고
    • Critical role of Trib1 in differentiation of tissueresident M2-like macrophages
    • Satoh T, Kidoya H, Naito H et al. Critical role of Trib1 in differentiation of tissueresident M2-like macrophages. Nature 495(7442), 524-528 (2013).
    • (2013) Nature , vol.495 , Issue.7442 , pp. 524-528
    • Satoh, T.1    Kidoya, H.2    Naito, H.3
  • 137
    • 84857192635 scopus 로고    scopus 로고
    • FOG-1 and GATA-1 act sequentially to specify definitive megakaryocytic and erythroid progenitors
    • Mancini E, Sanjuan-Pla A, Luciani L et al. FOG-1 and GATA-1 act sequentially to specify definitive megakaryocytic and erythroid progenitors. EMBO J. 31(2), 351-365 (2012).
    • (2012) EMBO J. , vol.31 , Issue.2 , pp. 351-365
    • Mancini, E.1    Sanjuan-Pla, A.2    Luciani, L.3
  • 138
    • 77956495743 scopus 로고    scopus 로고
    • Differential ability of Tribbles family members to promote degradation of C/ EBPalpha and induce acute myelogenous leukemia
    • Dedhia PH, Keeshan K, Uljon S et al. Differential ability of Tribbles family members to promote degradation of C/ EBPalpha and induce acute myelogenous leukemia. Blood 116(8), 1321-1328 (2010).
    • (2010) Blood , vol.116 , Issue.8 , pp. 1321-1328
    • Dedhia, P.H.1    Keeshan, K.2    Uljon, S.3
  • 140
    • 84863391280 scopus 로고    scopus 로고
    • Identification of TRIB1 R107L gain-offunction mutation in human acute megakaryocytic leukemia
    • Yokoyama T, Toki T, Aoki Y et al. Identification of TRIB1 R107L gain-offunction mutation in human acute megakaryocytic leukemia. Blood 119(11), 2608-2611 (2012).
    • (2012) Blood , vol.119 , Issue.11 , pp. 2608-2611
    • Yokoyama, T.1    Toki, T.2    Aoki, Y.3
  • 141
    • 0037954623 scopus 로고    scopus 로고
    • SKIP3, a novel Drosophila tribbles ortholog, is overexpressed in human tumors and is regulated by hypoxia
    • Bowers AJ, Scully S, Boylan JF. SKIP3, a novel Drosophila tribbles ortholog, is overexpressed in human tumors and is regulated by hypoxia. Oncogene 22(18), 2823-2835 (2003).
    • (2003) Oncogene , vol.22 , Issue.18 , pp. 2823-2835
    • Bowers, A.J.1    Scully, S.2    Boylan, J.F.3
  • 142
    • 78649732085 scopus 로고    scopus 로고
    • Transformation by Tribbles homolog 2 (Trib2) requires both the Trib2 kinase domain and COP1 binding
    • Keeshan K, Bailis W, Dedhia PH et al. Transformation by Tribbles homolog 2 (Trib2) requires both the Trib2 kinase domain and COP1 binding. Blood 116(23), 4948-4957 (2010).
    • (2010) Blood , vol.116 , Issue.23 , pp. 4948-4957
    • Keeshan, K.1    Bailis, W.2    Dedhia, P.H.3
  • 143
    • 84885418884 scopus 로고    scopus 로고
    • Structure of a pseudokinase-domain switch that controls oncogenic activation of Jak kinases
    • Toms AV, Deshpande A, McNally R et al. Structure of a pseudokinase-domain switch that controls oncogenic activation of Jak kinases. Nat. Struct. Mol. Biol. 20(10), 1221-1223 (2013).
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , Issue.10 , pp. 1221-1223
    • Toms, A.V.1    Deshpande, A.2    McNally, R.3
  • 145
    • 77955299093 scopus 로고    scopus 로고
    • JAK2 V617F constitutive activation requires JH2 residue F595: A pseudokinase domain target for specific inhibitors
    • Dusa A, Mouton C, Pecquet C, Herman M, Constantinescu SN. JAK2 V617F constitutive activation requires JH2 residue F595: a pseudokinase domain target for specific inhibitors. PLoS ONE 5(6), e11157 (2010).
    • (2010) PLoS ONE , vol.5 , Issue.6
    • Dusa, A.1    Mouton, C.2    Pecquet, C.3    Herman, M.4    Constantinescu, S.N.5
  • 147
    • 19944434344 scopus 로고    scopus 로고
    • Identification of novel p38alpha MAP kinase inhibitors using fragment-based lead generation
    • Gill AL, Frederickson M, Cleasby A et al. Identification of novel p38alpha MAP kinase inhibitors using fragment-based lead generation. J. Med. Chem. 48(2), 414-426 (2005).
    • (2005) J. Med. Chem. , vol.48 , Issue.2 , pp. 414-426
    • Gill, A.L.1    Frederickson, M.2    Cleasby, A.3
  • 148
    • 80255138640 scopus 로고    scopus 로고
    • Discovery of a novel class of non-ATP site DFG-out state p38 inhibitors utilizing computationally assisted virtual fragmentbased drug design (vFBDD)
    • Moffett K, Konteatis Z, Nguyen D et al. Discovery of a novel class of non-ATP site DFG-out state p38 inhibitors utilizing computationally assisted virtual fragmentbased drug design (vFBDD). Bioorg. Med. Chem. Lett. 21(23), 7155-7165 (2011).
    • (2011) Bioorg. Med. Chem. Lett. , vol.21 , Issue.23 , pp. 7155-7165
    • Moffett, K.1    Konteatis, Z.2    Nguyen, D.3
  • 149
    • 34248569419 scopus 로고    scopus 로고
    • Mutagenesis of p38a MAP kinase establishes key roles of Phe169 in function and structural dynamics and reveals a novel DFG-OUT state
    • Bukhtiyarova M, Karpusas M, Northrop K, Namboodiri HVM, Springman EB. Mutagenesis of p38a MAP kinase establishes key roles of Phe169 in function and structural dynamics and reveals a novel DFG-OUT state. Biochemistry 46, 5687-5696 (2007).
    • (2007) Biochemistry , vol.46 , pp. 5687-5696
    • Bukhtiyarova, M.1    Karpusas, M.2    Northrop, K.3    Hvm, N.4    Springman, E.B.5
  • 150
    • 74849131970 scopus 로고    scopus 로고
    • Displacement assay for the detection of stabilizers of inactive kinase conformations
    • Kluter S, Grutter C, Naqvi T et al. Displacement assay for the detection of stabilizers of inactive kinase conformations. J. Med. Chem. 53(1), 357-367 (2010).
    • (2010) J. Med. Chem. , vol.53 , Issue.1 , pp. 357-367
    • Kluter, S.1    Grutter, C.2    Naqvi, T.3
  • 151
    • 77957552568 scopus 로고    scopus 로고
    • Switch control pocket inhibitors of p38-MAP kinase. Durable type II inhibitors that do not require binding into the canonical ATP hinge region
    • Ahn YM, Clare M, Ensinger CL et al. Switch control pocket inhibitors of p38-MAP kinase. Durable type II inhibitors that do not require binding into the canonical ATP hinge region. Bioorg. Med. Chem. Lett. 20(19), 5793-5798 (2010).
    • (2010) Bioorg. Med. Chem. Lett. , vol.20 , Issue.19 , pp. 5793-5798
    • Ahn, Y.M.1    Clare, M.2    Ensinger, C.L.3
  • 152
    • 84871599677 scopus 로고    scopus 로고
    • Naturalproduct- derived fragments for fragment-based ligand discovery
    • Over B, Wetzel S, Grutter C et al. Naturalproduct- derived fragments for fragment-based ligand discovery. Nat. Chem. 5(1), 21-28 (2013).
    • (2013) Nat. Chem. , vol.5 , Issue.1 , pp. 21-28
    • Over, B.1    Wetzel, S.2    Grutter, C.3
  • 153
    • 70350552210 scopus 로고    scopus 로고
    • The design, synthesis and potential utility of fluorescence probes that target DFG-out conformation of p38alpha for high throughput screening binding assay
    • Tecle H, Feru F, Liu H et al. The design, synthesis and potential utility of fluorescence probes that target DFG-out conformation of p38alpha for high throughput screening binding assay. Chem. Biol. Drug Design 74(6), 547-559 (2009).
    • (2009) Chem. Biol. Drug Design , vol.74 , Issue.6 , pp. 547-559
    • Tecle, H.1    Feru, F.2    Liu, H.3
  • 155
    • 55549124151 scopus 로고    scopus 로고
    • 2-alkylamino- and alkoxy-substituted 2-amino-1,3,4-oxadiazoles-O-alkyl benzohydroxamate esters replacements retain the desired inhibition and selectivity against MEK (MAP ERK kinase)
    • Warmus JS, Flamme C, Zhang LY et al. 2-alkylamino- and alkoxy-substituted 2-amino-1,3,4-oxadiazoles-O-alkyl benzohydroxamate esters replacements retain the desired inhibition and selectivity against MEK (MAP ERK kinase). Bioorg. Med. Chem. Lett. 18(23), 6171-6174 (2008).
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , Issue.23 , pp. 6171-6174
    • Warmus, J.S.1    Flamme, C.2    Zhang, L.Y.3
  • 156
    • 65249090229 scopus 로고    scopus 로고
    • Crystal structures of MEK1 binary and ternary complexes with nucleotides and inhibitors
    • Fischmann TO, Smith CK, Mayhood TW et al. Crystal structures of MEK1 binary and ternary complexes with nucleotides and inhibitors. Biochemistry 48(12), 2661-2674 (2009).
    • (2009) Biochemistry , vol.48 , Issue.12 , pp. 2661-2674
    • Fischmann, T.O.1    Smith, C.K.2    Mayhood, T.W.3
  • 157
    • 70149119899 scopus 로고    scopus 로고
    • RDEA119/ BAY 869766: A potent, selective, allosteric inhibitor of MEK1/2 for the treatment of cancer
    • Iverson C, Larson G, Lai C et al. RDEA119/ BAY 869766: a potent, selective, allosteric inhibitor of MEK1/2 for the treatment of cancer. Cancer Res. 69(17), 6839-6847 (2009).
    • (2009) Cancer Res. , vol.69 , Issue.17 , pp. 6839-6847
    • Iverson, C.1    Larson, G.2    Lai, C.3
  • 158
    • 77953872377 scopus 로고    scopus 로고
    • Structure-based design and synthesis of pyrrole derivatives as MEK inhibitors
    • Wallace MB, Adams ME, Kanouni T et al. Structure-based design and synthesis of pyrrole derivatives as MEK inhibitors. Bioorg. Med. Chem. Lett. 20(14), 4156-4158 (2010).
    • (2010) Bioorg. Med. Chem. Lett. , vol.20 , Issue.14 , pp. 4156-4158
    • Wallace, M.B.1    Adams, M.E.2    Kanouni, T.3
  • 159
    • 79952360230 scopus 로고    scopus 로고
    • Design and synthesis of novel allosteric MEK inhibitor CH4987655 as an orally available anticancer agent
    • Isshiki Y, Kohchi Y, Iikura H et al. Design and synthesis of novel allosteric MEK inhibitor CH4987655 as an orally available anticancer agent. Bioorg. Med. Chem. Lett. 21(6), 1795-1801 (2011).
    • (2011) Bioorg. Med. Chem. Lett. , vol.21 , Issue.6 , pp. 1795-1801
    • Isshiki, Y.1    Kohchi, Y.2    Iikura, H.3
  • 160
    • 79951722555 scopus 로고    scopus 로고
    • Discovery of TAK-733, a potent and selective MEK allosteric site inhibitor for the treatment of cancer
    • Dong Q, Dougan DR, Gong X et al. Discovery of TAK-733, a potent and selective MEK allosteric site inhibitor for the treatment of cancer. Bioorg. Med. Chem. Lett. 21(5), 1315-1319 (2011).
    • (2011) Bioorg. Med. Chem. Lett. , vol.21 , Issue.5 , pp. 1315-1319
    • Dong, Q.1    Dougan, D.R.2    Gong, X.3
  • 161
    • 84861017745 scopus 로고    scopus 로고
    • Novel Carboxamide-Based Allosteric MEK Inhibitors: Discovery and Optimization Efforts toward XL518 (GDC-0973)
    • Rice KD, Aay N, Anand NK et al. Novel Carboxamide-Based Allosteric MEK Inhibitors: Discovery and Optimization Efforts toward XL518 (GDC-0973). ACS Med. Chem. Lett. 3, 416-421 (2012).
    • (2012) ACS Med. Chem. Lett. , vol.3 , pp. 416-421
    • Rice, K.D.1    Aay, N.2    Anand, N.K.3
  • 162
    • 84857030102 scopus 로고    scopus 로고
    • Engineering human MEK-1 for structural studies: A case study of combinatorial domain hunting
    • Meier C, Brookings DC, Ceska TA et al. Engineering human MEK-1 for structural studies: a case study of combinatorial domain hunting. J. Struct. Biol. 177(2), 329-334 (2012).
    • (2012) J. Struct. Biol. , vol.177 , Issue.2 , pp. 329-334
    • Meier, C.1    Brookings, D.C.2    Ceska, T.A.3
  • 163
    • 84861494447 scopus 로고    scopus 로고
    • Discovery of novel allosteric mitogen-activated protein kinase kinase (MEK) 1,2 inhibitors possessing bidentate Ser212 interactions
    • Heald RA, Jackson P, Savy P et al. Discovery of novel allosteric mitogen-activated protein kinase kinase (MEK) 1,2 inhibitors possessing bidentate Ser212 interactions. J. Med. Chem. 55, 4594-4604 (2012).
    • (2012) J. Med. Chem. , vol.55 , pp. 4594-4604
    • Heald, R.A.1    Jackson, P.2    Savy, P.3
  • 164
    • 84875411534 scopus 로고    scopus 로고
    • Optimization of allosteric MEK inhibitors Part 1: Venturing into underexplored SAR territories
    • Hartung IV, Hitchcock M, Puhler F et al. Optimization of allosteric MEK inhibitors. Part 1: venturing into underexplored SAR territories. Bioorg. Med. Chem. Lett. 23(8), 2384-2390 (2013).
    • (2013) Bioorg. Med. Chem. Lett. , vol.23 , Issue.8 , pp. 2384-2390
    • Hartung, I.V.1    Hitchcock, M.2    Puhler, F.3
  • 166
    • 84862996255 scopus 로고    scopus 로고
    • Roco kinase structures give insights into the mechanism of Parkinson disease-related leucine-rich-repeat kinase 2 mutations
    • Gilsbach BK, Ho FY, Vetter IR, Van Haastert PJ, Wittinghofer A, Kortholt A. Roco kinase structures give insights into the mechanism of Parkinson disease-related leucine-rich-repeat kinase 2 mutations. Proc. Natl Acad. Sci. USA 109(26), 10322-10327 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , Issue.26 , pp. 10322-10327
    • Gilsbach, B.K.1    Ho, F.Y.2    Vetter, I.R.3    Van Haastert, P.J.4    Wittinghofer, A.5    Kortholt, A.6
  • 167
    • 74549142415 scopus 로고    scopus 로고
    • Structural analysis of an MK2-inhibitor complex: Insight into the regulation of the secondary structure of the Gly-rich loop by TEI-I01800
    • Fujino A, Fukushima K, Namiki N, Kosugi T, Takimoto-Kamimura M. Structural analysis of an MK2-inhibitor complex: insight into the regulation of the secondary structure of the Gly-rich loop by TEI-I01800. Acta Crystallogr. D Biol. Crystallogr. 66(Pt 1), 80-87 (2010).
    • (2010) Acta Crystallogr. D Biol. Crystallogr , vol.66 , Issue.PART 1 , pp. 80-87
    • Fujino, A.1    Fukushima, K.2    Namiki, N.3    Kosugi, T.4    Takimoto-Kamimura, M.5
  • 168
    • 79953765304 scopus 로고    scopus 로고
    • Conformational control inhibition of the BCR-ABL1 tyrosine kinase, including the gatekeeper T315I mutant, by the switchcontrol inhibitor DCC-2036
    • Chan WW, Wise SC, Kaufman MD et al. Conformational control inhibition of the BCR-ABL1 tyrosine kinase, including the gatekeeper T315I mutant, by the switchcontrol inhibitor DCC-2036. Cancer Cell 19(4), 556-568 (2011).
    • (2011) Cancer Cell , vol.19 , Issue.4 , pp. 556-568
    • Chan, W.W.1    Wise, S.C.2    Kaufman, M.D.3
  • 169
    • 79953774130 scopus 로고    scopus 로고
    • Crystal structures of ABL-related gene (ABL2) in complex with imatinib, tozasertib (VX-680), and a type i inhibitor of the triazole carbothioamide class
    • Salah E, Ugochukwu E, Barr AJ, Von DF, Knapp S, Elkins JM. Crystal structures of ABL-related gene (ABL2) in complex with imatinib, tozasertib (VX-680), and a type I inhibitor of the triazole carbothioamide class. J. Med. Chem. 54 , 2359-2367 (2011).
    • (2011) J. Med. Chem. , vol.54 , pp. 2359-2367
    • Salah, E.1    Ugochukwu, E.2    Barr, A.J.3    Von Df Knapp, S.4    Elkins, J.M.5
  • 170
    • 77958576132 scopus 로고    scopus 로고
    • Crystal structure of human AKT1 with an allosteric inhibitor reveals a new mode of kinase inhibition
    • Wu WI, Voegtli WC, Sturgis HL, Dizon FP, Vigers GP, Brandhuber BJ. Crystal structure of human AKT1 with an allosteric inhibitor reveals a new mode of kinase inhibition. PLoS ONE 5(9), e12913 (2010).
    • (2010) PLoS ONE , vol.5 , Issue.9
    • Wu, W.I.1    Voegtli, W.C.2    Sturgis, H.L.3    Dizon, F.P.4    Vigers, G.P.5    Brandhuber, B.J.6
  • 172
    • 84870244642 scopus 로고    scopus 로고
    • Identification of novel series of pyrazole and indole-urea based DFG-out PYK2 inhibitors
    • Bhattacharya SK, Aspnes GE, Bagley SW et al. Identification of novel series of pyrazole and indole-urea based DFG-out PYK2 inhibitors. Bioorg. Med. Chem. Lett. 22(24), 7523-7529 (2012).
    • (2012) Bioorg. Med. Chem. Lett. , vol.22 , Issue.24 , pp. 7523-7529
    • Bhattacharya, S.K.1    Aspnes, G.E.2    Bagley, S.W.3
  • 173
    • 84874860953 scopus 로고    scopus 로고
    • Structural basis of RIP1 inhibition by necrostatins
    • Xie T, Peng W, Liu Y et al. Structural basis of RIP1 inhibition by necrostatins. Structure 21(3), 493-499 (2013).
    • (2013) Structure , vol.21 , Issue.3 , pp. 493-499
    • Xie, T.1    Peng, W.2    Liu, Y.3
  • 174
    • 75349102353 scopus 로고    scopus 로고
    • Insights into protein kinase regulation and inhibition by large scale structural comparison
    • Eswaran J, Knapp S. Insights into protein kinase regulation and inhibition by large scale structural comparison. Biochim. Biophys. Acta 1804(3), 429-432 (2010).
    • (2010) Biochim. Biophys. Acta , vol.1804 , Issue.3 , pp. 429-432
    • Eswaran, J.1    Knapp, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.