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Volumn 23, Issue 6, 2013, Pages 797-805

Allosteric inhibition of BACE1 by an exosite-binding antibody

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; ASPARTIC PROTEINASE; BETA SECRETASE 1; BETA SECRETASE 1 ANTIBODY; BETA SECRETASE 1 INHIBITOR; BETA SECRETASE INHIBITOR; CYSTEINE PROTEINASE; ENZYME ANTIBODY; EPITOPE; MONOCLONAL ANTIBODY; PEPTIDE DERIVATIVE; SERINE PROTEINASE; TAK 070; UNCLASSIFIED DRUG;

EID: 84888848645     PISSN: 0959440X     EISSN: 1879033X     Source Type: Journal    
DOI: 10.1016/j.sbi.2013.08.001     Document Type: Review
Times cited : (30)

References (66)
  • 1
    • 84859426282 scopus 로고    scopus 로고
    • MEROPS: the database of proteolytic enzymes, their substrates and inhibitors
    • Rawlings N.D., Barrett A.J., Bateman A. MEROPS: the database of proteolytic enzymes, their substrates and inhibitors. Nucleic Acids Res 2012, 40:D343-D350.
    • (2012) Nucleic Acids Res , vol.40
    • Rawlings, N.D.1    Barrett, A.J.2    Bateman, A.3
  • 2
    • 0026597063 scopus 로고
    • Alzheimer's disease: the amyloid cascade hypothesis
    • Hardy J.A., Higgins G.A. Alzheimer's disease: the amyloid cascade hypothesis. Science 1992, 256:184-185.
    • (1992) Science , vol.256 , pp. 184-185
    • Hardy, J.A.1    Higgins, G.A.2
  • 3
    • 80053598145 scopus 로고    scopus 로고
    • Protease regulation: the Yin and Yang of neural development and disease
    • Bai G., Pfaff S.L. Protease regulation: the Yin and Yang of neural development and disease. Neuron 2011, 72:9-21.
    • (2011) Neuron , vol.72 , pp. 9-21
    • Bai, G.1    Pfaff, S.L.2
  • 4
    • 0017413556 scopus 로고
    • Renin-angiotensin system: biochemistry and mechanisms of action
    • Peach M.J. Renin-angiotensin system: biochemistry and mechanisms of action. Physiol Rev 1977, 57:313-370.
    • (1977) Physiol Rev , vol.57 , pp. 313-370
    • Peach, M.J.1
  • 6
    • 0038324472 scopus 로고    scopus 로고
    • Inhibitors of the Plasmodium falciparum parasite aspartic protease plasmepsin II as potential antimalarial agents
    • Boss C., Richard-Bildstein S., Weller T., Fischli W., Meyer S., Binkert C. Inhibitors of the Plasmodium falciparum parasite aspartic protease plasmepsin II as potential antimalarial agents. Curr Med Chem 2003, 10:883-907.
    • (2003) Curr Med Chem , vol.10 , pp. 883-907
    • Boss, C.1    Richard-Bildstein, S.2    Weller, T.3    Fischli, W.4    Meyer, S.5    Binkert, C.6
  • 7
    • 79957929358 scopus 로고    scopus 로고
    • Aspartic protease inhibitors as potential anti-Candida albicans drugs: impacts on fungal biology, virulence and pathogenesis
    • Braga-Silva L.A., Santos A.L. Aspartic protease inhibitors as potential anti-Candida albicans drugs: impacts on fungal biology, virulence and pathogenesis. Curr Med Chem 2011, 18:2401-2419.
    • (2011) Curr Med Chem , vol.18 , pp. 2401-2419
    • Braga-Silva, L.A.1    Santos, A.L.2
  • 11
    • 20244388374 scopus 로고    scopus 로고
    • Napsin A, a member of the aspartic protease family, is abundantly expressed in normal lung and kidney tissue and is expressed in lung adenocarcinomas
    • Chuman Y., Bergman A., Ueno T., Saito S., Sakaguchi K., Alaiya A.A., Franzen B., Bergman T., Arnott D., Auer G., et al. Napsin A, a member of the aspartic protease family, is abundantly expressed in normal lung and kidney tissue and is expressed in lung adenocarcinomas. FEBS Lett 1999, 462:129-134.
    • (1999) FEBS Lett , vol.462 , pp. 129-134
    • Chuman, Y.1    Bergman, A.2    Ueno, T.3    Saito, S.4    Sakaguchi, K.5    Alaiya, A.A.6    Franzen, B.7    Bergman, T.8    Arnott, D.9    Auer, G.10
  • 14
    • 42949109643 scopus 로고    scopus 로고
    • Aliskiren: the first renin inhibitor for clinical treatment
    • Jensen C., Herold P., Brunner H.R. Aliskiren: the first renin inhibitor for clinical treatment. Nat Rev Drug Discov 2008, 7:399-410.
    • (2008) Nat Rev Drug Discov , vol.7 , pp. 399-410
    • Jensen, C.1    Herold, P.2    Brunner, H.R.3
  • 15
    • 34247876141 scopus 로고    scopus 로고
    • Therapies for Alzheimer's disease
    • Melnikova I. Therapies for Alzheimer's disease. Nat Rev Drug Discov 2007, 6:341-342.
    • (2007) Nat Rev Drug Discov , vol.6 , pp. 341-342
    • Melnikova, I.1
  • 16
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics
    • Hardy J., Selkoe D.J. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 2002, 297:353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 17
    • 0030946552 scopus 로고    scopus 로고
    • An etiological role of amyloidogenic carboxyl-terminal fragments of the β-amyloid precursor protein in Alzheimer's disease
    • Suh Y.H. An etiological role of amyloidogenic carboxyl-terminal fragments of the β-amyloid precursor protein in Alzheimer's disease. J Neurochem 1997, 68:1781-1791.
    • (1997) J Neurochem , vol.68 , pp. 1781-1791
    • Suh, Y.H.1
  • 18
    • 4344630985 scopus 로고    scopus 로고
    • BACE1: the β-secretase enzyme in Alzheimer's disease
    • Vassar R. BACE1: the β-secretase enzyme in Alzheimer's disease. J Mol Neurosci 2004, 23:105-114.
    • (2004) J Mol Neurosci , vol.23 , pp. 105-114
    • Vassar, R.1
  • 20
    • 77955792343 scopus 로고    scopus 로고
    • -/- mice exhibit seizure activity that does not correlate with sodium channel level or axonal localization
    • -/- mice exhibit seizure activity that does not correlate with sodium channel level or axonal localization. Mol Neurodegener 2010, 5:31.
    • (2010) Mol Neurodegener , vol.5 , pp. 31
    • Hitt, B.D.1    Jaramillo, T.C.2    Chetkovich, D.M.3    Vassar, R.4
  • 22
    • 84855691982 scopus 로고    scopus 로고
    • The β-secretase enzyme BACE1 as a therapeutic target for Alzheimer's disease
    • Vassar R., Kandalepas P.C. The β-secretase enzyme BACE1 as a therapeutic target for Alzheimer's disease. Alzheimers Res Ther 2011, 3:20-25.
    • (2011) Alzheimers Res Ther , vol.3 , pp. 20-25
    • Vassar, R.1    Kandalepas, P.C.2
  • 23
    • 0036714840 scopus 로고    scopus 로고
    • Crystal structure of memapsin 2 (β-secretase) in complex with an inhibitor OM00-3
    • Hong L., Turner R.T., Koelsch G., Shin D., Ghosh A.K., Tang J. Crystal structure of memapsin 2 (β-secretase) in complex with an inhibitor OM00-3. Biochemistry 2002, 41:10963-10967.
    • (2002) Biochemistry , vol.41 , pp. 10963-10967
    • Hong, L.1    Turner, R.T.2    Koelsch, G.3    Shin, D.4    Ghosh, A.K.5    Tang, J.6
  • 24
    • 0036882390 scopus 로고    scopus 로고
    • Structure and mechanism of the pepsin-like family of aspartic peptidases
    • Dunn B.M. Structure and mechanism of the pepsin-like family of aspartic peptidases. Chem Rev 2002, 102:4431-4458.
    • (2002) Chem Rev , vol.102 , pp. 4431-4458
    • Dunn, B.M.1
  • 25
    • 84877942877 scopus 로고    scopus 로고
    • Advances in the identification of β-secretase inhibitors
    • Hamada Y., Kiso Y. Advances in the identification of β-secretase inhibitors. Expert Opin Drug Discov 2013, 8:709-831.
    • (2013) Expert Opin Drug Discov , vol.8 , pp. 709-831
    • Hamada, Y.1    Kiso, Y.2
  • 26
    • 0033970139 scopus 로고    scopus 로고
    • The gene encoding DRAP (BACE2), a glycosylated transmembrane protein of the aspartic protease family, maps to the down critical region
    • Acquati F., Accarino M., Nucci C., Fumagalli P., Jovine L., Ottolenghi S., Taramelli R. The gene encoding DRAP (BACE2), a glycosylated transmembrane protein of the aspartic protease family, maps to the down critical region. FEBS Lett 2000, 468:59-64.
    • (2000) FEBS Lett , vol.468 , pp. 59-64
    • Acquati, F.1    Accarino, M.2    Nucci, C.3    Fumagalli, P.4    Jovine, L.5    Ottolenghi, S.6    Taramelli, R.7
  • 27
    • 0029083689 scopus 로고
    • Mice deficient for the lysosomal proteinase cathepsin D exhibit progressive atrophy of the intestinal mucosa and profound destruction of lymphoid cells
    • Saftig P., Hetman M., Schmahl W., Weber K., Heine L., Mossmann H., Koster A., Hess B., Evers M., von Figura K., et al. Mice deficient for the lysosomal proteinase cathepsin D exhibit progressive atrophy of the intestinal mucosa and profound destruction of lymphoid cells. EMBO J 1995, 14:3599-3608.
    • (1995) EMBO J , vol.14 , pp. 3599-3608
    • Saftig, P.1    Hetman, M.2    Schmahl, W.3    Weber, K.4    Heine, L.5    Mossmann, H.6    Koster, A.7    Hess, B.8    Evers, M.9    von Figura, K.10
  • 28
    • 33845339435 scopus 로고    scopus 로고
    • Protease inhibitors in the clinic
    • Abbenante G., Fairlie D.P. Protease inhibitors in the clinic. Med Chem 2005, 1:71-104.
    • (2005) Med Chem , vol.1 , pp. 71-104
    • Abbenante, G.1    Fairlie, D.P.2
  • 29
    • 0037727675 scopus 로고    scopus 로고
    • Aspartic peptidase inhibitors: implications in drug development
    • Dash C., Kulkarni A., Dunn B., Rao M. Aspartic peptidase inhibitors: implications in drug development. Crit Rev Biochem Mol Biol 2003, 38:89-119.
    • (2003) Crit Rev Biochem Mol Biol , vol.38 , pp. 89-119
    • Dash, C.1    Kulkarni, A.2    Dunn, B.3    Rao, M.4
  • 31
    • 0034613320 scopus 로고    scopus 로고
    • Structure of the protease domain of memapsin 2 (β-secretase) complexed with inhibitor
    • Hong L., Koelsch G., Lin X., Wu S., Terzyan S., Ghosh A.K., Zhang X.C., Tang J. Structure of the protease domain of memapsin 2 (β-secretase) complexed with inhibitor. Science 2000, 290:150-153.
    • (2000) Science , vol.290 , pp. 150-153
    • Hong, L.1    Koelsch, G.2    Lin, X.3    Wu, S.4    Terzyan, S.5    Ghosh, A.K.6    Zhang, X.C.7    Tang, J.8
  • 32
    • 46749092486 scopus 로고    scopus 로고
    • β-Secretase as a therapeutic target for Alzheimer's disease
    • Ghosh A.K., Gemma S., Tang J. β-Secretase as a therapeutic target for Alzheimer's disease. Neurotherapeutics 2008, 5:399-408.
    • (2008) Neurotherapeutics , vol.5 , pp. 399-408
    • Ghosh, A.K.1    Gemma, S.2    Tang, J.3
  • 36
    • 85012556332 scopus 로고
    • Accumulation of antibodies in the central nervous system
    • Freund J. Accumulation of antibodies in the central nervous system. J Exp Med 1930, 51:889-902.
    • (1930) J Exp Med , vol.51 , pp. 889-902
    • Freund, J.1
  • 37
    • 84878856619 scopus 로고    scopus 로고
    • Bispecific antibodies for delivery into the brain
    • Watts R.J., Dennis M.S. Bispecific antibodies for delivery into the brain. Curr Opin Chem Biol 2013, 17:393-399.
    • (2013) Curr Opin Chem Biol , vol.17 , pp. 393-399
    • Watts, R.J.1    Dennis, M.S.2
  • 39
    • 84871911898 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schechter I., Berger A. On the size of the active site in proteases. I. Papain. Biochem Biophys Res Commun 1967, 425:497-502.
    • (1967) Biochem Biophys Res Commun , vol.425 , pp. 497-502
    • Schechter, I.1    Berger, A.2
  • 40
    • 11844297294 scopus 로고    scopus 로고
    • Structural locations and functional roles of new subsites S5, S6, and S7 in memapsin 2 (β-secretase)
    • Turner R.T., Hong L., Koelsch G., Ghosh A.K., Tang J. Structural locations and functional roles of new subsites S5, S6, and S7 in memapsin 2 (β-secretase). Biochemistry 2005, 44:105-112.
    • (2005) Biochemistry , vol.44 , pp. 105-112
    • Turner, R.T.1    Hong, L.2    Koelsch, G.3    Ghosh, A.K.4    Tang, J.5
  • 43
    • 77954051527 scopus 로고    scopus 로고
    • Identification of β-secretase (BACE1) substrates using quantitative proteomics
    • Hemming M.L., Elias J.E., Gygi S.P., Selkoe D.J. Identification of β-secretase (BACE1) substrates using quantitative proteomics. PLoS ONE 2009, 4:e8477.
    • (2009) PLoS ONE , vol.4
    • Hemming, M.L.1    Elias, J.E.2    Gygi, S.P.3    Selkoe, D.J.4
  • 44
    • 77956726353 scopus 로고    scopus 로고
    • Structural and thermodynamic characteristics of the exosite binding pocket on the human BACE1: a molecular modeling approach
    • Gutierrez L.J., Enriz R.D., Baldoni H.A. Structural and thermodynamic characteristics of the exosite binding pocket on the human BACE1: a molecular modeling approach. J Phys Chem A 2010, 114:10261-10269.
    • (2010) J Phys Chem A , vol.114 , pp. 10261-10269
    • Gutierrez, L.J.1    Enriz, R.D.2    Baldoni, H.A.3
  • 46
    • 77955863408 scopus 로고    scopus 로고
    • A noncompetitive BACE1 inhibitor TAK-070 ameliorates Aβ pathology and behavioral deficits in a mouse model of Alzheimer's disease
    • Fukumoto H., Takahashi H., Tarui N., Matsui J., Tomita T., Hirode M., Sagayama M., Maeda R., Kawamoto M., Hirai K., et al. A noncompetitive BACE1 inhibitor TAK-070 ameliorates Aβ pathology and behavioral deficits in a mouse model of Alzheimer's disease. J Neurosci 2010, 30:11157-11166.
    • (2010) J Neurosci , vol.30 , pp. 11157-11166
    • Fukumoto, H.1    Takahashi, H.2    Tarui, N.3    Matsui, J.4    Tomita, T.5    Hirode, M.6    Sagayama, M.7    Maeda, R.8    Kawamoto, M.9    Hirai, K.10
  • 47
    • 77956310878 scopus 로고    scopus 로고
    • Emerging principles in protease-based drug discovery
    • Drag M., Salvesen G.S. Emerging principles in protease-based drug discovery. Nat Rev Drug Discov 2010, 9:690-701.
    • (2010) Nat Rev Drug Discov , vol.9 , pp. 690-701
    • Drag, M.1    Salvesen, G.S.2
  • 50
    • 77149171184 scopus 로고    scopus 로고
    • Structural and functional bases for allosteric control of MMP activities: can it pave the path for selective inhibition?
    • Sela-Passwell N., Rosenblum G., Shoham T., Sagi I. Structural and functional bases for allosteric control of MMP activities: can it pave the path for selective inhibition?. Biochim Biophys Acta 2010, 1803:29-38.
    • (2010) Biochim Biophys Acta , vol.1803 , pp. 29-38
    • Sela-Passwell, N.1    Rosenblum, G.2    Shoham, T.3    Sagi, I.4
  • 51
    • 0032523769 scopus 로고    scopus 로고
    • Purification, characterization and cloning of an aspartic proteinase inhibitor from squash phloem exudate
    • Christeller J.T., Farley P.C., Ramsay R.J., Sullivan P.A., Laing W.A. Purification, characterization and cloning of an aspartic proteinase inhibitor from squash phloem exudate. Eur J Biochem 1998, 254:160-167.
    • (1998) Eur J Biochem , vol.254 , pp. 160-167
    • Christeller, J.T.1    Farley, P.C.2    Ramsay, R.J.3    Sullivan, P.A.4    Laing, W.A.5
  • 54
    • 32344434479 scopus 로고    scopus 로고
    • The changing landscape of protein allostery
    • Swain J.F., Gierasch L.M. The changing landscape of protein allostery. Curr Opin Struct Biol 2006, 16:102-108.
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 102-108
    • Swain, J.F.1    Gierasch, L.M.2
  • 55
    • 84876266689 scopus 로고    scopus 로고
    • Allostery in disease and in drug discovery
    • Nussinov R., Tsai C.J. Allostery in disease and in drug discovery. Cell 2013, 153:293-305.
    • (2013) Cell , vol.153 , pp. 293-305
    • Nussinov, R.1    Tsai, C.J.2
  • 56
    • 33947092515 scopus 로고
    • Structural basis of the activation and action of trypsin
    • Huber R., Bode W. Structural basis of the activation and action of trypsin. Acc Chem Res 1978, 114-122.
    • (1978) Acc Chem Res , pp. 114-122
    • Huber, R.1    Bode, W.2
  • 57
    • 79960541421 scopus 로고    scopus 로고
    • Allostery in trypsin-like proteases suggests new therapeutic strategies
    • Gohara D.W., Di Cera E. Allostery in trypsin-like proteases suggests new therapeutic strategies. Trends Biotechnol 2011, 29:577-585.
    • (2011) Trends Biotechnol , vol.29 , pp. 577-585
    • Gohara, D.W.1    Di Cera, E.2
  • 60
    • 34250778996 scopus 로고    scopus 로고
    • Exosites in the substrate specificity of blood coagulation reactions
    • Bock P.E., Panizzi P., Verhamme I.M. Exosites in the substrate specificity of blood coagulation reactions. J Thromb Haemost 2007, 5(Suppl. 1):81-94.
    • (2007) J Thromb Haemost , vol.5 , Issue.SUPPL. 1 , pp. 81-94
    • Bock, P.E.1    Panizzi, P.2    Verhamme, I.M.3
  • 61
    • 0036139935 scopus 로고    scopus 로고
    • New insight into how tissue factor allosterically regulates factor VIIa
    • Eigenbrot C., Kirchhofer D. New insight into how tissue factor allosterically regulates factor VIIa. Trends Cardiovasc Med 2002, 12:19-26.
    • (2002) Trends Cardiovasc Med , vol.12 , pp. 19-26
    • Eigenbrot, C.1    Kirchhofer, D.2
  • 62
    • 77956700490 scopus 로고    scopus 로고
    • Structural and mechanistic insight into how antibodies inhibit serine proteases
    • Ganesan R., Eigenbrot C., Kirchhofer D Structural and mechanistic insight into how antibodies inhibit serine proteases. Biochem J 2010, 430:179-189.
    • (2010) Biochem J , vol.430 , pp. 179-189
    • Ganesan, R.1    Eigenbrot, C.2    Kirchhofer, D.3
  • 63
    • 47749087856 scopus 로고    scopus 로고
    • Inhibition of the proteolytic activity of pregnancy-associated plasma protein-A by targeting substrate exosite binding
    • Mikkelsen J.H., Gyrup C., Kristensen P., Overgaard M.T., Poulsen C.B., Laursen L.S., Oxvig C. Inhibition of the proteolytic activity of pregnancy-associated plasma protein-A by targeting substrate exosite binding. J Biol Chem 2008, 283:16772-16780.
    • (2008) J Biol Chem , vol.283 , pp. 16772-16780
    • Mikkelsen, J.H.1    Gyrup, C.2    Kristensen, P.3    Overgaard, M.T.4    Poulsen, C.B.5    Laursen, L.S.6    Oxvig, C.7
  • 65
    • 84864416870 scopus 로고    scopus 로고
    • Identification of exosite-targeting inhibitors of anthrax lethal factor by high-throughput screening
    • Bannwarth L., Goldberg A.B., Chen C., Turk B.E. Identification of exosite-targeting inhibitors of anthrax lethal factor by high-throughput screening. Chem Biol 2012, 19:875-882.
    • (2012) Chem Biol , vol.19 , pp. 875-882
    • Bannwarth, L.1    Goldberg, A.B.2    Chen, C.3    Turk, B.E.4
  • 66
    • 84888829528 scopus 로고    scopus 로고
    • The PyMOL Molecular Graphics System, Version 1.5.0.4. Schrödinger, LLC.
    • The PyMOL Molecular Graphics System, Version 1.5.0.4. Schrödinger, LLC.


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