메뉴 건너뛰기




Volumn 21, Issue 7, 2011, Pages 1023-1044

Low molecular weight inhibitors of Prolyl Oligopeptidase: A review of compounds patented from 2003 to 2010

Author keywords

Alzheimers disease; cognitive disorders; neurological disorders; Parkinsons disease; Prolyl Oligopeptidase; Prolyl Oligopeptidase inhibitors

Indexed keywords

1 [N (4 CHLOROBENZYL)SUCCINAMOYL]PROLINAL; 2 (8 DIMETHYLAMINOOCTYLTHIO) 6 ISOPROPYL 3 PYRIDYL 2 THIENYL KETONE CITRATE; 3 (2 INDANYLACETYL) 4 (1 PYRROLIDINYLCARBONYL)THIAZOLIDINE; ALKALOID DERIVATIVE; ANGIOTENSIN II; ARGIPRESSIN; BENZYLOXYCARBONYLPROLYLPROLINAL; BRADYKININ; HUMANIN; N BENZYL 2 [[2 (HYDROXYACETYL) 1 PYRROLIDINYL]CARBONYL] 1 PYRROLIDINECARBOXAMIDE; NEUROPEPTIDE; NEUROTENSIN; OXYTOCIN; PEPTIDE HORMONE; PEPTIDOMIMETIC AGENT; PROLYL ENDOPEPTIDASE; PROLYL ENDOPEPTIDASE INHIBITOR; PROTIRELIN; S 17092; SUAM 1221; SUBSTANCE P; UNCLASSIFIED DRUG;

EID: 79959422016     PISSN: 13543776     EISSN: 17447674     Source Type: Journal    
DOI: 10.1517/13543776.2011.577416     Document Type: Review
Times cited : (34)

References (129)
  • 1
    • 0032563162 scopus 로고    scopus 로고
    • Prolyl oligopeptidase: An unusual β-propeller domain regulates proteolysis
    • DOI 10.1016/S0092-8674(00)81416-6
    • Fulop V, Bocskei Z, Polgar L. Prolyl oligopeptidase: an unusual beta-propeller domain regulates proteolysis. Cell 1998;21(2):161-70 (Pubitemid 28348004)
    • (1998) Cell , vol.94 , Issue.2 , pp. 161-170
    • Fulop, V.1    Bocskei, Z.2    Polgar, L.3
  • 2
    • 0026669767 scopus 로고
    • Structural relationship between lipases and peptidases of the prolyl oligopeptidase family
    • Polgar L. Structural relationship between lipases and peptidases of the prolyl oligopeptidase family. FEBS Lett 1992;311(3):281-4
    • (1992) FEBS Lett , vol.311 , Issue.3 , pp. 281-4
    • Polgar, L.1
  • 3
    • 2942741114 scopus 로고    scopus 로고
    • Concerted structural changes in the peptidase and the propeller domains of prolyl oligopeptidase are required for substrate binding
    • DOI 10.1016/j.jmb.2004.05.011, PII S0022283604005662
    • Szeltner Z, Rea D, Juhasz T, et al. Concerted structural changes in the peptidase and the propeller domains of prolyl oligopeptidase are required for substrate binding. J Mol Biol 2004;340(3):627-37 (Pubitemid 38798005)
    • (2004) Journal of Molecular Biology , vol.340 , Issue.3 , pp. 627-637
    • Szeltner, Z.1    Rea, D.2    Juhasz, T.3    Renner, V.4    Fulop, V.5    Polgar, L.6
  • 4
    • 13844297579 scopus 로고    scopus 로고
    • Unclosed β-propellers display stable structures: Implications for substrate access to the active site of prolyl oligopeptidase
    • DOI 10.1016/j.jmb.2004.12.014
    • Juhasz T, Szeltner Z, Fulop V, Polgar L. Unclosed beta-propellers display stable structures: implications for substrate access to the active site of prolyl oligopeptidase. J Mol Biol 2005;346(3):907-17 (Pubitemid 40247726)
    • (2005) Journal of Molecular Biology , vol.346 , Issue.3 , pp. 907-917
    • Juhasz, T.1    Szeltner, Z.2    Fulop, V.3    Polgar, L.4
  • 6
    • 77954367132 scopus 로고    scopus 로고
    • Induced-fit Mechanism for Prolyl Endopeptidase
    • Li M, Chen C, Davies DR, Chiu TK. Induced-fit Mechanism for Prolyl Endopeptidase. J Biol Chem 2010;285(28):21487-95
    • (2010) J Biol Chem , vol.285 , Issue.28 , pp. 21487-95
    • Li, M.1    Chen, C.2    Davies, D.R.3    Chiu, T.K.4
  • 7
    • 70349979501 scopus 로고    scopus 로고
    • A new side opening on prolyl oligopeptidase revealed by electron microscopy
    • Tarrago T, Martin-Benito J, Sabido E, et al. A new side opening on prolyl oligopeptidase revealed by electron microscopy. FEBS Lett 2009;583:3344-48
    • (2009) FEBS Lett , vol.583 , pp. 3344-48
    • Tarrago, T.1    Martin-Benito, J.2    Sabido, E.3
  • 8
    • 73149085987 scopus 로고    scopus 로고
    • A cost-effective labeling strategy for the NMR study of large proteins: Selective 15N-labeling of the tryptophan side chains of prolyl oligopeptidase
    • Tarrago T, Claasen B, Kichik N, et al. A cost-effective labeling strategy for the NMR study of large proteins: selective 15N-labeling of the tryptophan side chains of prolyl oligopeptidase. ChemBioChem 2009;10:2736-9
    • (2009) ChemBioChem , vol.10 , pp. 2736-9
    • Tarrago, T.1    Claasen, B.2    Kichik, N.3
  • 10
    • 0026026164 scopus 로고
    • Stone SR. cDNA cloning of porcine brain prolyl endopeptidase and identification of the active-site seryl residue
    • Rennex D, Hemmings BA, Hofsteenge J, Stone SR. cDNA cloning of porcine brain prolyl endopeptidase and identification of the active-site seryl residue. Biochemistry 1991;30(8):2195-203
    • (1991) Biochemistry , vol.30 , Issue.8 , pp. 2195-203
    • Rennex, D.1    Hemmings, B.A.2    Hofsteenge, J.3
  • 11
    • 0026315205 scopus 로고
    • Prolyl endopeptidase from Flavobacterium meningosepticum: Cloning and sequencing of the enzyme gene
    • Yoshimoto T, Kanatani A, Shimoda T, et al. Prolyl endopeptidase from Flavobacterium meningosepticum: cloning and sequencing of the enzyme gene. J Biochem 1991;110(6):873-8
    • (1991) J Biochem , vol.110 , Issue.6 , pp. 873-8
    • Yoshimoto, T.1    Kanatani, A.2    Shimoda, T.3
  • 12
    • 0026662399 scopus 로고
    • Characterization of a prolyl endopeptidase from Flavobacterium meningosepticum. Complete sequence and localization of the active-site serine
    • Chevallier S, Goeltz P, Thibault P, et al. Characterization of a prolyl endopeptidase from Flavobacterium meningosepticum. Complete sequence and localization of the active-site serine. J Biol Chem 1992;267(12):8192-9
    • (1992) J Biol Chem , vol.267 , Issue.12 , pp. 8192-9
    • Chevallier, S.1    Goeltz, P.2    Thibault, P.3
  • 13
    • 0032188925 scopus 로고    scopus 로고
    • Prolyl endopeptidase from Sphingomonas capsulata: Isolation and characterization of the enzyme and nucleotide sequence of the gene
    • DOI 10.1006/abbi.1998.0836
    • Kabashima T, Fujii M, Meng Y, et al. Prolyl endopeptidase from Sphingomonas capsulata: isolation and characterization of the enzyme and nucleotide sequence of the gene. Arch Biochem Biophys 1998;358(1):141-8 (Pubitemid 28471383)
    • (1998) Archives of Biochemistry and Biophysics , vol.358 , Issue.1 , pp. 141-148
    • Kabashima, T.1    Fujii, M.2    Meng, Y.3    Ito, K.4    Yoshimoto, T.5
  • 14
    • 0031913776 scopus 로고    scopus 로고
    • CDNA cloning of mouse prolyl endopeptidase and its involvement in DNA synthesis by Swiss 3T3 cells
    • Ishino T, Ohtsuki S, Homma K, Natori S. cDNA cloning of mouse prolyl endopeptidase and its involvement in DNA synthesis by Swiss 3T3 cells. J Biochem 1998;123(3):540-5 (Pubitemid 28143512)
    • (1998) Journal of Biochemistry , vol.123 , Issue.3 , pp. 540-545
    • Ishino, T.1    Ohtsuki, S.2    Homma, K.-I.3    Natori, S.4
  • 15
    • 0028816361 scopus 로고
    • A gene from the hyperthermophile Pyrococcus furiosus whose deduced product is homologous to members of the prolyl oligopeptidase family of proteases
    • Robinson KA, Bartley DA, Robb FT, Schreier HJ. A gene from the hyperthermophile Pyrococcus furiosus whose deduced product is homologous to members of the prolyl oligopeptidase family of proteases. Gene 1995;152(1):103-6
    • (1995) Gene , vol.152 , Issue.1 , pp. 103-6
    • Robinson, K.A.1    Bartley, D.A.2    Robb, F.T.3    Schreier, H.J.4
  • 16
    • 0028198616 scopus 로고
    • Molecular cloning and characterization of prolyl endopeptidase from human T cells
    • Shirasawa Y, Osawa T, Hirashima A. Molecular cloning and characterization of prolyl endopeptidase from human T cells. J Biochem 1994;115(4):724-9 (Pubitemid 24119397)
    • (1994) Journal of Biochemistry , vol.115 , Issue.4 , pp. 724-729
    • Shirasawa, Y.1    Osawa, T.2    Hirashima, A.3
  • 18
    • 0021084784 scopus 로고
    • Prolyl endopeptidase
    • DOI 10.1016/0024-3205(83)90285-0
    • Wilk S. Prolyl endopeptidase. Life Sci 1983;33(22):2149-57 (Pubitemid 14234451)
    • (1983) Life Sciences , vol.33 , Issue.22 , pp. 2149-2157
    • Wilk, S.1
  • 19
    • 70249089694 scopus 로고    scopus 로고
    • Issues about the physiological functions of prolyl oligopeptidase based on its discordant spatial association with substrates and inconsistencies among mRNA, protein levels, and enzymatic activity
    • Myohanen TT, Garcia-Horsman JA, Tenorio-Laranga J, Mannisto PT. Issues about the physiological functions of prolyl oligopeptidase based on its discordant spatial association with substrates and inconsistencies among mRNA, protein levels, and enzymatic activity. J Histochem Cytochem 2009;57(9):831-48
    • (2009) J Histochem Cytochem , vol.57 , Issue.9 , pp. 831-48
    • Myohanen, T.T.1    Garcia-Horsman, J.A.2    Tenorio-Laranga, J.3    Mannisto, P.T.4
  • 21
    • 53249090063 scopus 로고    scopus 로고
    • Expression and traffic of cellular prolyl oligopeptidase are regulated during cerebellar granule cell differentiation, maturation, and aging
    • Moreno-Baylach MJ, Felipo V, Mannisto PT, Garcia-Horsman JA. Expression and traffic of cellular prolyl oligopeptidase are regulated during cerebellar granule cell differentiation, maturation, and aging. Neuroscience 2008;156(3):580-5
    • (2008) Neuroscience , vol.156 , Issue.3 , pp. 580-5
    • Moreno-Baylach, M.J.1    Felipo, V.2    Mannisto, P.T.3    Garcia-Horsman, J.A.4
  • 22
    • 33846203261 scopus 로고    scopus 로고
    • On the role of prolyl oligopeptidase in health and disease
    • DOI 10.1016/j.npep.2006.10.004, PII S0143417906001442
    • Garcia-Horsman JA, Mannisto PT, Venalainen JI. On the role of prolyl oligopeptidase in health and disease. Neuropeptides 2007;41(1):1-24 (Pubitemid 46091700)
    • (2007) Neuropeptides , vol.41 , Issue.1 , pp. 1-24
    • Garcia-Horsman, J.A.1    Mannisto, P.T.2    Venalainen, J.I.3
  • 23
    • 0019399069 scopus 로고
    • Biologically active peptide-containing fractions in schizophrenia and childhood autism
    • Reichelt KL, Hole K, Hamberger A, et al. Biologically active peptide-containing fractions in schizophrenia and childhood autism. Adv Biochem Psychopharmacol 1981;28:627-43
    • (1981) Adv Biochem Psychopharmacol , vol.28 , pp. 627-43
    • Reichelt, K.L.1    Hole, K.2    Hamberger, A.3
  • 24
    • 0028217535 scopus 로고
    • Lower serum prolyl endopeptidase enzyme activity in major depression: Further evidence that peptidases play a role in the pathophysiology of depression
    • DOI 10.1016/0006-3223(94)90101-5
    • Maes M, Goossens F, Scharpe S, et al. Lower serum prolyl endopeptidase enzyme activity in major depression: further evidence that peptidases play a role in the pathophysiology of depression. Biol Psychiatry 1994;35(8):545-52 (Pubitemid 24140097)
    • (1994) Biological Psychiatry , vol.35 , Issue.8 , pp. 545-552
    • Maes, M.1    Goossens, F.2    Scharpe, S.3    Meltzer, H.Y.4    D'Hondt, P.5    Cosyns, P.6
  • 25
    • 0028802506 scopus 로고
    • Alterations in plasma prolyl endopeptidase activity in depression, mania, and schizophrenia: Effects of antidepressants, mood stabilizers, and antipsychotic drugs
    • Maes M, Goossens F, Scharpe S, et al. Alterations in plasma prolyl endopeptidase activity in depression, mania, and schizophrenia: effects of antidepressants, mood stabilizers, and antipsychotic drugs. Psychiatry Res 1995;58(3):217-25
    • (1995) Psychiatry Res , vol.58 , Issue.3 , pp. 217-25
    • Maes, M.1    Goossens, F.2    Scharpe, S.3
  • 26
    • 0029061068 scopus 로고
    • Effect of a novel prolyl endopeptidase inhibitor, JTP-4819, on prolyl endopeptidase activity and substance P- and arginine-vasopressin-like immunoreactivity in the brains of aged rats
    • Toide K, Okamiya K, Iwamoto Y, Kato T. Effect of a novel prolyl endopeptidase inhibitor, JTP-4819, on prolyl endopeptidase activity and substance P- and arginine-vasopressin-like immunoreactivity in the brains of aged rats. J Neurochem 1995;65(1):234-40
    • (1995) J Neurochem , vol.65 , Issue.1 , pp. 234-40
    • Toide, K.1    Okamiya, K.2    Iwamoto, Y.3    Kato, T.4
  • 27
    • 0029027926 scopus 로고
    • JTP-4819: A novel prolyl endopeptidase inhibitor with potential as a cognitive enhancer
    • Toide K, Iwamoto Y, Fujiwara T, Abe H. JTP-4819: a novel prolyl endopeptidase inhibitor with potential as a cognitive enhancer. J Pharmacol Exp Ther 1995;274(3):1370-8
    • (1995) J Pharmacol Exp Ther , vol.274 , Issue.3 , pp. 1370-8
    • Toide, K.1    Iwamoto, Y.2    Fujiwara, T.3    Abe, H.4
  • 28
    • 0030959487 scopus 로고    scopus 로고
    • Effect of a novel prolyl endopeptidase inhibitor, JTP-4819, on spatial memory and central cholinergic neurons in aged rats
    • DOI 10.1016/S0091-3057(96)00238-9, PII S0091305796002389
    • Toide K, Shinoda M, Fujiwara T, Iwamoto Y. Effect of a novel prolyl endopeptidase inhibitor, JTP-4819, on spatial memory and central cholinergic neurons in aged rats. Pharmacol Biochem Behav 1997;56(3):427-34 (Pubitemid 27145822)
    • (1997) Pharmacology Biochemistry and Behavior , vol.56 , Issue.3 , pp. 427-434
    • Toide, K.1    Shinoda, M.2    Fujiwara, T.3    Iwamoto, Y.4
  • 29
    • 0043073112 scopus 로고    scopus 로고
    • Prolyl peptidases: A serine protease subfamily with high potential for drug discovery
    • DOI 10.1016/S1367-5931(03)00084-X
    • Rosenblum JS, Kozarich JW. Prolyl peptidases: a serine protease subfamily with high potential for drug discovery. Curr Opin Chem Biol 2003;7(4):496-504 (Pubitemid 36980841)
    • (2003) Current Opinion in Chemical Biology , vol.7 , Issue.4 , pp. 496-504
    • Rosenblum, J.S.1    Kozarich, J.W.2
  • 31
    • 33845477051 scopus 로고    scopus 로고
    • Suggested functions for prolyl oligopeptidase: A puzzling paradox
    • DOI 10.1016/j.cca.2006.09.001, PII S0009898106006048
    • Brandt I, Scharpe S, Lambeir AM. Suggested functions for prolyloligopeptidase: a puzzling paradox. Clin Chim Acta 2007;377(1-2):50-61 (Pubitemid 44914066)
    • (2007) Clinica Chimica Acta , vol.377 , Issue.1-2 , pp. 50-61
    • Brandt, I.1    Scharpe, S.2    Lambeir, A.-M.3
  • 32
    • 2342466215 scopus 로고    scopus 로고
    • Prolyl Oligopeptidase Is Involved in Release of the Antifibrotic Peptide Ac-SDKP
    • DOI 10.1161/01.HYP.0000126172.01673.84
    • Cavasin MA, Rhaleb NE, Yang XP, Carretero OA. Prolyl oligopeptidase is involved in release of the antifibrotic peptide Ac-SDKP. Hypertension 2004;43(5):1140-5 (Pubitemid 38579927)
    • (2004) Hypertension , vol.43 , Issue.5 , pp. 1140-1145
    • Cavasin, M.A.1    Rhaleb, N.-E.2    Yang, X.-P.3    Carretero, O.A.4
  • 33
    • 79960905130 scopus 로고    scopus 로고
    • Prolyl oligopeptidase induces angiogenesis both in vitro and in vivo in a novel regulatory manner
    • Doi: 10.1111/j.1476-5381.2010.01146.x
    • Myohanen T, Tenorio-Laranga J, Jokinen B, et al. Prolyl oligopeptidase induces angiogenesis both in vitro and in vivo in a novel regulatory manner. Br J Pharmacol 2010. Doi: 10.1111/j.1476-5381.2010.01146.x
    • (2010) Br J Pharmacol
    • Myohanen, T.1    Tenorio-Laranga, J.2    Jokinen, B.3
  • 34
    • 77953915476 scopus 로고    scopus 로고
    • Increased prolyl endopeptidase activity in human neoplasia
    • Larrinaga G, Perez I, Blanco L, et al. Increased prolyl endopeptidase activity in human neoplasia. Regul Pept 2010;163(1-3):102-6
    • (2010) Regul Pept , vol.163 , Issue.1-3 , pp. 102-6
    • Larrinaga, G.1    Perez, I.2    Blanco, L.3
  • 35
    • 0033577733 scopus 로고    scopus 로고
    • Loss of A Prolyl Oligopeptidase Confers Resistance to Lithium by Elevation of Inositol (1,4,5) Trisphosphate
    • Williams RS, Eames M, Ryves WJ, et al. Loss of a prolyl oligopeptidase confers resistance to lithium by elevation of inositol (1,4,5) trisphosphate. EMBO J 1999;18(10):2734-45
    • (1999) EMBO J , vol.18 , Issue.10 , pp. 2734-45
    • Williams, R.S.1    Eames, M.2    Ryves, W.J.3
  • 36
    • 0029662057 scopus 로고    scopus 로고
    • 2+ release are involved in the induction of long- term potentiation at visual cortical inhibitory synapses
    • Komatsu Y. GABAB receptors, monoamine receptors, and postsynaptic inositol trisphosphate-induced Ca2+ release are involved in the induction of long-term potentiation at visual cortical inhibitory synapses. J Neurosci 1996;16(20):6342-52 (Pubitemid 26337358)
    • (1996) Journal of Neuroscience , vol.16 , Issue.20 , pp. 6342-6352
    • Komatsu, Y.1
  • 37
    • 0038771254 scopus 로고    scopus 로고
    • Search for a common mechanism of mood stabilizers
    • DOI 10.1016/S0006-2952(03)00187-4
    • Harwood AJ, Agam G. Search for a common mechanism of mood stabilizers. Biochem Pharmacol 2003;66(2):179-89 (Pubitemid 36776392)
    • (2003) Biochemical Pharmacology , vol.66 , Issue.2 , pp. 179-189
    • Harwood, A.J.1    Agam, G.2
  • 38
    • 0037118050 scopus 로고    scopus 로고
    • A common mechanism of action for three mood-stabilizing drugs
    • DOI 10.1038/417292a
    • Williams RS, Cheng L, Mudge AW, Harwood AJ. A common mechanism of action for three mood-stabilizing drugs. Nature 2002;417(6886):292-5 (Pubitemid 34534711)
    • (2002) Nature , vol.417 , Issue.6886 , pp. 292-295
    • Williams, R.S.B.1    Cheng, L.2    Mudge, A.W.3    Harwood, A.J.4
  • 41
    • 66949120705 scopus 로고    scopus 로고
    • Prolyl oligopeptidase binds to GAP-43 and functions without its peptidase activity
    • Di Daniel E, Glover CP, Grot E, et al. Prolyl oligopeptidase binds to GAP-43 and functions without its peptidase activity. Mol Cell Neurosci 2009;41(3):373-82
    • (2009) Mol Cell Neurosci , vol.41 , Issue.3 , pp. 373-82
    • Di Daniel, E.1    Glover, C.P.2    Grot, E.3
  • 42
    • 77957965147 scopus 로고    scopus 로고
    • GAP43 shows partial co-localisation but no strong physical interaction with prolyl oligopeptidase
    • Szeltner Z, Morawski M, Juhasz T, et al. GAP43 shows partial co-localisation but no strong physical interaction with prolyl oligopeptidase. Biochim Biophys Acta 2010;1804(12):2162-76
    • (2010) Biochim Biophys Acta , vol.1804 , Issue.12 , pp. 2162-76
    • Szeltner, Z.1    Morawski, M.2    Juhasz, T.3
  • 43
    • 0031027044 scopus 로고    scopus 로고
    • GAP-43: An intrinsic determinant of neuronal development and plasticity
    • DOI 10.1016/S0166-2236(96)10072-2, PII S0166223696100722
    • Benowitz LI, Routtenberg A. GAP-43: an intrinsic determinant of neuronal development and plasticity. Trends Neurosci 1997;20(2):84-91 (Pubitemid 27050703)
    • (1997) Trends in Neurosciences , vol.20 , Issue.2 , pp. 84-91
    • Benowitz, L.I.1    Routtenberg, A.2
  • 44
    • 49049103926 scopus 로고    scopus 로고
    • Prolyl oligopeptidase stimulates the aggregation of alpha-synuclein
    • Brandt I, Gerard M, Sergeant K, et al. Prolyl oligopeptidase stimulates the aggregation of alpha-synuclein. Peptides 2008;29(9):1472-8
    • (2008) Peptides , vol.29 , Issue.9 , pp. 1472-8
    • Brandt, I.1    Gerard, M.2    Sergeant, K.3
  • 46
    • 0029938257 scopus 로고    scopus 로고
    • Pharmacological studies of a novel prolyl endopeptidase inhibitor, JTP-4819, in rats with middle cerebral artery occlusion
    • DOI 10.1016/0014-2999(96)00173-2
    • Shinoda M, Matsuo A, Toide K. Pharmacological studies of a novel prolyl endopeptidase inhibitor, JTP-4819, in rats with middle cerebral artery occlusion. Eur J Pharmacol 1996;305(1-3):31-8 (Pubitemid 26196814)
    • (1996) European Journal of Pharmacology , vol.305 , Issue.1-3 , pp. 31-38
    • Shinoda, M.1    Matsuo, A.2    Toide, K.3
  • 47
    • 77949431008 scopus 로고    scopus 로고
    • Different effects of scopolamine and inhibition of prolyl oligopeptidase on mnemonic and motility functions of young and 8- to 9-month-old rats in the radial-arm maze
    • Peltonen I, Jalkanen AJ, Sinerva V, et al. Different effects of scopolamine and inhibition of prolyl oligopeptidase on mnemonic and motility functions of young and 8- to 9-month-old rats in the radial-arm maze. Basic Clin Pharmacol Toxicol 2010;106(4):280-7
    • (2010) Basic Clin Pharmacol Toxicol , vol.106 , Issue.4 , pp. 280-7
    • Peltonen, I.1    Jalkanen, A.J.2    Sinerva, V.3
  • 49
    • 0036146663 scopus 로고    scopus 로고
    • Effects of the prolyl endopeptidase inhibitor S 17092 on cognitive deficits in Chronic low dose MPTP-treated monkeys
    • DOI 10.1016/S0893-133X(01)00307-4, PII S0893133X01003074
    • Schneider JS, Giardiniere M, Morain P. Effects of the prolyl endopeptidase inhibitor S 17092 on cognitive deficits in chronic low dose MPTP-treated monkeys. Neuropsychopharmacology 2002;26(2):176-82 (Pubitemid 34093080)
    • (2002) Neuropsychopharmacology , vol.26 , Issue.2 , pp. 176-182
    • Schneider, J.S.1    Giardiniere, M.2    Morain, P.3
  • 50
    • 0030822531 scopus 로고    scopus 로고
    • Prevention of amyloid-like deposition by a selective prolyl endopeptidase inhibitor, Y-29794, in senescence-accelerated mouse
    • Kato A, Fukunari A, Sakai Y, Nakajima T. Prevention of amyloid-like deposition by a selective prolyl endopeptidase inhibitor, Y-29794, in senescence-accelerated mouse. J Pharmacol Exp Ther 1997;283(1):328-35 (Pubitemid 27438978)
    • (1997) Journal of Pharmacology and Experimental Therapeutics , vol.283 , Issue.1 , pp. 328-335
    • Kato, A.1    Fukunari, A.2    Sakai, Y.3    Nakajima, T.4
  • 51
    • 0031853803 scopus 로고    scopus 로고
    • A novel prolyl endopeptidase inhibitor, JTP-4819. Its behavioral and neurochemical properties for the treatment of Alzheimer's disease
    • Toide K, Shinoda M, Miyazaki A. A novel prolyl endopeptidase inhibitor, JTP-4819-its behavioral and neurochemical properties for the treatment of Alzheimer's disease. Rev Neurosci 1998;9(1):17-29 (Pubitemid 28334037)
    • (1998) Reviews in the Neurosciences , vol.9 , Issue.1 , pp. 17-29
    • Toide, K.1    Shinoda, M.2    Miyazaki, A.3
  • 52
    • 0032935542 scopus 로고    scopus 로고
    • ONO-1603, a potential antidementia drug, delays age-induced apoptosis and suppresses overexpression of glyceraldehyde-3-phosphate dehydrogenase in cultured central nervous system neurons
    • Katsube N, Sunaga K, Aishita H, et al. ONO-1603, a potential antidementia drug, delays age-induced apoptosis and suppresses overexpression of glyceraldehyde-3-phosphate dehydrogenase in cultured central nervous system neurons. J Pharmacol Exp Ther 1999;288(1):6-13 (Pubitemid 29113466)
    • (1999) Journal of Pharmacology and Experimental Therapeutics , vol.288 , Issue.1 , pp. 6-13
    • Katsube, N.1    Sunaga, K.2    Aishita, H.3    Chuang, D.-M.4    Ishitani, R.5
  • 53
    • 0033774426 scopus 로고    scopus 로고
    • Pharmacodynamic and pharmacokinetic profile of S 17092, a new orally active prolyl endopeptidase inhibitor, in elderly healthy volunteers. A phase i study
    • Morain P, Robin JL, De Nanteuil G, et al. Pharmacodynamic and pharmacokinetic profile of S 17092, a new orally active prolyl endopeptidase inhibitor, in elderly healthy volunteers. A phase I study. Br J Clin Pharmacol 2000;50(4):350-9
    • (2000) Br J Clin Pharmacol , vol.50 , Issue.4 , pp. 350-9
    • Morain, P.1    Robin, J.L.2    De Nanteuil, G.3
  • 54
    • 34948825441 scopus 로고    scopus 로고
    • Psychotropic profile of S 17092, a prolyl endopeptidase inhibitor, using quantitative EEG in young healthy volunteers
    • DOI 10.1159/000107070
    • Morain P, Boeijinga PH, Demazieres A, et al. Psychotropic profile of S 17092, a prolyl endopeptidase inhibitor, using quantitative EEG in young healthy volunteers. Neuropsychobiology 2007;55(3-4):176-83 (Pubitemid 47525238)
    • (2007) Neuropsychobiology , vol.55 , Issue.3-4 , pp. 176-183
    • Morain, P.1    Boeijinga, P.H.2    Demazieres, A.3    De Nanteuil, G.4    Luthringer, R.5
  • 56
    • 0031897652 scopus 로고    scopus 로고
    • Prolyl endopeptidase inhibitors: A new class of memory enhancing drugs
    • DOI 10.1358/dof.1998.023.02.858346
    • De Nanteuil G, Portevin B, Lepagnol J. Prolyl endopeptidase inhibitors: a new class of memory enhancing drugs. Drugs Future 1998;23(2):167-79 (Pubitemid 28191589)
    • (1998) Drugs of the Future , vol.23 , Issue.2 , pp. 167-179
    • De Nanteul, G.1    Portevin, B.2    Lepagnol, J.3
  • 57
    • 77952024780 scopus 로고    scopus 로고
    • Inhibitors of prolyl oligopeptidases for the therapy of human diseases: Defining diseases and inhibitors
    • Lawandi J, Gerber-Lemaire S, Juillerat-Jeanneret L, Moitessier N. Inhibitors of prolyl oligopeptidases for the therapy of human diseases: defining diseases and inhibitors. J Med Chem 2010;53(9):3423-38
    • (2010) J Med Chem , vol.53 , Issue.9 , pp. 3423-38
    • Lawandi, J.1    Gerber-Lemaire, S.2    Juillerat-Jeanneret, L.3    Moitessier, N.4
  • 58
    • 0022341245 scopus 로고
    • Comparison of inhibitory effects of prolinal-containing peptide derivatives on prolyl endopeptidases from bovine brain and Flavobacterium
    • Yoshimoto T, Kawahara K, Matsubara F, et al. Comparison of inhibitory effects of prolinal-containing peptide derivatives on prolyl endopeptidases from bovine brain and Flavobacterium. J Biochem 1985;98(4):975-9 (Pubitemid 16234376)
    • (1985) Journal of Biochemistry , vol.98 , Issue.4 , pp. 975-979
    • Yoshimoto, T.1    Kawahara, K.2    Matsubara, F.3
  • 59
    • 0030868993 scopus 로고    scopus 로고
    • Low barrier hydrogen bond is absent in the catalytic triads in the ground state but is present in a transition-state complex in the prolyl oligopeptidase family of serine proteases
    • DOI 10.1074/jbc.272.41.25547
    • Kahyaoglu A, Haghjoo K, Guo F, et al. Low barrier hydrogen bond is absent in the catalytic triads in the ground state but is present in a transition-state complex in the prolyl oligopeptidase family of serine proteases. J Biol Chem 1997;272(41):25547-54 (Pubitemid 27438864)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.41 , pp. 25547-25554
    • Kahyaoglu, A.1    Haghjoo, K.2    Guo, F.3    Jordan, F.4    Kettner, C.5    Felfoldi, F.6    Polgar, L.7
  • 60
    • 0025983559 scopus 로고
    • Structure activity relationship of inhibitors specific for prolyl endopeptidase
    • Yoshimoto T, Tsuru D, Yamamoto N, et al. Structure activity relationship of inhibitors specific for prolyl endopeptidase. Agric Biol Chem 1991;55(1):37-43
    • (1991) Agric Biol Chem , vol.55 , Issue.1 , pp. 37-43
    • Yoshimoto, T.1    Tsuru, D.2    Yamamoto, N.3
  • 61
    • 33846904812 scopus 로고    scopus 로고
    • Synthesis and structure-activity relationship of N-acyl-Gly-, N-acyl-Sar- and N-blocked-boroPro inhibitors of FAP, DPP4, and POP
    • DOI 10.1016/j.bmcl.2006.11.072, PII S0960894X06013643
    • Tran T, Quan C, Edosada CY, et al. Synthesis and structure-activity relationship of N-acyl-Gly-, N-acyl-Sarand N-blocked-boroPro inhibitors of FAP, DPP4, and POP. Bioorg Med Chem Lett 2007;17(5):1438-42 (Pubitemid 46240826)
    • (2007) Bioorganic and Medicinal Chemistry Letters , vol.17 , Issue.5 , pp. 1438-1442
    • Tran, T.1    Quan, C.2    Edosada, C.Y.3    Mayeda, M.4    Wiesmann, C.5    Sutherlin, D.6    Wolf, B.B.7
  • 62
    • 1542571783 scopus 로고    scopus 로고
    • Electrostatic environment at the active site of prolyl oligopeptidase is highly influential during substrate binding
    • DOI 10.1074/jbc.M309555200
    • Szeltner Z, Rea D, Renner V, et al. Electrostatic environment at the active site of prolyl oligopeptidase is highly influential during substrate binding. J Biol Chem 2003;278(49):48786-93 (Pubitemid 41079521)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.49 , pp. 48786-48793
    • Szeltneri, Z.1    Rea, D.2    Renner, V.3    Juliano, L.4    Fulop, V.5    Polgar, L.6
  • 63
    • 0014211618 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;27(2):157-62
    • (1967) Biochem Biophys Res Commun , vol.27 , Issue.2 , pp. 157-62
    • Schechter, I.1    Berger, A.2
  • 64
    • 0014220976 scopus 로고
    • On the size of the active site in proteases. II. Carboxypeptidase-A
    • Abramowitz N, Schechter I, Berger A. On the size of the active site in proteases. II. Carboxypeptidase-A. Biochem Biophys Res Commun 1967;29(6):862-7
    • (1967) Biochem Biophys Res Commun , vol.29 , Issue.6 , pp. 862-7
    • Abramowitz, N.1    Schechter, I.2    Berger, A.3
  • 65
    • 0023736168 scopus 로고
    • Thiazolidine derivatives as potent inhibitors specific for prolyl endopeptidase
    • Tsuru D, Yoshimoto T, Koriyama N, Furukawa S. Thiazolidine derivatives as potent inhibitors specific for prolyl endopeptidase. J Biochem 1988;104(4):580-6
    • (1988) J Biochem , vol.104 , Issue.4 , pp. 580-6
    • Tsuru, D.1    Yoshimoto, T.2    Koriyama, N.3    Furukawa, S.4
  • 66
    • 0343990112 scopus 로고    scopus 로고
    • Prolyl endopeptidase inhibitors: N-acyl derivatives of L-thioproline-pyrrolidine
    • Kanai K, Erd S, Susan E, et al. Prolyl endopeptidase inhibitors: N-acyl derivatives of L-thioproline-pyrrolidine. Bioorg Med Chem Lett 1997;7(13):1701-4
    • (1997) Bioorg Med Chem Lett , vol.7 , Issue.13 , pp. 1701-4
    • Kanai, K.1    Erd, S.2    Susan, E.3
  • 69
    • 57349144413 scopus 로고    scopus 로고
    • Prolyl oligopeptidase inhibition by N-acyl-pro-pyrrolidine-type molecules
    • Kanai K, Aranyi P, Bocskei Z, et al. Prolyl oligopeptidase inhibition by N-acyl-pro-pyrrolidine-type molecules. J Med Chem 2008;51(23):7514-22
    • (2008) J Med Chem , vol.51 , Issue.23 , pp. 7514-22
    • Kanai, K.1    Aranyi, P.2    Bocskei, Z.3
  • 70
    • 0025117586 scopus 로고
    • Synthesis and inhibitory activity of acyl-peptidyl-prolinal derivatives toward post-proline cleaving enzyme as nootropic agents
    • Saito M, Hashimoto M, Kawaguchi N, et al. Synthesis and inhibitory activity of acyl-peptidyl-prolinalderivatives toward post-proline cleaving enzyme as nootropic agents. J Enzyme Inhib 1990;3(3):163-78 (Pubitemid 20080687)
    • (1990) Journal of Enzyme Inhibition , vol.3 , Issue.3 , pp. 163-178
    • Saito, M.1    Hashimoto, M.2    Kawaguchi, N.3    Fukami, H.4    Tanaka, T.5    Higuchi, N.6
  • 71
    • 0025892450 scopus 로고
    • Synthesis and inhibitory activity of acyl-peptidyl-pyrrolidine derivatives toward post-proline cleaving enzyme; A study of subsite specificity
    • Saito M, Hashimoto M, Kawaguchi N, et al. Synthesis and inhibitory activity of acyl-peptidyl-pyrrolidine derivatives toward post-proline cleaving enzyme; a study of subsite specificity. J Enzyme Inhib 1991;5(1):51-75
    • (1991) J Enzyme Inhib , vol.5 , Issue.1 , pp. 51-75
    • Saito, M.1    Hashimoto, M.2    Kawaguchi, N.3
  • 72
    • 0029874503 scopus 로고    scopus 로고
    • Inhibition of prolyl oligopeptidase by Fmoc-aminoacylpyrrolidine-2- nitriles
    • Li J, Wilk E, Wilk S. Inhibition of prolyl oligopeptidase by Fmoc-aminoacylpyrrolidine-2-nitriles. J Neurochem 1996;66(5):2105-12 (Pubitemid 126580078)
    • (1996) Journal of Neurochemistry , vol.66 , Issue.5 , pp. 2105-2112
    • Li, J.1    Wilk, E.2    Wilk, S.3
  • 73
    • 0029977323 scopus 로고    scopus 로고
    • New prolyl endopeptidase inhibitors: In vitro and in vivo activities of azabicyclo[2.2.2]octane, azabicyclo[2.2.1]heptane, and perhydroindole derivatives
    • DOI 10.1021/jm950858c
    • Portevin B, Benoist A, Remond G, et al. New prolyl endopeptidase inhibitors: in vitro and in vivo activities of azabicyclo[2.2.2]octane, azabicyclo[2.2.1] heptane, and perhydroindole derivatives. J Med Chem 1996;39(12):2379-91 (Pubitemid 26191128)
    • (1996) Journal of Medicinal Chemistry , vol.39 , Issue.12 , pp. 2379-2391
    • Portevin, B.1    Benoist, A.2    Remond, G.3    Herve, Y.4    Vincent, M.5    Lepagnol, J.6    De Nanteuil, G.7
  • 75
    • 0025934184 scopus 로고
    • Novel in vitro and in vivo inhibitors of prolyl endopeptidase
    • Bakker AV, Daffeh J, Jung S, et al. Novel in vitro and in vivo inhibitors of prolyl endopeptidase. Bioorg Med Chem Lett 1991;1(11):585-90
    • (1991) Bioorg Med Chem Lett , vol.1 , Issue.11 , pp. 585-90
    • Bakker, A.V.1    Daffeh, J.2    Jung, S.3
  • 78
    • 0020615453 scopus 로고
    • Inhibition of rabbit brain prolyl endopeptidase by N-benzyloxycarbonyl- prolyl-prolinal, a transition state aldehyde inhibitor
    • Wilk S, Orlowski M. Inhibition of rabbit brain prolyl endopeptidase by n-benzyloxycarbonyl-prolyl-prolinal, a transition state aldehyde inhibitor. J Neurochem 1983;41(1):69-75 (Pubitemid 13064897)
    • (1983) Journal of Neurochemistry , vol.41 , Issue.1 , pp. 69-75
    • Wilk, S.1    Orlowski, M.2
  • 82
    • 79959453289 scopus 로고
    • 1,3- dicarbonyl) derivatives, a process for their preparation, agents containing them, and their use. EP0286927 (A2 and A3)
    • Hoechst AG. Novel pyrrolidine-2-(1,3- dicarbonyl) derivatives, a process for their preparation, agents containing them, and their use. EP0286927 (A2 and A3); 1988
    • (1988) Novel pyrrolidine-2
    • Hoechst, A.G.1
  • 84
    • 0037179618 scopus 로고    scopus 로고
    • Dicarboxylic acid bis(L-prolyl-pyrrolidine) amides as prolyl oligopeptidase inhibitors
    • Wallen EA, Christiaans JA, Forsberg MM, et al. Dicarboxylic acid bis(L-prolyl-pyrrolidine) amides as prolyl oligopeptidase inhibitors. J Med Chem 2002;45(20):4581-4
    • (2002) J Med Chem , vol.45 , Issue.20 , pp. 4581-4
    • Wallen, E.A.1    Christiaans, J.A.2    Forsberg, M.M.3
  • 97
    • 0007806295 scopus 로고
    • Anti-amnesic effect of ONO-1603, a novel prolyl endopeptidase inhibitor
    • Katsube N, Tateishi N, Matsushita Y, et al. Anti-amnesic effect of ONO-1603, a novel prolyl endopeptidase inhibitor. Jpn J Pharmacol 1989;49:91-8
    • (1989) Jpn J Pharmacol , vol.49 , pp. 91-8
    • Katsube, N.1    Tateishi, N.2    Matsushita, Y.3
  • 100
    • 0026725142 scopus 로고
    • Y-29794-a non-peptide prolyl endopeptidase inhibitor that can penetrate into the brain
    • Nakajima T, Ono Y, Kato A, et al. Y-29794-a non-peptide prolyl endopeptidase inhibitor that can penetrate into the brain. Neurosci Lett 1992;141(2):156-60
    • (1992) Neurosci Lett , vol.141 , Issue.2 , pp. 156-60
    • Nakajima, T.1    Ono, Y.2    Kato, A.3
  • 101
    • 79959438919 scopus 로고
    • Japan Tobaccom, Inc. Yoshitomi Pharmaceutical.
    • Japan Tobacco, Inc. Yoshitomi Pharmaceutical. New proline derivative. JP5025125 (A); 1993
    • (1993) New Proline Derivative JP5025125 (A)
  • 102
    • 79959407468 scopus 로고
    • Japan Tobacco Inc. Yoshitomi Pharmaceutical.
    • Japan Tobacco, Inc. Yoshitomi Pharmaceutical. Proline derivative. JP5186498 (A); 1993
    • (1993) Proline Derivative JP5186498 (A)
  • 103
    • 79959420024 scopus 로고
    • Japan Tobacco, Inc. Yoshitomi Pharmaceutical.
    • Japan Tobacco, Inc. Yoshitomi Pharmaceutical. New proline derivative. JP5201970 (A); 1993
    • (1993) New Proline Derivative JP5201970 (A)
  • 114
    • 22744434280 scopus 로고    scopus 로고
    • Dicarboxylic acid azacycle L-prolyl-pyrrolidine amides as prolyl oligopeptidase inhibitors and three-dimensional quantitative structure-activity relationship of the enzyme-inhibitor interactions
    • DOI 10.1021/jm0500020
    • Jarho EM, Wallen EA, Christiaans JA, et al. Dicarboxylic acid azacycle l-prolyl-pyrrolidine amides as prolyl oligopeptidase inhibitors and three-dimensional quantitative structure-activity relationship of the enzyme-inhibitor interactions. J Med Chem 2005;48(15):4772-82 (Pubitemid 41033120)
    • (2005) Journal of Medicinal Chemistry , vol.48 , Issue.15 , pp. 4772-4782
    • Jarho, E.M.1    Wallen, E.A.A.2    Christiaans, J.A.M.3    Forsberg, M.M.4    Venalainen, J.I.5    Mannisto, P.T.6    Gynther, J.7    Poso, A.8
  • 119
    • 52049109838 scopus 로고    scopus 로고
    • Natural products in drug discovery
    • Harvey AL. Natural products in drug discovery. Drug Discov Today 2008;13(19-20):894-901
    • (2008) Drug Discov Today , vol.13 , Issue.19-20 , pp. 894-901
    • Harvey, A.L.1
  • 120
    • 33646782270 scopus 로고    scopus 로고
    • 19F NMR of traditional Chinese medicinal plants possessing prolyl oligopeptidase inhibitory activity
    • DOI 10.1002/cbic.200500424
    • Tarrago T, Frutos S, Rodriguez-Mias RA, Giralt E. Identification by 19F NMR of traditional Chinese medicinal plants possessing prolyl oligopeptidase inhibitory activity. Chembiochem 2006;7(5):827-33 (Pubitemid 43764193)
    • (2006) ChemBioChem , vol.7 , Issue.5 , pp. 827-833
    • Tarrago, T.1    Frutos, S.2    Rodriguez-Mias, R.A.3    Giralt, E.4
  • 121
    • 0034039890 scopus 로고    scopus 로고
    • Protective effect of oren-gedoku-to against induction of neuronal death by transient cerebral ischemia in the C57BL/6 mouse
    • DOI 10.1023/A:1007515318434
    • Kondo Y, Kondo F, Asanuma M, et al. Protective effect of oren-gedoku-to against induction of neuronal death by transient cerebral ischemia in the C57BL/6 mouse. Neurochem Res 2000;25(2):205-9 (Pubitemid 30210085)
    • (2000) Neurochemical Research , vol.25 , Issue.2 , pp. 205-209
    • Kondo, Y.1    Kondo, F.2    Asanuma, M.3    Tanaka, K.-I.4    Ogawa, N.5
  • 122
    • 0033696121 scopus 로고    scopus 로고
    • Protective effect of Oren-gedoku-to (Huang-Lian-Jie-Du-Tang) against impairment of learning and memory induced by transient cerebral ischemia in mice
    • Xu J, Murakami Y, Matsumoto K, et al. Protective effect of Oren-gedoku-to (Huang-Lian-Jie-Du-Tang) against impairment of learning and memory induced by transient cerebral ischemia in mice. J Ethnopharmacol 2000;73(3):405-13
    • (2000) J Ethnopharmacol , vol.73 , Issue.3 , pp. 405-13
    • Xu, J.1    Murakami, Y.2    Matsumoto, K.3
  • 123
    • 34748916412 scopus 로고    scopus 로고
    • The natural product berberine is a human prolyl oligopeptidase inhibitor
    • Tarrago T, Kichik N, Segui J, Giralt E. The natural product berberine is a human prolyl oligopeptidase inhibitor. ChemMedChem 2007;2(3):354-9
    • (2007) ChemMedChem , vol.2 , Issue.3 , pp. 354-9
    • Tarrago, T.1    Kichik, N.2    Segui, J.3    Giralt, E.4
  • 124
    • 0037969021 scopus 로고    scopus 로고
    • Efficacy and safety of berberine for congestive heart failure secondary to ischemic or idiopathic dilated cardiomyopathy
    • Zeng XH, Zeng XJ, Li YY. Efficacy and safety of berberine for congestive heart failure secondary to ischemic or idiopathic dilated cardiomyopathy. Am J Cardiol 2003;92(2):173-6
    • (2003) Am J Cardiol , vol.92 , Issue.2 , pp. 173-6
    • Zeng, X.H.1    Zeng, X.J.2    Li, Y.Y.3
  • 126
    • 26444578905 scopus 로고    scopus 로고
    • Kinetic difference of berberine between hippocampus and plasma in rat after intravenous administration of Coptidis rhizoma extract
    • DOI 10.1016/j.lfs.2005.02.033, PII S0024320505005886
    • Wang X, Wang R, Xing D, et al. Kinetic difference of berberine between hippocampus and plasma in rat after intravenous administration of Coptidis rhizoma extract. Life Sci 2005;77(24):3058-67 (Pubitemid 41423743)
    • (2005) Life Sciences , vol.77 , Issue.24 , pp. 3058-3067
    • Wang, X.1    Wang, R.2    Xing, D.3    Su, H.4    Ma, C.5    Ding, Y.6    Du, L.7
  • 127
    • 17044422955 scopus 로고    scopus 로고
    • The uptake and transport behavior of berberine in Coptidis Rhizoma extract through rat primary cultured cortical neurons
    • Wang X, Xing D, Wang W, et al. The uptake and transport behavior of berberine in Coptidis Rhizoma extract through rat primary cultured cortical neurons. Neurosci Lett 2005;379(2):132-7
    • (2005) Neurosci Lett , vol.379 , Issue.2 , pp. 132-7
    • Wang, X.1    Xing, D.2    Wang, W.3
  • 128
    • 54849405942 scopus 로고    scopus 로고
    • Benzimidazolium salts as small, nonpeptidic and BBB-permeable human prolyl oligopeptidase inhibitors
    • Tarrago T, Masdeu C, Gomez E, et al. Benzimidazolium salts as small, nonpeptidic and BBB-permeable human prolyl oligopeptidase inhibitors. ChemMedChem 2008;3:1558-65
    • (2008) ChemMedChem , vol.3 , pp. 1558-65
    • Tarrago, T.1    Masdeu, C.2    Gomez, E.3
  • 129
    • 48449104380 scopus 로고    scopus 로고
    • Baicalin, a prodrug able to reach the CNS, is a prolyl oligopeptidase inhibitor
    • Tarrago T, Kichik N, Claasen B, et al. Baicalin, a prodrug able to reach the CNS, is a prolyl oligopeptidase inhibitor. Bioorg Med Chem 2008;16:7516-24
    • (2008) Bioorg Med Chem , vol.16 , pp. 7516-24
    • Tarrago, T.1    Kichik, N.2    Claasen, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.