메뉴 건너뛰기




Volumn 51, Issue 23, 2008, Pages 7514-7522

Prolyl oligopeptidase inhibition by N-acyl-pro-pyrrolidine-type molecules

Author keywords

[No Author keywords available]

Indexed keywords

N ACYL PROLYLPYRROLIDINE; PROLYL ENDOPEPTIDASE; PYRROLIDINE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 57349144413     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm800944x     Document Type: Article
Times cited : (38)

References (91)
  • 1
    • 0017650254 scopus 로고
    • Postproline cleaving enzyme: Identification as serine protease using active site specific inhibitors
    • Yoshimoto, T.; Orlowski, R. C.; Walter, R. Postproline cleaving enzyme: identification as serine protease using active site specific inhibitors. Biochemistry 1977, 16, 2942-2948.
    • (1977) Biochemistry , vol.16 , pp. 2942-2948
    • Yoshimoto, T.1    Orlowski, R.C.2    Walter, R.3
  • 2
    • 0023733678 scopus 로고
    • Porcine muscle prolyl endopeptidase and its endogenous substrates
    • Moriyama, A.; Nakanishi, M.; Sasaki, M. Porcine muscle prolyl endopeptidase and its endogenous substrates. J. Biochem. (Tokyo) 1988, 104, 112-117.
    • (1988) J. Biochem. (Tokyo) , vol.104 , pp. 112-117
    • Moriyama, A.1    Nakanishi, M.2    Sasaki, M.3
  • 3
    • 0015242348 scopus 로고
    • Leucylglycinamide released from oxytocin by human uterine enzyme
    • Walter, R.; Shlank, H.; Glass, J. D.; Schwartz, I. L.; Kerenyi, T. D. Leucylglycinamide released from oxytocin by human uterine enzyme. Science 1971, 173, 827-829.
    • (1971) Science , vol.173 , pp. 827-829
    • Walter, R.1    Shlank, H.2    Glass, J.D.3    Schwartz, I.L.4    Kerenyi, T.D.5
  • 4
    • 0017085135 scopus 로고
    • Post-proline cleaving enzyme. Purification of this endopeotidase by affinity chromatography
    • Koida, M.; Walter, R. Post-proline cleaving enzyme. Purification of this endopeotidase by affinity chromatography. J. Biol. Chem. 1976, 251, 7593-7599.
    • (1976) J. Biol. Chem , vol.251 , pp. 7593-7599
    • Koida, M.1    Walter, R.2
  • 5
    • 0018750650 scopus 로고
    • Postproline cleaving enzyme. Synthesis of a new fluorogenic substrate and distribution of the endopeptidase in rat tissues and body fluids of man
    • Yoshimoto, T.; Ogita, K.; Walter, R.; Koida, M.; Tsuru, D. Postproline cleaving enzyme. Synthesis of a new fluorogenic substrate and distribution of the endopeptidase in rat tissues and body fluids of man. Biochem. Biophys. Acta 1979, 569, 184-192.
    • (1979) Biochem. Biophys. Acta , vol.569 , pp. 184-192
    • Yoshimoto, T.1    Ogita, K.2    Walter, R.3    Koida, M.4    Tsuru, D.5
  • 6
    • 0018290958 scopus 로고
    • Purification and properties of prolyl endopeptidase from rabbit brain
    • Orlowski, M.; Wilk, E.; Pearce, S.; Wilk, S. Purification and properties of prolyl endopeptidase from rabbit brain. J. Neurochem. 1979, 33, 461-469.
    • (1979) J. Neurochem , vol.33 , pp. 461-469
    • Orlowski, M.1    Wilk, E.2    Pearce, S.3    Wilk, S.4
  • 7
    • 0018641022 scopus 로고
    • Characterization of 'thyroliberin-deamidating enzyme' as a post-proline-cleaving enzyme. Partial purification and enzyme-chemical analysis of the enzyme from anterior pituitary tissue
    • Knisatschek, H.; Bauer, K. Characterization of 'thyroliberin-deamidating enzyme' as a post-proline-cleaving enzyme. Partial purification and enzyme-chemical analysis of the enzyme from anterior pituitary tissue. J. Biol. Chem. 1979, 254, 10936-10943.
    • (1979) J. Biol. Chem , vol.254 , pp. 10936-10943
    • Knisatschek, H.1    Bauer, K.2
  • 8
    • 0019277674 scopus 로고
    • Distribution of postproline cleaving enzyme in human brain and peripheral tissues
    • Kato, T.; Okada, M.; Nagatsu, T. Distribution of postproline cleaving enzyme in human brain and peripheral tissues. Mol Cell. Biochem. 1980, 32, 117-121.
    • (1980) Mol Cell. Biochem , vol.32 , pp. 117-121
    • Kato, T.1    Okada, M.2    Nagatsu, T.3
  • 9
    • 0025797359 scopus 로고
    • Purification and characterization of human brain prolyl endopeptidase
    • Kalwant, S.; Porter, A. G. Purification and characterization of human brain prolyl endopeptidase. Biochem. J. 1991, 276, 237-244.
    • (1991) Biochem. J , vol.276 , pp. 237-244
    • Kalwant, S.1    Porter, A.G.2
  • 11
    • 0018287028 scopus 로고
    • Effect of oxytocin and vasopressin on memory consolidation: Sites of action and catecholaminergic correlates after local microinjections into limbic-midbrain structures
    • Kovacs, G. L.; Bohus, B.; Versteeg, D. H. G.; De Kloet, E. R.; De Wied, D. Effect of oxytocin and vasopressin on memory consolidation: sites of action and catecholaminergic correlates after local microinjections into limbic-midbrain structures. Brain Res. 1979, 175, 303-314.
    • (1979) Brain Res , vol.175 , pp. 303-314
    • Kovacs, G.L.1    Bohus, B.2    Versteeg, D.H.G.3    De Kloet, E.R.4    De Wied, D.5
  • 12
    • 0028217535 scopus 로고
    • Lower serum prolyl endopeptidase enzyme activity in major depression: Further evidence that peptidases play a role in the pathophysiology of depression
    • Maes, M.; Goossens, F.; Scharpé, S.; Meltzer, H. Y.; D'Hondt, P.; Cosyns, P. 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, 545-552.
    • (1994) Biol. Psychiatry , vol.35 , pp. 545-552
    • Maes, M.1    Goossens, F.2    Scharpé, S.3    Meltzer, H.Y.4    D'Hondt, P.5    Cosyns, P.6
  • 13
    • 0027406861 scopus 로고
    • A comparison of properties and enzymatic activities of three angiotensin processing enzymes: Angiotensin converting enzyme, prolyl endopeptidase and neutral endopeptidase 24.11
    • Welches, W. R.; Brosnihan, K. B.; Ferrario, C. M. A comparison of properties and enzymatic activities of three angiotensin processing enzymes: angiotensin converting enzyme, prolyl endopeptidase and neutral endopeptidase 24.11. Life. Sci. 1993, 52, 1461-1480.
    • (1993) Life. Sci , vol.52 , pp. 1461-1480
    • Welches, W.R.1    Brosnihan, K.B.2    Ferrario, C.M.3
  • 14
    • 33845477051 scopus 로고    scopus 로고
    • Suggested function for prolyl oligopeptidase: A puzzling paradox
    • (a) Brandt, I.; Schärpe, S.; Lambeir, A. M. Suggested function for prolyl oligopeptidase: A puzzling paradox. Clin. Chim. Acta 2007, 377, 50-61.
    • (2007) Clin. Chim. Acta , vol.377 , pp. 50-61
    • Brandt, I.1    Schärpe, S.2    Lambeir, A.M.3
  • 15
    • 23144447999 scopus 로고    scopus 로고
    • Pharmacogenetics in model systems: Defining a common mechanism of action for mood stabilizers
    • (b) Williams, R. S. B. Pharmacogenetics in model systems: Defining a common mechanism of action for mood stabilizers. Prog. Neuropsychopharmacol Biol. Psychiatry 2005, 29, 1029-1037.
    • (2005) Prog. Neuropsychopharmacol Biol. Psychiatry , vol.29 , pp. 1029-1037
    • Williams, R.S.B.1
  • 16
    • 0037118050 scopus 로고    scopus 로고
    • A common mechanism of action for three mood-stabilizing drugs
    • (c) Williams, R. S. B.; Cheng, L.; Mudge, A. W.; Harwood, A. J. A common mechanism of action for three mood-stabilizing drugs. Nature 2002, 417, 292-295.
    • (2002) Nature , vol.417 , pp. 292-295
    • Williams, R.S.B.1    Cheng, L.2    Mudge, A.W.3    Harwood, A.J.4
  • 19
  • 20
    • 13344282048 scopus 로고    scopus 로고
    • Prolyl oligopeptidase and bipolar disorder
    • (c) Williams, R. S. B. Prolyl oligopeptidase and bipolar disorder. Clin. Neurosci. Res. 2004, 4, 233-242.
    • (2004) Clin. Neurosci. Res , vol.4 , pp. 233-242
    • Williams, R.S.B.1
  • 22
    • 0031897652 scopus 로고    scopus 로고
    • Prolyl endopeptidase inhibitors: A new class of memory enhancing drugs
    • De Nanteuil, G.; Portevin, B.; Lepagnol, J. Prolyl endopeptidase inhibitors: a new class of memory enhancing drugs. Drugs Future 1998, 23, 167-179.
    • (1998) Drugs Future , vol.23 , pp. 167-179
    • De Nanteuil, G.1    Portevin, B.2    Lepagnol, J.3
  • 24
    • 0028827159 scopus 로고
    • The purification, characterization and analysis of primary and secondary structure of prolyl endopeptidase from human lymphocytes. Evidence that the enzyme belongs to the α;/β hydrolase fold family
    • Goossens, F.; De Meester, I.; Vanhoof, G.; Hendriks, D.; Vriend, G.; Scharpé, S. The purification, characterization and analysis of primary and secondary structure of prolyl endopeptidase from human lymphocytes. Evidence that the enzyme belongs to the α;/β hydrolase fold family. Eur. J. Biochem. 1995, 233, 432-441.
    • (1995) Eur. J. Biochem , vol.233 , pp. 432-441
    • Goossens, F.1    De Meester, I.2    Vanhoof, G.3    Hendriks, D.4    Vriend, G.5    Scharpé, S.6
  • 25
    • 0026669767 scopus 로고
    • Structural relationship between lipases and peptidases of the prolyl oligopeptidase family
    • Polgár, L. Structural relationship between lipases and peptidases of the prolyl oligopeptidase family. FEBS Lett. 1992, 311, 281-284.
    • (1992) FEBS Lett , vol.311 , pp. 281-284
    • Polgár, L.1
  • 26
    • 0032563162 scopus 로고    scopus 로고
    • Prolyl oligopeptidase: An unusual β-propeller domain regulates proteolysis
    • Fülöp, V.; Böcskei, Zs.; Polgár, L. Prolyl oligopeptidase: an unusual β-propeller domain regulates proteolysis. Cell 1998, 94, 161-170.
    • (1998) Cell , vol.94 , pp. 161-170
    • Fülöp, V.1    Böcskei, Z.2    Polgár, L.3
  • 27
    • 0032213932 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of porcine muscle prolyl oligopeptidase
    • Böcskei, Zs.; Fuxreiter, M.; Náray-Szabó, G.; Szabó, E.; Polgár, L. Crystallization and preliminary X-ray analysis of porcine muscle prolyl oligopeptidase. Acta Crystallogr. 1998, D54, 1414-1415.
    • (1998) Acta Crystallogr , vol.D54 , pp. 1414-1415
    • Böcskei, Z.1    Fuxreiter, M.2    Náray-Szabó, G.3    Szabó, E.4    Polgár, L.5
  • 28
    • 41949135032 scopus 로고    scopus 로고
    • Structure, function and biological relevance of prolyl oligopeptidase
    • (a) Szeltner, Z.; Polgár, L. Structure, function and biological relevance of prolyl oligopeptidase. Curr. Protein Pept. Sci. 2008, 9, 96-107.
    • (2008) Curr. Protein Pept. Sci , vol.9 , pp. 96-107
    • Szeltner, Z.1    Polgár, L.2
  • 29
    • 14844366112 scopus 로고    scopus 로고
    • Structural and mechanistic analysis of two prolyl endopeptidases: Role of interdomain dynamics in catalysis and specificity
    • (b) Shan, L.; Mathews, I. I.; Khosla, C. Structural and mechanistic analysis of two prolyl endopeptidases: Role of interdomain dynamics in catalysis and specificity. Proc. Natl. Acad. Sci. U.S.A. 2005, 102, 3599-3604.
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 3599-3604
    • Shan, L.1    Mathews, I.I.2    Khosla, C.3
  • 30
    • 23044435795 scopus 로고    scopus 로고
    • Flexibility of prolyl oligopeptidase: Molecular Dynamics and molecular framework analysis of the potential substrate pathways
    • (c) Fuxreiter, M.; Magyar, Cs.; Juhász, T.; Szeltner, Z.; Polgár, L.; Simon, I. Flexibility of prolyl oligopeptidase: Molecular Dynamics and molecular framework analysis of the potential substrate pathways. Proteins 2005, 60, 504-512.
    • (2005) Proteins , vol.60 , pp. 504-512
    • Fuxreiter, M.1    Magyar, C.2    Juhász, T.3    Szeltner, Z.4    Polgár, L.5    Simon, I.6
  • 31
    • 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.; Kado, K.; Tsuru, D. Comparison of inhibitory effects of prolinal-containing peptide derivatives on prolyl endopeptidases from bovine brain and Flavobacterium. J. Biochem. 1985, 98, 975-979.
    • (1985) J. Biochem , vol.98 , pp. 975-979
    • Yoshimoto, T.1    Kawahara, K.2    Matsubara, F.3    Kado, K.4    Tsuru, D.5
  • 32
    • 0034279642 scopus 로고    scopus 로고
    • Catalysis of serine oligopeptidases is controlled by a gating filter mechanism
    • Fülöp, V.; Szeltner, Z.; Polgár, L. Catalysis of serine oligopeptidases is controlled by a gating filter mechanism. EMBO Rep. 2000, 1, 277-281.
    • (2000) EMBO Rep , vol.1 , pp. 277-281
    • Fülöp, V.1    Szeltner, Z.2    Polgár, L.3
  • 33
    • 0035847042 scopus 로고    scopus 로고
    • Structures of prolyl oligopeptidase substrate/inhibitor complexes. Use of inhibitor binding for titration of the catalytic histidine residue
    • Fülöp, V.; Szeltner, Z.; Renner, V.; Polgár, L. Structures of prolyl oligopeptidase substrate/inhibitor complexes. Use of inhibitor binding for titration of the catalytic histidine residue. J. Biol. Chem. 2001, 276, 1262-1266.
    • (2001) J. Biol. Chem , vol.276 , pp. 1262-1266
    • Fülöp, V.1    Szeltner, Z.2    Renner, V.3    Polgár, L.4
  • 35
    • 0037044875 scopus 로고    scopus 로고
    • Electrostatic effects and binding determinants in the catalysis of prolyl oligopeptidase. Site-specific mutagenesis at the oxyanion binding site
    • Szeltner, Z.; Rea, D.; Renner, V.; Fülöp, V.; Polgár, L. Electrostatic effects and binding determinants in the catalysis of prolyl oligopeptidase. Site-specific mutagenesis at the oxyanion binding site. J. Biol. Chem. 2002, 277, 42613-42622.
    • (2002) J. Biol. Chem , vol.277 , pp. 42613-42622
    • Szeltner, Z.1    Rea, D.2    Renner, V.3    Fülöp, V.4    Polgár, L.5
  • 37
    • 33846608684 scopus 로고    scopus 로고
    • Jarho, E. M.; Venäläinen, J. I.; Poutiainen, S.; Leskinen, H.; Vepsnäläinen, J.; Christiaans, J. A. M.; Forsberg, M. M.; Männistö, P. T.; Wallén, E. A. A. 2(S)-(Cycloalk-1- enecarbonyl)-1-(4-phenylbutanoyl)pyrrolidines and 2(S)-(aroyl)-1-(4- phenylbutanoyl)pyrrolidines as prolyl oligopeptidase inhibitors. Bioorg. Med. Chem. 2007, 15, 2024-2031.
    • (b) Jarho, E. M.; Venäläinen, J. I.; Poutiainen, S.; Leskinen, H.; Vepsnäläinen, J.; Christiaans, J. A. M.; Forsberg, M. M.; Männistö, P. T.; Wallén, E. A. A. 2(S)-(Cycloalk-1- enecarbonyl)-1-(4-phenylbutanoyl)pyrrolidines and 2(S)-(aroyl)-1-(4- phenylbutanoyl)pyrrolidines as prolyl oligopeptidase inhibitors. Bioorg. Med. Chem. 2007, 15, 2024-2031.
  • 39
    • 28544442797 scopus 로고    scopus 로고
    • Venäläinen, J. I.; Wallén, E. A.; A.; Poso, A.; García-Horsman, J. A.; Männistö, P. T. Synthesis and characterization of the novel fluorescent prolyl oligopeptidase inhibitor 4-fluoresceinthiocarbonyl-6-aminocaproyl-L-prolyl-2(S)-hydroxyacetyl) pyrrolidine. J. Med. Chem. 2005, 48, 7093-7095.
    • (d) Venäläinen, J. I.; Wallén, E. A.; A.; Poso, A.; García-Horsman, J. A.; Männistö, P. T. Synthesis and characterization of the novel fluorescent prolyl oligopeptidase inhibitor 4-fluoresceinthiocarbonyl-6-aminocaproyl-L-prolyl-2(S)-hydroxyacetyl) pyrrolidine. J. Med. Chem. 2005, 48, 7093-7095.
  • 40
    • 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
    • (e) Jarho, E. M.; Wallén, E. A. A.; Christiaans, J. A. M.; Forsberg, M. M.; Venäläinen, J. I.; Männistö, P. T.; Gynther, J.; Poso, A. 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, 4772-4782.
    • (2005) J. Med. Chem , vol.48 , pp. 4772-4782
    • Jarho, E.M.1    Wallén, E.A.A.2    Christiaans, J.A.M.3    Forsberg, M.M.4    Venäläinen, J.I.5    Männistö, P.T.6    Gynther, J.7    Poso, A.8
  • 41
    • 7444243231 scopus 로고    scopus 로고
    • Jarho, E. M.; Venäläinen, J. I.; Huuskonen, J.; Christiaans, J. A. M.; García-Horsman, J. A.; Forsberg, M. M.; Järvinen, T.; Gynther, J.; Männistö, P. T.; Wallén, E. A. A. A cyclopent-2-enecarbonyl group mimics proline at the P2 position of prolyl oligopeptidase inhibitors. J. Med. Chem. 2004, 47, 5605-5607.
    • (f) Jarho, E. M.; Venäläinen, J. I.; Huuskonen, J.; Christiaans, J. A. M.; García-Horsman, J. A.; Forsberg, M. M.; Järvinen, T.; Gynther, J.; Männistö, P. T.; Wallén, E. A. A. A cyclopent-2-enecarbonyl group mimics proline at the P2 position of prolyl oligopeptidase inhibitors. J. Med. Chem. 2004, 47, 5605-5607.
  • 47
    • 1842331464 scopus 로고    scopus 로고
    • Conformational analysis of two inhibitors of prolyl endopeptidase: Comparison of 4-phenylbutyryl- and octanoyl-prolyl-pyrrolidine
    • Fehér, M.; Kánai, K.; Podányi, B.; Hermecz, I. Conformational analysis of two inhibitors of prolyl endopeptidase: comparison of 4-phenylbutyryl- and octanoyl-prolyl-pyrrolidine. Quant. Struct.-Act. Relat. 1997, 16, 136-141.
    • (1997) Quant. Struct.-Act. Relat , vol.16 , pp. 136-141
    • Fehér, M.1    Kánai, K.2    Podányi, B.3    Hermecz, I.4
  • 49
    • 57349161662 scopus 로고    scopus 로고
    • Chem. Abstr. 2000, 133, 86.
    • (2000) Chem. Abstr , vol.133 , pp. 86
  • 50
    • 0343953620 scopus 로고    scopus 로고
    • Prolyl endopeptidase inhibitors
    • Hermecz, I.; Kánai, K. Prolyl endopeptidase inhibitors. Il Farmaco 2000, 55, 188-190.
    • (2000) Il Farmaco , vol.55 , pp. 188-190
    • Hermecz, I.1    Kánai, K.2
  • 53
    • 0027443854 scopus 로고
    • Synthesis of prolyl endopeptidase inhibitors and evaluation of their structure-activity relationships: In vitro inhibition of prolyl endopeptidase from canine brain
    • Arai, H.; Nishioka, H.; Niwa, S.; Yamanaka, I.; Tanaka, Y.; Yoshinaga, K.; Kobayashi, N.; Miura, N.; Ikade, Y. Synthesis of prolyl endopeptidase inhibitors and evaluation of their structure-activity relationships: in vitro inhibition of prolyl endopeptidase from canine brain. Chem. Pharm. Bull. 1993, 41, 1583-1588.
    • (1993) Chem. Pharm. Bull , vol.41 , pp. 1583-1588
    • Arai, H.1    Nishioka, H.2    Niwa, S.3    Yamanaka, I.4    Tanaka, Y.5    Yoshinaga, K.6    Kobayashi, N.7    Miura, N.8    Ikade, Y.9
  • 54
    • 0018576997 scopus 로고
    • Hypolipidemic activity of phthalimide derivatives. 1. N-substituted phthalimide derivatives
    • Chapman, J. M.; Cocolas, G. H.; Hall, I. H. Hypolipidemic activity of phthalimide derivatives. 1. N-substituted phthalimide derivatives. J. Med. Chem. 1979, 22, 1399-1402.
    • (1979) J. Med. Chem , vol.22 , pp. 1399-1402
    • Chapman, J.M.1    Cocolas, G.H.2    Hall, I.H.3
  • 55
    • 0014288435 scopus 로고
    • Substitution in the hydantoin ring. VII. N-propionic acid and its ethyl ester and N-3-(2-cyanoethyl) derivatives
    • (a) Shaffer, J. W.; Steinberg, E.; Krimsley, V.; Winstead, M. B. Substitution in the hydantoin ring. VII. N-propionic acid and its ethyl ester and N-3-(2-cyanoethyl) derivatives. J. Med. Chem. 1968, 11, 462-466.
    • (1968) J. Med. Chem , vol.11 , pp. 462-466
    • Shaffer, J.W.1    Steinberg, E.2    Krimsley, V.3    Winstead, M.B.4
  • 56
    • 0022217733 scopus 로고    scopus 로고
    • Result of spin immunoassay for simultaneous measurement of phenytoin and phenobarbital in serum compared with those of liquid chromatography
    • (b) Sayo, H.; Hosokawa, M. Result of spin immunoassay for simultaneous measurement of phenytoin and phenobarbital in serum compared with those of liquid chromatography. Chem. Pharm. Bull. 1998, 33, 2866-2870.
    • (1998) Chem. Pharm. Bull , vol.33 , pp. 2866-2870
    • Sayo, H.1    Hosokawa, M.2
  • 57
    • 0001280221 scopus 로고    scopus 로고
    • Nishio, T. (2 + 2) photocycloaddition of the carbon-nitrogen double bond of quinoxalin-2(1H)-ones to electron-deficient olefins. J. Org. Chem. 1984, 49, 827-832.
    • Nishio, T. (2 + 2) photocycloaddition of the carbon-nitrogen double bond of quinoxalin-2(1H)-ones to electron-deficient olefins. J. Org. Chem. 1984, 49, 827-832.
  • 58
    • 49449097238 scopus 로고    scopus 로고
    • The many roles for fluorine in medicinal chemistry
    • (a) Hagmann, W. K. The many roles for fluorine in medicinal chemistry. J. Med. Chem. 2008, 51, 4359-4369.
    • (2008) J. Med. Chem , vol.51 , pp. 4359-4369
    • Hagmann, W.K.1
  • 60
    • 35348938545 scopus 로고    scopus 로고
    • The role of fluorine in medicinal chemistry
    • (c) Shah, P.; Westwell, A. D. The role of fluorine in medicinal chemistry. J. Enzyme Inhib. Med. Chem. 2007, 22, 527-540.
    • (2007) J. Enzyme Inhib. Med. Chem , vol.22 , pp. 527-540
    • Shah, P.1    Westwell, A.D.2
  • 61
    • 34848848499 scopus 로고    scopus 로고
    • Fluorine in pharmaceuticals: Looking beyond intuition
    • (d) Müller, K.; Faeh, C.; Diederich, F. Fluorine in pharmaceuticals: Looking beyond intuition. Science 2007, 317, 1881-1886.
    • (2007) Science , vol.317 , pp. 1881-1886
    • Müller, K.1    Faeh, C.2    Diederich, F.3
  • 62
    • 0036430153 scopus 로고    scopus 로고
    • Fluorinated amino acids in protein design and engineering
    • (e) Yoder, N. C.; Kumar, K. Fluorinated amino acids in protein design and engineering. Chem. Soc. Rev. 2002, 31, 335-341.
    • (2002) Chem. Soc. Rev , vol.31 , pp. 335-341
    • Yoder, N.C.1    Kumar, K.2
  • 63
    • 1842663065 scopus 로고    scopus 로고
    • Some influences of fluorine in bioorganic chemistry
    • (f) O'Hagan, D.; Rzepa, H. S. Some influences of fluorine in bioorganic chemistry. Chem. Commun. 1997, 645-652.
    • (1997) Chem. Commun , pp. 645-652
    • O'Hagan, D.1    Rzepa, H.S.2
  • 64
    • 84986637914 scopus 로고
    • What is the structure of peptide antibiotic Tü 1718 B? previously proposed structure disproved by synthesis
    • Posteis, H.-T.; König, W. A. What is the structure of peptide antibiotic Tü 1718 B? previously proposed structure disproved by synthesis. Liebigs Ann. Chem. 1992, 1281-1287.
    • (1992) Liebigs Ann. Chem , pp. 1281-1287
    • Posteis, H.-T.1    König, W.A.2
  • 65
    • 0032485422 scopus 로고    scopus 로고
    • Practical synthesis of Boc and Fmoc protected 4-fluoro and 4-difluoroprolines from trans-4-hydroxyroproline
    • (a) Demange, L.; Ménez, A. É.; Dugave, C. Practical synthesis of Boc and Fmoc protected 4-fluoro and 4-difluoroprolines from trans-4-hydroxyroproline. Tetrahedron Lett. 1998, 39, 1169-1172.
    • (1998) Tetrahedron Lett , vol.39 , pp. 1169-1172
    • Demange, L.1    Ménez, A.E.2    Dugave, C.3
  • 66
    • 33847800447 scopus 로고
    • New fluorinating reagents. Dialkylaminosulfur fluorides
    • (b) Middleton, W. J. New fluorinating reagents. Dialkylaminosulfur fluorides. J. Org. Chem. 1975, 40, 574-578.
    • (1975) J. Org. Chem , vol.40 , pp. 574-578
    • Middleton, W.J.1
  • 67
    • 0033121421 scopus 로고    scopus 로고
    • Investigations on flexible prolyl-endopeptidase inhibitor in solution by NMR techniques
    • Podányi, B.; Bokotey, S.; Kánai, K.; Fehér, M.; Hermecz, I. Investigations on flexible prolyl-endopeptidase inhibitor in solution by NMR techniques. Magn. Reson. Chem. 1999, 37, 346-352.
    • (1999) Magn. Reson. Chem , vol.37 , pp. 346-352
    • Podányi, B.1    Bokotey, S.2    Kánai, K.3    Fehér, M.4    Hermecz, I.5
  • 69
    • 0025762537 scopus 로고
    • pH-Dependent mechanism in the catalysis of prolyl oligopeptidase from pig muscle
    • Polgár, L. pH-Dependent mechanism in the catalysis of prolyl oligopeptidase from pig muscle. Eur. J. Biochem. 1991, 197, 441-447.
    • (1991) Eur. J. Biochem , vol.197 , pp. 441-447
    • Polgár, L.1
  • 70
    • 0028672897 scopus 로고
    • Prolyl oligopeptidases
    • Polgár, L. Prolyl oligopeptidases. Methods Enzymol. 1994, 244, 188-200.
    • (1994) Methods Enzymol , vol.244 , pp. 188-200
    • Polgár, L.1
  • 71
    • 0002414103 scopus 로고
    • Molecular data processing
    • Moras, D, Podjarny, A, Thierry, J, Eds, Oxford University Press: Oxford, chapter 4, pp
    • Leslie, A. G. W. Molecular data processing. In Crystallographic Computing 5: From Chemistry to Biology, Moras, D., Podjarny, A., Thierry, J., Eds.; Oxford University Press: Oxford, 1991; chapter 4, pp 50-61.
    • (1991) Crystallographic Computing 5: From Chemistry to Biology , pp. 50-61
    • Leslie, A.G.W.1
  • 72
    • 57349145981 scopus 로고    scopus 로고
    • BioteX, Version 1.0, Molecular Structure Corporation, The Woodlands, TX, 1995
    • BioteX, Version 1.0, Molecular Structure Corporation, The Woodlands, TX, 1995.
  • 73
    • 0002584126 scopus 로고
    • Proc. of CCP4 Study Weekend on Data Collection & Processing
    • Evans, P. R. Proc. of CCP4 Study Weekend on Data Collection & Processing. Data Reduction 1993, 114-122.
    • (1993) Data Reduction , pp. 114-122
    • Evans, P.R.1
  • 74
    • 0000952473 scopus 로고
    • On the treatment of negative intensity observations
    • French, S.; Wilson, K. On the treatment of negative intensity observations. Acta Crystallogr. 1978, A34, 517-525.
    • (1978) Acta Crystallogr , vol.A34 , pp. 517-525
    • French, S.1    Wilson, K.2
  • 75
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. AMoRe: an automated package for molecular replacement. Acta Crystallogr. 1994, A50, 157-163.
    • (1994) Acta Crystallogr , vol.A50 , pp. 157-163
    • Navaza, J.1
  • 76
    • 0028103275 scopus 로고
    • CCP4 suite: Programs for protein crystallography
    • Collaborative Computing Project 4 The
    • Collaborative Computing Project 4 The CCP4 suite: programs for protein crystallography Acta Cryst. 1994, D50, 760-763.
    • (1994) Acta Cryst , vol.D50 , pp. 760-763
  • 78
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A.; Zou, J.-Y.; Cowan, S. W.; Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. 1994, A47, 110-119.
    • (1994) Acta Crystallogr , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 80
    • 0028155689 scopus 로고
    • A new method for predicting binding affinity in computer-aided drug design
    • Aqvist, J.; Medina, C.; Samuelsson, J.-E. A new method for predicting binding affinity in computer-aided drug design. Protein Eng. 1994, 7, 385-391.
    • (1994) Protein Eng , vol.7 , pp. 385-391
    • Aqvist, J.1    Medina, C.2    Samuelsson, J.-E.3
  • 82
    • 0029011701 scopus 로고    scopus 로고
    • Cornell, W. D.; Cieplak, P.; Bayly, C. I.; Gould, I. R.; Merz, K. M., Jr.; Ferguson, D. M.; Spellmeyer, D. C.; Fox, T.; Caldwell, J. W.; Kollman, P. A. A second generation force field for the simulation of proteins, nucleic acids, and organic molecules. J. Am. Chem. Soc. 1995, 117, 5179-5197.
    • Cornell, W. D.; Cieplak, P.; Bayly, C. I.; Gould, I. R.; Merz, K. M., Jr.; Ferguson, D. M.; Spellmeyer, D. C.; Fox, T.; Caldwell, J. W.; Kollman, P. A. A second generation force field for the simulation of proteins, nucleic acids, and organic molecules. J. Am. Chem. Soc. 1995, 117, 5179-5197.
  • 83
    • 0001389325 scopus 로고
    • Charges derived from distributed multipole series
    • Ferenczy, G. G. Charges derived from distributed multipole series. J. Comput. Chem. 1991, 12, 913-917.
    • (1991) J. Comput. Chem , vol.12 , pp. 913-917
    • Ferenczy, G.G.1
  • 84
    • 0001675597 scopus 로고
    • Transferable net atomic charges from a distributed multipole analysis for the description of electrostatic properties: A case study of saturated hydrocarbons
    • Chipot, C.; Ángyán, J. G.; Ferenczy, G. G.; Scheraga, H. A. Transferable net atomic charges from a distributed multipole analysis for the description of electrostatic properties: a case study of saturated hydrocarbons. J. Phys. Chem. 1993, 97, 6628-6636.
    • (1993) J. Phys. Chem , vol.97 , pp. 6628-6636
    • Chipot, C.1    Ángyán, J.G.2    Ferenczy, G.G.3    Scheraga, H.A.4
  • 85
    • 57349086515 scopus 로고    scopus 로고
    • Frisch, M. J, Trucks, G. W, Schlegel, H. B, Scuseria, G. E, Robb, M. A, Cheeseman, J. R, Zakrzewski, V. G, Montgomery, Jr. J. A, Stratmann, R. E, Burant, J. C, Dapprich, S, Millam, J. M, Daniels, A. D, Kudin, K. N, Strain, M. C, Farkas, Ö, Tomas:, J, Barone, V, Cossi, M, Cammi, R, Mennucci, B, Pomelli, C, Adamo, C, Clifford, S, Ochterski, J, Petersson, G. A, Ayala, P. Y, Cui, Q, Morokuma, K, Malick, D. K, Rabuck, A. D, Raghavachari, K, Foresman, J. B, Cioslowski, J, Ortiz, J. V, Stefanov, B. B, Liu, G, Liashenko, A, Piskorz, P, Komáromi, I, Gomperts, R, Martin, R. L, Fox, D. J, Keith, T, Al-Laham, M. A, Peng, C. Y, Nanayakkara, A, Gonzalez, C, Challacombe, M, Gill, P. M. W, Johnson, B, Chen, W, Wong, M. W, Andres, J. L, Gonzalez, C, Head-Gordon, M, Replogle, E. S, Pople, J. A. Gaussian 98, revision A.6; Gaussian, Inc, Pittsburgh PA, 1998
    • Frisch, M. J.; Trucks, G. W.; Schlegel, H. B.; Scuseria, G. E.; Robb, M. A.; Cheeseman, J. R.; Zakrzewski, V. G.; Montgomery, Jr. J. A.; Stratmann, R. E.; Burant, J. C.; Dapprich, S.; Millam, J. M.; Daniels, A. D.; Kudin, K. N.; Strain, M. C.; Farkas, Ö.; Tomas:, J.; Barone, V.; Cossi, M.; Cammi, R.; Mennucci, B.; Pomelli, C.; Adamo, C.; Clifford, S.; Ochterski, J.; Petersson, G. A.; Ayala, P. Y.; Cui, Q.; Morokuma, K.; Malick, D. K.; Rabuck, A. D.; Raghavachari, K.; Foresman, J. B.; Cioslowski, J.; Ortiz, J. V.; Stefanov, B. B.; Liu, G.; Liashenko, A.; Piskorz, P.; Komáromi, I.; Gomperts, R.; Martin, R. L.; Fox, D. J.; Keith, T.; Al-Laham, M. A.; Peng, C. Y.; Nanayakkara, A.; Gonzalez, C.; Challacombe, M.; Gill, P. M. W.; Johnson, B.; Chen, W.; Wong, M. W.; Andres, J. L.; Gonzalez, C.; Head-Gordon, M.; Replogle, E. S.; Pople, J. A. Gaussian 98, revision A.6; Gaussian, Inc.: Pittsburgh PA, 1998.
  • 86
    • 33646940952 scopus 로고
    • Numerical integration of the Cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • Ryckaert, J.-P.; Ciccotti, G.; Berendsen, H. J. C. Numerical integration of the Cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes. J. Comput. Phys. 1977, 23, 327-341.
    • (1977) J. Comput. Phys , vol.23 , pp. 327-341
    • Ryckaert, J.-P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 87
    • 84946450438 scopus 로고
    • Algorithms for macromolecular dynamics and constraint dynamics
    • van Gunsteren, W. F.; Berendsen, H. J. C. Algorithms for macromolecular dynamics and constraint dynamics. Mol. Phys. 1977, 34, 1311-1327.
    • (1977) Mol. Phys , vol.34 , pp. 1311-1327
    • van Gunsteren, W.F.1    Berendsen, H.J.C.2
  • 89
    • 57349176678 scopus 로고    scopus 로고
    • SYBYL Version 6.7, Tripos. Inc, St. Louis, MO
    • SYBYL Version 6.7, Tripos. Inc., St. Louis, MO.
  • 91
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 1991, 24, 945-949.
    • (1991) J. Appl. Crystallogr , vol.24 , pp. 945-949
    • Kraulis, P.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.