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Volumn 48, Issue 24, 2005, Pages 7688-7707

Interaction of papain-like cysteine proteases with dipeptide-derived nitriles

Author keywords

[No Author keywords available]

Indexed keywords

ACETONE; ALDEHYDE; AMINOACETONITRILE; BROMINE; CATHEPSIN K; CATHEPSIN L; CATHEPSIN S; CYSTEINE PROTEINASE; CYSTEINE PROTEINASE INHIBITOR; DIPEPTIDE; ENZYME INHIBITOR; FLUORINE; N (BENZYLOXYCARBONYL)GLYCYLGLYCINE NITRILE; N (BENZYLOXYCARBONYL)LEUCYLGLYCINE NITRILE; N (TERT BUTOXYCARBONYL) 2 AMINOBUTANOYLGLYCINE NITRILE; N (TERT BUTOXYCARBONYL)ALANYLGLYCINE NITRILE; N (TERT BUTOXYCARBONYL)CYCLOHEXYLALANYLGLYCINE NITRILE; N (TERT BUTOXYCARBONYL)CYCLOPROPYLALANYLGLYCINE NITRILE; N (TERT BUTOXYCARBONYL)GLYCYLGLYCINE NITRILE; N (TERT BUTOXYCARBONYL)ISOLEUCYLGLYCINE NITRILE; N (TERT BUTOXYCARBONYL)LEUCYLGLYCINE NITRILE; N (TERT BUTOXYCARBONYL)METHIONYLGLYCINE NITRILE; N (TERT BUTOXYCARBONYL)NORLEUCYLGLYCINE NITRILE; N (TERT BUTOXYCARBONYL)NORVALYLGLYCINE NITRILE; N (TERT BUTOXYCARBONYL)PHENYLALANYLGLYCINE NITRILE; N (TERT BUTOXYCARBONYL)VALYLGLYCINE NITRLE; NITRILE; PAPAIN; PHENYLALANINE; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 28144443719     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm050686b     Document Type: Article
Times cited : (80)

References (66)
  • 1
    • 0036260967 scopus 로고    scopus 로고
    • Thiol-dependent enzymes and their inhibitors: A review
    • Leung-Tong, R.; Li, W.; Tam, T. F.; Karimian, K. Thiol-Dependent Enzymes and Their Inhibitors: A Review. Curr. Med. Chem. 2002, 9, 979-1002.
    • (2002) Curr. Med. Chem. , vol.9 , pp. 979-1002
    • Leung-Tong, R.1    Li, W.2    Tam, T.F.3    Karimian, K.4
  • 3
    • 0034930561 scopus 로고    scopus 로고
    • Evolutionary lines of cysteine proteinases
    • Barrett, A. J.; Rawlings, N. D. Evolutionary Lines of Cysteine Proteinases. Biol. Chem. 2001, 382, 727-733.
    • (2001) Biol. Chem. , vol.382 , pp. 727-733
    • Barrett, A.J.1    Rawlings, N.D.2
  • 4
    • 0036882393 scopus 로고    scopus 로고
    • Human and parasitic papain-like cysteine proteases: Their role in physiology and pathology and recent developments in inhibitor design
    • Lecaille, F.; Kaleta, J.; Brömme, D. Human and Parasitic Papain-Like Cysteine Proteases: Their Role in Physiology and Pathology and Recent Developments in Inhibitor Design. Chem. Rev. 2002, 102, 4459-4488.
    • (2002) Chem. Rev. , vol.102 , pp. 4459-4488
    • Lecaille, F.1    Kaleta, J.2    Brömme, D.3
  • 5
    • 1542495414 scopus 로고    scopus 로고
    • Papain-like lysosomal cysteine proteases and their inhibitors: Drug discovery targets?
    • Turk, D.; Turk, B.; Turk, V. Papain-like lysosomal cysteine proteases and their inhibitors: drug discovery targets? Biochem. Soc. Symp. 2003, 70, 15-30.
    • (2003) Biochem. Soc. Symp. , vol.70 , pp. 15-30
    • Turk, D.1    Turk, B.2    Turk, V.3
  • 7
    • 0035801514 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases: Facts and opportunities
    • Turk, V.; Turk, B.; Turk, D. Lysosomal cysteine proteases: facts and opportunities. EMBO J. 2001, 20, 4629-4633.
    • (2001) EMBO J , vol.20 , pp. 4629-4633
    • Turk, V.1    Turk, B.2    Turk, D.3
  • 9
    • 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, 157-162.
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 10
    • 0345310073 scopus 로고    scopus 로고
    • Revised definition of substrate binding sites of Papain-like cysteine proteases
    • Turk, D.; Guncar, G.; Podobnik, M.; Turk, B. Revised Definition of Substrate Binding Sites of Papain-Like Cysteine Proteases. Biol. Chem. 1998, 379, 137-147.
    • (1998) Biol. Chem. , vol.379 , pp. 137-147
    • Turk, D.1    Guncar, G.2    Podobnik, M.3    Turk, B.4
  • 11
    • 0034615570 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases: More than scavengers
    • Turk, B.; Turk, D.; Turk, V. Lysosomal cysteine proteases: more than scavengers. Biochim. Biophys. Acta 2000, 1477, 98-111.
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 98-111
    • Turk, B.1    Turk, D.2    Turk, V.3
  • 12
    • 0037810410 scopus 로고    scopus 로고
    • Family C1 cysteine proteases: Biological diversity or redundancy?
    • Nägler, D. K.; Menard, R. Family C1 Cysteine Proteases: Biological Diversity or Redundancy? Biol. Chem. 2003, 384, 837-843.
    • (2003) Biol. Chem. , vol.384 , pp. 837-843
    • Nägler, D.K.1    Menard, R.2
  • 15
    • 10844291804 scopus 로고    scopus 로고
    • Cysteine cathepsins are central contributors of invasion by cultured adenosylmethionine decarboxylase-transformed rodent fibroblasts
    • Ravanko, K.; Järvinen, K.; Helin, J.; Kalkkinen, N.; Hölttä, E. Cysteine Cathepsins Are Central Contributors of Invasion by Cultured Adenosylmethionine Decarboxylase-Transformed Rodent Fibroblasts. Cancer Res. 2004, 64, 8831-8838.
    • (2004) Cancer Res , vol.64 , pp. 8831-8838
    • Ravanko, K.1    Järvinen, K.2    Helin, J.3    Kalkkinen, N.4    Hölttä, E.5
  • 16
    • 1642535587 scopus 로고    scopus 로고
    • Inhibition of tumorigenicity and metastasis of human melanoma cells by anti-cathepsin L single chain variable fragment
    • Rousselet, N.; Mills, L.; Jean, D.; Tellez, C.; Bar-Eli, M.; Frade; R. Inhibition of Tumorigenicity and Metastasis of Human Melanoma Cells by Anti-Cathepsin L Single Chain Variable Fragment. Cancer Res. 2004, 64, 146-151.
    • (2004) Cancer Res , vol.64 , pp. 146-151
    • Rousselet, N.1    Mills, L.2    Jean, D.3    Tellez, C.4    Bar-Eli, M.5    Frade, R.6
  • 17
    • 0037805704 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases regulate antigen presentation
    • Honey, K.; Rudensky, A. Y. Lysosomal Cysteine Proteases Regulate Antigen Presentation. Nat. Rev. Immunol. 2003, 3, 472-482.
    • (2003) Nat. Rev. Immunol. , vol.3 , pp. 472-482
    • Honey, K.1    Rudensky, A.Y.2
  • 18
    • 12444288446 scopus 로고    scopus 로고
    • Cathepsin S controls MHC class II-mediated antigen presentaion of epithelial cells in vivo
    • Beers, C.; Burich, A.; Kleijmeer, M. J.; Griffith, J. M.; Wong, P.; Rudensky, A. Y. Cathepsin S Controls MHC Class II-Mediated Antigen Presentaion of Epithelial Cells In Vivo. J. Immunol. 2005, 175, 1205-1212.
    • (2005) J. Immunol. , vol.175 , pp. 1205-1212
    • Beers, C.1    Burich, A.2    Kleijmeer, M.J.3    Griffith, J.M.4    Wong, P.5    Rudensky, A.Y.6
  • 19
    • 12444250686 scopus 로고    scopus 로고
    • Cathepsin S is required for murine autoimmune myasthenia gravis pathogenesis
    • Yang, H.; Kala, M.; Scott, B. G.; Goluszko, E.; Chapman, H. A.; Christadoss, P. Cathepsin S Is Required for Murine Autoimmune Myasthenia gravis Pathogenesis. J. Immunol. 2005, 174, 1729-1737.
    • (2005) J. Immunol. , vol.174 , pp. 1729-1737
    • Yang, H.1    Kala, M.2    Scott, B.G.3    Goluszko, E.4    Chapman, H.A.5    Christadoss, P.6
  • 20
    • 0030026637 scopus 로고    scopus 로고
    • Human cathepsin O2, a matrix protein-degrading cysteine protease expressed in osteoclasts
    • Brömme, D.; Okamoto, K.; Wang, B. B.; Biroc, S. Human Cathepsin O2, a Matrix Protein-degrading Cysteine Protease Expressed in Osteoclasts. J. Biol. Chem. 1998, 271, 2126-2132.
    • (1998) J. Biol. Chem. , vol.271 , pp. 2126-2132
    • Brömme, D.1    Okamoto, K.2    Wang, B.B.3    Biroc, S.4
  • 22
    • 0037047275 scopus 로고    scopus 로고
    • Collagenase activity of cathepsin K depends on complex formation with chondroitin sulfate
    • Li, Z.; Hou, W.-S.; Escalente-Torres, C. R.; Gelb, B. D.; Brömme, D. Collagenase Activity of Cathepsin K Depends on Complex Formation with Chondroitin Sulfate. J. Biol. Chem. 2002, 277, 28669-28676.
    • (2002) J. Biol. Chem. , vol.277 , pp. 28669-28676
    • Li, Z.1    Hou, W.-S.2    Escalente-Torres, C.R.3    Gelb, B.D.4    Brömme, D.5
  • 23
    • 0025033039 scopus 로고
    • Cysteinyl proteinases and their selective inactivation
    • Shaw, E. Cysteinyl Proteinases and their Selective Inactivation. Adv. Enzymol. Relat. Areas Mol. Biol. 1990, 63, 271-347.
    • (1990) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.63 , pp. 271-347
    • Shaw, E.1
  • 24
    • 0343433408 scopus 로고    scopus 로고
    • Cysteine proteases and their inhibitors
    • Otto, H.-H.; Schirmeister, T. Cysteine Proteases and Their Inhibitors. Chem. Rev. 1997, 97, 133-171.
    • (1997) Chem. Rev. , vol.97 , pp. 133-171
    • Otto, H.-H.1    Schirmeister, T.2
  • 28
    • 0022977803 scopus 로고
    • Benzoylamidoacetonitrile is bound as a thioimidate in the active site of Papain
    • Brisson, J.-R.; Carey, P. R.; Storer, A. C. Benzoylamidoacetonitrile Is Bound as a Thioimidate in the Active Site of Papain. J. Biol. Chem. 1986, 261, 9087-9089.
    • (1986) J. Biol. Chem. , vol.261 , pp. 9087-9089
    • Brisson, J.-R.1    Carey, P.R.2    Storer, A.C.3
  • 29
    • 0023098601 scopus 로고
    • Inhibition of Papain by nitriles: Mechanistic studies using NMR and kinetic measurements
    • Liang, T.-C.; Abeles, R. H. Inhibition of Papain by Nitriles: Mechanistic Studies Using NMR and Kinetic Measurements. Arch. Biochem. Biophys. 1987, 252, 626-634.
    • (1987) Arch. Biochem. Biophys. , vol.252 , pp. 626-634
    • Liang, T.-C.1    Abeles, R.H.2
  • 30
    • 0021094368 scopus 로고
    • Transition-state stabilization at the oxyanion binding sites of serine and thiol proteinases: Hydrolyses of thiono and oxygen esters
    • Asboth, B.; Polgar, L. Transition-State Stabilization at the Oxyanion Binding Sites of Serine and Thiol Proteinases: Hydrolyses of Thiono and Oxygen Esters. Biochemistry 1983, 22, 117-122.
    • (1983) Biochemistry , vol.22 , pp. 117-122
    • Asboth, B.1    Polgar, L.2
  • 31
    • 0021920109 scopus 로고
    • Mechanism of action of cysteine proteinases: Oxyanion binding site is not essential in the hydrolysis of specific substrates
    • Asboth, B.; Stokum, E.; Khan, I. U.; Polgar, L. Mechanism of Action of Cysteine Proteinases: Oxyanion Binding Site Is Not Essential in the Hydrolysis of Specific Substrates. Biochemistry 1985, 24, 606-609.
    • (1985) Biochemistry , vol.24 , pp. 606-609
    • Asboth, B.1    Stokum, E.2    Khan, I.U.3    Polgar, L.4
  • 32
    • 84952232383 scopus 로고
    • Über peptidsynthesen. 3. Die verwendung von anhydriden aus N-acylierten aminosäuren und derivaten anorganischer säuren
    • Wieland, T.; Bernhard, H. Über Peptidsynthesen. 3. Die Verwendung von Anhydriden aus N-acylierten Aminosäuren und Derivaten anorganischer Säuren. Liebigs Ann. Chem. 1951, 572, 190-194.
    • (1951) Liebigs Ann. Chem. , vol.572 , pp. 190-194
    • Wieland, T.1    Bernhard, H.2
  • 33
    • 2042507954 scopus 로고
    • Palladium-catalyzed cross-coupling reactions of organoboron compounds
    • Miyaura, N.; Suzuki, A. Palladium-Catalyzed Cross-Coupling Reactions of Organoboron Compounds. Chem. Rev. 1995, 95, 2547-2483.
    • (1995) Chem. Rev. , vol.95 , pp. 2547-12483
    • Miyaura, N.1    Suzuki, A.2
  • 34
    • 0036738330 scopus 로고    scopus 로고
    • Microwave-accelerated homogeneous catalysis in organic chemistry
    • Larhed, M.; Moberg, C.; Hallberg, A. Microwave-Accelerated Homogeneous Catalysis in Organic Chemistry. Acc. Chem. Res. 2002, 35, 717-727.
    • (2002) Acc. Chem. Res. , vol.35 , pp. 717-727
    • Larhed, M.1    Moberg, C.2    Hallberg, A.3
  • 35
    • 0041570557 scopus 로고    scopus 로고
    • Direct synthesis of unprotected 4-aryl phenylalanines via the Suzuki reaction under microwave irradiation
    • Gong, Y.; He, W. Direct Synthesis of Unprotected 4-Aryl Phenylalanines via the Suzuki Reaction under Microwave Irradiation. Org. Lett. 2002, 4, 3803-3805.
    • (2002) Org. Lett. , vol.4 , pp. 3803-3805
    • Gong, Y.1    He, W.2
  • 36
    • 0025803608 scopus 로고
    • Sodium cyanoborohydride reduction of (benzyloxycarbonyl)- and (tert-butoxycarbonyl)hydrazones
    • Calabretta, R.; Gallina, C.; Giordano, C. Sodium cyanoborohydride reduction of (benzyloxycarbonyl)- and (tert-butoxycarbonyl)hydrazones. Synthesis 1991, 536-539.
    • (1991) Synthesis , pp. 536-539
    • Calabretta, R.1    Gallina, C.2    Giordano, C.3
  • 39
    • 27844466269 scopus 로고
    • N-methoxy-N-methylamides as effective acylating agents
    • Nahm, S.; Weinreb, S. M. N-Methoxy-N-methylamides as Effective Acylating Agents. Tetrahedron Lett. 1981, 22, 3815-3818.
    • (1981) Tetrahedron Lett , vol.22 , pp. 3815-3818
    • Nahm, S.1    Weinreb, S.M.2
  • 40
    • 0242417008 scopus 로고    scopus 로고
    • Interaction with aromatic rings in chemical and biological recognition
    • Meyer, E. A.; Castellano, R. K.; Diederich, F. Interaction with Aromatic Rings in Chemical and Biological Recognition. Angew. Chem., Int. Ed. 2003, 42, 1210-1240.
    • (2003) Angew. Chem., Int. Ed. , vol.42 , pp. 1210-1240
    • Meyer, E.A.1    Castellano, R.K.2    Diederich, F.3
  • 41
    • 0037663879 scopus 로고    scopus 로고
    • A fluorine scan of thrombin inhibitors to map the fluorophilicity/ fluorophobicity of an enzyme active site: Evidence for C-F⋯C=O interactions
    • Olsen, J. A.; Banner, D. W.; Seiler, P.; Obst-Sander, U.; D'Arcy, A.; Stihle, M.; Müller, K.; Diederich, F. A Fluorine Scan of Thrombin Inhibitors to Map the Fluorophilicity/Fluorophobicity of an Enzyme Active Site: Evidence for C-F⋯C=O Interactions. Angew. Chem., Int. Ed. 2003, 42, 2507-2511.
    • (2003) Angew. Chem., Int. Ed. , vol.42 , pp. 2507-2511
    • Olsen, J.A.1    Banner, D.W.2    Seiler, P.3    Obst-Sander, U.4    D'Arcy, A.5    Stihle, M.6    Müller, K.7    Diederich, F.8
  • 42
    • 4544318450 scopus 로고    scopus 로고
    • Fluorine interactions at the thrombin active site: Protein backbone fragments H-C-C=O comprise a favorable C-F environment and interactions of C-F with electrophiles
    • Olsen, J. A.; Banner, D. W.; Seiler, P.; Wagner, B.; Tschopp, T.; Obst-Sander, U.; Kansy, M.; Müller, K.; Diederich, F. Fluorine Interactions at the Thrombin Active Site: Protein Backbone Fragments H-C-C=O Comprise a Favorable C-F Environment and Interactions of C-F with Electrophiles. ChemBioChem 2004, 5, 666-675.
    • (2004) ChemBioChem , vol.5 , pp. 666-675
    • Olsen, J.A.1    Banner, D.W.2    Seiler, P.3    Wagner, B.4    Tschopp, T.5    Obst-Sander, U.6    Kansy, M.7    Müller, K.8    Diederich, F.9
  • 44
    • 17244364283 scopus 로고    scopus 로고
    • Proteases universally recognize beta strands in their active sites
    • Tyndall, J.; Nall, T.; Fairlie, D. P. Proteases Universally Recognize Beta Strands In Their Active Sites. Chem. Rev. 2005, 105, 973-999.
    • (2005) Chem. Rev. , vol.105 , pp. 973-999
    • Tyndall, J.1    Nall, T.2    Fairlie, D.P.3
  • 45
    • 0037068629 scopus 로고    scopus 로고
    • Azapeptides structurally based upon inhibitory sites of cystatins as potent and selective inhibitors of cysteine proteases
    • Wieczerzak, E.; Drabik, P.; Lankiewicz, L.; Oldziej, S.; Grzonka, Z.; Abrahamson, M.; Grubb, A.; Brömme, D. Azapeptides Structurally Based upon Inhibitory Sites of Cystatins as Potent and Selective Inhibitors of Cysteine Proteases. J. Med. Chem. 2002, 45, 4202-4211.
    • (2002) J. Med. Chem. , vol.45 , pp. 4202-4211
    • Wieczerzak, E.1    Drabik, P.2    Lankiewicz, L.3    Oldziej, S.4    Grzonka, Z.5    Abrahamson, M.6    Grubb, A.7    Brömme, D.8
  • 47
    • 0023728105 scopus 로고
    • The behavior and significance of slow-binding enzyme inhibitors
    • Morrison, J. F.; Walsh, C. T. The Behavior and Significance of Slow-Binding Enzyme Inhibitors. Adv. Enzymol. Relat. Areas Mol. Biol. 1988, 61, 201-301.
    • (1988) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.61 , pp. 201-301
    • Morrison, J.F.1    Walsh, C.T.2
  • 48
    • 0034618541 scopus 로고    scopus 로고
    • Privileged molecules for protein binding identified from NMR-based screening
    • Hajduk, P. J.; Bures, M.; Praestgard, J.; Fesik, S. W. Privileged Molecules for Protein Binding Identified from NMR-Based Screening. J. Med. Chem. 2000, 43, 3443-3447.
    • (2000) J. Med. Chem. , vol.43 , pp. 3443-3447
    • Hajduk, P.J.1    Bures, M.2    Praestgard, J.3    Fesik, S.W.4
  • 49
    • 0033015988 scopus 로고    scopus 로고
    • Revisiting the S2 specificity of papain by structural analogs of Phe
    • Lecaille, F.; Serveau, C.; Gauthier, F.; Lalmanach, G. Revisiting the S2 specificity of papain by structural analogs of Phe. FEBS Lett. 1999, 445, 311-314.
    • (1999) FEBS Lett , vol.445 , pp. 311-314
    • Lecaille, F.1    Serveau, C.2    Gauthier, F.3    Lalmanach, G.4
  • 50
    • 0001885748 scopus 로고    scopus 로고
    • Recent insights into cysteine protease specificity: Lessons for drug design
    • Storer, A. C.; Menard, R. Recent insights into cysteine protease specificity: Lessons for drug design. Perspect. Drug Discovery Des. 1996, 6, 33-46.
    • (1996) Perspect. Drug Discovery Des. , vol.6 , pp. 33-46
    • Storer, A.C.1    Menard, R.2
  • 51
    • 4744365526 scopus 로고    scopus 로고
    • Two polymorphe of a covalent complex between papain and a diazomethylketone inhibitor
    • Janowski, R.; Kozak, M.; Jankowska, E.; Grzonka, Z. Two polymorphe of a covalent complex between papain and a diazomethylketone inhibitor. J. Pept. Res. 2004, 64, 141-150.
    • (2004) J. Pept. Res. , vol.64 , pp. 141-150
    • Janowski, R.1    Kozak, M.2    Jankowska, E.3    Grzonka, Z.4
  • 54
    • 0024818636 scopus 로고
    • The specificity of bovine spleen cathepsin S. A comparison with rat liver cathepsins L and B
    • Brömme, D.; Steinert, A.; Friebe, S.; Fittkau, S.; Wiederanders, B.; Kirschke, H. The specificity of bovine spleen cathepsin S. A comparison with rat liver cathepsins L and B. Biochem. J. 1989, 264, 475-481.
    • (1989) Biochem. J. , vol.264 , pp. 475-481
    • Brömme, D.1    Steinert, A.2    Friebe, S.3    Fittkau, S.4    Wiederanders, B.5    Kirschke, H.6
  • 55
    • 0031030808 scopus 로고    scopus 로고
    • Crystal structure of human cathepsin K complexed with a potent inhibitor
    • McGrath, M. E.; Klaus, J. E.; Barnes, M. G.; Brömme, D. Crystal structure of human cathepsin K complexed with a potent inhibitor. Nat. Struct. Biol. 1997, 4, 105-108.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 105-108
    • McGrath, M.E.1    Klaus, J.E.2    Barnes, M.G.3    Brömme, D.4
  • 58
    • 28144442371 scopus 로고
    • Preparation of arylsulfonyl derivatives of amino acids
    • Nikolenko, L. M. Preparation of arylsulfonyl derivatives of amino acids. Zh. Obshch. Khim. 1956, 26, 806-808.
    • (1956) Zh. Obshch. Khim. , vol.26 , pp. 806-808
    • Nikolenko, L.M.1
  • 59
    • 0038776040 scopus 로고    scopus 로고
    • EASY-FIT: A software system for data fitting in dynamic systems
    • Schittkowski, K. EASY-FIT: A Software System for Data Fitting in Dynamic Systems. Struct. Multidiscip. Optim. 2002, 23, 153-169.
    • (2002) Struct. Multidiscip. Optim. , vol.23 , pp. 153-169
    • Schittkowski, K.1
  • 60
    • 0001182323 scopus 로고
    • 130. Poly(dipeptamidinium)-salze: Definition und methoden zur präparativen herstellung
    • Moser, H.; Fliri, A.; Steiger, A.; Costello, G.; Schreiber, J.; Eschenmoser, A. 130. Poly(dipeptamidinium)-Salze: Definition und Methoden zur präparativen Herstellung. Helv. Chim. Acta 1986, 69, 1224-1262.
    • (1986) Helv. Chim. Acta , vol.69 , pp. 1224-1262
    • Moser, H.1    Fliri, A.2    Steiger, A.3    Costello, G.4    Schreiber, J.5    Eschenmoser, A.6
  • 61
    • 0010567592 scopus 로고
    • Tetrazole analogues of amino acides and peptides-V. Syntheses of peptide derivatives containing tetrazole analogues of amino acids in C-terminal position
    • Grzonka, Z.; Rekowska, E.; Liberek, B. Tetrazole Analogues of Amino Acides and Peptides-V. Syntheses of Peptide Derivatives Containing Tetrazole Analogues of Amino Acids in C-terminal Position. Tetrahedron 1971, 27, 2317-2322.
    • (1971) Tetrahedron , vol.27 , pp. 2317-2322
    • Grzonka, Z.1    Rekowska, E.2    Liberek, B.3
  • 62
    • 0035878728 scopus 로고    scopus 로고
    • Variation in aspects of cysteine proteinase catalytic mechanism deduced by spectroscopic observation of dithioester intermediates, kinetic analysis and molecular dynamic simulations
    • Reid, J. D.; Hussain, S.; Sreedharan, S. K.; Bailey, T. S. F.; Surapong, P.; Thomas, E. W.; Verma, C. S.; Brocklehurst, K. Variation in aspects of cysteine proteinase catalytic mechanism deduced by spectroscopic observation of dithioester intermediates, kinetic analysis and molecular dynamic simulations. Biochem. J. 2001, 357, 343-352.
    • (2001) Biochem. J. , vol.357 , pp. 343-352
    • Reid, J.D.1    Hussain, S.2    Sreedharan, S.K.3    Bailey, T.S.F.4    Surapong, P.5    Thomas, E.W.6    Verma, C.S.7    Brocklehurst, K.8
  • 64
    • 0042190071 scopus 로고    scopus 로고
    • π-ligands for generating transition metal-peptide complexes: Coordination of amino acid derivatives to Tungsten utilizing alkyne ligands
    • Curran, T. P.; Grant, A. L.; Lucht, R. L.; Carter, J. C.; Affonso, J. π-Ligands for Generating Transition Metal-Peptide Complexes: Coordination of Amino Acid Derivatives to Tungsten Utilizing Alkyne Ligands. Org. Lett. 2002, 4, 2917-2920.
    • (2002) Org. Lett. , vol.4 , pp. 2917-2920
    • Curran, T.P.1    Grant, A.L.2    Lucht, R.L.3    Carter, J.C.4    Affonso, J.5
  • 65
    • 0024261151 scopus 로고
    • Studies on analgesic oligopeptides. V. Structure-activity relationship of tripeptide alkylamides, Tyr-D-Arg-Phe-X
    • Suzuki, K.; Hiroki, F.; Sasaki, Y.; Shiratori, M.; Sakadura, S.; Kisara, K. Studies on analgesic oligopeptides. V. Structure-activity relationship of tripeptide alkylamides, Tyr-D-Arg-Phe-X. Chem. Pharm. Bull. 1988, 36, 4834-4840.
    • (1988) Chem. Pharm. Bull. , vol.36 , pp. 4834-4840
    • Suzuki, K.1    Hiroki, F.2    Sasaki, Y.3    Shiratori, M.4    Sakadura, S.5    Kisara, K.6
  • 66
    • 0025959153 scopus 로고
    • Photometric or fluorometric assay of cathepsin B, L and H and papain using substrates with an aminotrifluoromethylcoumarin leaving group
    • Tchoupe, J. R.; Moreau, T.; Gauthier, F.; Bieth, J. G. Photometric or fluorometric assay of cathepsin B, L and H and papain using substrates with an aminotrifluoromethylcoumarin leaving group. Biochim. Biophys. Acta 1991, 1076, 149-151.
    • (1991) Biochim. Biophys. Acta , vol.1076 , pp. 149-151
    • Tchoupe, J.R.1    Moreau, T.2    Gauthier, F.3    Bieth, J.G.4


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