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Cathepsin L is an intracellular and extracellular protease in Paramecium tetraurelia. Purification, cloning, sequencing and specific inhibition by its expressed propeptide
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Völkel, H.; Kurz, U.; Linder, J.; Klumpp, S.; Gnau, V.; Jung, G.; Schultz, J. Cathepsin L is an intracellular and extracellular protease in Paramecium tetraurelia. Purification, cloning, sequencing and specific inhibition by its expressed propeptide. Eur. J. Biochem. 1996, 238, 198-206.
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58
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E-64 analogues as inhibitors of cathepsin L and cathepsin S: Importance of the S2-P2 interactions for potency and selectivity
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Gour-Salin, B.; Lachance, P.; Bonneau, P.; Storer, A.; Kirschke, H.; Broemme, D. E-64 Analogues as inhibitors of cathepsin L and cathepsin S: Importance of the S2-P2 interactions for potency and selectivity. Bioorg. Chem. 1994, 22, 227-241.
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59
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Comparative specificity and kinetic stucies on porcine calpain I and calpain II with naturally occurring peptides and synthetic fluorogenic substrates
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Sasaki, T.; Kikuchi, T.; Yumoto, N.; Yoshimura, N.; Murachi, T. Comparative specificity and kinetic stucies on porcine calpain I and calpain II with naturally occurring peptides and synthetic fluorogenic substrates. J. Biol. Chem. 1984, 259, 12489-12494.
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Mechanism of reaction of human plasmin with α-N-benzoyl-L-arginine-p-nitroanilide (titration of the enzyme)
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Christensen, U.; Muellertz, S. Mechanism of reaction of human plasmin with α-N-Benzoyl-L-arginine-p-nitroanilide (Titration of the enzyme). Biochim. Biophys. Acta 1974, 334, 187-190.
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A spectrophotometric assay for neutral protease
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Feder, J. A spectrophotometric assay for neutral protease. Biochem. Biophys. Res. Commun. 1968, 32, 326-332.
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Kinetics of the pepsin-catalyzed hydrolysis of N-acetyl-L-phenylalanyl-L-diiodotyrosine
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Jackson, W.; Schlamowitz, M.; Shaw, A. Kinetics of the pepsin-catalyzed hydrolysis of N-acetyl-L-phenylalanyl-L-diiodotyrosine. Biochemistry 1965, 4, 1537-1543.
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Determination of the rate constant of enzyme modification by measuring the substrate reaction in the presence of the modifier
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Tian, W.-X.; Tsou, C.-L. Determination of the rate constant of enzyme modification by measuring the substrate reaction in the presence of the modifier. Biochemistry 1982, 21, 1028-1032.
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Esters of methanesulfonic acid as irreversible inhibitors of acetylcholinesterase
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Kitz, R.; Wilson, I. Esters of methanesulfonic acid as irreversible inhibitors of acetylcholinesterase. J. Biol. Chem. 1962, 237, 3245-3249.
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67
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Inhibitory effect of di- and tripeptidyl aldehydes on calpains and cathepsins
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Sasaki, T.; Kishi, M.; Saito, M.; Tanaka, T.; Higuchi, N.; Kominami, E.; Katunuma, N.; Murachi, T. Inhibitory effect of di- and tripeptidyl aldehydes on calpains and cathepsins. J. Enzyme Inhib. 1990, 3, 195-201.
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, vol.3
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Sasaki, T.1
Kishi, M.2
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Tanaka, T.4
Higuchi, N.5
Kominami, E.6
Katunuma, N.7
Murachi, T.8
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68
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0344058268
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GraFit, version 3.0; Erithacus Software Ltd.: London, 1992
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GraFit, version 3.0; Erithacus Software Ltd.: London, 1992.
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69
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0001095726
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Addition of azoles and amines to unsymmetrical fumaric esters
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Zaderenko, P.; López, M. C.; Ballesteros, P. Addition of azoles and amines to unsymmetrical fumaric esters. J. Org. Chem. 1996, 61, 6825-6828.
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Zaderenko, P.1
López, M.C.2
Ballesteros, P.3
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70
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85066051603
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The michael type addition of free sulfilimine
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Furukawa, N.; Oae, S. The Michael type addition of free sulfilimine. Synthesis 1976, 1, 30-32.
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, vol.1
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Oae, S.2
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71
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0344920582
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note
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4) C,H,N. Assignment of NMR signals was carried out by INEPT long-range NMR spectroscopy. (matrix presented)
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72
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0344920581
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note
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-1).
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73
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0344058266
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note
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-1).
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74
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0344489471
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note
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-1.
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75
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0025364110
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Recent developments in inhibiting cysteine and serine proteases
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Demuth, H. Recent developments in inhibiting cysteine and serine proteases. J. Enzyme Inhib. 1990, 3, 249-278.
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(1990)
J. Enzyme Inhib.
, vol.3
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Demuth, H.1
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76
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33847800887
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The hard soft acids bases (HSAB) principle and organic chemistry
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Ho, T.-L. The hard soft acids bases (HSAB) principle and organic chemistry. Chem. Rev. 1975, 75, 1-20.
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Ho, T.-L.1
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77
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0345351876
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note
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-1. The superposition has been performed using the program Multifit from Sybyl 6.4.
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78
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0344058263
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note
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The docking of 26a into the active site of papain has been performed using the program FlexiDock from the Sybyl 6.4 Biopolymer Module (Tripos Associates Inc., St. Louis, MO). Energy minimization: Tripos force field, Gasteiger-Hueckel charges on ligand, Kollmann charges on protein. As FlexiDock pocket a region of 0.4 nm around the amino acids Cys25, Tyr67, Pro68, Trp69, Val133, Val157, His159, Ala160, and Phe207 of papain has been defined. The structure of papain has been taken from the Brookhaven Protein Databank (entry 1pe6).
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