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Results 1 - 10 of 231 > >>
EC Number
Inhibitors
Commentary
Structure
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no inhibition by protein C inhibitor from Bos taurus
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inhibition of ERK1/2 by MEK inhibitor U0126 does not affect plasmin-mediated expression of TNF-alpha
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pretreatment with plasmin, thrombin and trypsin significantly but, only partly, attenuates subsequent relaxation induced by plasmin. Major part of the plasmin-induced relaxation is resistant to these pretreatments
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synthetic peptides GHRPam, GHRPLam, and GHRPYam mimicking the B knobs, render fibrin less vulnerable to attack by plasmin. None of the three synthetic peptides have a significant effect on the plasmin catalyzed hydrolysis of the chromogenic peptide D-Val-Leu-Lys-p-nitroanilide. Even in the absence of synthetic peptides there is a lag in plasmin generation accompanying fibrin formation
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peptide inhibitors that incorporate 3-oxotetrahydrofuran and 3-oxotetrahydrothiophene 1,1-dioxide groups have the highest activities. For cyclopentanone-based inhibitors, incorporation of electron-withdrawing groups such as O and SO2 into the ring improves their activities. Alkylamino substituents, with an optimal spacer length of 6 carbon atoms, can be added to the inhibitors to bind in the S1 subsite. Incorporating conformationally constrained peptide segments into the inhibitors do not improve their activities
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dilution of normal plasma with 0.9% NaCl does not significantly affect plasmin-mediated decreases in the maximum rate of thrombus and total thrombus generation compared with undiluted plasma
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inactive plasmin, in which the catalytic site has been irreversibly blocked with a peptide inhibitor
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noninhibitory plasminogen activator inhibitor-type 1 has no effect on plasmin activity and degradation of casein
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development and evaluation of alternative potent and selective serine lysine analogues to inhibit plasmin, usage of a noncombinatorial peptide library to define plasmin's extended substrate specificity and guide the design of potent transition state analogue inhibitors, molecular modeling, overview
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preparation and analysis of lysine-nitrile derivatives having a trisubstituted benzene for inhibitory activities against plasmin and the highly homologous plasma kallikrein and urokinase. Development of specific and selective inhibitors based on 9, overview. No inhibition by N-[(1S)-5-amino-1-cyanopentyl]-3-([3-[1-(4-fluorobenzyl)-1H-indol-3-yl]propanoyl]amino)-4-methoxybenzamide
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Results 1 - 10 of 231 > >>