3.4.21.7	additional information	no inhibition by protein C inhibitor from Bos taurus	2	
3.4.21.7	additional information	inhibition of ERK1/2 by MEK inhibitor U0126 does not affect plasmin-mediated expression of TNF-alpha	2	
3.4.21.7	additional information	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	2	
3.4.21.7	additional information	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	2	
3.4.21.7	additional information	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	2	
3.4.21.7	additional information	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	2	
3.4.21.7	additional information	inactive plasmin, in which the catalytic site has been irreversibly blocked with a peptide inhibitor	2	
3.4.21.7	additional information	noninhibitory plasminogen activator inhibitor-type 1 has no effect on plasmin activity and degradation of casein	2	
3.4.21.7	additional information	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	2	
3.4.21.7	additional information	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	2