collagenase inhibitor
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2020 ◽  
Vol 401 ◽  
pp. 115078
Author(s):  
Yoke-Chen Chang ◽  
Rita A. Hahn ◽  
Marion K. Gordon ◽  
Jeffrey D. Laskin ◽  
Donald R. Gerecke

2019 ◽  
Vol 33 (S1) ◽  
Author(s):  
Yoke‐Chen Chang ◽  
Tracy Peng ◽  
Rita A Hahn ◽  
Marion K Gordon ◽  
Donald R Gerecke

2018 ◽  
Vol 39 (4) ◽  
pp. 87
Author(s):  
Sergio Roberto De Andrade Leite

Different common drugs (Meloxicam, Tenoxicam and Piroxicam, and sodium alendronate) were tested both experimental and theoretically as inhibitors of interstitial human collagenase, also known as matrix metalloproteinase 1 (MMP-1). The in vitro collagenase activity, alone and in the presence of inhibitors, was quantified by the reaction with a fluorescent synthetic substrate and measuring the change of emission. Collagenase-inhibitor interaction was studied theoretically by computational calculations. Three among the four tested substances showed moderate inhibiting activity against the human collagenase.


ChemInform ◽  
2010 ◽  
Vol 31 (20) ◽  
pp. no-no
Author(s):  
Junji Inokoshi ◽  
Kazuro Shiomi ◽  
Rokuro Masuma ◽  
Haruo Tanaka ◽  
Haruki Yamada ◽  
...  

2009 ◽  
Vol 34 (4) ◽  
pp. 87-102 ◽  
Author(s):  
Sergio Roberto de Andrade Leite

Different common drugs (Meloxicam, Tenoxicam and Piroxicam, and sodium alendronate) were tested both experimental and theoretically as inhibitors of interstitial human collagenase, also known as matrix metalloproteinase 1 (MMP-1). The in vitro collagenase activity, alone and in the presence of inhibitors, was quantified by the reaction with a fluorescent synthetic substrate and measuring the change of emission. Collagenase-inhibitor interaction was studied theoretically by computational calculations. Three among the four tested substances showed moderate inhibiting activity against the human collagenase.


2009 ◽  
Vol 62 (2) ◽  
pp. 187-193 ◽  
Author(s):  
Satoru Nishizawa ◽  
Hisayo Yamaoka ◽  
Masateru Matsui ◽  
Shinichi Hirabayashi ◽  
Kazuto Hoshi ◽  
...  

2008 ◽  
Vol 33 (4) ◽  
pp. 47-52 ◽  
Author(s):  
S. R. A. Leite

Different substances were tested as inhibitors of Clostridium histolyticum collagenase, both experimental and theoretically. The in vitro collagenase activity, alone and in the presence of inhibitors, was quantified by reaction with bovine collagen and dosage of the releasing amino acids. Collagenase-inhibitor interaction was studied theoretically by docking computational calculations. Only one among the tested substances showed inhibitor activity against the bacterial collagenase.


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