نتایج جستجو برای: collagenases

تعداد نتایج: 417  

2015
Steven R. Van Doren

Most abundant in the extracellular matrix are collagens, joined by elastin that confers elastic recoil to the lung, aorta, and skin. These fibrils are highly resistant to proteolysis but can succumb to a minority of the matrix metalloproteinases (MMPs). Considerable inroads to understanding how such MMPs move to the susceptible sites in collagen and then unwind the triple helix of collagen mono...

2017
Siddharth Tevatia Nikhil Sharma Rahul Chopra

Periodontal diseases are bacterial infections characterized by inflammation and destruction of the attachment apparatus, often leading to tooth loss. The most common forms of periodontal diseases, gingivitis and periodontitis are caused by bacteria adjacent to or associated with periodontal structures. These bacteria, along with calculus and other local factors, are the principal components tha...

Journal: :The Journal of clinical investigation 1997
R C Billinghurst L Dahlberg M Ionescu A Reiner R Bourne C Rorabeck P Mitchell J Hambor O Diekmann H Tschesche J Chen H Van Wart A R Poole

We demonstrate the direct involvement of increased collagenase activity in the cleavage of type II collagen in osteoarthritic human femoral condylar cartilage by developing and using antibodies reactive to carboxy-terminal (COL2-3/4C(short)) and amino-terminal (COL2-1/4N1) neoepitopes generated by cleavage of native human type II collagen by collagenase matrix metalloproteinase (MMP)-1 (collage...

2015
Ryan Bauer Katarzyna Janowska Kelly Taylor Brad Jordan Steve Gann Tomasz Janowski Ethan C. Latimer Osamu Matsushita Joshua Sakon

Clostridium histolyticum collagenases ColG and ColH are segmental enzymes that are thought to be activated by Ca(2+)-triggered domain reorientation to cause extensive tissue destruction. The collagenases consist of a collagenase module (s1), a variable number of polycystic kidney disease-like (PKD-like) domains (s2a and s2b in ColH and s2 in ColG) and a variable number of collagen-binding domai...

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