Self-association of type I collagen directed by thymoquinone through alteration of molecular forces

2019 ◽  
Vol 140 ◽  
pp. 614-620
Author(s):  
K. Rasheeda ◽  
D. Samyuktha ◽  
N. Nishad Fathima
2013 ◽  
Vol 54 ◽  
pp. 155-159 ◽  
Author(s):  
Ganesh Shanmugam ◽  
Samala Murali Mohan Reddy ◽  
Venkatachalam Natarajan ◽  
Balaraman Madhan

Author(s):  
Arthur J. Wasserman ◽  
Kathy C. Kloos ◽  
David E. Birk

Type I collagen is the predominant collagen in the cornea with type V collagen being a quantitatively minor component. However, the content of type V collagen (10-20%) in the cornea is high when compared to other tissues containing predominantly type I collagen. The corneal stroma has a homogeneous distribution of these two collagens, however, immunochemical localization of type V collagen requires the disruption of type I collagen structure. This indicates that these collagens may be arranged as heterpolymeric fibrils. This arrangement may be responsible for the control of fibril diameter necessary for corneal transparency. The purpose of this work is to study the in vitro assembly of collagen type V and to determine whether the interactions of these collagens influence fibril morphology.


2007 ◽  
Vol 177 (4S) ◽  
pp. 314-314 ◽  
Author(s):  
Joon-Yang Kim ◽  
Hoon Seog Jean ◽  
Beom Joon Kim ◽  
Kye Yong Song

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