alexa The collagen superfamily: from the extracellular matrix to the cell membrane.
Nutrition

Nutrition

Journal of Nutrition & Food Sciences

Author(s): RicardBlum S, Ruggiero F

Abstract Share this page

Abstract The collagen superfamily is highly complex and shows a remarkable diversity in molecular and supramolecular organization, tissue distribution and function. However, all its members share a common structural feature, the presence of at least one triple-helical domain, which corresponds to a number of (Gly-X-Y)n repeats (X being frequently proline and Y hydroxyproline) in the amino acid sequence. Several sub-families have been determined according to sequence homologies and to similarities in the structural organization and supramolecular assembly. In the present review, we focus on the newly described fibrillar collagens, fibrillar-associated collagens with interrupted triple helix, membrane collagens and multiplexins. Recent advances in the characterization of proteins containing triple-helical domains but not referred to as collagens are also discussed. This article was published in Pathol Biol (Paris) and referenced in Journal of Nutrition & Food Sciences

Relevant Expert PPTs

Relevant Speaker PPTs

Recommended Conferences

  • Food & Beverages
    July 27-29, 2017 Chicago, USA
  • Food Processing & Technology
    October 02-04, 2017 London, UK
  • Public Health, Epidemiology & Nutrition
    November 13-14, 2017 Osaka, Japan
  • Food Processing & Technology
    December 05-07, 2016 San Antonio, USA
Peer Reviewed Journals
 
Make the best use of Scientific Research and information from our 700 + peer reviewed, Open Access Journals
International Conferences 2017-18
 
Meet Inspiring Speakers and Experts at our 3000+ Global Annual Meetings

Contact Us

 
© 2008-2017 OMICS International - Open Access Publisher. Best viewed in Mozilla Firefox | Google Chrome | Above IE 7.0 version
adwords