The Extracellular Matrix Factsbook by Shirley Ayad

By Shirley Ayad

I discovered this to be a truly thorough reference throughout a extensive diversity of extracellular matrix proteins. specifically, deciding upon which serious ECM proteins so as to add again to 3D telephone tradition stipulations to re-approximate the in vivo milieu. It used to be hugely touted at http://home.ease.lsoft.com/archives/3d-cell-biology.html and www.puramatrix.com as a key handbook for examine and bioproduction concerning ECM proteins.

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K. (1982)Preparation and characterization of the different types of collagen. Methods Enzymol. 82: 33-64. C. S. (1990)m e s JJI and V procollagens: Homology in genetic organization and diversity in structure. In: Extracellular Matrix Genes, ed. J. , Academic Press, New York, pp. 57-78. J. D. (1990)Conserved and divergent sequence and functional elements within collagen genes. In: Extracellular Matrix Genes, ed. , Academic Press, New York, pp. 1-56. L. J. (1993)Collagen: Gene structure. In: Connective Tissue and Its Heritable Disorders, ed.

Dynamics 199: 129- 140. -J. et al. (1991)Sites of stromelysin cleavage in collagen types 11, IX,X and XI of cartilage. J. Biol. Chem. 266: 5625-5628. K. (1982)Preparation and characterization of the different types of collagen. Methods Enzymol. 82: 33-64. Ala-Kokko, L. J. (1990)Completion of the intron-exon structure of the gene for human type 11procollagen (COLZAl]:variations in the nucleotide sequences of the alleles from three chromosomes. Genomics 8: 454-460. D. (1990)Conserved and divergent sequence and functional elements within collagen genes.

Lo Collagen type IV m e IV collagen is found exclusively in basement membranes where it provides the major structural support for this matrix. The molecule contains a long (approximately350 nm) triple-helicaldomain containing approximately 20 short interruptions that are thought to introduce flexibility into the helix. m e IV collagen self-assemblesinto a meshwork by the anti-parallel interaction and extensive disulphide bondmg of four molecules at their NH2termini to form the 7S domain, by the interaction of two molecules at their COOH-terminal non-collagenous (NC1)domains, and by lateral aggregations.

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