pages 519-638, 2 unnumbered folded leaves of plates : illustrations ; 30 cm
OCLC
ocm31040685
"Protein sequence alignments" on two folded leaves of plates at end of text.
Includes bibliographical references (pages 576-638).
General overview of collagens -- Diseases of fibrillar collagens -- Animal models of collagen diseases -- Synthesis and degradation of collagens -- Biosynthesis of procollagen -- Intracellular steps in collagen biosynthesis; extracellular steps in collagen biosynthesis; effects of cytokines and growth factors in collagen synthesis -- Extracellular degradation of collagens -- Structure of collagens -- Molecular conformation of the triple helix -- Fibril formation -- Fibril structure -- Covalent cross-linking of collagen fibrils -- Type I collagen (collagen I) -- Domain structures; pre-proα1(I) chain (COL1A1); pre-proα2(I) chain (COL1A2) -- Purification; type I procollagen; type I collagen -- Binding properties of type I collagen -- Naturally occurring mutations -- Type II colagen (collagen II) -- Domain structures; pre-proα1(II) chain (COL2A1) -- Purification; type II procollagen; type II collagen -- Naturally occurring mutations -- Type III collagen (collagen III) -- Domain structures; pre-proα(III) chain (COL3A1) -- Purification; type III procollagen; type III collagen -- Fibril structure
(cont) Naturally occurring mutations -- Type V collagen (collagen V) -- Domain structures; pre-proα1(V) chain COL5A1); pre-proα2(V) chain (COL5A2) -- Purification -- Fibril structure -- Type XI collagen (collagen XI) -- Domain structures; pre-proα1(XI) chain (COL11A1); pre-proα2(XI) chain (COL11A2) -- Fibril structure -- Invertebrate collagens -- Domain structures; collagen 1α-chain from sea urchin (S. purpuratus); collagen 2α-chain from sea urchin (S. purpuratus); procollagen Emf1α; fibril-forming collagen α-chain from tube worm (Rifta pachyptila); collagen 2α-chain from sea urchin (P. lividus); collagen 1α-chain from sea urchin (Paracentrotus lividus)