The amino acid composition of collagen is described and the status of knowledge about the synthesis of its unique amino acids, hydroxyproline and hydroxylysine, presented. This is followed by a schematic overview of collagen metabolism. Scurvy and lathyrism, the only two abnormalities of collagen metabolism which can now be reasonably elucidated at a molecular level, are then discussed in some detail. The paper concludes by stressing the importance of recognizing the role of histoarchitecture and of interactions of collagen with other compounds when studying collagen or its metabolism in the whole animal
Abstract Collagens are the most abundant proteins in the extracellular matrix. They provide a frame...
and collagen metabolism: glucocorticoid-mediated alterations of prolyl hydroxylase activity and coll...
A three-chained peptide from type I collagen, crosslinked by hydroxyaldolhistidine, has been isolate...
The amino acid composition of collagen is described and the status of knowledge about the synthesis ...
The organization of the normal collagen molecule and fibrils is reviewed and the detection, assay, a...
Collagen is a family of proteins which consists of several genetically distinct molecular species an...
The presence of 0.1 - 0.2 moles of free N-terminal groups per 100.000 g. of soluble collagen was dem...
The collagen proteins are the principal component of the extracellular matrix and are the most abund...
A summary of results and ideas concerning special features of the covalent structure of collagen is ...
Type I collagen is the most abundant structural protein in vertebrates. It is a heterotrimeric molec...
The literature on collagen has been reviewed, with especial emphasis on structural aspects of collag...
In this communication evidence is presented that collagen-proline hydroxylation occurs on polypeptid...
The most abundant proteins in vertebrates – the collagen family proteins – play structural and biolo...
Hydroxylysine (Hyl) glycosides were determined both on the collagen produced by in-vitro cultures of...
This chapter discusses the physiologic, metabolic, and clinical aspects of collagen, including the r...
Abstract Collagens are the most abundant proteins in the extracellular matrix. They provide a frame...
and collagen metabolism: glucocorticoid-mediated alterations of prolyl hydroxylase activity and coll...
A three-chained peptide from type I collagen, crosslinked by hydroxyaldolhistidine, has been isolate...
The amino acid composition of collagen is described and the status of knowledge about the synthesis ...
The organization of the normal collagen molecule and fibrils is reviewed and the detection, assay, a...
Collagen is a family of proteins which consists of several genetically distinct molecular species an...
The presence of 0.1 - 0.2 moles of free N-terminal groups per 100.000 g. of soluble collagen was dem...
The collagen proteins are the principal component of the extracellular matrix and are the most abund...
A summary of results and ideas concerning special features of the covalent structure of collagen is ...
Type I collagen is the most abundant structural protein in vertebrates. It is a heterotrimeric molec...
The literature on collagen has been reviewed, with especial emphasis on structural aspects of collag...
In this communication evidence is presented that collagen-proline hydroxylation occurs on polypeptid...
The most abundant proteins in vertebrates – the collagen family proteins – play structural and biolo...
Hydroxylysine (Hyl) glycosides were determined both on the collagen produced by in-vitro cultures of...
This chapter discusses the physiologic, metabolic, and clinical aspects of collagen, including the r...
Abstract Collagens are the most abundant proteins in the extracellular matrix. They provide a frame...
and collagen metabolism: glucocorticoid-mediated alterations of prolyl hydroxylase activity and coll...
A three-chained peptide from type I collagen, crosslinked by hydroxyaldolhistidine, has been isolate...