Collagens contain sequence- and conformation-dependent epitopes responsible for their digestion by collagenases at specific loci. A synthetic heterotrimer construct containing the collagenase cleavage site of collagen type I was found to mimic perfectly native collagen in terms of selectivity and mode of enzymatic degradation. The NMR conformational analysis of this molecule clearly revealed the presence of two structural domains, i.e. a triple helix spanning the Gly-Pro-Hyp repeats and a less ordered portion corresponding to the collagenase cleavage site where the three chains are aligned in extended conformation with loose interchain contacts. These structural properties allow for additional insights into the very particular mechanism of ...
The collagen triple helix consists of three supercoiled solvent-exposed polypeptide chains, and by d...
Thesis: Ph. D., Massachusetts Institute of Technology, Department of Civil and Environmental Enginee...
The most abundant member of the collagen protein family, collagen I (COL1), is composed of two simil...
Collagens contain sequence- and conformation-dependent epitopes responsible for their digestion by c...
Collagenases are the principal enzymes responsible for the degradation of collagens during embryonic...
Background: The general consensus is that interstitial collagens are digested by collagenases and de...
AbstractBackground: The general consensus is that interstitial collagens are digested by collagenase...
BACKGROUND: The general consensus is that interstitial collagens are digested by collagenases and de...
Abstract Fibrillar collagen molecules are synthesized as precursors, procollagens, with large propep...
ABSTRACT In this report, we present a hypothesis on the mechanism used by interstitial collagenases ...
Type I collagen cleavage is crucial for tissue remodeling, but its homotrimeric isoform is resistant...
The collagen triple helix is a unique protein fold found in all domains of life where is has diverse...
ABSTRACT: Degradation of fibrillar collagen is critical for tissue maintenance. Yet, understanding c...
Degradation of fibrillar collagen is critical for tissue maintenance. Yet, understanding collagen ca...
The repeating Gly-X-Y sequences and uniform rod-like structure makes collagen-like peptides a unique...
The collagen triple helix consists of three supercoiled solvent-exposed polypeptide chains, and by d...
Thesis: Ph. D., Massachusetts Institute of Technology, Department of Civil and Environmental Enginee...
The most abundant member of the collagen protein family, collagen I (COL1), is composed of two simil...
Collagens contain sequence- and conformation-dependent epitopes responsible for their digestion by c...
Collagenases are the principal enzymes responsible for the degradation of collagens during embryonic...
Background: The general consensus is that interstitial collagens are digested by collagenases and de...
AbstractBackground: The general consensus is that interstitial collagens are digested by collagenase...
BACKGROUND: The general consensus is that interstitial collagens are digested by collagenases and de...
Abstract Fibrillar collagen molecules are synthesized as precursors, procollagens, with large propep...
ABSTRACT In this report, we present a hypothesis on the mechanism used by interstitial collagenases ...
Type I collagen cleavage is crucial for tissue remodeling, but its homotrimeric isoform is resistant...
The collagen triple helix is a unique protein fold found in all domains of life where is has diverse...
ABSTRACT: Degradation of fibrillar collagen is critical for tissue maintenance. Yet, understanding c...
Degradation of fibrillar collagen is critical for tissue maintenance. Yet, understanding collagen ca...
The repeating Gly-X-Y sequences and uniform rod-like structure makes collagen-like peptides a unique...
The collagen triple helix consists of three supercoiled solvent-exposed polypeptide chains, and by d...
Thesis: Ph. D., Massachusetts Institute of Technology, Department of Civil and Environmental Enginee...
The most abundant member of the collagen protein family, collagen I (COL1), is composed of two simil...