tripeptide sequence pattern suggest a physical basis for their differential susceptibility to matrix metalloproteinases in type X collagen. doi:10.1016/j.jmb.2007.11.075 Available online at www © 2007 Elsevier Ltd. All rights reserved. Edited by F. Schmid Keywords: collagen; triple-helix; interruptions; structure; peptide
A systematic molecular dynamics (MD) simulation has been carried out on collagen-like peptides with ...
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...
This year marks the 50th anniversary of the coiled?–?coil triple helical structure of collagen, firs...
The collagen triple helix is a unique protein fold found in all domains of life where is has diverse...
This year marks the 50th anniversary of the coiled?-?coil triple helical structure of collagen, firs...
The analysis of factors contributing to the stability of proteins is a subject of intense debate. Pa...
Collagens are the most abundant structural proteins in the extracellular matrix of animals and play ...
The triple-helix is a unique secondary structural motif found primarily within the collagens. In col...
Understanding the structure, folding, and stability of collagen is complex because of its length and...
Ottl J, Gabriel D, Murphy G, et al. Recognition and catabolism of synthetic heterotrimeric collagen ...
SummarySkeletal development and invasion by tumor cells depends on proteolysis of collagen by the pe...
<p>The X and Y letters refer to the consensus sequence pattern (Gly-X-Y)<i><sub>n</sub></i> characte...
The consequences of improper regulation of collagen turnover include diseases such as tumor cell met...
Collagen is a widespread protein family involved in a variety of biological processes. The complexit...
A systematic molecular dynamics (MD) simulation has been carried out on collagen-like peptides with ...
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...
This year marks the 50th anniversary of the coiled?–?coil triple helical structure of collagen, firs...
The collagen triple helix is a unique protein fold found in all domains of life where is has diverse...
This year marks the 50th anniversary of the coiled?-?coil triple helical structure of collagen, firs...
The analysis of factors contributing to the stability of proteins is a subject of intense debate. Pa...
Collagens are the most abundant structural proteins in the extracellular matrix of animals and play ...
The triple-helix is a unique secondary structural motif found primarily within the collagens. In col...
Understanding the structure, folding, and stability of collagen is complex because of its length and...
Ottl J, Gabriel D, Murphy G, et al. Recognition and catabolism of synthetic heterotrimeric collagen ...
SummarySkeletal development and invasion by tumor cells depends on proteolysis of collagen by the pe...
<p>The X and Y letters refer to the consensus sequence pattern (Gly-X-Y)<i><sub>n</sub></i> characte...
The consequences of improper regulation of collagen turnover include diseases such as tumor cell met...
Collagen is a widespread protein family involved in a variety of biological processes. The complexit...
A systematic molecular dynamics (MD) simulation has been carried out on collagen-like peptides with ...
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...
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