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Integrin αvβ3 is a receptor for the extracellular matrix proteins containing arginine glycine aspartic (RGD) tripeptide sequence.
This observation is consistent with a limited number of peroxisomal matrix proteins containing PTS2 receptors.
This linkage depends on the "functional glycosylation" of α-DG and its subsequent ability to bind to extracellular matrix proteins containing laminin globular (LG) domains.
The expression level of PEX5 was much higher than that of PEX7, consistent with only a limited number of peroxisomal matrix proteins containing the PTS2 receptor [ 40].
For example, it is possible that the cellular responses we observed may be specific to cardiac fibroblasts interacting with extracellular matrix proteins containing RGD (Arg-Gly-Asp) domains, such as fibronectin and collagen IV [ 29, 36].
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The molecular structure of many kinds of extracellular matrix proteins contains nitrogen atoms; polymers of PS, PDMS and PLA do not include nitrogen.
Most peroxisomal matrix proteins contain a peroxisomal targeting signal 1 (PTS1), a tripeptide at the protein extreme C-terminus.
Today, we know that majority of the peroxisomal matrix proteins contain a C-terminal PTS1, and very few an N-terminal PTS2.
Peroxisomal matrix proteins contain specific peroxisomal targeting signals (PTS1 or PTS2) that are post-translationally recognized in the cytosol by the import receptors Pex5 and Pex7, respectively [ 3 7,8 ].
The Drosophila dumpy gene consists of seventy eight coding exons and encodes a huge extracellular matrix protein containing large numbers of epidermal growth factor-like (EGF) modules and a novel module called dumpy (DPY).
Collagen is an extracellular matrix protein containing the repeating motif (GLY-X-X′ n.
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