Periostin and its interacting proteins in the construction of extracellular architectures

Periostin is a matricellular protein that is composed of a multi-domain structure with an amino-terminal EMI domain, a tandem repeat of four FAS 1 domains, and a carboxyl-terminal domain. These distinct domains have been demonstrated to bind to many proteins including extracellular matrix proteins (...

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Vydáno v:	Cellular and molecular life sciences : CMLS Ročník 74; číslo 23; s. 4269 - 4277
Hlavní autoři:	Kii, Isao, Ito, Harumi
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	Cham Springer International Publishing 01.12.2017 Springer Nature B.V
Témata:	Amino acids Assembly Binding sites Biochemistry Biomedical and Life Sciences Biomedicine Bone Morphogenetic Protein 1 - genetics Bone Morphogenetic Protein 1 - metabolism Bone morphogenetic proteins Cell Adhesion Molecules - genetics Cell Adhesion Molecules - metabolism Cell Biology chemical interactions collagen Collagen (type I) Collagen - genetics Collagen - metabolism Connective Tissue - anatomy & histology Connective Tissue - metabolism Connective tissues Construction Crosslinking disease course Electromagnetic interference enzymes Extracellular matrix Fibronectin fibronectins Fibronectins - genetics Fibronectins - metabolism Gene Expression Homeostasis Humans Laminin Laminin - genetics Laminin - metabolism Life Sciences Lysyl oxidase Multi-Author Review Nephroblastoma Overexpressed Protein - genetics Nephroblastoma Overexpressed Protein - metabolism Protein Binding Protein Interaction Domains and Motifs Protein Interaction Mapping Protein Isoforms - genetics Protein Isoforms - metabolism Proteins Proteoglycans - metabolism Signal Transduction Tenascin Tenascin - genetics Tenascin - metabolism EMI FAS 1 Tenascin Collagen Fibronectin BMP-1
ISSN:	1420-682X, 1420-9071, 1420-9071
On-line přístup:	Získat plný text
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