Small leucine-rich proteoglycans/proteins (SLRPs) are associated with collagen fibril formation, and therefore important for the proper formation of extracellular matrices. SLRPs are differentially expressed in tissues and during pathological conditions, contributing to the development of connective tissue properties. The binding of SLRPs to collagens have recently been characterized, and may give some clues to the significance of these interactions. In this mini review, we summarize published work in this field, and propose several mechanisms for how SLRPs can control collagen matrix structure and function. SLRPs appear to influence collagen cross-linking patterns. We also propose that the SLRP-collagen interactions can assist in the proce...
Background: Despite detailed knowledge about the structure and signaling properties of individual co...
AbstractBackgroundDespite detailed knowledge about the structure and signaling properties of individ...
Type I collagen, the predominant protein of vertebrates, polymerizes with type III and V collagens a...
Small leucine-rich proteoglycans (SLRPs) are involved in a variety of biological and pathological pr...
Biological properties of connective tissues rely heavily on collagen and its use in formation of ext...
The small leucine-rich proteoglycans (SLRPs) are biologically active components of the extracellular...
Small leucine-rich repeat proteoglycan (SLRP) proteins have an important role in the organization of...
The extracellular matrix (ECM) is a complex mixture composed of fibrillar collagens as well as addit...
The small leucine-rich proteoglycans (SLRPs) are important regulators of extracellular matrix assemb...
The controlled assembly of collagen monomers into fibrils, with accompanying intermolecular cross-li...
We have previously reported that COMP (cartilage oligomeric matrix protein) is prominent in cartilag...
Current wisdom on intermolecular interactions in the extracellular matrix assumes that small proteog...
Current wisdom on intermolecular interactions in the extracellular matrix assumes that small proteog...
The organization of type I collagen and how it is affected by glycosaminoglycans (GAGs), proteoglyca...
Type I collagen is the most abundant structural protein in the extracellular matrix (ECM), forming a...
Background: Despite detailed knowledge about the structure and signaling properties of individual co...
AbstractBackgroundDespite detailed knowledge about the structure and signaling properties of individ...
Type I collagen, the predominant protein of vertebrates, polymerizes with type III and V collagens a...
Small leucine-rich proteoglycans (SLRPs) are involved in a variety of biological and pathological pr...
Biological properties of connective tissues rely heavily on collagen and its use in formation of ext...
The small leucine-rich proteoglycans (SLRPs) are biologically active components of the extracellular...
Small leucine-rich repeat proteoglycan (SLRP) proteins have an important role in the organization of...
The extracellular matrix (ECM) is a complex mixture composed of fibrillar collagens as well as addit...
The small leucine-rich proteoglycans (SLRPs) are important regulators of extracellular matrix assemb...
The controlled assembly of collagen monomers into fibrils, with accompanying intermolecular cross-li...
We have previously reported that COMP (cartilage oligomeric matrix protein) is prominent in cartilag...
Current wisdom on intermolecular interactions in the extracellular matrix assumes that small proteog...
Current wisdom on intermolecular interactions in the extracellular matrix assumes that small proteog...
The organization of type I collagen and how it is affected by glycosaminoglycans (GAGs), proteoglyca...
Type I collagen is the most abundant structural protein in the extracellular matrix (ECM), forming a...
Background: Despite detailed knowledge about the structure and signaling properties of individual co...
AbstractBackgroundDespite detailed knowledge about the structure and signaling properties of individ...
Type I collagen, the predominant protein of vertebrates, polymerizes with type III and V collagens a...