The main features of the triple helical structure of collagen were deduced in the mid-1950s
from fibre X-ray diffraction of tendons. Yet, the resulting models only could offer an average …

Collagen is a major component in a wide range of drug delivery systems and biomaterial
applications. Its basic physical and structural properties, together with its low …

Co-and post-translational hydroxylation of proline residues is critical for the stability of the
triple helical collagen structure. In this review, we summarise the biology of collagen prolyl 4 …

The α2β1 integrin, also known as VLA-2, GPIa-IIa, CD49b, was first identified as an
extracellular matrix receptor for collagens and/or laminins [55, 56]. It is now recognized that …

Collagens are the most abundant extracellular matrix proteins in vertebrates and have a
characteristic triple-helix structure. Hydroxylation of proline residues is critical for helix …

The best-known (fibrillar) collagens support cellular adhesion primarily through a subset of
collagen-binding integrins, α1β1, α2β1, α10β1 and α11β1, which have been shown to …

Abstract The Collagen Toolkits are libraries of 56 and 57 triple-helical synthetic peptides
spanning the length of the collagen II and collagen III helices. These have been used in …

Structural studies on integrins have recently made great strides in recent years. Crystal
structures of the complete extracellular fragments of three integrins in open and closed …

Integrin receptors bind collagen via metal-mediated interactions that are modulated by
magnesium (Mg 2+) levels in the extracellular matrix. Nuclear magnetic resonance-based …

Integrins are transmembrane cell-extracellular matrix adhesion receptors that impact many
cellular functions. A subgroup of integrins contain an i nserted (I) domain within the α …