The majority of collagen in the extracellular matrix is found in a fibrillar form, with long
slender filaments each displaying a characteristic∼ 67 nm D-repeat. Here they provide the …

The structure and remodeling of collagen in vivo is critical to the pathology and healing of
many human diseases, as well as to normal tissue development and regeneration. In …

Atomic force microscopy is an amazing technique that allies a versatile methodology (that
allows measurement of samples in liquid, vacuum or air) to imaging with unprecedented …

Collagen, a unique connective tissue protein finds extensive application as biocompatible
biomaterial in wound healing, as drug carriers, cosmetics, etc. A work has been undertaken …

Excessive cathepsin K (catK)-mediated turnover of fibrillar type I and II collagens in bone
and cartilage leads to osteoporosis and osteoarthritis. However, little is known about how …

Stabilization of type I rat tail tendon (RTT) collagen by various aldehydes, viz. formaldehyde,
gluteraldehyde, glyoxal and crotanaldehyde was studied to understand the effect of each on …

The triple‐helix is a unique secondary structural motif found primarily within the collagens. In
collagen, it is a homo‐or hetero‐tripeptide with a repeating primary sequence of (Gly‐X‐Y) …

Collagen I is one of the most abundant molecules in vertebrates constituting major parts of
the fibrillar extracellular matrix (ECM), thus providing structural integrity and mechanical …

Collagens were isolated and partially characterized from the marine demosponge, Ircinia
fusca from Gulf of Mannar (GoM), India, with an aim to develop potentially applicable …

Atomic force microscopy (AFM) has been emerging as a multifunctional molecular tool in
nanobiology and nanomedicine. This review summarizes the recent advances in AFM study …