To better understand some aspects of bone matrix glycation, we used an in vitro glycation
approach. Within two weeks, our glycation procedures led to the formation of advanced …

Post-translational modifications of collagen, such as non-enzymatic glycation (NEG), occur
through the presence of extracellular sugars and cause the formation of advanced glycation …

Non-enzymatic glycation (NEG) and enzymatic biochemical processes create crosslinks that
modify the extracellular matrix (ECM) and affect the turnover of bone tissue. Because NEG …

Chemical crosslinks known as advanced glycation end-products (AGEs) are associated with
increased bone fracture risk and deteriorated bone mechanical properties. However …

Advanced glycation end products (AGEs) accumulate in bone extracellular matrix as people
age. Although previous evidence shows that the accumulation of AGEs in bone matrix may …

Advanced glycation end-products (AGEs) are a category of post translational modification
associated with the degradation of the structural properties of multiple different types of …

Type I collagen, the major organic component of bone matrix, undergoes a series of post-
translational modifications that occur with aging, such as the non-enzymatic glycation. This …

INTRODUCTION: The accumulation of advanced glycation end-products (AGEs) in bone
has been suggested to adversely affect the fracture resistance of bone with aging, diabetes …

We developed an in vitro model which provides the ability to test the effects of advanced
glycation end products (AGEs), specifically pentosidine (PEN) and one of its inhibitors, the …

Objectives Advanced glycation end-products (AGEs) are a post-translational modification of
collagen that form spontaneously in the skeletal matrix due to the presence of reducing …