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After modifications of collagen and laminin deposition, we investigated the effects of NPs on the expression of the main integrin-type receptors for these molecules, very late antigen 2, α2β1 integrin (VLA-2) and very late antigen 6, α6β1 integrin (VLA-6), by analysing their alpha chains (CD49b and CD49f, respectively) through flow cytometry.
Although it is known that the various (fibro cartilaginous tissues (articular cartilage, annulus fibrosus, nucleus pulposus, and meniscus) differ from one each other with respect to their molecular make-up, remarkable little quantitative information is available with respect to its biochemical constituents, such as collagen content, or the various posttranslational modifications of collagen.
It is also true that post-transcriptional modifications of collagen can occur that modify the peptide bound to the DR4 molecule.
We will now further discuss the characteristics of the posttranslational modifications of collagen in the mandible.
The nature and extent of posttranslational modifications of collagen, many of which are unique to collagen [ 19], are related to the organization of mineral and collagen fibrils [ 18].
Posttranslational modifications of collagen, such as intermolecular crosslinking and lysine hydroxylation, are the most essential determinants of bone strength, although the amount of collagen is also important.
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The chemical modification of collagen was confirmed by 1H NMR and FT-IR spectroscopy.
Electrophoretic mobility pattern of α, β and γ components of PAC shifted to higher molecular weight by 16,300 Da indicating modification of collagen.
Thus, vertebral fragility may not only be due to alterations in bone architecture but also to modification of collagen cross-link patterns thereby influencing bone's mechanical behavior.
The modification of collagen biomaterials to achieve the desired structures and functions is also addressed, with particular emphasis on mechanical control of collagen structure, creation of collagen composite materials and crosslinking of collagenous matrices.
In addition to MMPs, advanced glycemic end products (AGEs) are prominent candidates possibly responsible for a disturbance in collagen breakdown and chemical modification of collagen [20], [21].
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