Results 21 to 30 of about 23,206 (306)

Advanced glycation end-products reduce collagen molecular sliding to affect collagen fibril damage mechanisms but not stiffness. [PDF]

open access: yesPLoS ONE, 2014
Advanced glycation end-products (AGE) contribute to age-related connective tissue damage and functional deficit. The documented association between AGE formation on collagens and the correlated progressive stiffening of tissues has widely been presumed ...
Gion Fessel   +7 more
doaj   +1 more source

D-band strain underestimates fibril strain for twisted collagen fibrils at low strains [PDF]

open access: yes, 2021
Collagen fibrils are the main structural component of load-bearing tissues such as tendons, ligaments, skin, the cornea of the eye, and the heart. The D-band of collagen fibrils is an axial periodic density modulation that can be easily characterized by tissue-level X-ray scattering. During mechanical testing, D-band strain is often used as a proxy for
arxiv   +1 more source

Thermal Destabilization of Collagen Matrix Hierarchical Structure by Freeze/Thaw. [PDF]

open access: yesPLoS ONE, 2016
This study aims to characterize and understand the effects of freezing on collagen structures and functionality. Specifically, thermodynamic destabilization of collagen at molecular- and fibril-levels by combination of low temperatures and freezing were ...
Altug Ozcelikkale, Bumsoo Han
doaj   +1 more source

Collagen Fibril Orientation Instructs Fibroblast Differentiation Via Cell Contractility

open access: yesAdvanced Science, 2023
Collagen alignment is one of the key microarchitectural signatures of many pathological conditions, including scarring and fibrosis. Investigating how collagen alignment modulates cellular functions will pave the way for understanding tissue scarring and
Jiranuwat Sapudom   +6 more
doaj   +1 more source

Understanding the viscoelastic behavior of collagen matrices through relaxation time distribution spectrum [PDF]

open access: yes, 2013
This study aims to provide understanding of the macroscopic viscoelastic behavior of collagen matrices through studying the relaxation time distribution spectrum obtained from stress relaxation tests.
Li, Haiyue, Xu, Bin, Zhang, Yanhang
core   +1 more source

Analysis of opticin binding to collagen fibrils identifies a single binding site in the gap region and a high specificity towards thin heterotypic fibrils containing collagens II, and XI or V/XI.

open access: yesPLoS ONE, 2020
Opticin is a class III member of the extracellular matrix small leucine-rich repeat protein/proteoglycan (SLRP) family found in vitreous humour and cartilage.
Uwe Hansen   +3 more
doaj   +1 more source

Multiscale Modeling of Collagen Fibril in Bone at Various Crosslink Densities: An Insight into Its Deformation Mechanisms [PDF]

open access: yes, 2014
Multiscale modeling of collagen fibril is carried out by incorporating the material properties of collagen obtained from steered molecular dynamics into the finite element model of collagen fibril with inclusion of crosslinks.
D.R. Katti, K.S.Katti, S.M. Pradhan
core   +2 more sources

Molecular origin of viscoelasticity in mineralized collagen fibrils [PDF]

open access: yesBiomaterials Science, 9(9), 3390-3400 (2021), 2021
Bone is mineralized tissue constituting the skeletal system, supporting and protecting body organs and tissues. At the molecular level, mineralized collagen fibril is the basic building block of bone tissue, and hence, understanding bone properties down to fundamental tissue structures enables to better identify the mechanisms of structural failures ...
arxiv   +1 more source

Revealing Accessibility of Cryptic Protein Binding Sites within the Functional Collagen Fibril

open access: yesBiomolecules, 2017
Fibrillar collagens are the most abundant proteins in the extracellular matrix. Not only do they provide structural integrity to all of the connective tissues in the human body, but also their interactions with multiple cell receptors and other matrix ...
Cody L. Hoop   +4 more
doaj   +1 more source

Uniform spatial distribution of collagen fibril radii within tendon implies local activation of pC-collagen at individual fibrils [PDF]

open access: yesPhysical Biology, v. 13 (2016) 046008, 2016
Collagen fibril cross-sectional radii show no systematic variation between the interior and the periphery of fibril bundles, indicating an effectively constant rate of collagen incorporation into fibrils throughout the bundle. Such spatially homogeneous incorporation constrains the extracellular diffusion of collagen precursors from sources at the ...
arxiv   +1 more source

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