Results 1 to 10 of about 5,562 (218)

Morphometric analysis of the human endoneurial extracellular matrix components during aging [PDF]

open access: yesArchives of Biological Sciences, 2021
The aim of this study was to analyze the expression of extracellular matrix (ECM) proteins in human endoneurium during aging. We harvested 15 cadaveric sural nerves, distributed in 3 age groups (I: 25-44, II: 45-64, III: 65-86 years old).
Kundalić Braca K.   +8 more
doaj   +1 more source

Streptococcus mutans Proteases Degrade Dentinal Collagen

open access: yesDentistry Journal, 2022
Here, we explored the role of S. mutans’s whole cell and discrete fractions in the degradation of type I collagen and dentinal collagen. Type I collagen gels and human demineralized dentin slabs (DS) were incubated in media alone or with one of the ...
Bo Huang   +5 more
doaj   +1 more source

Current Insights into Collagen Type I [PDF]

open access: yesPolymers, 2021
Collagen type I (Col-I) is unique due to its high biocompatibility in human tissue. Despite its availability from various sources, Col-I naturally mimics the extracellular matrix (ECM) and generally makes up the larger protein component (90%) in vasculature, skin, tendon bone, and other tissue.
Ruth Naomi   +2 more
openaire   +2 more sources

Correlation between Collagen Type I/III Ratio and Scar Formation in Patients Undergoing Immediate Reconstruction with the Round Block Technique after Breast-Conserving Surgery

open access: yesBiomedicines, 2023
The aim of this study was to investigate the relationship between the collagen type I/III ratio and scarring in patients who underwent immediate reconstruction with the round block technique (RBT) after breast conservation surgery. Seventy-eight patients
Hyo-young Kim   +7 more
doaj   +1 more source

Bioprinting of Collagen Type I and II via Aerosol Jet Printing for the Replication of Dense Collagenous Tissues

open access: yesFrontiers in Bioengineering and Biotechnology, 2021
Collagen has grown increasingly present in bioprinting, however collagen bioprinting has mostly been limited to the extrusion printing of collagen type I to form weak collagen hydrogels.
Rory Gibney   +2 more
doaj   +1 more source

Nanomechanics of Type I Collagen [PDF]

open access: yesBiophysical Journal, 2016
Type I collagen is the predominant collagen in mature tendons and ligaments, where it gives them their load-bearing mechanical properties. Fibrils of type I collagen are formed by the packing of polypeptide triple helices. Higher-order structures like fibril bundles and fibers are assembled from fibrils in the presence of other collagenous molecules ...
Sameer, Varma   +2 more
openaire   +2 more sources

Cycloheximide promotes type I collagen maturation mainly via collagen prolyl 4-hydroxylase subunit α2

open access: yesActa Biochimica et Biophysica Sinica, 2022
Aberrant deposition of collagen is associated with cancer development and tissue fibrosis. Proline hydroxylation, catalyzed by collagen prolyl 4-hydroxylases (C-P4Hs), is necessary for collagen maturation and secretion.
Shi Run   +6 more
doaj   +1 more source

Characterization of Type I and Type III Collagen in the Intramuscular Connective Tissue of Wuzhumuqin Sheep

open access: yesAnimals, 2023
Intramuscular connective tissue (IMCT) collagen is an important factor in meat quality. This study analyzed the characteristics of type I and III collagen in the IMCT of the semitendinosus (SD) and longissimus dorsi (LD) of Wuzhumuqin sheep at different ...
Xige He   +9 more
doaj   +1 more source

Collagen fibril formation in vitro: From origin to opportunities

open access: yesMaterials Today Bio, 2022
Sometimes, to move forward, it is necessary to look back. Collagen type I is one of the most commonly used biomaterials in tissue engineering and regenerative medicine.
Diana M. Darvish
doaj   +1 more source

A Comprehensive Review on Collagen Type I Development of Biomaterials for Tissue Engineering: From Biosynthesis to Bioscaffold

open access: yesBiomedicines, 2022
Collagen is the most abundant structural protein found in humans and mammals, particularly in the extracellular matrix (ECM). Its primary function is to hold the body together.
Ibrahim N. Amirrah   +5 more
doaj   +1 more source

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