collagen fibril

This polymer of tropocollogen is known as a collagen fibril.

In the adventitial layer there was an abundance of collagen fibrils.

Cross-links, or chemical interactions, between collagen fibrils are also affected.

The crosslinks are important to the high strength and chemical resistance necessary for the functioning collagen fibrils.

They originally nucleate at the gaps between collagen fibrils.

Collagen fibrils are often abnormally sized and have unusually large amounts of space between them.

Fibronectin was also observed to be closely associated with the newly deposited collagen fibrils.

As a result, collagen fibrils are not assembled properly; they appear ribbon-like and disorganized under the microscope.

The appearance of collagen fibrils and stromal keratocytes was close to normal in both groups of specimens.

The size and arrangement of type II collagen fibrils is essential for the normal structure of these tissues.

Multiple collagen fibrils form into collagen fibers.

The corneal stroma consists of approximately 200 layers of mainly type I collagen fibrils.

PFM has been successfully applied to a range of biological materials such as teeth, bone, and single collagen fibrils.

When mutations in the COL11A2 gene affect the structure of collagen fibrils, hearing loss can result.

Collagen fibrils are semicrystalline aggregates of collagen molecules.

This protein is a component of connective tissue, binds to type I collagen fibrils, and plays a role in matrix assembly.

Elastic connective tissue and an abundance of collagen fibrils occupied intercellular spaces between smooth muscle cells.

In addition, ingestion of hydrolyzed collagen was shown to increase the density of collagen fibrils.

The crimps in the collagen fibrils allow the tendons to have some flexibility as well as a low compressive stiffness.

The disease is caused by a defect in the structure of the type-IV collagen fibrils of the glomerular basement membrane.

Bone is actually a composite of soft, flexible microscopic threads, known as collagen fibrils, and hard, inflexible calcium and phosphorous crystals.

More particularly, bone mineral is formed from globular and plate structures, distributed among the collagen fibrils of bone and forming yet larger structure.

The dermatan sulfate side chains of decorin aggregate in solution, and this behavior can assist with the assembly of the collagen fibrils.

The tenocytes produce the collagen molecules, which aggregate end-to-end and side-to-side to produce collagen fibrils.

Unlike primary dentin, mantle dentin lacks phosphoryn, has loosely packed collagen fibrils and is less mineralized.