Fibril example sentences
Related (4): collagen, myofibril, microfibril, neurofibril
"Fibril" Example Sentences
Common Phrases
- Microtubules and neurofilaments are formed from bundles of fibrils organized in parallel arrays.
- The fibrils of collagen give connective tissue strength and elasticity.
- Amyloid fibrils are associated with Alzheimer's disease and other neurodegenerative disorders.
- Aggregates of amyloid fibrils can build up in the brain, interfering with neuronal function.
- The amyloid fibril plaques found in the brains of Alzheimer's patients contain abnormally folded amyloid beta protein.
- Scientists are studying how amyloid fibrils form and accumulate with the hope of developing new treatments for Alzheimer's.
- The cytoskeleton of eukaryotic cells consists of three types of fibrils: microtubules, actin filaments, and intermediate filaments.
- Microtubule fibrils are assembled from tubulin proteins.
- Actin filaments are fibrils composed of actin monomers.
- Keratin intermediate filaments provide mechanical strength and resistance to stress within cells.
- Muscle cells contain elongated actin and myosin fibrils that slide past each other, allowing for contraction.
- Interstitial fibrils form a framework that supports the structure of connective tissues.
- The collagen fibrils of tendons connect muscle to bone.
- Elastic fibrils allow tissues like skin and blood vessels to stretch and retract.
- Neurofilaments and microtubules together make up the cytoskeleton of axons in neurons.
- Muscle fibrils become shorter and thicker during muscle atrophy.
- Protein aggregation results in the formation of insoluble protein fibrils and amyloid fibrils.
- Fibril formation is a characteristic feature of many neurodegenerative diseases.
- Scientists are studying how proteins misfold and aggregate to better understand fibril formation.
- Microglia become activated in response to the presence of amyloid fibrils and neuronal damage.
- Brain trauma and brain lesions can lead to abnormal tau fibril formation.
- Tau fibrils accumulate inside neural cells forming neurofibrillary tangles, a hallmark of Alzheimer's disease.
- Fragmented axonal fibrils may occur after traumatic brain or spinal cord injury.
- Crosslinking agents can be used to stabilize collagen fibrils for use in tissue engineering applications.
- Vitamin C promotes the formation of collagen fibrils that are stronger and more stable.
- Magnetically aligned fibrils can be used to guide the growth of neurons and other cells.
- Pharmacological compounds that inhibit fibril formation are being investigated for potential neuroprotective effects.
- Transmission electron microscopy can be used to visualize individual amyloid fibrils and determine their morphology.
- At high concentrations, insulin forms fibrils that can precipitate out of solution.
- Fibril forming proteins contain regions that are prone to adopt beta sheet structures.
- Branched fibrils form when multiple filaments associate laterally.
- Immunohistochemistry stains can be used to detect the presence of fibrils in tissue sections.
- Heat shock proteins may inhibit protein aggregation by binding to partially folded intermediates and preventing fibril formation.
- Disrupting hydrogen bonds within fibrils can halt their growth and proliferation.
- Scientists are working to develop fibril disrupting molecules that could be used as future therapeutics.
- Chaperone proteins may help degrade fibrils by unravelling their structures.
- Fibril structure can be characterized using atomic force microscopy.
- Certain strains of bacteria produce extracellular protein fibrils known as curli.
- Shorter fibrils tend to aggregate more quickly than longer fibrils due to higher surface area to volume ratios.
- Cryo-electron microscopy is being used to visualize the structure of amyloid fibrils at high resolution.
- Cytoskeletal fibrils help maintain cell shape, polarity and mechanical integrity.
- Heating samples can induce protein fibrils to unfold and dissociate back into monomers.
- Solid-state NMR spectroscopy provides information about conformation and packing of proteins within fibrils.
- Fibril forming propensities vary among different proteins and protein isoforms.
- Transgenic animal models are used to study fibril formation in vivo.
- Fibrils usually grow by laterally incorporating soluble proteins.
- Chemical modifications can disrupt hydrophobic interactions that stabilize fibril structures.
- Competitive inhibitors can bind to fibrils and prevent them from elongating.
- Fibrils tend to be insoluble and resistant to proteolytic degradation.
- Thioflavin T dye selectively binds to amyloid fibrils and is commonly used to detect their presence.
- Some microorganisms produce crosslinked extracellular fibrils that provide structural support.
- Fibril formation generally follows a nucleation-polymerization mechanism.
- Modified proteins that are prone to forming fibrils can be used as markers for certain disease states.
- Fibrils often form elongated, unbranched structures with high aspect ratios.
- Mechanisms that disrupt fibril elongation may help slow the progression of neurodegenerative diseases.
- Scientists are working to develop anti-fibril antibodies for diagnostic and therapeutic applications.
- Crystalline fibril structures can diffract X-rays, enabling their 3D structure to be determined.
- Breakdown products of degenerating fibrils may activate microglia and immune cells in the brain.
- Fibrous proteins contain amino acid sequences that promote alignment of polypeptide chains into fibrils.
- Mutations that enhance fibril formation are associated with familial forms of some neurodegenerative disorders.