Fibrillin-1 is a large, extracellular matrix glycoprotein that serves as a structural component of 10-12 nm calcium-binding microfibrils.
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They have overlapping binding sites for several basement-membrane proteins, tropoelastin, fibrillin, fibronectin and proteoglycans, and they participate in diverse supramolecular structures.
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The gene normally makes a protein called fibrillin, which forms hairlike structures called microfibrils that give ligaments, tendons, artery walls and other tissues strength and resilience.
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Simply put, homocysteine is a'corrosive'of long-living proteins, i . e . collagen or elastin, or lifelong proteins, i . e . fibrillin.
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A transgenic mouse has been created carrying a single copy of a mutant fibrillin-1, a mutation similar to that found in the human gene known to cause Marfan syndrome.
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Such proteins are involved in blood coagulation or are components of the extracellular matrix like fibrillin and LTBP-1 ( Latent-transforming growth factor beta-binding protein 1 ).
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The elastic fiber is formed from the elastic microfibril ( consisting of numerous proteins such as microfibrillar-associated glycoproteins, fibrillin, fibullin, and the elastin receptor ) and amorphous elastin.
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This suggests that while the symptoms of Marfan syndrome may seem consistent with a connective tissue disorder, the mechanism is more likely related to reduced sequestration of TGF-? by fibrillin.
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Marfan's syndrome results from mutations in the " FBN1 " gene, defective production of the protein fibrillin-1, and a number of physical abnormalities including aneurysm of the aortic root.
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Truncations of the FBN1 protein in these patients were seen to have two consequences for protein production : a mutant / truncated fibrillin protein and very low plasma asprosin levels ( from a postulated dominant negative effect ).
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