Results 151 to 160 of about 1,756 (189)
Fibrillin-containing microfibrils are structural components of extracellular matrices of a diverse range of tissues, including bone. Their importance in bone biology is illustrated by the skeletal abnormalities manifest in the congenital disorder, Marfan
A Evdokiou +2 more
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© 2004 by The American Society for Biochemistry and Molecular Biology, Inc.The interactions of microfibril-associated glycoprotein (MAGP)-2 have been investigated with fibrillins and fibrillin-containing microfibrils.
Eric Hanssen, Mark A Gibson
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The organisation of elastin and fibrillins 1 and 2 in the cruciate ligament complex
Although elastin fibres and oxytalan fibres (bundles of microfibrils) have important mechanical, biochemical and cell regulatory functions, neither their distribution nor their function in cruciate ligaments has been investigated.
David G Spiller +2 more
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Fibrillins: From Biogenesis of Microfibrils to Signaling Functions
Dirk Hubmacher +2 more
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2005
Fibrillin microfibrils are widely distributed extracellular matrix assemblies that endow elastic and nonelastic connective tissues with long-range elasticity. They direct tropoelastin deposition during elastic fibrillogenesis and form an outer mantle for mature elastic fibers.
Kielty, Cay M. +3 more
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Fibrillin microfibrils are widely distributed extracellular matrix assemblies that endow elastic and nonelastic connective tissues with long-range elasticity. They direct tropoelastin deposition during elastic fibrillogenesis and form an outer mantle for mature elastic fibers.
Kielty, Cay M. +3 more
openaire +4 more sources
Immunohistochemical expression of fibrillin‐1 and fibrillin‐2 during tooth development
Journal of Periodontal Research, 2014Background and ObjectiveOxytalan fibers are categorized as a microfibril assembly without elastin deposition, and are unique components in the periodontal ligament (PDL). However, little is known about their formation during PDL development. To clarify the mechanisms of oxytalan fiber formation in developing PDL, we performed immunohistochemical ...
M, Kira-Tatsuoka +4 more
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The fibrillin‐marfan syndrome connection
BioEssays, 1993AbstractA few years ago no one would have suspected that the well‐known disorder of connective tissue, Marfan syndrome, could be caused by mutations in a recently discovered extracellular component, fibrillin. Likewise, nobody would have predicted that fibrillin represents a small family of proteins that are associated with several pheno‐typically ...
F, Ramirez, L, Pereira, H, Zhang, B, Lee
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Fibrillin immunofluorescence in pseudoxanthoma elasticum
Journal of the American Academy of Dermatology, 1995Pseudoxanthoma elasticum (PXE) is a rare heritable connective tissue disorder manifested by skin, ocular, and cardiovascular anomalies. The basic defect is unknown; however, the microscopic findings are indicative of defects in elastic fibers. Among the components of the elastic fibers are elastin and elastin-associated microfibrils.We assessed the ...
M, Godfrey +6 more
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2010
Microfibrils are supramolecular structures ubiquitously found in the extracellular matrix of elastic and nonelastic tissues. The three members of the cysteine-rich fibrillin family constitute the core of microfibrils. Mutations in fibrillin-1 and -2 lead to a number of heritable connective tissue disorders termed fibrillinopathies.
Dirk Hubmacher, Dieter P. Reinhardt
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Microfibrils are supramolecular structures ubiquitously found in the extracellular matrix of elastic and nonelastic tissues. The three members of the cysteine-rich fibrillin family constitute the core of microfibrils. Mutations in fibrillin-1 and -2 lead to a number of heritable connective tissue disorders termed fibrillinopathies.
Dirk Hubmacher, Dieter P. Reinhardt
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Proteomic analysis of fibrillin‐rich microfibrils
PROTEOMICS, 2006Abstract MS has been used to investigate the composition of fibrillin‐rich microfibrils from non‐elastic and elastic tissues, and to compare fibrillin‐1 tryptic fingerprints derived from whole zonules, microfibrils and recombinant fibrillin‐1.
Cain, Stuart A.; id_orcid 0000-0001-8417-1058 +5 more
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