Results 11 to 20 of about 1,605 (151)
Frontiers in Aging Neuroscience, 2016 Tendons among connective tissue, mainly collagen, contain also elastic fibres made of fibrillin 1, fibrillin 2 and elastin that are broadly distributed in tendons and represent 1-2% of the dried mass of the tendon.
Betti Giusti, Guglielmina Pepe
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British Journal of Ophthalmology, 2000 The glycoprotein fibrillin is the principal component of the ciliary zonule and has an important role in the strength and elasticity of ocular connective tissues. Fibrillin polymers form the structural scaffold of extensible microfibrils1-3 which are present in ocular elastic tissues and are arranged in parallel bundles to form the zonular fibres.4 ...
J L, Ashworth, C M, Kielty, D, McLeod
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LTBP-2 Has a Single High-Affinity Binding Site for FGF-2 and Blocks FGF-2-Induced Cell Proliferation. [PDF]
PLoS ONE, 2015 Latent transforming growth factor-beta-1 binding protein-2 (LTBP-2) belongs to the fibrillin-LTBP superfamily of extracellular matrix proteins. LTBPs and fibrillins are involved in the sequestration and storage of latent growth factors, particularly ...
Clementine Menz +6 more
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Transcriptome-Wide Expression Profiling in Skin Fibroblasts of Patients with Joint Hypermobility Syndrome/Ehlers-Danlos Syndrome Hypermobility Type. [PDF]
PLoS ONE, 2016 Joint hypermobility syndrome/Ehlers-Danlos syndrome hypermobility type (JHS/EDS-HT), is likely the most common systemic heritable connective tissue disorder, and is mostly recognized by generalized joint hypermobility, joint instability complications ...
Nicola Chiarelli +7 more
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Transcriptome analysis of skin fibroblasts with dominant negative COL3A1 mutations provides molecular insights into the etiopathology of vascular Ehlers-Danlos syndrome. [PDF]
PLoS ONE, 2018 Vascular Ehlers-Danlos syndrome (vEDS) is a dominantly inherited connective tissue disorder caused by mutations in the COL3A1 gene that encodes type III collagen (COLLIII), which is the major expressed collagen in blood vessels and hollow organs.
Nicola Chiarelli +4 more
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eLife, 2015 During development, biomechanical forces contour the body and provide shape to internal organs. Using genetic and molecular approaches in combination with a FRET-based tension sensor, we characterized a pulling force exerted by the elongating pharynx ...
Melissa Kelley +11 more
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Fibrillin Assembly Requires Fibronectin [PDF]
Molecular Biology of the Cell, 2009 Fibrillins constitute the major backbone of multifunctional microfibrils in elastic and nonelastic extracellular matrices. Proper assembly mechanisms are central to the formation and function of these microfibrils, and their properties are often compromised in pathological circumstances such as in Marfan syndrome and in other fibrillinopathies.
Laetitia, Sabatier +7 more
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Fibrillin microfibrils in bone physiology [PDF]
Matrix Biology, 2016 The severe skeletal abnormalities associated with Marfan syndrome (MFS) and congenital contractural arachnodactyly (CCA) underscore the notion that fibrillin assemblies (microfibrils and elastic fibers) play a critical role in bone formation and function in spite of representing a low abundance component of skeletal matrices.
Silvia, Smaldone, Francesco, Ramirez
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Colony formation in Phaeocystis antarctica: connecting molecular mechanisms with iron biogeochemistry [PDF]
Biogeosciences, 2018 Phaeocystis antarctica is an important phytoplankter of the Ross Sea where it dominates the early season bloom after sea ice retreat and is a major contributor to carbon export.
S. J. Bender +11 more
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Calcium Determines the Shape of Fibrillin [PDF]
Journal of Biological Chemistry, 1997 Velocity sedimentation experiments using authentic fibrillin-1 demonstrated sedimentation coefficients of s20,w0 = 5.1 +/- 0.1 in the Ca2+ form and s20,w0 = 6.2 +/- 0.1 in the Ca2+-free form. Calculations based on these results and the corresponding molecular mass predicted a shortening of fibrillin by approximately 25% and an increase in width of ...
Reinhardt, Dieter P. +5 more
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