Results 21 to 30 of about 2,560 (174)

FBN-1, a fibrillin-related protein, is required for resistance of the epidermis to mechanical deformation during C. elegans embryogenesis

open access: yeseLife, 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
doaj   +1 more source

Elastin is Localised to the Interfascicular Matrix of Energy Storing Tendons and Becomes Increasingly Disorganised With Ageing [PDF]

open access: yes, 2017
Tendon is composed of fascicles bound together by the interfascicular matrix (IFM). Energy storing tendons are more elastic and extensible than positional tendons; behaviour provided by specialisation of the IFM to enable repeated interfascicular sliding
A Heinz   +48 more
core   +4 more sources

Fibrillin microfibrils in bone physiology [PDF]

open access: yesMatrix 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
openaire   +2 more sources

Fibrillines et fibrillinopathies [PDF]

open access: yesmédecine/sciences, 1996
Microfibrils contain a variety of proteins, the most prominent of which are the two fibrillins. Fibrillins are large glycoproteins (320 kDa) ubiquitously distributed in connective tissues. Together with amorphous elastin, fibrillin-containing microfibrils form the elastic fibers.
Collod-Beroud, Gwenaëlle   +1 more
openaire   +2 more sources

Assembly of Epithelial Cell Fibrillins [PDF]

open access: yesJournal of Investigative Dermatology, 2001
Fibrillins are large structural macromolecules that are components of connective tissue microfibrils. Fibrillin microfibrils have been found in association with basement membranes, where microfibrils appear to insert directly into the lamina densa.
Karaman-Jurukovska, Nevena   +6 more
openaire   +2 more sources

Colony formation in Phaeocystis antarctica: connecting molecular mechanisms with iron biogeochemistry [PDF]

open access: yesBiogeosciences, 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
doaj   +1 more source

Dual role for the latent transforming growth factor-beta binding protein in storage of latent TGF-beta in the extracellular matrix and as a structural matrix protein [PDF]

open access: yes, 1995
The role of the latent TGF-beta binding protein (LTBP) is unclear. In cultures of fetal rat calvarial cells, which form mineralized bonelike nodules, both LTBP and the TGF-beta 1 precursor localized to large fibrillar structures in the extracellular ...
Bonewald, L.F.   +4 more
core   +2 more sources

A tandem duplication within the fibrillin 1 gene is associated with the mouse tight skin mutation. [PDF]

open access: yes, 1996
Mice carrying the Tight skin (Tsk) mutation have thickened skin and visceral fibrosis resulting from an accumulation of extracellular matrix molecules.
Buchberg, Arthur M.   +7 more
core   +3 more sources

Fibrillin-1 mutations causing Weill-Marchesani syndrome and acromicric and geleophysic dysplasias disrupt heparan sulfate interactions.

open access: yesPLoS ONE, 2012
The extracellular glycoprotein fibrillin-1 forms microfibrils that act as the template for elastic fibers. Most mutations in fibrillin-1 cause Marfan syndrome with severe cardiovascular and ocular symptoms, and tall stature.
Stuart A Cain   +4 more
doaj   +1 more source

The evolution of metazoan extracellular matrix [PDF]

open access: yes, 2011
The modular domain structure of extracellular matrix (ECM) proteins and their genes has allowed extensive exon/domain shuffling during evolution to generate hundreds of ECM proteins.
Adams   +55 more
core   +1 more source

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