Results 61 to 70 of about 22,293 (293)

Conserved Function of Fibrillin5 in the Plastoquinone-9 Biosynthetic Pathway in Arabidopsis and Rice

open access: yesFrontiers in Plant Science, 2017
Plastoquinone-9 (PQ-9) is essential for plant growth and development. Recently, we found that fibrillin5 (FBN5), a plastid lipid binding protein, is an essential structural component of the PQ-9 biosynthetic pathway in Arabidopsis.
Eun-Ha Kim   +5 more
doaj   +1 more source

Microscopic Anatomy of the Lining of Hemal Spaces in the Penaeid Shrimp, Sicyonia ingentis

open access: yesJournal of Marine Science and Engineering, 2021
The purpose of this paper is to present a morphological description of three different types of acellular material lining hemal spaces in a shrimp, providing a background for addressing future questions.
Rachel Brittany Sidebottom   +2 more
doaj   +1 more source

Metabolic and molecular events occurring during chromoplast biogenesis [PDF]

open access: yes, 2011
Chromoplasts are nonphotosynthetic plastids that accumulate carotenoids. They derive from other plastid forms, mostly chloroplasts. The biochemical events responsible for the interconversion of one plastid form into another are poorly documented. However,
Barsan, Cristina   +8 more
core   +2 more sources

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

Fibrillin Immunoreactive Fibers Constitute a Unique Network in the Human Dermis: Immunohistochemical Comparison of the Distributions of Fibrillin, Vitronectin, Amyloid P Component, and Orcein Stainable Structures in Normal Skin and Elastosis [PDF]

open access: yes, 1990
Fibrillin, a 350-kD glycoprotein, was recently localized to elastin-associated 10nm microfibrils. Here, the distribution of fibrillin immunoreactivity was determined in normal skin in individuals of different ages and in lesions of solar elastosis or ...
Dahlbäck, Björn   +5 more
core   +1 more source

The fibrillin microfibril/elastic fibre network: A critical extracellular supramolecular scaffold to balance skin homoeostasis

open access: yesExperimental Dermatology, 2020
Supramolecular networks composed of fibrillins (fibrillin‐1 and fibrillin‐2) and associated ligands form intricate cellular microenvironments which balance skin homoeostasis and direct remodelling. Fibrillins assemble into microfibrils which are not only
Christin S. Adamo   +2 more
semanticscholar   +1 more source

Fibrillin-1 and fibrillin-2 in human embryonic and early fetal development

open access: yesMatrix Biology, 2002
The extracellular glycoproteins fibrillin-1 and fibrillin-2 are major components of connective tissue microfibrils. Mutations in the fibrillin-1 and fibrillin-2 genes are responsible for the phenotypical manifestations of Marfan syndrome and congenital contractural arachnodactyly respectively, which emphasizes their essential roles in developmental ...
Quondamatteo, Fabio   +5 more
openaire   +4 more sources

Cell adhesion and integrin binding to recombinant human fibrillin-1 [PDF]

open access: yes, 1996
Fibrillin-1 is a major constituent of tissue microfibrils that occur in most connective tissues, either in close association with or independent of elastin.
Pfaff, Martin   +3 more
core   +1 more source

Fibrillin-1 Misfolding and Disease

open access: yesAntioxidants & Redox Signaling, 2006
Fibrillin-1 is a 350 kDa calcium-binding protein which assembles to form 10-12 nm microfibrils in the extracellular matrix (ECM). The structure of fibrillin-1 is dominated by two types of disulfide-rich motifs, the calcium- binding epidermal growth factor-like (cbEGF) and transforming growth factor beta binding protein-like (TB) domains.
Whiteman, P, Hutchinson, S, Handford, P
openaire   +4 more sources

Fibrillin-1 regulates the bioavailability of TGFβ1 [PDF]

open access: yesThe Journal of Cell Biology, 2007
We have discovered that fibrillin-1, which forms extracellular microfibrils, can regulate the bioavailability of transforming growth factor (TGF) β1, a powerful cytokine that modulates cell survival and phenotype. Altered TGFβ signaling is a major contributor to the pathology of Marfan syndrome (MFS) and related diseases.
Cay M. Kielty   +7 more
openaire   +3 more sources

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