Results 131 to 140 of about 1,871 (159)
Interaction of fibrillin-1 fragments with transforming growth factor 1
, 2012 Fibrillins are large structural glycoproteins in the extracellular matrix that multimerize to form microfibril suprastructures in connective tissues. Fibrillin-containing microfibrils confer mechanical stability to tissues and regulate bioavailability of
Kaur, Jasvir
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ADAMTSL-6 Is a Novel Extracellular Matrix Protein That Binds to Fibrillin-1 and Promotes Fibrillin-1 Fibril FormationThis research was originally published in the Journal of Biological Chemistry. Ko Tsutsui, Ri-ichiroh Manabe, Tomiko Yamada, Itsuko Nakano, Yasuko Oguri, Douglas R. Keene, Gerhard Sengle, Lynn Y. Sakai and Kiyotoshi Sekiguchi. ADAMTSL-6 Is a Novel Extracellular Matrix Protein That Binds to Fibrillin-1 and Promotes Fibrillin-1 Fibril Formation. J. Biol.
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Fibrillin-1: Organization in Microfibrils and Structural Properties
Journal of Molecular Biology, 1996 To investigate the microfibrillar organization and structural properties of fibrillin-1, we produced overlapping recombinant peptides in human cells which altogether span the fibrillin-1 molecule. The peptides were purified under non-denaturing conditions and extensive characterization indicated correct folding.
Dieter P Reinhardt +2 more
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Fibrillin-3 expression in human development
Matrix Biology, 2011 Fibrillin proteins are the major components of extracellular microfibrils found in many connective tissues. Fibrillin-1 and fibrillin-2 are well studied and mutations in these proteins cause a number of fibrillinopathies including Marfan syndrome and ...
Laetitia Sabatier +2 more
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Proteomic analysis of fibrillin-rich microfibrils
Proteomics, 2006 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.
Stuart A Cain +2 more
exaly +2 more sources
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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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Journal of Molecular Biology, 1999
Fibrillin-1 is a major structural component of 10-12 nm connective tissue microfibrils and has a modular organisation that includes 43 calcium binding epidermal growth factor-like (cbEGF) domains and seven transforming growth factor beta-binding protein-like (TB) domains.
S, Kettle +5 more
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Fibrillin-1 is a major structural component of 10-12 nm connective tissue microfibrils and has a modular organisation that includes 43 calcium binding epidermal growth factor-like (cbEGF) domains and seven transforming growth factor beta-binding protein-like (TB) domains.
S, Kettle +5 more
openaire +2 more sources
Journal of Dental Research, 2002
The elastic system fibers consist of three types—oxytalan, elaunin, and elastic fibers—differing in their relative microfibril and elastin contents. All three types are found in human gingiva, but human periodontal ligaments contain only elastin-free fibers.
E, Tsuruga, K, Irie, T, Yajima
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The elastic system fibers consist of three types—oxytalan, elaunin, and elastic fibers—differing in their relative microfibril and elastin contents. All three types are found in human gingiva, but human periodontal ligaments contain only elastin-free fibers.
E, Tsuruga, K, Irie, T, Yajima
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The Anatomical Record, 2019
ABSTRACTImmunolocalization studies have shown that fibrillin‐1 is distributed ubiquitously in the connective tissue space from early embryonic times through old age. When mutated, the gene for fibrillin‐1 (FBN1) causes the Marfan syndrome, a common inherited disorder of connective tissue.
Noe L. Charbonneau +6 more
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ABSTRACTImmunolocalization studies have shown that fibrillin‐1 is distributed ubiquitously in the connective tissue space from early embryonic times through old age. When mutated, the gene for fibrillin‐1 (FBN1) causes the Marfan syndrome, a common inherited disorder of connective tissue.
Noe L. Charbonneau +6 more
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Non-Enzymatic Glycation of Human Fibrillin-1
Gerontology, 2008Non-enzymatic glycation of proteins is one of the key mechanisms in the pathogenesis of diabetic complications and may be significant in the age-related changes of tissues. We isolated and investigated the in vitro glycation of human aortic fibrillin-1. Fibrillin-1 was prepared from thoracic aortas of 9 accident victims distributed in three age groups.
Milena, Atanasova +3 more
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