Fibrillins: from biogenesis of microfibrils to signaling functions.

No abstract is available for this paper.

• Publication year

  2006

• Venue

  Current Topics in Developmental Biology

• Publication date

  Unknown publication date

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1016/S0070-2153(06)75004-9PMID 16984811
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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• Fibrillins 1 and 2 Perform Partially Overlapping Functions during Aortic Development*

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• Evidence for a critical contribution of haploinsufficiency in the complex pathogenesis of Marfan syndrome.

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• Fine tuning of growth factor signals depends on fibrillin microfibril networks.

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• Latent TGF-beta binding proteins: extracellular matrix association and roles in TGF-beta activation.

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• Fibrillin-rich microfibrils: elastic biopolymers of the extracellular matrix

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• Structure of the integrin binding fragment from fibrillin-1 gives new insights into microfibril organization.

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• Fibrillin-1 and -2 contain heparin-binding sites important for matrix deposition and that support cell attachment.

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• Cell Adhesion to Fibrillin-1 Molecules and Microfibrils Is Mediated by α5β1 and αvβ3 Integrins*

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• Solution structure of the third TB domain from LTBP1 provides insight into assembly of the large latent complex that sequesters latent TGF-beta.

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• Raman Microscopy and X-ray Diffraction, a Combined Study of Fibrillin-rich Microfibrillar Elasticity*

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• Dysregulation of TGF-beta activation contributes to pathogenesis in Marfan syndrome.

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• Latent Transforming Growth Factor β-binding Protein 1 Interacts with Fibrillin and Is a Microfibril-associated Protein*

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• Making sense of latent TGFbeta activation.

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• Fibrillins Can Co-assemble in Fibrils, but Fibrillin Fibril Composition Displays Cell-specific Differences*

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• Mutations of FBN1 and genotype–phenotype correlations in Marfan syndrome and related fibrillinopathies

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

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• Ultrastructural properties of ciliary zonule microfibrils.

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• Homo- and Heterotypic Fibrillin-1 and -2 Interactions Constitute the Basis for the Assembly of Microfibrils*

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• Ten novel FBN2 mutations in congenital contractural arachnodactyly: Delineation of the molecular pathogenesis and clinical phenotype

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• Mutation of the gene encoding fibrillin-2 results in syndactyly in mice.

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• Phenotypic Alteration of Vascular Smooth Muscle Cells Precedes Elastolysis in a Mouse Model of Marfan Syndrome

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• Latent TGF-beta binding protein LTBP-1 contains three potential extracellular matrix interacting domains.

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• Role of Ca2+ for the mechanical properties of fibrillin

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• Interactions of Fibrillin-1 with Heparin/Heparan Sulfate, Implications for Microfibrillar Assembly*

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• The Supramolecular Organization of Fibrillin-Rich Microfibrils

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• Distribution of fibrillin I in extracellular matrix and epithelia during early development of avian embryos

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• Specific sequence motif of 8-Cys repeats of TGF-beta binding proteins, LTBPs, creates a hydrophobic interaction surface for binding of small latent TGF-beta.

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• The microfibrillar proteins MAGP-1 and fibrillin-1 form a ternary complex with the chondroitin sulfate proteoglycan decorin.

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• Specific Sequence Motif of 8-Cys Repeats of TGF-β Binding Proteins, LTBPs, Creates a Hydrophobic Interaction Surface for Binding of Small Latent TGF-β

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• New Insights into the Assembly of Extracellular Microfibrils from the Analysis of the Fibrillin 1 Mutation in the Tight skin Mouse

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• Fibrillin-1, a calcium binding protein of extracellular matrix.

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