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

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

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

http://www.wikidata.org/entity/Q42157069

about

Heparin/heparan sulfate controls fibrillin-1, -2 and -3 self-interactions in microfibril assembly The molecular genetics of Marfan syndrome and related disorders Fibrillins in Tendon Microfibrillar proteins MAGP-1 and MAGP-2 induce Notch1 extracellular domain dissociation and receptor activation A systems biology approach for the investigation of the heparin/heparan sulfate interactome ADAMTSL-6 is a novel extracellular matrix protein that binds to fibrillin-1 and promotes fibrillin-1 fibril formation Xenopus fibrillin regulates directed convergence and extension.Identification of cell surface targets through meta-analysis of microarray data.Defining elastic fiber interactions by molecular fishing: an affinity purification and mass spectrometry approach.Biogenesis and function of fibrillin assemblies.Fibrillin-1 mutations causing Weill-Marchesani syndrome and acromicric and geleophysic dysplasias disrupt heparan sulfate interactions Rat mammary extracellular matrix composition and response to ibuprofen treatment during postpartum involution by differential GeLC-MS/MS analysis.Complex contributions of fibronectin to initiation and maturation of microfibrils Fibrillin-containing microfibrils are key signal relay stations for cell function.Fibrillin assembly requires fibronectin.Molecular mechanisms of thoracic aortic dissection.Analysis of dermal elastic fibers in the absence of fibulin-5 reveals potential roles for fibulin-5 in elastic fiber assembly.ADAMTS-10 and -6 differentially regulate cell-cell junctions and focal adhesions.Extracellular microfibrils: contextual platforms for TGFbeta and BMP signaling.Vascular extracellular matrix and arterial mechanics.Epithelial-mesenchymal status influences how cells deposit fibrillin microfibrils.Fibrillin-1 interactions with heparin. Implications for microfibril and elastic fiber assembly.Classical and neonatal Marfan syndrome mutations in fibrillin-1 cause differential protease susceptibilities and protein function.Fibrillin expression and localization in various types of carcinomas of the thyroid gland.Polygenic Causes of Congenital Diaphragmatic Hernia Produce Common Lung Pathologies.Selective integrin subunit reduction disrupts fibronectin extracellular matrix deposition and fibrillin 1 gene expression.Assembly of fibrillin microfibrils governs extracellular deposition of latent TGF beta.Osteosarcoma in a Marfan patient with a novel premature termination codon in the FBN1 gene.Potential role for heparan sulfate proteoglycans in regulation of transforming growth factor-beta (TGF-beta) by modulating assembly of latent TGF-beta-binding protein-1.Heparanase Inhibitors Facilitate the Assembly of the Basement Membrane in Artificial Skin Fell-Muir Lecture: Fibrillin microfibrils: structural tensometers of elastic tissues?Early fibrillin-1 assembly monitored through a modifiable recombinant cell approach.Fibrillin-2 and Tenascin-C bridge the age gap in lung epithelial regeneration.Modification of the structure and function of fibrillin-1 by homocysteine suggests a potential pathogenetic mechanism in homocystinuria.Heparan sulfate regulates fibrillin-1 N- and C-terminal interactions.Arg-Gly-Asp-containing domains of fibrillins-1 and -2 distinctly regulate lung fibroblast migration.The FBN2 gene: new mutations, locus-specific database (Universal Mutation Database FBN2), and genotype-phenotype correlations.Genomic Identification and Functional Characterization of Essential Genes in Caenorhabditis elegans.Enhanced fibrillin-2 expression is a general feature of wound healing and sclerosis: potential alteration of cell attachment and storage of TGF-beta.

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P2860

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

http://www.wikidata.org/entity/Q42157069

description

2003 nî lūn-bûn

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2003年の論文

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年学术文章

@zh-my

2003年学术文章

@zh-sg

2003年學術文章

@yue

2003年學術文章

@zh

2003年學術文章

@zh-hant

name

Fibrillin-1 and -2 contain hep ...... that support cell attachment.

@en

Fibrillin-1 and -2 contain hep ...... that support cell attachment.

@nl

type

label

Fibrillin-1 and -2 contain hep ...... that support cell attachment.

@en

Fibrillin-1 and -2 contain hep ...... that support cell attachment.

@nl

prefLabel

Fibrillin-1 and -2 contain hep ...... that support cell attachment.

@en

Fibrillin-1 and -2 contain hep ...... that support cell attachment.

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P1433

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P1433

Biochemical Journal

P1476

Fibrillin-1 and -2 contain hep ...... that support cell attachment.

@en

P2093

Robert P Mecham

http://www.w3.org/2001/XMLSchema#string

Thomas J Broekelmann

http://www.w3.org/2001/XMLSchema#string

Timothy M Ritty

http://www.w3.org/2001/XMLSchema#string

P2860

Syndecans: multifunctional cell-surface co-receptors

Interactions of fibrillin-1 with heparin/heparan sulfate, implications for microfibrillar assembly

Cell adhesion and integrin binding to recombinant human fibrillin-1

Cell surface proteoglycan binds mouse mammary epithelial cells to fibronectin and behaves as a receptor for interstitial matrix

Functions of cell surface heparan sulfate proteoglycans

Identification of the developmental marker, JB3-antigen, as fibrillin-2 and its de novo organization into embryonic microfibrous arrays.

The syndecans, tuners of transmembrane signaling.

A mutation in FBN1 disrupts profibrillin processing and results in isolated skeletal features of the Marfan syndrome.

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

Marfan syndrome: defective synthesis, secretion, and extracellular matrix formation of fibrillin by cultured dermal fibroblasts.

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425-432

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scholarly article

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10.1042/BJ20030649

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P433

Pt 2

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P478

375

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P50

Claudio C Werneck

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2003-10-01T00:00:00Z

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12837131

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1223679

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