ArticleThe Journal of biological chemistry2009
Motogenic sites in human fibronectin are masked by long range interactions.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
29 citing papers in PubMed, 47 citations in OpenAlex.
- Cultured Bacteria Provide Insight into the Functional Potential of the Coral-Associated Microbiome.mSystems · 2022Article
- Three-Dimensional Bioprinting of Decellularized Extracellular Matrix-Based Bioinks for Tissue Engineering.Molecules (Basel, Switzerland) · 2022Review
- Altered Protein Function Caused by AMD-associated Variant rs704 Links Vitronectin to Disease Pathology.Investigative ophthalmology & visual science · 2020Article
- The Interaction between the Third Type III Domain from Fibronectin and Anastellin Involves β-Strand Exchange.Biochemistry · 2017Article
- Fibronectin Conformation and Assembly: Analysis of Fibronectin Deletion Mutants and Fibronectin Glomerulopathy (GFND) Mutants.Biochemistry · 2017Article
- Allosteric Regulation of Fibronectin/α5β1 Interaction by Fibronectin-Binding MSCRAMMs.PloS one · 2016Article
- Stuck in the Middle: Fibronectin-Binding Proteins in Gram-Positive Bacteria.Frontiers in microbiology · 2016Review
- Structure and unfolding of the third type III domain from human fibronectin.Biochemistry · 2015Article
- Molecular architecture of native fibronectin fibrils.Nature communications · 2015Article
- Bivalent ligation of the collagen-binding modules of fibronectin by SFS, a non-anchored bacterial protein of Streptococcus equi.The Journal of biological chemistry · 2015Article
- On-Off Kinetics of Engagement of FNI Modules of Soluble Fibronectin by β-Strand Addition.PloS one · 2015Article
- Opposing effects of collagen I and vitronectin on fibronectin fibril structure and function.Matrix biology : journal of the International Society for Matrix Biology · 2014Article
- Regulation of the innate immune response by fibronectin: synergism between the III-1 and EDA domains.PloS one · 2014Article
- Structural analysis of collagen type I interactions with human fibronectin reveals a cooperative binding mode.The Journal of biological chemistry · 2013Article
- Regulation of matrix assembly through rigidity-dependent fibronectin conformational changes.The Journal of biological chemistry · 2013Article
- Fibronectin molecular status determination useful to differentiate between rheumatoid arthritis and systemic lupus erythematosus patients.Rheumatology international · 2013Article
- Ligation of the fibrin-binding domain by β-strand addition is sufficient for expansion of soluble fibronectin.The Journal of biological chemistry · 2012Article
- Article
- Fibronectin aggregation and assembly: the unfolding of the second fibronectin type III domain.The Journal of biological chemistry · 2011Article
- Structural and functional analysis of the tandem β-zipper interaction of a Streptococcal protein with human fibronectin.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Fibronectin (FN) is a large extracellular matrix glycoprotein important for development and wound healing in vertebrates. Recent work has focused on the ability of FN fragments and embryonic or tumorigenic splicing variants to stimulate fibroblast migration into collagen gels. This activity has been localized to specific sites and is not exhibited by full-length FN. Here we show that an N-terminal FN fragment, spanning the migration stimulation sites and including the first three type III FN domains, also lacks this activity. A screen for interdomain interactions by solution-state NMR spectroscopy revealed specific contacts between the Fn N terminus and two of the type III domains. A single amino acid substitution, R222A, disrupts the strongest interaction, between domains (4-5)FnI and (3)FnIII, and restores motogenic activity to the FN N-terminal fragment. Anastellin, which promotes fibril formation, destabilizes (3)FnIII and disrupts the observed (4-5)FnI-(3)FnIII interaction. We discuss these findings in the context of the control of cellular activity through exposure of masked sites.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.