ArticleThe Journal of biological chemistry2004
Interdomain tilt angle determines integrin-dependent function of the ninth and tenth FIII domains of human fibronectin.
Article in The Journal of biological chemistry, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
21 citing papers in PubMed, 56 citations in OpenAlex.
- FN9-10ELP, an ECM-Mimetic Fusion Protein, Protects Human Mesenchymal Stem Cells from Etoposide-Induced Senescence.International journal of molecular sciences · 2025Article
- VE-cadherin RGD motifs are dispensable for cell-cell junctions, endothelial barrier function and monocyte extravasation.Tissue barriers · 2025Article
- Structural insights into integrin αScience advances · 2021Article
- Article
- Hydrogels with precisely controlled integrin activation dictate vascular patterning and permeability.Nature materials · 2017Article
- Integrin α3β1 Binding to Fibronectin Is Dependent on the Ninth Type III Repeat.The Journal of biological chemistry · 2015Article
- Utilizing Fibronectin Integrin-Binding Specificity to Control Cellular Responses.Advances in wound care · 2015Review
- Interrogating protonated/deuterated fibronectin fragment layers adsorbed to titania by neutron reflectivity and their concomitant control over cell adhesion.Journal of the Royal Society, Interface · 2015Article
- Biologically-active laminin-111 fragment that modulates the epithelial-to-mesenchymal transition in embryonic stem cells.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Plasma and cellular fibronectin: distinct and independent functions during tissue repair.Fibrogenesis & tissue repair · 2011Article
- Identification of novel and distinct binding sites within tenascin-C for soluble and fibrillar fibronectin.The Journal of biological chemistry · 2011Article
- Nanoscale engineering of extracellular matrix-mimetic bioadhesive surfaces and implants for tissue engineering.Biochimica et biophysica acta · 2011Review
- Guiding epithelial cell phenotypes with engineered integrin-specific recombinant fibronectin fragments.Tissue engineering. Part A · 2011Article
- Emerging concepts in engineering extracellular matrix variants for directing cell phenotype.Regenerative medicine · 2009Review
- Motogenic sites in human fibronectin are masked by long range interactions.The Journal of biological chemistry · 2009Article
- Controlling integrin specificity and stem cell differentiation in 2D and 3D environments through regulation of fibronectin domain stability.Biomaterials · 2009Article
- Designing an extracellular matrix protein with enhanced mechanical stability.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Interdomain association in fibronectin: insight into cryptic sites and fibrillogenesis.The EMBO journal · 2007Article
- The solution structure of the invasive tip complex from Afa/Dr fibrils.Molecular microbiology · 2006Article
- Integrin switching modulates adhesion dynamics and cell migration.Cell adhesion & migrationReview
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Integrins are an important family of signaling receptors that mediate diverse cellular processes. The binding of the abundant extracellular matrix ligand fibronectin to integrins alpha(5)beta(1) and alpha(v)beta(3) is known to depend upon the Arg-Gly-Asp (RGD) motif on the tenth fibronectin FIII domain. The adjacent ninth FIII domain provides a synergistic effect on RGD-mediated integrin alpha(5)beta(1) binding and downstream function. The precise molecular basis of this synergy remains elusive. Here we have dissected further the function of FIII9 in integrin binding by analyzing the biological activity of the FIII9-10 interdomain interface variants and by determining their structural and dynamic properties in solution. We demonstrate that the contribution of FIII9 to both alpha(5)beta(1) and alpha(v)beta(3) binding and downstream function critically depends upon the interdomain tilt between the FIII9 and FIII10 domains. Our data suggest that modulation of integrin binding by FIII9 may arise in part from its steric properties that determine accessibility of the RGD motif. These findings have wider implications for mechanisms of integrin-ligand binding in the physiological context.
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What OpenQuestion holds
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.