ArticleThe EMBO journal2007
Interdomain association in fibronectin: insight into cryptic sites and fibrillogenesis.
Article in The EMBO journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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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.
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Who cites it
51 citing papers in PubMed, 75 citations in OpenAlex.
- Fibronectin matrix assembly at a glance.Journal of cell science · 2025Review
- Developmental Changes in Patterns of Distribution of Fibronectin and Tenascin-C in the Chicken Cornea: Evidence for Distinct and Independent Functions during Corneal Development and Morphogenesis.International journal of molecular sciences · 2023Article
- Up-regulated fibronectin in 3D culture facilitates spreading of triple negative breast cancer cells on 2D through integrin β-5 and Src.Scientific reports · 2019Article
- Integrative Protein Modeling in RosettaNMR from Sparse Paramagnetic Restraints.Structure (London, England : 1993) · 2019Article
- Unique structural features of a bacterial autotransporter adhesin suggest mechanisms for interaction with host macromolecules.Nature communications · 2019Article
- Genetic Suppression of Basement Membrane Defects inGenetics · 2018Article
- Crystal structure of the second fibronectin type III (FN3) domain from human collagen α1 type XX.Acta crystallographica. Section F, Structural biology communications · 2017Article
- Mutations in Fibronectin Cause a Subtype of Spondylometaphyseal Dysplasia with "Corner Fractures".American journal of human genetics · 2017Article
- The Interaction between the Third Type III Domain from Fibronectin and Anastellin Involves β-Strand Exchange.Biochemistry · 2017Article
- Structure of unliganded membrane-proximal domains FN4-FN5-FN6 of DCC.Protein & cell · 2017Article
- Spontaneous Unfolding-Refolding of Fibronectin Type III Domains Assayed by Thiol Exchange: THERMODYNAMIC STABILITY CORRELATES WITH RATES OF UNFOLDING RATHER THAN FOLDING.The Journal of biological chemistry · 2017Article
- Prediction of HBF-0259 interactions with hepatitis B Virus receptors and surface antigen secretory factors.Virusdisease · 2016Article
- Extracellular matrix bioscaffolds in tissue remodeling and morphogenesis.Developmental dynamics : an official publication of the American Association of Anatomists · 2016Review
- Poly(Lactic Acid) Nanoparticles Targeting α5β1 Integrin as Vaccine Delivery Vehicle, a Prospective Study.PloS one · 2016Article
- Structure and unfolding of the third type III domain from human fibronectin.Biochemistry · 2015Article
- Molecular architecture of native fibronectin fibrils.Nature communications · 2015Article
- The ultrastructure of fibronectin fibers pulled from a protein monolayer at the air-liquid interface and the mechanism of the sheet-to-fiber transition.Biomaterials · 2015Article
- Extracellular matrix and liver disease.Antioxidants & redox signaling · 2014Review
- Structural determinants of the interaction between the Haemophilus influenzae Hap autotransporter and fibronectin.Microbiology (Reading, England) · 2014Article
- Extracellular matrix as an inductive scaffold for functional tissue reconstruction.Translational research : the journal of laboratory and clinical medicine · 2014Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The process by which fibronectin (FN), a soluble multidomain protein found in tissue fluids, forms insoluble fibrillar networks in the extracellular matrix is poorly understood. Cryptic sites found in FN type III domains have been hypothesized to function as nucleation points, thereby initiating fibrillogenesis. Exposure of these sites could occur upon tension-mediated mechanical rearrangement of type III domains. Here, we present the solution structures of the second type III domain of human FN ((2)FNIII), and that of an interaction complex between the first two type III domains ((1-2)FNIII). The two domains are connected through a long linker, flexible in solution. A weak but specific interdomain interaction maintains (1-2)FNIII in a closed conformation that associates weakly with the FN N-terminal 30 kDa fragment (FN30 kDa). Disruption of the interdomain interaction by amino-acid substitutions dramatically enhances association with FN30 kDa. Truncation analysis of (1-2)FNIII reveals that the interdomain linker is necessary for robust (1-2)FNIII-FN30 kDa interaction. We speculate on the importance of this interaction for FN function and present a possible mechanism by which tension could initiate fibrillogenesis.
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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.