ArticleProtein engineering2002
Novel mutant human fibronectin FIII9-10 domain pair with increased conformational stability and biological activity.
Article in Protein engineering, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 30 citations in OpenAlex.
- Modulating Integrin and Growth Factor Signaling With Peptides: Strategies to Synergistically Enhance Bone Tissue Regeneration.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
- The Body's Cellular and Molecular Response to Protein-Coated Medical Device Implants: A Review Focused on Fibronectin and BMP Proteins.International journal of molecular sciences · 2020Review
- Detection of an Integrin-Binding Mechanoswitch within Fibronectin during Tissue Formation and Fibrosis.ACS nano · 2017Article
- 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
- Using self-assembled monolayers to model cell adhesion to the 9th and 10th type III domains of fibronectin.Langmuir : the ACS journal of surfaces and colloids · 2009Article
- Emerging concepts in engineering extracellular matrix variants for directing cell phenotype.Regenerative medicine · 2009Review
- Controlling integrin specificity and stem cell differentiation in 2D and 3D environments through regulation of fibronectin domain stability.Biomaterials · 2009Article
- The influence of surfactant on PLGA microsphere glass transition and water sorption: remodeling the surface morphology to attenuate the burst release.Pharmaceutical research · 2006Article
- Interdomain tilt angle determines integrin-dependent function of the ninth and tenth FIII domains of human fibronectin.The Journal of biological chemistry · 2004Article
- Synergistic activity of the ninth and tenth FIII domains of human fibronectin depends upon structural stability.The Journal of biological chemistry · 2003Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The ninth and tenth type III domains (FIII9-10) in the central cell binding domain of human fibronectin contain integrin receptor binding sites, including RGD in FIII10 and a synergy site, PHSRN, in FIII9. The specific amino acids that contribute to cell binding have been identified by the use of wild-type and mutant fragments of human fibronectin containing the FIII9-10 domain pair. At high concentrations FIII9-10 mimics, to a large extent, the biological activity of the full-length fibronectin molecule. However, FIII9 is conformationally unstable, even in the context of the FIII9-10 pair. Here we report the construction of a series of hybrid mouse-human FIII9-10 pairs that confer varying degrees of conformational stability to FIII9. The conformational stability of the human FIII9 module was increased 2-3-fold by substitution of Leu1408 with Pro. We demonstrate that the biological activity of this mutant is enhanced. The resulting FIII9-10 mutant has good solution properties and will provide a template into which further mutations can be incorporated in order to probe the structure-function relationship of the cell binding module of fibronectin.
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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.