ArticleThe Journal of biological chemistry2011
Probing the folded state of fibronectin type III domains in stretched fibrils by measuring buried cysteine accessibility.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Strain-dependent glutathionylation of fibronectin fibers impacts mechano-chemical behavior and primes an integrin switch.Nature communications · 2024Article
- Review
- Fibronectin fiber creep under constant force loading.Acta biomaterialia · 2019Article
- Rationally designed synthetic protein hydrogels with predictable mechanical properties.Nature communications · 2018Article
- Multiple Cryptic Binding Sites are Necessary for Robust Fibronectin Assembly: An In Silico Study.Scientific reports · 2017Article
- Fibronectin Conformation and Assembly: Analysis of Fibronectin Deletion Mutants and Fibronectin Glomerulopathy (GFND) Mutants.Biochemistry · 2017Article
- Detection of an Integrin-Binding Mechanoswitch within Fibronectin during Tissue Formation and Fibrosis.ACS nano · 2017Article
- Fibronectin fibrils regulate TGF-β1-induced Epithelial-Mesenchymal Transition.Matrix biology : journal of the International Society for Matrix Biology · 2017Article
- Mechanotransduction Dynamics at the Cell-Matrix Interface.Biophysical journal · 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
- Structure and unfolding of the third type III domain from human fibronectin.Biochemistry · 2015Article
- Studying early stages of fibronectin fibrillogenesis in living cells by atomic force microscopy.Molecular biology of the cell · 2015Article
- SLLISWD sequence in the 10FNIII domain initiates fibronectin fibrillogenesis.The Journal of biological chemistry · 2013Article
- Forced protein unfolding leads to highly elastic and tough protein hydrogels.Nature communications · 2013Article
- Finding the weakest link: exploring integrin-mediated mechanical molecular pathways.Journal of cell science · 2012Review
- Using molecular mechanics to predict bulk material properties of fibronectin fibers.PLoS computational biology · 2012Article
- GFP's mechanical intermediate states.PloS one · 2012Article
- Contribution of unfolding and intermolecular architecture to fibronectin fiber extensibility.Biophysical journal · 2011Article
- Dynamic structure of plasma fibronectin.Critical reviews in biochemistry and molecular biologyReview
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Fibronectin (FN) is an extracellular matrix protein that is assembled into fibrils by cells during tissue morphogenesis and wound healing. FN matrix fibrils are highly elastic, but the mechanism of elasticity has been debated: it may be achieved by mechanical unfolding of FN-III domains or by a conformational change of the molecule without domain unfolding. Here, we investigate the folded state of FN-III domains in FN fibrils by measuring the accessibility of buried cysteines. Four of the 15 FN-III domains (III-2, -3, -9, and -11) appear to unfold in both stretched fibrils and in solution, suggesting that these domains spontaneously open and close even in the absence of tension. Two FN-III domains (III-6 and -12) appear to unfold only in fibrils and not in solution. These results suggest that domain unfolding can at best contribute partially to the 4-fold extensibility of fibronectin fibrils.
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