ArticleBiophysical journal2013
Folding factors and partners for the intrinsically disordered protein micro-exon gene 14 (MEG-14).
Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Schistosome esophageal gland factor MEG-8.2 drives host cell lysis and interacts with host immune proteins.PLoS pathogens · 2026Article
- The research contribution of the Schistosomiasis Collection at the Natural History Museum (SCAN): highlights, challenges and future directions.Infectious diseases of poverty · 2025Review
- RevisitingBiomolecules · 2023Article
- DichroIDP: a method for analyses of intrinsically disordered proteins using circular dichroism spectroscopy.Communications biology · 2023Article
- Divide, conquer and reconstruct: How to solve the 3D structure of recalcitrant Micro-Exon Gene (MEG) protein from Schistosoma mansoni.PloS one · 2023Article
- Characterization of a novel glycosylated glutathione transferase ofParasitology · 2019Article
- The yeast GRASP Grh1 displays a high polypeptide backbone mobility along with an amyloidogenic behavior.Scientific reports · 2018Article
- Advantages of synchrotron radiation circular dichroism spectroscopy to study intrinsically disordered proteins.European biophysics journal : EBJ · 2017Article
- Going deep into protein secondary structure with synchrotron radiation circular dichroism spectroscopy.Biophysical reviews · 2017Review
- Differential dehydration effects on globular proteins and intrinsically disordered proteins during film formation.Protein science : a publication of the Protein Society · 2017Article
- Dynamic footprint of sequestration in the molecular fluctuations of osteopontin.Journal of the Royal Society, Interface · 2015Article
- Distinct circular dichroism spectroscopic signatures of polyproline II and unordered secondary structures: applications in secondary structure analyses.Protein science : a publication of the Protein Society · 2014Article
- Another disordered chameleon: the Micro-Exon Gene 14 protein from Schistosomiasis.Biophysical journal · 2013Article
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Abstract
The micro-exon genes (MEG) of Schistosoma mansoni, a parasite responsible for the second most widely spread tropical disease, code for small secreted proteins with sequences unique to the Schistosoma genera. Bioinformatics analyses suggest the soluble domain of the MEG-14 protein will be largely disordered, and using synchrotron radiation circular dichroism spectroscopy, its secondary structure was shown to be essentially completely unfolded in aqueous solution. It does, however, show a strong propensity to fold into more ordered structures under a wide range of conditions. Partial folding was produced by increasing temperature (in a reversible process), contrary to the behavior of most soluble proteins. Furthermore, significant folding was observed in the presence of negatively charged lipids and detergents, but not in zwitterionic or neutral lipids or detergents. Absorption onto a surface followed by dehydration stimulated it to fold into a helical structure, as it did when the aqueous solution was replaced by nonaqueous solvents. Hydration of the dehydrated folded protein was accompanied by complete unfolding. These results support the identification of MEG-14 as a classic intrinsically disordered protein, and open the possibility of its interaction/folding with different partners and factors being related to multifunctional roles and states within the host.
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