Thermodynamic Interrogation of a Folding Disease. Mutant Mapping of Position 107 in Human Carbonic Anhydrase II Linked to Marble Brain Disease
Author:
Affiliation:
1. IFM-Department of Chemistry, Linköping University, 581 83 Linköping, Sweden
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi701720p
Reference44 articles.
1. Reshaping the folding energy landscape by chloride salt: impact on molten-globule formation and aggregation behavior of carbonic anhydrase
2. Cis-transisomerization is rate-determining in the reactivation of denatured human carbonic anhydrase II as evidenced by proline isomerase
3. High-Resolution Probing of Local Conformational Changes in Proteins by the Use of Multiple Labeling: Unfolding and Self-Assembly of Human Carbonic Anhydrase II Monitored by Spin, Fluorescent, and Chemical Reactivity Probes
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1. Mechanism of Action of Non-Synonymous Single Nucleotide Variations Associated with α-Carbonic Anhydrase II Deficiency;Molecules;2019-11-04
2. Molecular modelling and dynamics of CA2 missense mutations causative to carbonic anhydrase 2 deficiency syndrome;Journal of Biomolecular Structure and Dynamics;2019-10-08
3. Can Predicted Protein 3D Structures Provide Reliable Insights into whether Missense Variants Are Disease Associated?;Journal of Molecular Biology;2019-05
4. Identification of putative unfolding intermediates of the mutant His-107-tyr of human carbonic anhydrase II in a multidimensional property space;Proteins: Structure, Function, and Bioinformatics;2016-02-15
5. Perturbed Amelogenin Secondary Structure Leads to Uncontrolled Aggregation in Amelogenesis Imperfecta Mutant Proteins;Journal of Biological Chemistry;2010-12
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