Protein structural features predict responsiveness to pharmacological chaperone treatment for three lysosomal storage disorders

Three-dimensional structures of proteins can provide important clues into the efficacy of personalized treatment. We perform a structural analysis of variants within three inherited lysosomal storage disorders, comparing variants responsive to pharmacological chaperone treatment to those unresponsiv...

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Bibliographic Details
Main Authors:	Woodard, J. (Author), Zhang, Y. (Author), Zheng, W. (Author)
Format:	Article
Language:	English
Published:	Public Library of Science 2021
Subjects:	amino acid substitution Article biology chaperone chemistry Computational Biology crystal structure decision tree Decision Trees drug effect endoplasmic reticulum Fabry disease Fabry Disease Gaucher disease Gaucher Disease genetics glycogen storage disease type 2 Glycogen Storage Disease Type II human Humans kinetics Kinetics ligand binding lysosome storage disease machine learning Machine Learning metabolism missense mutation Models, Molecular molecular dynamics molecular library molecular model mutant protein Mutant Proteins Mutation, Missense personalized medicine Precision Medicine prediction protein binding Protein Binding protein conformation Protein Conformation protein folding Protein Folding protein localization protein stability Protein Stability protein structure Small Molecule Libraries steady state structure analysis treatment response
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Protein structural features predict responsiveness to pharmacological chaperone treatment for three lysosomal storage disorders

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