ArticleThe Journal of biological chemistry2014
Structural basis of pharmacological chaperoning for human β-galactosidase.
Article in The Journal of biological chemistry, 2014. 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, 65 citations in OpenAlex.
- Mutations in Glycosyltransferases and Glycosidases: Implications for Associated Diseases.Biomolecules · 2024Article
- Validation of a highly sensitive HaloTag-based assay to evaluate the potency of a novel class of allosteric β-Galactosidase correctors.PloS one · 2023Article
- spJournal of enzyme inhibition and medicinal chemistry · 2022Article
- Design and synthesis of biologically active carbaglycosylamines: From glycosidase inhibitors to pharmacological chaperones.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2022Review
- Activatable Second Near-Infrared Fluorescent Probes: A New Accurate Diagnosis Strategy for Diseases.Biosensors · 2021Review
- Structure of the murine lysosomal multienzyme complex core.Science advances · 2021Article
- Mechanistic Insights into the Chaperoning of Human Lysosomal-Galactosidase Activity: Highly Functionalized Aminocyclopentanes andMolecules (Basel, Switzerland) · 2020Article
- A Pharmacological Chaperone Therapy for Acute Intermittent Porphyria.Molecular therapy : the journal of the American Society of Gene Therapy · 2020Article
- Novel stereoselective syntheses ofRSC advances · 2019Article
- Thiol-ene "Click" Synthesis and Pharmacological Evaluation ofMolecules (Basel, Switzerland) · 2019Article
- Structural Insights into the Molecular Evolution of the Archaeal Exo-β-d-Glucosaminidase.International journal of molecular sciences · 2019Review
- Chain-Branched Polyhydroxylated Octahydro-Pharmaceuticals (Basel, Switzerland) · 2019Article
- Clinical and molecular characteristics of 11 Chinese probands with GM1 gangliosidosis.Metabolic brain disease · 2018Article
- Cloning, purification and biochemical characterisation of a GH35 beta-1,3/beta-1,6-galactosidase from the mucin-degrading gut bacterium Akkermansia muciniphila.Glycoconjugate journal · 2018Article
- SAAMP 2.0: An algorithm to predict genotype-phenotype correlation of lysosomal storage diseases.Clinical genetics · 2018Article
- Probing the Inhibitor versus Chaperone Properties of sp²-Iminosugars towards Human β-Glucocerebrosidase: A Picomolar Chaperone for Gaucher Disease.Molecules (Basel, Switzerland) · 2018Article
- From structural biology to designing therapy for inborn errors of metabolism.Journal of inherited metabolic disease · 2016Review
- Histone deacetylase inhibitors attenuate P-aIgA1-induced cell proliferation and extracellular matrix synthesis in human renal mesangial cells in vitro.Acta pharmacologica Sinica · 2016Article
- Emerging novel concept of chaperone therapies for protein misfolding diseases.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2014Review
Corrections and comments
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Authors and funding
10 authors at 6 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
GM1 gangliosidosis and Morquio B disease are autosomal recessive diseases caused by the defect in the lysosomal β-galactosidase (β-Gal), frequently related to misfolding and subsequent endoplasmic reticulum-associated degradation. Pharmacological chaperone (PC) therapy is a newly developed molecular therapeutic approach by using small molecule ligands of the mutant enzyme that are able to promote the correct folding and prevent endoplasmic reticulum-associated degradation and promote trafficking to the lysosome. In this report, we describe the enzymological properties of purified recombinant human β-Gal(WT) and two representative mutations in GM1 gangliosidosis Japanese patients, β-Gal(R201C) and β-Gal(I51T). We have also evaluated the PC effect of two competitive inhibitors of β-Gal. Moreover, we provide a detailed atomic view of the recognition mechanism of these compounds in comparison with two structurally related analogues. All compounds bind to the active site of β-Gal with the sugar-mimicking moiety making hydrogen bonds to active site residues. Moreover, the binding affinity, the enzyme selectivity, and the PC potential are strongly affected by the mono- or bicyclic structure of the core as well as the orientation, nature, and length of the exocyclic substituent. These results provide understanding on the mechanism of action of β-Gal selective chaperoning by newly developed PC compounds.
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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.