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Chaperones as potential therapeutics for Krabbe disease

https://doi.org/10.1002/jnr.23755
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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1001/archneur.56.8.1014openalex-snapshot
Protracted Course of Krabbe Disease in an Adult Patient Bearing a Novel Mutation
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Molecular genetics of Krabbe disease (globoid cell leukodystrophy): Diagnostic and clinical implications
inferredcites →https://doi.org/10.1002/cmdc.201402411openalex-snapshot
Iminosugar‐Based Galactoside Mimics as Inhibitors of Galactocerebrosidase: SAR Studies and Comparison with Other Lysosomal Galactosidases
inferredcites →https://doi.org/10.1002/emmm.200900036openalex-snapshot
Treating lysosomal storage diseases with pharmacological chaperones: from concept to clinics
inferredcites →https://doi.org/10.1002/humu.21516openalex-snapshot
Chemical chaperone therapy: chaperone effect on mutant enzyme and cellular pathophysiology in β-galactosidase deficiency
inferredcites →https://doi.org/10.1002/iub.1288openalex-snapshot
Impairment of homeostasis in lysosomal storage disorders
inferredcites →https://doi.org/10.1006/bbrc.1994.1071openalex-snapshot
Krabbe Disease: Isolation and Characterization of a Full-Length cDNA for Human Galactocerebrosidase
inferredcites →https://doi.org/10.1006/bbrc.1995.2416openalex-snapshot
Galactose Stabilizes Various Missense Mutants of α-Galactosidase in Fabry Disease
inferredcites →https://doi.org/10.1007/bf02185759openalex-snapshot
Two different mutations are responsible for Krabbe disease in the Druze and Moslem Arab populations in Israel
inferredcites →https://doi.org/10.1007/s10545-010-9047-0openalex-snapshot
Therapeutic approaches for neuronopathic lysosomal storage disorders
inferredcites →https://doi.org/10.1016/0022-2836(91)90499-vopenalex-snapshot
Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coli
inferredcites →https://doi.org/10.1016/0968-0004(89)90168-0openalex-snapshot
Molecular chaperones: proteins essential for the biogenesis of some macromolecular structures
inferredcites →https://doi.org/10.1016/j.ab.2012.10.034openalex-snapshot
A high-throughput screening assay using Krabbe disease patient cells
inferredcites →https://doi.org/10.1016/j.bbapap.2006.08.012openalex-snapshot
Small molecule pharmacological chaperones: From thermodynamic stabilization to pharmaceutical drugs
inferredcites →https://doi.org/10.1016/j.braindev.2006.02.002openalex-snapshot
Fibroblast screening for chaperone therapy in β-galactosidosis
inferredcites →https://doi.org/10.1016/j.braindev.2012.12.002openalex-snapshot
Chaperone therapy update: Fabry disease, GM1-gangliosidosis and Gaucher disease
inferredcites →https://doi.org/10.1016/j.cbpa.2007.05.035openalex-snapshot
Gaucher disease
inferredcites →https://doi.org/10.1016/j.ceb.2010.05.005openalex-snapshot
Quality and quantity control at the endoplasmic reticulum
inferredcites →https://doi.org/10.1016/j.gene.2014.09.046openalex-snapshot
History, genetic, and recent advances on Krabbe disease
inferredcites →https://doi.org/10.1016/j.nbd.2009.07.030openalex-snapshot
Structure and function of the blood–brain barrier
inferredcites →https://doi.org/10.1016/j.pediatrneurol.2014.08.003openalex-snapshot
Experimental Therapies in the Murine Model of Globoid Cell Leukodystrophy
inferredcites →https://doi.org/10.1016/j.tem.2004.05.003openalex-snapshot
Pharmacological chaperones: potential treatment for conformational diseases
inferredcites →https://doi.org/10.1016/j.tibs.2006.05.001openalex-snapshot
Molecular chaperones: assisting assembly in addition to folding
inferredcites →https://doi.org/10.1016/j.ymgme.2006.09.010openalex-snapshot
Chemical chaperones improve transport and enhance stability of mutant α-glucosidases in glycogen storage disease type II
inferredcites →https://doi.org/10.1016/j.ymgme.2011.10.010openalex-snapshot
Krabbe disease: Clinical, biochemical and molecular information on six new patients and successful retrospective diagnosis using stored newborn screening cards
inferredcites →https://doi.org/10.1016/j.ymgme.2012.02.012openalex-snapshot
Therapeutic chaperone effect of N-Octyl 4-Epi-β-valienamine on murine GM1-gangliosidosis
inferredcites →https://doi.org/10.1016/j.ymgme.2012.05.021openalex-snapshot
Bone marrow transplantation increases efficacy of central nervous system-directed enzyme replacement therapy in the murine model of globoid cell leukodystrophy
inferredcites →https://doi.org/10.1016/j.ymgme.2014.05.009openalex-snapshot
Pharmacological chaperones increase residual β-galactocerebrosidase activity in fibroblasts from Krabbe patients
inferredcites →https://doi.org/10.1016/s0022-2275(20)39536-5openalex-snapshot
A simplified assay method for galactosyl ceramide β-galactosidase
inferredcites →https://doi.org/10.1016/s0079-6603(00)66026-9openalex-snapshot
Folding of a nascent peptide on the ribosome
inferredcites →https://doi.org/10.1016/s0092-8674(00)81881-4openalex-snapshot
ER Quality Control: The Cytoplasmic Connection
inferredcites →https://doi.org/10.1016/s0165-6147(03)00158-5openalex-snapshot
A contradictory treatment for lysosomal storage disorders: inhibitors enhance mutant enzyme activity
inferredcites →https://doi.org/10.1016/s0959-440x(00)00172-xopenalex-snapshot
Macromolecular crowding: an important but neglected aspect of the intracellular environment
inferredcites →https://doi.org/10.1016/s0968-0896(02)00005-6openalex-snapshot
Chemical Modification of the β-Glucocerebrosidase Inhibitor N-Octyl-β-valienamine: Synthesis and Biological Evaluation of 4-Epimeric and 4-O-(β-?-Galactopyranosyl) Derivatives
inferredcites →https://doi.org/10.1017/cbo9780511546310.002openalex-snapshot
Chaperone Function: The Orthodox View
inferredcites →https://doi.org/10.1038/4801openalex-snapshot
Accelerated transport and maturation of lysosomal α–galactosidase A in Fabry lymphoblasts by an enzyme inhibitor
inferredcites →https://doi.org/10.1038/gim.2015.211openalex-snapshot
Newborn screening for Krabbe disease in New York State: the first eight years’ experience
inferredcites →https://doi.org/10.1038/jhg.2015.61openalex-snapshot
Chaperone therapy for Krabbe disease: potential for late-onset GALC mutations
inferredcites →https://doi.org/10.1038/nature02262openalex-snapshot
Quality control in the endoplasmic reticulum protein factory
inferredcites →https://doi.org/10.1038/nrm1052openalex-snapshot
Quality control in the endoplasmic reticulum
inferredcites →https://doi.org/10.1038/nsmb.1591openalex-snapshot
Converging concepts of protein folding in vitro and in vivo
inferredcites →https://doi.org/10.1038/sj.bmt.1705970openalex-snapshot
Emerging trends in transplantation of inherited metabolic diseases
inferredcites →https://doi.org/10.1038/sj.mt.6300074openalex-snapshot
Pharmacological Enhancement of Mutated α-Glucosidase Activity in Fibroblasts from Patients with Pompe Disease
inferredcites →https://doi.org/10.1039/c5sc00754bopenalex-snapshot
Azasugar inhibitors as pharmacological chaperones for Krabbe disease
inferredcites →https://doi.org/10.1056/nejmoa042604openalex-snapshot
Transplantation of Umbilical-Cord Blood in Babies with Infantile Krabbe's Disease
inferredcites →https://doi.org/10.1056/nejmoa1409547openalex-snapshot
Lumacaftor–Ivacaftor in Patients with Cystic Fibrosis Homozygous for Phe508del CFTR
inferredcites →https://doi.org/10.1073/pnas.1105639108openalex-snapshot
Insights into Krabbe disease from structures of galactocerebrosidase
inferredcites →https://doi.org/10.1073/pnas.1112653108openalex-snapshot
Sneak peak at galactocerebrosidase, Krabbe disease's lysosomal hydrolase
inferredcites →https://doi.org/10.1073/pnas.1311990110openalex-snapshot
Structural snapshots illustrate the catalytic cycle of β-galactocerebrosidase, the defective enzyme in Krabbe disease
inferredcites →https://doi.org/10.1073/pnas.192582899openalex-snapshot
Chemical chaperones increase the cellular activity of N370S β-glucosidase: A therapeutic strategy for Gaucher disease
inferredcites →https://doi.org/10.1073/pnas.2536657100openalex-snapshot
Chemical chaperone therapy for brain pathology in G M1 -gangliosidosis
inferredcites →https://doi.org/10.1073/pnas.66.2.302openalex-snapshot
Globoid Cell Leucodystrophy (Krabbe's Disease): Deficiency of Galactocerebroside β-Galactosidase
inferredcites →https://doi.org/10.1073/pnas.95.6.2727openalex-snapshot
The ubiquitin-proteasome pathway: The complexity and myriad functions of proteins death
inferredcites →https://doi.org/10.1074/jbc.m308523200openalex-snapshot
Pharmacological Enhancement of β-Hexosaminidase Activity in Fibroblasts from Adult Tay-Sachs and Sandhoff Patients
inferredcites →https://doi.org/10.1074/jbc.m609304200openalex-snapshot
Pyrimethamine as a Potential Pharmacological Chaperone for Late-onset Forms of GM2 Gangliosidosis
inferredcites →https://doi.org/10.1084/jem.20122005openalex-snapshot
Resetting translational homeostasis restores myelination in Charcot-Marie-Tooth disease type 1B mice
inferredcites →https://doi.org/10.1089/adt.2011.0370openalex-snapshot
Identification and Characterization of Pharmacological Chaperones to Correct Enzyme Deficiencies in Lysosomal Storage Disorders
inferredcites →https://doi.org/10.1093/brain/39.1-2.74openalex-snapshot
A NEW FAMILIAL, INFANTILE FORM OF DIFFUSE BRAIN-SCLEROSIS
inferredcites →https://doi.org/10.1093/hmg/2.11.1841openalex-snapshot
Cloning and expression cDNA encoding human galactocerebrosidase, the enzyme deficient in globoid cell leukodystrophy
inferredcites →https://doi.org/10.1096/fj.05-3826fjeopenalex-snapshot
Enzyme replacement therapy results in substantial improvements in early clinical phenotype in a mouse model of globoid cell leukodystrophy
inferredcites →https://doi.org/10.1096/fj.06-6169comopenalex-snapshot
Single‐dose intracerebroventricular administration of galactocerebrosidase improves survival in a mouse model of globoid cell leukodystrophy
inferredcites →https://doi.org/10.1101/cshperspect.a006734openalex-snapshot
Integration of Clearance Mechanisms: The Proteasome and Autophagy
inferredcites →https://doi.org/10.1101/cshperspect.a007526openalex-snapshot
Protein Folding and Quality Control in the ER
inferredcites →https://doi.org/10.1111/j.1600-0854.2004.00232.xopenalex-snapshot
Pharmacologic Rescue of Conformationally‐Defective Proteins: Implications for the Treatment of Human Disease
inferredcites →https://doi.org/10.1111/j.1742-4658.2006.05410.xopenalex-snapshot
Hydrophilic iminosugar active‐site‐specific chaperones increase residual glucocerebrosidase activity in fibroblasts from Gaucher patients
inferredcites →https://doi.org/10.1111/j.1742-4658.2007.06041.xopenalex-snapshot
Active‐site‐specific chaperone therapy for Fabry disease
inferredcites →https://doi.org/10.1111/j.1742-4658.2007.06043.xopenalex-snapshot
Introduction: Pharmacological chaperone therapy for lysosomal storage disorders – leveraging aspects of the folding pathway to maximize activity of misfolded mutant proteins
inferredcites →https://doi.org/10.1124/mi.2.5.308openalex-snapshot
Protein Origami: Therapeutic Rescue of Misfolded Gene Products
inferredcites →https://doi.org/10.1126/science.1068408openalex-snapshot
Molecular Chaperones in the Cytosol: from Nascent Chain to Folded Protein
inferredcites →https://doi.org/10.1126/science.171.3966.73openalex-snapshot
Krabbe's Globoid Cell Leukodystrophy: Deficiency of Galactocerebrosidase in Serum, Leukocytes, and Fibroblasts
inferredcites →https://doi.org/10.1128/mcb.01453-06openalex-snapshot
Autophagy Is Activated for Cell Survival after Endoplasmic ReticulumStress
inferredcites →https://doi.org/10.1159/000112332openalex-snapshot
Partial Enzyme Deficiencies: Residual Activities and the Development of Neurological Disorders
inferredcites →https://doi.org/10.1159/000133703openalex-snapshot
Regional mapping of the human galactocerebrosidase gene (GALC) to 14q31 by in situ hybridization
inferredcites →https://doi.org/10.1177/2326409813517663openalex-snapshot
Lysosomal Storage Diseases
inferredcites →https://doi.org/10.1186/jbiol186openalex-snapshot
What are pharmacological chaperones and why are they interesting?
inferredcites →https://doi.org/10.1523/jneurosci.3095-15.2016openalex-snapshot
Altered Trafficking and Processing ofGALCMutants Correlates with Globoid Cell Leukodystrophy Severity
inferredcites →https://doi.org/10.1523/jneurosci.4199-14.2015openalex-snapshot
Mechanism-Based Combination Treatment Dramatically Increases Therapeutic Efficacy in Murine Globoid Cell Leukodystrophy
inferredcites →https://doi.org/10.1523/jneurosci.6383-09.2010openalex-snapshot
Molecular Characterization of Mutations That Cause Globoid Cell Leukodystrophy and Pharmacological Rescue Using Small Molecule Chemical Chaperones
inferredcites →https://doi.org/10.4137/pmc.s2332openalex-snapshot
Chaperone Therapy for Neuronopathic Lysosomal Diseases: Competitive Inhibitors as Chemical Chaperones for Enhancement of Mutant Enzyme Activities
inferredcites →https://doi.org/10.4172/2329-6682.1000118openalex-snapshot
Genetic Test and Gene Therapy for Krabbe Disease: An Update
inferredcites →https://doi.org/10.4414/smw.2002.09861openalex-snapshot
Endoplasmic reticulum storage diseases
inferredcites →https://doi.org/10.5114/fn.2012.32364openalex-snapshot
Original article Diagnostic difficulties in Krabbe disease: a report of two cases and review of literature

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.2139/ssrn.4647251openalex-extracted
First Example of Multivalent Pyrrolidines Acting as Pharmacological Chaperones Against Gaucher Disease
inferred← citeshttps://doi.org/10.1002/9781119013112.ch29openalex-snapshot
Sphingolipidoses and Related Disorders
inferred← citeshttps://doi.org/10.1002/jnr.24558openalex-snapshot
Proteostasis network alteration in lysosomal storage disorders: Insights from the mouse model of Krabbe disease
inferred← citeshttps://doi.org/10.1016/b978-0-323-99616-7.00030-xopenalex-snapshot
Drug delivery systems in Krabbe disease—present and prospective approaches
inferred← citeshttps://doi.org/10.1016/b978-0-443-16156-8.00007-9openalex-snapshot
Glycosphingolipids and central nervous system–related diseases
inferred← citeshttps://doi.org/10.1016/j.bioorg.2024.107295openalex-snapshot
Multivalent pyrrolidines acting as pharmacological chaperones against Gaucher disease
inferred← citeshttps://doi.org/10.1016/j.neuroscience.2025.10.017openalex-snapshot
Beyond Krabbe disease, the intriguing connection of galactocerebrosidase (GALC) with nervous system illness: A novel risk factor?
inferred← citeshttps://doi.org/10.1017/9781108556767openalex-snapshot
Movement Disorders and Inherited Metabolic Disorders
inferred← citeshttps://doi.org/10.1021/acscatal.0c02609openalex-snapshot
The Catalytic Reaction Mechanism of the β-Galactocerebrosidase Enzyme Deficient in Krabbe Disease
inferred← citeshttps://doi.org/10.1021/acsmedchemlett.0c00377openalex-snapshot
The Bicyclic Form of galacto-Noeurostegine Is a Potent Inhibitor of β-Galactocerebrosidase
inferred← citeshttps://doi.org/10.1042/ebc20220218openalex-snapshot
In silicomodelling of the function of disease-related CAZymes
inferred← citeshttps://doi.org/10.1055/s-0039-1685529openalex-snapshot
Opening New Horizons in the Treatment of Childhood Onset Leukodystrophies
inferred← citeshttps://doi.org/10.1080/07391102.2020.1742790openalex-snapshot
Molecular dynamics simulations to decipher the structural and functional consequences of pathogenic missense mutations in the galactosylceramidase (GALC) protein causing Krabbe’s disease
inferred← citeshttps://doi.org/10.1111/neup.12967openalex-snapshot
From pathological mechanisms in Krabbe disease to cutting‐edge therapy: A comprehensive review
inferred← citeshttps://doi.org/10.3390/ijms18102049openalex-snapshot
E-Learning for Rare Diseases: An Example Using Fabry Disease
inferred← citeshttps://doi.org/10.3390/molecules25143145openalex-snapshot
Second-Generation Pharmacological Chaperones: Beyond Inhibitors
inferred← citeshttps://doi.org/10.3390/molecules31101678openalex-snapshot
From Biodiversity to Biocompatibility: Insights from the Special Issue “Analysis and Biological Evaluation of Bioactive Compounds from Natural Sources—Second Edition”
inferred← citeshttps://doi.org/10.3390/nu16183114openalex-snapshot
Diet and Nutrients in Rare Neurological Disorders: Biological, Biochemical, and Pathophysiological Evidence
inferred← citeshttps://doi.org/10.4018/978-1-5225-5282-6.ch018openalex-snapshot
Childhood Neurodegenerative Disorders
inferred← citeshttps://doi.org/10.4103/1673-5374.228712openalex-snapshot
Heterozygous carriers of galactocerebrosidase mutations that cause Krabbe disease have impaired microglial function and defective repair of myelin damage
inferred← citeshttps://doi.org/10.4103/jpn.jpn_283_20openalex-snapshot
Persisting irritability with fever is not always meningitis
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