Impaired trafficking of mutants of lysosomal glucocerebrosidase in Gaucher's disease.
about
Inhibition of endoplasmic reticulum-associated degradation rescues native folding in loss of function protein misfolding diseasesGlucocerebrosidase mutations in clinical and pathologically proven Parkinson's diseaseThe iminosugar isofagomine increases the activity of N370S mutant acid beta-glucosidase in Gaucher fibroblasts by several mechanismsImpairment of homeostasis in lysosomal storage disordersBinding of 3,4,5,6-Tetrahydroxyazepanes to the Acid-β-glucosidase Active Site: Implications for Pharmacological Chaperone Design for Gaucher DiseaseDecreased glucocerebrosidase activity in Gaucher disease parallels quantitative enzyme loss due to abnormal interaction with TCP1 and c-Cbl.Partial restoration of mutant enzyme homeostasis in three distinct lysosomal storage disease cell lines by altering calcium homeostasisThree classes of glucocerebrosidase inhibitors identified by quantitative high-throughput screening are chaperone leads for Gaucher diseaseIdentification of pharmacological chaperones for Gaucher disease and characterization of their effects on beta-glucocerebrosidase by hydrogen/deuterium exchange mass spectrometry.Detection of ligand binding hot spots on protein surfaces via fragment-based methods: application to DJ-1 and glucocerebrosidase.Identification and characterization of ambroxol as an enzyme enhancement agent for Gaucher diseaseAlteration of the proteostasis network of plant cells promotes the post-endoplasmic reticulum trafficking of recombinant mutant (L444P) human β-glucocerebrosidase.Discovery, structure-activity relationship, and biological evaluation of noninhibitory small molecule chaperones of glucocerebrosidaseGaucher disease and parkinsonism, a molecular link theoryX-ray and biochemical analysis of N370S mutant human acid β-glucosidase.Remodeling the proteostasis network to rescue glucocerebrosidase variants by inhibiting ER-associated degradation and enhancing ER folding.Chemical and biological approaches synergize to ameliorate protein-folding diseases.Evaluation of quinazoline analogues as glucocerebrosidase inhibitors with chaperone activityHistone deacetylase inhibitors prevent the degradation and restore the activity of glucocerebrosidase in Gaucher diseasePharmacological chaperones facilitate the post-ER transport of recombinant N370S mutant β-glucocerebrosidase in plant cells: evidence that N370S is a folding mutant.A counterintuitive approach to treat enzyme deficiencies: use of enzyme inhibitors for restoring mutant enzyme activity.A Guided Tour of the Structural Biology of Gaucher Disease: Acid-β-Glucosidase and Saposin C.Gaucher disease paradigm: from ERAD to comorbidity.Innovative strategies to treat protein misfolding in inborn errors of metabolism: pharmacological chaperones and proteostasis regulators.Genetic convergence of Parkinson's disease and lysosomal storage disorders.Pharmaceutical Chaperones and Proteostasis Regulators in the Therapy of Lysosomal Storage Disorders: Current Perspective and Future Promises.Molecular Mechanisms of Disease Pathogenesis Differ in Krabbe Disease Variants.New Directions in Gaucher Disease.FKBP10 depletion enhances glucocerebrosidase proteostasis in Gaucher disease fibroblasts.Diltiazem, a L-type Ca(2+) channel blocker, also acts as a pharmacological chaperone in Gaucher patient cells.Isofagomine induced stabilization of glucocerebrosidase.Stabilization of Glucocerebrosidase by Active Site Occupancy.Endoplasmic reticulum Ca2+ increases enhance mutant glucocerebrosidase proteostasis.Enzyme enhancers for the treatment of Fabry and Pompe disease.Mutant alpha-galactosidase A enzymes identified in Fabry disease patients with residual enzyme activity: biochemical characterization and restoration of normal intracellular processing by 1-deoxygalactonojirimycin.ERdj3 is an endoplasmic reticulum degradation factor for mutant glucocerebrosidase variants linked to Gaucher's disease.A systematic investigation of iminosugar click clusters as pharmacological chaperones for the treatment of Gaucher disease.Pharmacoperones as Novel Therapeutics for Diverse Protein Conformational Diseases.A common and two novel GBA mutations in Thai patients with Gaucher disease.
P2860
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P2860
Impaired trafficking of mutants of lysosomal glucocerebrosidase in Gaucher's disease.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
2005年论文
@zh
2005年论文
@zh-cn
name
Impaired trafficking of mutants of lysosomal glucocerebrosidase in Gaucher's disease.
@en
Impaired trafficking of mutants of lysosomal glucocerebrosidase in Gaucher's disease.
@nl
type
label
Impaired trafficking of mutants of lysosomal glucocerebrosidase in Gaucher's disease.
@en
Impaired trafficking of mutants of lysosomal glucocerebrosidase in Gaucher's disease.
@nl
prefLabel
Impaired trafficking of mutants of lysosomal glucocerebrosidase in Gaucher's disease.
@en
Impaired trafficking of mutants of lysosomal glucocerebrosidase in Gaucher's disease.
@nl
P2093
P1476
Impaired trafficking of mutants of lysosomal glucocerebrosidase in Gaucher's disease
@en
P2093
Hassan Y Naim
Klaus-Peter Zimmer
Martina Schmitz
Marwan Alfalah
P304
P356
10.1016/J.BIOCEL.2005.05.008
P50
P577
2005-11-01T00:00:00Z