A synthetic chaperone corrects the trafficking defect and disease phenotype in a protein misfolding disorder
about
The iminosugar isofagomine increases the activity of N370S mutant acid beta-glucosidase in Gaucher fibroblasts by several mechanismsEmbolic Strokes of Unknown Source and Cryptogenic Stroke: Implications in Clinical PracticeEffects of pH and Iminosugar Pharmacological Chaperones on Lysosomal Glycosidase Structure and StabilityPharmacological chaperones for human -N-acetylgalactosaminidaseThe Molecular Basis of Pharmacological Chaperoning in Human α-GalactosidaseOral Migalastat HCl Leads to Greater Systemic Exposure and Tissue Levels of Active α-Galactosidase A in Fabry Patients when Co-Administered with Infused AgalsidaseTrafficking and quality control of the gonadotropin releasing hormone receptor in health and diseaseSmall-molecule structure correctors target abnormal protein structure and function: structure corrector rescue of apolipoprotein E4-associated neuropathologyHigh-throughput screening for human lysosomal beta-N-Acetyl hexosaminidase inhibitors acting as pharmacological chaperones.Identification of pharmacological chaperones for Gaucher disease and characterization of their effects on beta-glucocerebrosidase by hydrogen/deuterium exchange mass spectrometry.The validation of pharmacogenetics for the identification of Fabry patients to be treated with migalastatCase study on the pathophysiology of Fabry disease: abnormalities of cellular membranes can be reversed by substrate reduction in vitro.The pharmacological chaperone 1-deoxygalactonojirimycin reduces tissue globotriaosylceramide levels in a mouse model of Fabry disease.Biophysical characterization of the olfactomedin domain of myocilin, an extracellular matrix protein implicated in inherited forms of glaucoma.Oral pharmacological chaperone migalastat compared with enzyme replacement therapy in Fabry disease: 18-month results from the randomised phase III ATTRACT study.Small molecule structure correctors abolish detrimental effects of apolipoprotein E4 in cultured neurons.Safety and pharmacodynamic effects of a pharmacological chaperone on α-galactosidase A activity and globotriaosylceramide clearance in Fabry disease: report from two phase 2 clinical studies.Fabry disease - current treatment and new drug development.Imino sugar inhibitors for treating the lysosomal glycosphingolipidoses.Migalastat HCl reduces globotriaosylsphingosine (lyso-Gb3) in Fabry transgenic mice and in the plasma of Fabry patients.Identification and characterization of pharmacological chaperones to correct enzyme deficiencies in lysosomal storage disorders.A pharmacogenetic approach to identify mutant forms of α-galactosidase A that respond to a pharmacological chaperone for Fabry diseasePharmacological chaperone therapy for Fabry diseaseStorage solutions: treating lysosomal disorders of the brain.Current and emerging therapies for the lysosomal storage disorders.Protein quality control: the who's who, the where's and therapeutic escapes.Rapid profiling of disease alleles using a tunable reporter of protein misfolding.Unfolding the Therapeutic Potential of Chemical Chaperones for Age-related Macular DegenerationPharmacotherapeutic strategies using small molecules for the treatment of glycolipid lysosomal storage disorders.Coformulation of a Novel Human α-Galactosidase A With the Pharmacological Chaperone AT1001 Leads to Improved Substrate Reduction in Fabry MiceReview of miglustat for clinical management in Gaucher disease type 1.Chemical and pharmacological chaperones as new therapeutic agents.Active-site-specific chaperone therapy for Fabry disease. Yin and Yang of enzyme inhibitors.A counterintuitive approach to treat enzyme deficiencies: use of enzyme inhibitors for restoring mutant enzyme activity.Pharmacokinetics, safety, and tolerability following single-dose migalastat hydrochloride (GR181413A/AT1001) in healthy male Japanese subjectsPrediction of response of mutated alpha-galactosidase A to a pharmacological chaperone.Cln6 mutants associated with neuronal ceroid lipofuscinosis are degraded in a proteasome-dependent manner.Screening for pharmacological chaperones in Fabry diseaseStrategies for delivery of therapeutics into the central nervous system for treatment of lysosomal storage disorders.New biotechnological and nanomedicine strategies for treatment of lysosomal storage disorders
P2860
Q24673451-46830C86-B1F8-4718-98C9-B4159333B236Q26752352-DD69AAF3-106D-423E-915A-FCDE5D3E49FCQ27654912-C110878D-50D9-479E-BDE3-E91BA97F6F08Q27674346-3F63DD88-C19F-4BC1-BFBB-391A98E04560Q27676392-7E860658-9F7D-4E75-860D-703369CF4B35Q28547115-1BDABAD9-C996-4D53-80EC-FA75B7D364C3Q28755163-25479114-99F1-4935-A7F0-AE7F1818A7D2Q30421643-CF768D9C-450D-4820-AEC1-D26719B86EEAQ33275131-6C1B44FA-FB4D-415F-9CEF-C49F5C0045EEQ33381275-068DA385-C074-433B-91BC-8922280C96DCQ33567658-A6CE1C55-F14C-4740-8354-82F638E5EDE8Q33613449-5DF6883B-C999-414B-8552-5F88D7F98CBEQ33730412-D56B9B5C-62AB-4173-A2F6-9D3875377D3EQ33808845-82107F88-C8FB-4F59-8B3D-2494BC649606Q33886219-60103A99-C63B-4198-9D9E-937C83E13891Q34096644-7CE4CCEC-6595-4A9C-AF97-D549BA9FB081Q34313390-12197E72-1FB5-4A69-B2EB-C46E8DBA8835Q34368512-C4C06A8B-CF3B-45D0-B613-9702859E1BADQ34557737-1B863D48-9B71-4428-919E-8AD3E6F3343DQ34614418-EE2982FB-CDF6-4131-8624-83F323A6A450Q35007910-545C3C84-A923-49CF-8E6B-6A5F72BC2847Q35207863-15648FDD-C0D2-4CF6-8B27-5CAF13AD1796Q35755438-7D6B58BF-2F47-4231-A6E0-7669A5EDB843Q36210235-5BDFB65C-3E18-47F3-9808-588DF2CA1282Q36302871-E95312B4-1039-4177-A300-035BFECD64EFQ36432134-3212594C-B372-416C-869A-3344952EE961Q36466309-72CD0CE1-FFC4-4A01-83DF-CA564DAFC352Q36697237-05B79AF5-789C-4AD7-9D63-B72B89AEAC6FQ36739788-65C09F9E-DDC1-44C4-AE95-FA6574E56373Q36756784-2562BC31-1024-4846-ADB6-AC9952C81298Q36823551-60C9B830-A476-40DA-A3FD-29AF61F74A47Q36863386-581FBD93-67C8-4B8B-A0DB-47CA86BF7E96Q36951293-E512B6A9-8A30-4DE0-BE2F-A5DBA4ABBCF2Q37038867-C1F3F4CC-8EBA-4410-94BF-6A9E117E7B7DQ37077180-20DB043C-92AF-4198-A79A-3DF709CA19E1Q37131892-3F0669D9-EF43-4D50-BACF-FF03BA630060Q37171634-3ED82C9F-F24A-4CCD-8B56-333BC101C608Q37312295-8D54C6AB-D939-44C6-A3AA-5CB9364B9C8FQ37672410-097B9E52-3EE5-4B9F-8144-933E43106B72Q37683644-9CBDD42E-915A-4ACC-A9EF-60198EBA0A2F
P2860
A synthetic chaperone corrects the trafficking defect and disease phenotype in a protein misfolding disorder
description
2005 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի հունվարին հրատարակված գիտական հոդված
@hy
artikull shkencor
@sq
artículu científicu espublizáu en 2005
@ast
im Januar 2005 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
wetenschappelijk artikel
@nl
наукова стаття, опублікована в січні 2005
@uk
مقالة علمية (نشرت عام 2005)
@ar
name
A synthetic chaperone corrects ...... a protein misfolding disorder
@ast
A synthetic chaperone corrects ...... a protein misfolding disorder
@en
A synthetic chaperone corrects ...... a protein misfolding disorder
@nl
type
label
A synthetic chaperone corrects ...... a protein misfolding disorder
@ast
A synthetic chaperone corrects ...... a protein misfolding disorder
@en
A synthetic chaperone corrects ...... a protein misfolding disorder
@nl
prefLabel
A synthetic chaperone corrects ...... a protein misfolding disorder
@ast
A synthetic chaperone corrects ...... a protein misfolding disorder
@en
A synthetic chaperone corrects ...... a protein misfolding disorder
@nl
P3181
P356
P1433
P1476
A synthetic chaperone corrects ...... a protein misfolding disorder
@en
P2093
Christian Zuber
Jürgen Roth
P3181
P356
10.1096/FJ.04-2375COM
P407
P577
2005-01-01T00:00:00Z