Fabry disease: preclinical studies demonstrate the effectiveness of alpha-galactosidase A replacement in enzyme-deficient mice.
about
Patients affected with Fabry disease have an increased incidence of progressive hearing loss and sudden deafness: an investigation of twenty-two hemizygous male patients.Crystal structure of rice alpha-galactosidase complexed with D-galactoseTelomerase immortalization upregulates Rab9 expression and restores LDL cholesterol egress from Niemann-Pick C1 late endosomesA phase 1/2 clinical trial of enzyme replacement in fabry disease: pharmacokinetic, substrate clearance, and safety studiesCyclodextrin induces calcium-dependent lysosomal exocytosisNeurological deficits and glycosphingolipid accumulation in saposin B deficient mice.Cardiomyopathy and response to enzyme replacement therapy in a male mouse model for Fabry diseaseThe pharmacological chaperone 1-deoxygalactonojirimycin reduces tissue globotriaosylceramide levels in a mouse model of Fabry disease.Characterization of Fabry mice treated with recombinant adeno-associated virus 2/8-mediated gene transfer.Enhancement of drug delivery: enzyme-replacement therapy for murine Morquio A syndrome.A symptomatic Fabry disease mouse model generated by inducing globotriaosylceramide synthesis.Long-term systemic therapy of Fabry disease in a knockout mouse by adeno-associated virus-mediated muscle-directed gene transfer.Pain related channels are differentially expressed in neuronal and non-neuronal cells of glabrous skin of fabry knockout male miceHeat shock protein-based therapy as a potential candidate for treating the sphingolipidoses.Increased globotriaosylceramide levels in a transgenic mouse expressing human alpha1,4-galactosyltransferase and a mouse model for treating Fabry disease.Advances in the management of Anderson-Fabry disease: enzyme replacement therapy.Migalastat HCl reduces globotriaosylsphingosine (lyso-Gb3) in Fabry transgenic mice and in the plasma of Fabry patients.α-Galactosidase A expressed in the salivary glands partially corrects organ biochemical deficits in the fabry mouse through endocrine traffickingStructure-function relationships in alpha-galactosidase A.Long-term correction of globotriaosylceramide storage in Fabry mice by recombinant adeno-associated virus-mediated gene transferGlycosphingolipid lysosomal storage diseases: therapy and pathogenesis.PKC activation in Niemann pick C1 cells restores subcellular cholesterol transportFabry disease: recent advances in enzyme replacement therapy.Enzyme therapy in mannose receptor-null mucopolysaccharidosis VII mice defines roles for the mannose 6-phosphate and mannose receptorsComparative evaluation of alpha-galactosidase A infusions for treatment of Fabry disease.Sex differences of urinary and kidney globotriaosylceramide and lyso-globotriaosylceramide in Fabry mice.Practical murine hematopathology: a comparative review and implications for research.Efficient uptake of recombinant α-galactosidase A produced with a gene-manipulated yeast by Fabry mice kidneysEnzyme replacement therapy for Fabry disease: lessons from two alpha-galactosidase A orphan products and one FDA approval.Efficacy of Enzyme and Substrate Reduction Therapy with a Novel Antagonist of Glucosylceramide Synthase for Fabry DiseaseMannose receptor-mediated delivery of moss-made α-galactosidase A efficiently corrects enzyme deficiency in Fabry miceEffects of switching from agalsidase Beta to agalsidase alfa in 10 patients with anderson-fabry diseaseUse of a modified alpha-N-acetylgalactosaminidase in the development of enzyme replacement therapy for Fabry disease.Transduction of human recombinant proteins into mitochondria as a protein therapeutic approach for mitochondrial disorders.Treatment options for lysosomal storage disorders: developing insights.Gene therapy for fabry disease: a review of the literature.Sphingolipid lysosomal storage disorders.Enzymes approved for human therapy: indications, mechanisms and adverse effects.Mannose 6-phosphate receptor-mediated uptake is defective in acid sphingomyelinase-deficient macrophages: implications for Niemann-Pick disease enzyme replacement therapy.Plasmid-based gene transfer ameliorates visceral storage in a mouse model of Sandhoff disease.
P2860
Q24794000-43B42C29-61C2-45C9-B879-36A6E0734CA7Q27640805-6DA1FF2D-215C-41A4-8465-342549A9093FQ28208268-8AFACB06-D791-4079-B1A2-D9E816729B98Q28348809-B04F5940-88BE-4024-AC29-93F8B6F7335DQ28476365-2AE50EAA-4D28-440E-A83E-359C3C19954AQ28594479-619D0F5D-1AA3-4C00-A9D1-EC62890274D6Q28730130-B0211290-92F9-49D6-AD18-F2F1CEECA823Q33730412-D5702238-771E-4712-96C8-7B535A8935CDQ33818578-445D7C27-A640-496B-9B13-BBC1917BDFC8Q33930155-47DC27FE-A5FB-40BC-8F69-5E7A483F0B2CQ34159448-C9249BF3-95A4-42CB-8F73-0591AB4886C3Q34161415-4B3150FB-019A-45B9-BA82-E6792BCD63A9Q34387316-BCA189DB-CD16-411B-B3D3-8E773B2A8322Q34539778-C2AA37ED-5B41-4BC2-8B53-74159F2174BAQ34541244-CABC5E1B-68DF-43D8-B1B6-6357502B73C3Q34560688-D623BAC9-14C2-4FBF-B480-6AE57C53F3DFQ34614418-878B2E47-A3ED-4A75-AFF5-686BC1202067Q34671627-DCAF271B-E464-47FB-9FDF-EA48CF6D1AC9Q34731206-B608B839-79B3-42A3-AE15-3B4D0F9FAAEEQ34870564-86219FD8-0FE4-4B26-8785-4D798A9922B7Q34941895-EAD5EA0D-72D3-41DA-828B-54B07E6AB177Q34974271-11242E04-7FBF-450C-9806-4BB459C39746Q34974879-0F8B62F5-7477-477C-B15B-D352C3410DD0Q35108117-499F2ED8-FFD4-4D73-8DE6-61C58C3B4653Q35147741-4EC42F09-B06B-4BC9-8963-0A1E6DCE551BQ35152240-28DE6D50-3AF7-4654-89AF-44663DC9AFB2Q35535242-EF58C7B0-D78B-4760-A37E-808017BA7D3DQ35719001-AC1C437F-AEDB-4496-9836-5E539AA0A331Q35842694-A50B54AD-04AB-4396-8F5E-A13BFB402D1AQ36025702-B71D25C9-EA95-4D31-A7D3-963766414FC5Q36582247-15A32F0C-236B-41AC-9AD9-08E1BB5050E7Q36590934-994AF122-CC3E-4BC3-94C6-6BA4ABEEEE8AQ37417886-0F88BE9F-BB82-476D-82AD-8586E8C5F48DQ37923355-1A76C7EB-8563-47B9-AD5D-4B891ABF980EQ38046227-84A0EF14-3773-4F68-9390-B5889563559CQ38098070-C5490EB5-84A7-44F4-A055-2CFA579E2E77Q38217766-77696985-1F98-47A1-84F2-73D0A7C61351Q38342838-4194884E-54DB-45FC-9534-AEAAD3D2FC2FQ38349291-E7C1020E-AF21-486E-A140-7A6D3609D65FQ40656536-4A961473-E906-4C53-8481-2F7363E1AD64
P2860
Fabry disease: preclinical studies demonstrate the effectiveness of alpha-galactosidase A replacement in enzyme-deficient mice.
description
2000 nî lūn-bûn
@nan
2000 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Fabry disease: preclinical stu ...... ement in enzyme-deficient mice
@nl
Fabry disease: preclinical stu ...... ment in enzyme-deficient mice.
@ast
Fabry disease: preclinical stu ...... ment in enzyme-deficient mice.
@en
type
label
Fabry disease: preclinical stu ...... ement in enzyme-deficient mice
@nl
Fabry disease: preclinical stu ...... ment in enzyme-deficient mice.
@ast
Fabry disease: preclinical stu ...... ment in enzyme-deficient mice.
@en
prefLabel
Fabry disease: preclinical stu ...... ement in enzyme-deficient mice
@nl
Fabry disease: preclinical stu ...... ment in enzyme-deficient mice.
@ast
Fabry disease: preclinical stu ...... ment in enzyme-deficient mice.
@en
P2093
P2860
P356
P1476
Fabry disease: preclinical stu ...... ment in enzyme-deficient mice.
@en
P2093
K M Zeidner
R E Gordon
R J Desnick
Y A Ioannou
P2860
P356
10.1086/316953
P407
P577
2000-12-13T00:00:00Z