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2,5-anhydro-3-O-alpha-L-idopyranuronosyl-D-mannitol + H2O
?
-
-
-
-
?
2,5-anhydro-4-O-alpha-L-idopyranuronosyl-D-mannitol 6-sulfate + H2O
?
-
-
-
-
?
4-methylcoumarin-7-yl-alpha-L-iduronic acid + H2O
4-methylcoumarin + alpha-L-iduronic acid
-
design and development of an improved and less expensive synthesis method for the fluorogenic substrate, overview. The method is based on the double ketal fixation of the 1,2 and 3,5-hydroxy groups of D-glucose to form a cis-anti-cis-fused tricyclic D-glucofuranosyl derivative, which could undergo elimination to form a 5-exo-double bond followed by electrophilic addition, a Mitsunobu-type glycosylation reaction is used for the coupling of the hemiacetal with the acceptor
-
-
?
4-methylumbelliferyl alpha-L-iduronide + H2O
4-methylumbelliferone + alpha-L-iduronic acid
4-methylumbelliferyl-alpha-L-iduronide + H2O
4-methylumbelliferol + alpha-L-iduronic acid
4-methylumbelliferyl-alpha-L-iduronide + H2O
4-methylumbelliferone + alpha-L-iduronic acid
4-methylumbelliferyl-alpha-L-iduronide + H2O
?
4-methylumbelliferyl-alpha-L-iduronide + methanol
?
-
methanolysis
-
-
?
4-methylumbelliferyl-alpha-L-iduronoside + H2O
4-methylumbelliferone + alpha-L-iduronic acid
-
-
-
-
?
4-nitrophenyl-alpha-L-idopyranosiduronate + H2O
4-nitrophenol + alpha-L-iduronic acid
-
-
-
-
?
4-nitrophenyl-alpha-L-iduronide + H2O
4-nitrophenol + alpha-L-iduronic acid
-
-
-
-
?
5-fluoro-alpha-L-idopyranosyluronic acid fluoride + H2O
fluoride + ?
-
-
-
-
?
alpha-L-iduronosyl(1-4)anhydromannitol-6-sulfate + H2O
?
-
-
-
?
alpha-L-iduronosyl-(1->3)-2,5-anhydro-D-talitol 4-sulfate + H2O
?
-
-
-
-
?
alpha-L-iduronysyl-(alpha-1,4)2,5-anhydro-D-mannitol-6-sulfate + H2O
2,5-anhydro-D-mannitol 6-sulfate + alpha-L-iduronic acid
-
-
-
-
?
anhydromannitol iduronide + H2O
?
-
-
-
-
?
dermatan sulfate + H2O
? + alpha-iduronic acid
-
-
-
?
glycosaminoglycan + H2O
? + alpha-iduronic acid
-
-
-
?
heparan sulfate + H2O
? + alpha-L-iduronic acid
-
-
-
?
IdoA-GlcNAc6S-IdoA2S-anM6S + H2O
?
-
O-(alpha-L-iduronic acid)-(1,4)-D-O-(alpha-N-acetylglucosamine 6-sulphate)-L-O-(alpha-iduronic acid 2-sulphate)-O-D-2,5-anhydro-D-mannitol 6-sulphate
-
-
?
IdoA-GlcNH6S-IdoA2S-anM6S + H2O
?
-
-
-
-
?
IdoA-GlcNS6S-IdoA2S-anM6S + H2O
?
-
-
-
-
?
phenyl alpha-L-iduronide + H2O
?
additional information
?
-
4-methylumbelliferyl alpha-L-iduronide + H2O
4-methylumbelliferone + alpha-L-iduronic acid
-
-
-
?
4-methylumbelliferyl alpha-L-iduronide + H2O
4-methylumbelliferone + alpha-L-iduronic acid
-
-
-
-
?
4-methylumbelliferyl alpha-L-iduronide + H2O
4-methylumbelliferone + alpha-L-iduronic acid
-
-
-
?
4-methylumbelliferyl alpha-L-iduronide + H2O
4-methylumbelliferone + alpha-L-iduronic acid
-
-
-
-
?
4-methylumbelliferyl-alpha-L-iduronide + H2O
4-methylumbelliferol + alpha-L-iduronic acid
-
-
-
-
?
4-methylumbelliferyl-alpha-L-iduronide + H2O
4-methylumbelliferol + alpha-L-iduronic acid
-
-
-
-
?
4-methylumbelliferyl-alpha-L-iduronide + H2O
4-methylumbelliferol + alpha-L-iduronic acid
-
-
-
-
?
4-methylumbelliferyl-alpha-L-iduronide + H2O
4-methylumbelliferone + alpha-L-iduronic acid
-
-
654383, 654716, 654856, 655246, 655683, 665552, 666375, 680058, 680077, 681942, 682312, 696554, 715115 -
-
?
4-methylumbelliferyl-alpha-L-iduronide + H2O
4-methylumbelliferone + alpha-L-iduronic acid
-
-
-
?
4-methylumbelliferyl-alpha-L-iduronide + H2O
4-methylumbelliferone + alpha-L-iduronic acid
-
-
-
-
?
4-methylumbelliferyl-alpha-L-iduronide + H2O
?
-
-
-
-
?
4-methylumbelliferyl-alpha-L-iduronide + H2O
?
-
-
-
-
?
4-methylumbelliferyl-alpha-L-iduronide + H2O
?
-
-
-
-
?
4-methylumbelliferyl-alpha-L-iduronide + H2O
?
-
-
-
-
?
phenyl alpha-L-iduronide + H2O
?
-
-
-
-
?
phenyl alpha-L-iduronide + H2O
?
-
-
-
-
?
additional information
?
-
-
cleaves alpha-L-iduronic acid from the nonreducing ends of dermatan sulfate, heparin, and heparan sulfate, deficiency in alpha-L-iduronidase causes mucopolysaccharidosis type I
-
-
?
additional information
?
-
-
involved in the degradation of dermatan sulfate and heparan sulfate
-
-
?
additional information
?
-
-
involved in the degradation of dermatan sulfate and heparan sulfate, deficiency in alpha-L-iduronidase causes mucopolysaccharidosis type I
-
-
?
additional information
?
-
-
involved in the degradation of dermatan sulfate and heparan sulfate, deficiency in alpha-L-iduronidase causes mucopolysaccharidosis type I
-
-
?
additional information
?
-
-
involved in the degradation of dermatan sulfate and heparan sulfate, deficiency in alpha-L-iduronidase causes mucopolysaccharidosis type I
-
-
?
additional information
?
-
-
involved in the degradation of dermatan sulfate and heparan sulfate, deficiency in alpha-L-iduronidase causes mucopolysaccharidosis type I
-
-
?
additional information
?
-
-
enzyme deficiency causes mucopolysaccharidosis type I, MPSI
-
-
?
additional information
?
-
-
enzyme deficiency causes the lysosomal storage disorder mucopolysaccharidosis type I, MPSI
-
-
?
additional information
?
-
enzyme deficiency causes the lysosomal storage disorder mucopolysaccharidosis type I, MPSI
-
-
?
additional information
?
-
-
enzyme deficiency causes the lysosomal storage disorder mucopolysaccharidosis type I, MPSI
-
-
?
additional information
?
-
the enzyme is involved in mucopolysaccharidosis type I
-
-
?
additional information
?
-
-
the enzyme is involved in mucopolysaccharidosis type I
-
-
?
additional information
?
-
-
the enzyme is involved in the sequential degradation of heparan sufate and dermatan sulfate, enzyme deficiency results in the accumulation and urinary secretion of partially degraded glycosaminoglycans and causes the lysosomal storage disorder mucopolysaccharidosis type I, MPSI
-
-
?
additional information
?
-
-
substrate specificity of recombinant enzyme with and without a C-terminal ER-retention signal from seeds of Brassica napus and Nicotiana tabacum, overview
-
-
?
additional information
?
-
the enzyme cleaves terminal alpha-iduronic acid residues from glycosaminoglycan, heparan sulfate and dermatan sulfate
-
-
?
additional information
?
-
-
the enzyme hydrolyses the glycosidic bond between the terminal L-iduronic acid and the second sugar of N-acetylgalactosamine-4-sulfate/N-sulfo-D-glucosamine-6-sulfate, which are the major components of dermatan/heparan sulfate
-
-
?
additional information
?
-
-
the enzyme hydrolyzes terminal iduronic acid residues on glycosaminoglycans
-
-
?
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125000
-
x * 83000, recombinant wild-type enzyme, SDS-PAGE, x * 125000, recombinant RAP-fusion enzyme, SDS-PAGE
30000
-
2 * 30000, SDS-PAGE
31000
-
2 * 31000, SDS-PAGE
480000
-
gel filtration and native PAGE
49000
x * 77000, recombinant wild-tyype enzyme, extracellular secreted precursor enzyme form, SDS-PAGE, x * 74000, recombinant wild-type enzyme, intracellular precursor enzyme form, SDS-PAGE, x * 69000, recombinant wild-type enzyme, intracellular processed enzyme form 1, SDS-PAGE, x * 65000, recombinant wild-type enzyme, intracellular processed enzyme form 2, SDS-PAGE, x * 49000, recombinant wild-type enzyme, intracellular processed enzyme form 3, SDS-PAGE
67000
-
gel filtration, L-iduronidase II
68000
-
gel filtration, soluble form
69908
x * 69908, sequence calculation
76000
-
Western blot analysis, mature component after incorporation into cells
76600
-
x * 76600, recombinant glycosylated enzyme expressed from Brassica napus seeds, SDS-PAGE, x * 76700, recombinant glycosylated enzyme expressed from Nicotiana tabacum seeds, SDS-PAGE
76700
-
x * 76600, recombinant glycosylated enzyme expressed from Brassica napus seeds, SDS-PAGE, x * 76700, recombinant glycosylated enzyme expressed from Nicotiana tabacum seeds, SDS-PAGE
77000
x * 77000, recombinant wild-tyype enzyme, extracellular secreted precursor enzyme form, SDS-PAGE, x * 74000, recombinant wild-type enzyme, intracellular precursor enzyme form, SDS-PAGE, x * 69000, recombinant wild-type enzyme, intracellular processed enzyme form 1, SDS-PAGE, x * 65000, recombinant wild-type enzyme, intracellular processed enzyme form 2, SDS-PAGE, x * 49000, recombinant wild-type enzyme, intracellular processed enzyme form 3, SDS-PAGE
78000
-
x * 78000, recombinant glycosylated enzyme, SDS-PAGE
87000
-
gel filtration, L-iduronidase I
60000
-
gel filtration
60000
-
sedimentation equilibrium
65000
-
gel filtration, form I and II from liver
65000
x * 77000, recombinant wild-tyype enzyme, extracellular secreted precursor enzyme form, SDS-PAGE, x * 74000, recombinant wild-type enzyme, intracellular precursor enzyme form, SDS-PAGE, x * 69000, recombinant wild-type enzyme, intracellular processed enzyme form 1, SDS-PAGE, x * 65000, recombinant wild-type enzyme, intracellular processed enzyme form 2, SDS-PAGE, x * 49000, recombinant wild-type enzyme, intracellular processed enzyme form 3, SDS-PAGE
69000
-
Western blot analysis, mature component after incorporation into cells
69000
x * 77000, recombinant wild-tyype enzyme, extracellular secreted precursor enzyme form, SDS-PAGE, x * 74000, recombinant wild-type enzyme, intracellular precursor enzyme form, SDS-PAGE, x * 69000, recombinant wild-type enzyme, intracellular processed enzyme form 1, SDS-PAGE, x * 65000, recombinant wild-type enzyme, intracellular processed enzyme form 2, SDS-PAGE, x * 49000, recombinant wild-type enzyme, intracellular processed enzyme form 3, SDS-PAGE
74000
-
SDS-PAGE
74000
-
wild type enzyme, SDS-PAGE, intracellulary processed to form fragments of 69000 Da and 65000 Da
74000
x * 77000, recombinant wild-tyype enzyme, extracellular secreted precursor enzyme form, SDS-PAGE, x * 74000, recombinant wild-type enzyme, intracellular precursor enzyme form, SDS-PAGE, x * 69000, recombinant wild-type enzyme, intracellular processed enzyme form 1, SDS-PAGE, x * 65000, recombinant wild-type enzyme, intracellular processed enzyme form 2, SDS-PAGE, x * 49000, recombinant wild-type enzyme, intracellular processed enzyme form 3, SDS-PAGE
83000
-
Western blot analysis, before incorporation into cells
83000
-
x * 83000, recombinant wild-type enzyme, SDS-PAGE, x * 125000, recombinant RAP-fusion enzyme, SDS-PAGE
85000
-
gel filtration, membrane associated form
85000
-
x * 85000, SDS-PAGE
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134del12
-
homozygous genotype with only residual enzyme activity
A160D
-
severe mucopolysaccharidosis type I phenotype
A319V
-
attenuated mucopolysaccharidosis type I phenotype
A327P/R383H
-
a genotype with only residual enzyme activity
A75T
-
severe mucopolysaccharidosis type I phenotype
C205Y
-
attenuated mucopolysaccharidosis type I phenotype
C577GfsX15
-
naturally occuring mutation in the IDUA gene from an MPS I patient
D203N
-
the missense mutation is associated with mucopolysaccharidosis type I
D349Y
-
severe mucopolysaccharidosis type I phenotype
E178K
-
intermediate mucopolysaccharidosis type I phenotype
E182A
-
catalytically inactive
E276K
-
E276K/E276K is a naturally occuring rare homozygous mutant genotype with only residual enzyme activity and thermal instability at 37°C
E299A
-
catalytically inactive
E640Cfs
-
naturally occuring mutation in the IDUA gene from an MPS I patient
F602I
naturally occurring mutation in the IDUA gene of a mucopolysaccharidosis type I patient, construction by site-directed mutagenesis for expression in CHO cells, the recombinant mutant shows about 5fold increased activity in CHO cell lysate and altered subcellular localization compared to the recombinant wild-type enzyme
G208D
-
severe mucopolysaccharidosis type I phenotype
G208V
-
severe mucopolysaccharidosis type I phenotype
G265R
naturally occurring mutation in the IDUA gene of a mucopolysaccharidosis type I patient, construction by site-directed mutagenesis for expression in CHO cells, the recombinant mutant shows reduced activity in CHO cell lysate and altered subcellular localization compared to the recombinant wild-type enzyme
G51D
-
severe mucopolysaccharidosis type I phenotype
H240R
-
attenuated mucopolysaccharidosis type I phenotype
H82P
-
intermediate mucopolysaccharidosis type I phenotype
H82Q
naturally occurring mutation in the IDUA gene of a mucopolysaccharidosis type I patient, construction by site-directed mutagenesis for expression in CHO cells, the recombinant mutant shows 8fold increased activity in CHO cell lysate and altered subcellular localization compared to the recombinant wild-type enzyme
I270S
-
severe mucopolysaccharidosis type I phenotype
I270S/P533R/R268X
-
identification of naturally occurring mutation of a tunesian patient, homoallelic for P533R mutation, heteroallelic for missense mutation I270S and nonsense mutation R268X, and a deletion mutation in exon 13, the mutations are involved in development of the lysosomal storage disorder mucopolysaccharidosis type I, MPSI, the patient shows the Huler phenotype, overview
L238Q
naturally occurring mutation in the IDUA gene of a mucopolysaccharidosis type I patient, construction by site-directed mutagenesis for expression in CHO cells, the recombinant mutant shows about 3.5fold increased activity in CHO cell lysate and altered subcellular localization compared to the recombinant wild-type enzyme
N350I
-
attenuated mucopolysaccharidosis type I phenotype
P183R
-
severe mucopolysaccharidosis type I phenotype
P496L
-
intermediate mucopolysaccharidosis type I phenotype
P496R
-
severe mucopolysaccharidosis type I phenotype
Q584X
-
the missense mutation is associated with mucopolysaccharidosis type I
Q60X
-
the missense mutation is associated with mucopolysaccharidosis type I
Q70X/R383H
-
a genotype with only residual enzyme activity
R363H
-
the missense mutation is associated with hepatosplenomegaly, joint stiffness, corneal clouding, and slightly mental delay in mucopolysaccharidosis type I patients and displays 2.3% of wild type activity
R489P
-
severe mucopolysaccharidosis type I phenotype
R492P
-
attenuated mucopolysaccharidosis type I phenotype
R619G
-
the missense mutation is associated with mucopolysaccharidosis type I
R621X/974ins12
-
a genotype with only residual enzyme activity
R628X
-
naturally occuring mutation in the IDUA gene from an MPS I patient
R98W
-
strongly reduced activity, protein level not effected
S260F
-
intermediate mucopolysaccharidosis type I phenotype
S423R
naturally occurring mutation in the IDUA gene of a mucopolysaccharidosis type I patient, construction by site-directed mutagenesis for expression in CHO cells, the recombinant mutant shows 11fold increased activity in CHO cell lysate and altered subcellular localization compared to the recombinant wild-type enzyme
T366P
-
severe mucopolysaccharidosis type I phenotype
T388R
-
severe mucopolysaccharidosis type I phenotype
V620F
-
naturally occuring mutation in the IDUA gene from an MPS I patient
W626X
-
naturally occuring mutation in the IDUA gene from an MPS I patient
Y167X
-
naturally occuring mutation in the IDUA gene from an MPS I patient
Y343X
-
the missense mutation is associated with mucopolysaccharidosis type I
A327P
-
severe mucopolysaccharidosis type I phenotype
A327P
-
naturally occuring mutation in the IDUA gene from an MPS I patient
A327P
-
A327P/A327P and A327P/unknown, naturally occuring homozygous and indefinite mutant genotypes with only residual enzyme activity at 37°C
A327P
-
homozygous genotype with only residual enzyme activity
A79V
naturally occurring mutation in the IDUA gene of a mucopolysaccharidosis type I patient, construction by site-directed mutagenesis for expression in CHO cells, the recombinant mutant shows about 2fold increased activity in CHO cell lysate and altered subcellular localization compared to the recombinant wild-type enzyme
A79V
-
intermediate mucopolysaccharidosis type I phenotype
A79V
-
the missense mutation is associated with mucopolysaccharidosis type I
D315Y
-
severe mucopolysaccharidosis type I phenotype
D315Y
-
naturally occuring mutation in the IDUA gene from an MPS I patient
E182K
-
mutation found in patients with mucopolysaccharidosis type I, catalytically inactive
E182K
-
severe mucopolysaccharidosis type I phenotype
L218P
-
severe mucopolysaccharidosis type I phenotype
L218P
-
homozygous genotype with only residual enzyme activity
L346R
-
intermediate mucopolysaccharidosis type I phenotype
L346R
-
the missense mutation is associated with mucopolysaccharidosis type I
L490P
-
intermediate mucopolysaccharidosis type I phenotype
L490P
-
homozygous genotype with only residual enzyme activity
P533R
-
identification of naturally occurring mutation of two tunesian patient, homoallelic for P533R mutation, the mutation is involved in development of the lysosomal storage disorder mucopolysaccharidosis type I, MPSI, the patient shows the Huler-Scheie phenotype, overview
P533R
-
homozygous genotype with only residual enzyme activity
Q380R
-
attenuated mucopolysaccharidosis type I phenotype
Q380R
-
naturally occuring mutation in the IDUA gene from an MPS I patient
Q70X
-
naturally occuring mutation in the IDUA gene from an MPS I patient
Q70X
-
homozygous genotype with only residual enzyme activity
R363C
naturally occurring mutation in the IDUA gene of a mucopolysaccharidosis type I patient, construction by site-directed mutagenesis for expression in CHO cells, inactive recombinant mutant
R363C
-
severe mucopolysaccharidosis type I phenotype
R383H
-
attenuated mucopolysaccharidosis type I phenotype
R383H
-
homozygous genotype with only residual enzyme activity
R89Q
-
protein level is lowered to 10% of normal control
R89Q
-
attenuated mucopolysaccharidosis type I phenotype
T364M
-
intermediate mucopolysaccharidosis type I phenotype
T364M
-
the missense mutation is associated with mucopolysaccharidosis type I
W402X
-
naturally occuring mutation in the IDUA gene from an MPS I patient
W402X
-
the missense mutation is associated with mucopolysaccharidosis type I
W402X
-
homozygous genotype with only residual enzyme activity
additional information
diverse missense mutations of the human enzyme's core, surface, and active site are correlated to the development of the lysosomal storage disorder mucopolysaccharidosis type I, MPSI, structural implications, detailed overview
additional information
-
diverse missense mutations of the human enzyme's core, surface, and active site are correlated to the development of the lysosomal storage disorder mucopolysaccharidosis type I, MPSI, structural implications, detailed overview
additional information
-
exploitation of alternative receptor systems that are independent of glycosylation but allow for efficient delivery to the lysosome, fusions of the human lysosomal enzyme with the receptor-associated protein, RAP, are efficiently endocytosed by lysosomal storage disorder patient fibroblasts, rat C6 glioma cells, mouse C2C12 myoblasts, and recombinant CHO cells expressing individual members of the low-density lipoprotein receptor family, uptake of the fusion exceeds that of phosphorylated enzyme in all cases, uptake is mediated by oligosaccharide receptors including the cation-independent mannose 6-phosphate receptor and the mannose receptor, and is specifically mediated by members of the low-density lipoprotein receptor protein family and is followed by delivery of the fusions to the lysosome, stability or recombinant fusion enzymes, overview
additional information
identification and molecular characterization of 14 different enzyme mutations and 13 different polymorphic changes present in 10 mucopolysaccharidosis type I patients undergoing enzyme replacement therapy
additional information
-
identification and molecular characterization of 14 different enzyme mutations and 13 different polymorphic changes present in 10 mucopolysaccharidosis type I patients undergoing enzyme replacement therapy
additional information
-
identification of naturally occurring mutations of residues Q70, W402, R268, Q400, Y343, W180 to premature stop codons, mutations are involved in development of the lysosomal storage disorder mucopolysaccharidosis type I, MPSI, natural stop codon read-through and clinical MPSI phenotype, overview
additional information
-
nonsense mutation of residue Q70 is involved in the disease mucopolysaccharidosis type I, MPSI, changes in hair morphology of MPSI patients treated with recombinant human enzyme in enzyme replacement therapy, overview
additional information
-
over 100 disease-causing IDUA mutations identified in patients with mucopolysaccharidosis type I. Most common mutations that introduce premature stop codons are p.W402X and p.Q70X. Deficient IDUA activity results in the accumulation of dermatan and heparan sulfate in urine of affected individuals
additional information
-
construction of a protein mutant AGT-181, that is a genetically engineered fusion protein of human iduronidase and a chimeric monoclonal antibody against the human insulin receptor. The mutant AG-181 is administered to Maccaca mulatta, chronic AGT-181 dosing does not result in toxicity at any dose, and causes no changes in organ histology, no change in plasma or cerebrospinal fluid glucose, and no significant immune response. AGT-181 is rapidly removed from plasma, but shows iduronidase enzyme activity
additional information
-
gene IDUA, screening and genotyping of nonsense, 4 missense, 1 deletion, and 2 splice site intron mutations in 10 MPS I patients, development and evaluation of a dHPLC screening method, overview
additional information
-
mutations in the IDUA gene cause mucopolysaccharidosis type I, MPS I, a progressive multisystem disorder, phenotype with and without treatment with laronidase, overview
additional information
-
mutations in the IDUA gene cause mucopolysaccharidosis type I, MPS I, a progressive multisystem disorder, phenotypes, overview. Growth patterns in terms of body height, weight, head and chest circumference in patients with MPS I without treatment and after enzyme replacement therapy with alpha-L-iduronidase, overview
additional information
-
ability of recombinant baby hamster kidney cells transfected with human IDUA cDNA in correcting skin fibroblasts from mucopolysaccharidosis I patients in vitro, after encapsulation in alginate microcapsules, overview. The cells use the mannose-6-phosphate receptor to internalize the recombinant enzyme
additional information
-
construction of knockout mice from C57BL/6 parents
additional information
-
construction of knockout mice from C57BL/6 parents
-
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Matalon, R.; Cifonelli, J.A.; Dorfmann, A.
L-Iduronidase in cultured human fibroblasts and liver
Biochem. Biophys. Res. Commun.
42
340-345
1971
Homo sapiens
brenda
Weissmann, B.; Santiago, R.
alpha-L-Iduronidase in lysosomal extracts
Biochem. Biophys. Res. Commun.
46
1430-1433
1972
Rattus norvegicus
brenda
Hall, C.W.; Neufeld, E.F.
alpha-L-iduronidase activity in cultured skin fibroblasts and amniotic fluid cells
Arch. Biochem. Biophys.
158
817-821
1993
Homo sapiens
brenda
Shapiro, L.J.; Hall, C.W.; Leder, I.G.; Neufeld, E.F.
The relationship of alpha-L-iduronidase and hurler corrective faktor
Arch. Biochem. Biophys.
172
156-161
1976
Homo sapiens
brenda
Rome, L.H.; Garvin, A.J.; Neufeld, E.F.
Human kidney alpha-L-iduronidase: purification and characterization
Arch. Biochem. Biophys.
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1978
Homo sapiens
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Clements, P.R.; Brooks, D.A.; McCourt, P.A.G.; Hopwood, J.J.
Immunopurification and characterization of human alpha-L-iduronidase with the use of monoclonal antibodies
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1989
Homo sapiens
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Ohshita, T.; Sakuda, H.; Nakasone, S.; Iwamasa, T.
Purification, characterization and localization of pig liver alpha-L-iduronidase
Eur. J. Biochem.
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1989
Sus scrofa
brenda
di Bello, I.C.; Dorling, P.; Fellows, L.; Winchester, B.
Specifc inhibition of human beta-D-glucuronidase and alpha-L-iduronidase by a trihydroxy pipecolic acid of plant origin
FEBS Lett.
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1984
Homo sapiens
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Myerowitz R.; Neufeld, E.F.
Maturation of alpha-L-iduronidase in cultured human fibroblasts
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256
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1981
Homo sapiens
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Clements, P.R.; Brooks, D.A.; Saccone, G.T.P; Hopwood, J.J.
Human alpha-L-iduronidase. 1. purification, monoclonal antibody production, native and subunit molecular mass
Eur. J. Biochem.
152
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1985
Homo sapiens
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Clements, P.R.; Muller, V.; Hopwood, J.J.
Human alpha-L-iduronidase. 2. catalytic properties
Eur. J. Biochem.
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1985
Homo sapiens
brenda
Schuchmann, E.H.; Astrin, K.H.; Aula, P.; Desnick, R.J.
Regional assignment of the structural gene for human alpha-L-iduronidase
Proc. Natl. Acad. Sci. USA
81
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1984
Homo sapiens
brenda
Schuchmann, E.H.; Guzmann, N.A.; Desnick, R.J.
Human alpha-L-iduronidase. I. Purification and properties of the high uptake (higher molecular weight) and the low uptake (processed) forms
J. Biol. Chem.
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1984
Homo sapiens
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Rome, L.H.
alpha-L-Iduronidase from human kidney
Methods Enzymol.
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1982
Homo sapiens
brenda
Kosaka, H.; Isemura, M.; Ono, T.; Nishimura, Y.; Kato, K.
Studies on the alpha-L-iduronidase activity of beta-glucuronidase preparations from bovine liver, rat liver, and rat preputial gland
J. Biochem.
88
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1980
Bos taurus, Rattus norvegicus
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Freeman, C.; Hopwood, J.J.
Human alpha-L-iduronidase. Catalytic properties and an integrated role in the lysosomal degradation of heparan sulphate
Biochem. J.
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1992
Homo sapiens
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Stoltzfus, L.J.; Sosa-Pineda, B.; Moskowitz, S.M.; Menon, K.P.; Dlott, B.; Hooper, L.; Teplow, D.B.; Shull, R.M.; Neufeld, E.F.
Cloning and characterization of cDNA encoding canine alpha-L-iduronidase
J. Biol. Chem.
267
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1992
Canis sp.
brenda
Unger, E.G.; Durrant, J.; Anson, D.S.; Hopwood, J.J.
Recombinant alpha-L-iduronidase: characterization of the purified enzyme and correction of mucopolysaccharidosis type I fibroblasts
Biochem. J.
304
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1994
Homo sapiens
brenda
Brooks, D.A.; Harper, G.S.; Gibson, G.J.; Ashton, L.J.; Taylor, J.A.; McCourt, P.A.D.; Freeman, C.; Clements, P.R.; Hoffmann, J.W.; Hopwood, J.J.
Hurler Syndrome: a patient with abnormally high levels of alpha-L-iduronidase
Biochem. Med. Metab. Biol.
47
211-220
1992
Homo sapiens
brenda
Kakkis, E.D.; Matynia, A.; Jonas, A.J.; Neufeld, E.F.
Overexpression of the human lysosomal enzyme alpha-L-iduronidase in chinese hamster ovary cells
Protein Expr. Purif.
5
225-232
1994
Homo sapiens
brenda
Stewart, K.; Brown, O.A.; Morelli, A.E.; Fairbairn, L.J.; Lashford, L.S.; Cooper, A.; Hatton, C.E.; Dexter, T.M.; Castro, M.G.; Lowenstein, P.R.
Uptake of alpha-(L)-iduronidase produced by retrovirally transduced fibroblasts into neuronal and glial cells in vitro
Gene Ther.
4
63-75
1997
Homo sapiens
brenda
Clarke, L.A.; Nasir, J.; Zhang, H.; McDonald, H.; Applegarth, D.A.; Hayden, M.R.; Toone, J.
Murine alpha-L-iduronidase: cDNA isolation and expression
Genomics
24
311-316
1994
Mus musculus
brenda
Sakuda, H.; Kusaba, A.; Ohshita, T.; Iwamasw, T.
Tissue and cellular distribution of alpha-L-iduronidase in the pig
J. Histochem. Cytochem.
38
785-792
1990
Sus scrofa
brenda
Ruth, L.; Eisenberg, D.; Neufeld, E.F.
alpha-L-Iduronidase forms semi-crystalline spherulites with amyloid-like properties
Acta Crystallogr. Sect. D
56
524-528
2000
Homo sapiens
-
brenda
Mandelli, J.; Wajner, A.; Pires, R.F.; Giugliani, R.; Coelho, J.C.
Detection of mucopolysaccharidosis type I heterozygotes based on the biochemical characteristics of leukocyte alpha-L-iduronidase
Arch. Med. Res.
33
20-24
2002
Homo sapiens
brenda
Nieman, C.E.; Wong, A.W.; He, S.; Clarke, L.; Hopwood, J.J.; Withers, S.G.
Family 39 alpha-L-iduronidases and beta-D-xylosidases react through similar glycosyl-enzyme intermediates: Identification of the human iduronidase nucleophile
Biochemistry
42
8054-8065
2003
Homo sapiens
brenda
Hein, L.K.; Hopwood, J.J.; Clements, P.R.; Brooks, D.A.
The alpha-L-iduronidase mutations R89Q and R89W result in an attenuated mucopolysaccharidosis type I clinical presentation
Biochim. Biophys. Acta
1639
95-103
2003
Homo sapiens
brenda
Mandelli, J.; Wajner, A.; Pires, R.; Giugliani, R.; Coelho, J.C.
Effect of CuCl2, NaCl and EDTA on the enzyme alpha-L-iduronidase in the plasma of normal individuals and heterozygotes for MPS I
Clin. Chim. Acta
318
83-89
2002
Homo sapiens
brenda
Brooks, D.A.; Fabrega, S.; Hein, L.K.; Parkinson, E.J.; Durand, P.; Yogalingam, G.; Matte, U.; Giugliani, R.; Dasvarma, A.; Eslahpazire, J.; Henrissat, B.; Mornon, J.P.; Hopwood, J.J.; Lehn, P.
Glycosidase active site mutations in human alpha-L-iduronidase
Glycobiology
11
741-750
2001
Homo sapiens
brenda
Kloska, A.; Bohdanowicz, J.; Konopa, G.; Tylki-Szym?ska, A.; Jakobkiewicz-Banecka, J.; Czartoryska, B.; Liberek, A.; Wegrzyn, A.; Wegrzyn, G.
Changes in hair morphology of mucopolysaccharidosis I patients treated with recombinant human alpha-L-iduronidase (laronidase, Aldurazyme)
Am. J. Med. Genet. A
139
199-203
2005
Homo sapiens
brenda
Yogalingam, G.; Guo, X.H.; Muller, V.J.; Brooks, D.A.; Clements, P.R.; Kakkis, E.D.; Hopwood, J.J.
Identification and molecular characterization of alpha-L-iduronidase mutations present in mucopolysaccharidosis type I patients undergoing enzyme replacement therapy
Hum. Mutat.
24
199-207
2004
Homo sapiens (P35475), Homo sapiens
brenda
Prince, W.S.; McCormick, L.M.; Wendt, D.J.; Fitzpatrick, P.A.; Schwartz, K.L.; Aguilera, A.I.; Koppaka, V.; Christianson, T.M.; Vellard, M.C.; Pavloff, N.; Lemontt, J.F.; Qin, M.; Starr, C.M.; Bu, G.; Zankel, T.C.
Lipoprotein receptor binding, cellular uptake, and lysosomal delivery of fusions between the receptor-associated protein (RAP) and alpha-L-iduronidase or acid alpha-glucosidase
J. Biol. Chem.
279
35037-35046
2004
Homo sapiens
brenda
Laradi, S.; Tukel, T.; Erazo, M.; Shabbeer, J.; Chkioua, L.; Khedhiri, S.; Ferchichi, S.; Chaabouni, M.; Miled, A.; Desnick, R.J.
Mucopolysaccharidosis I: alpha-L-iduronidase mutations in three tunisian families
J. Inherit. Metab. Dis.
28
1019-1026
2005
Homo sapiens
brenda
Hein, L.K.; Bawden, M.; Muller, V.J.; Sillence, D.; Hopwood, J.J.; Brooks, D.A.
alpha-L-Iduronidase premature stop codons and potential read-through in mucopolysaccharidosis type I patients
J. Mol. Biol.
338
453-462
2004
Homo sapiens
brenda
Rempel, B.P.; Clarke, L.A.; Withers, S.G.
A homology model for human alpha-L-iduronidase: insights into human disease
Mol. Genet. Metab.
85
28-37
2005
Homo sapiens (P35475), Homo sapiens
brenda
Belichenko, P.V.; Dickson, P.I.; Passage, M.; Jungles, S.; Mobley, W.C.; Kakkis, E.D.
Penetration, diffusion, and uptake of recombinant human alpha-L-iduronidase after intraventricular injection into the rat brain
Mol. Genet. Metab.
86
141-149
2005
Homo sapiens
brenda
Pabba, J.; Rempel, B.P.; Withers, S.G.; Vasella, A.
Synthesis of glycaro-1,5-lactams and tetrahydrotetrazolopyridine-5-carboxylates: inhibitors of beta-D-glucuronidase and alpha-L-iduronidase
Helv. Chim. Acta
89
635-666
2006
Homo sapiens
-
brenda
Di Domenico, C.; Di Napoli, D.; Gonzalez Y. Reyero, E.; Lombardo, A.; Naldini, L.; Di Natale, P.
Limited transgene immune response and long-term expression of human alpha-L-iduronidase in young adult mice with mucopolysaccharidosis type I by liver-directed gene therapy
Hum. Gene Ther.
17
1112-1121
2006
Homo sapiens
brenda
Wang, D.; Worsham, D.N.; Pan, D.
Co-expression of MGMT(P140K) and alpha-L-iduronidase in primary hepatocytes from mucopolysaccharidosis type I mice enables efficient selection with metabolic correction
J. Gene Med.
10
249-259
2008
Mus musculus
brenda
Chen, F.; Vitry, S.; Hocquemiller, M.; Desmaris, N.; Ausseil, J.; Heard, J.M.
Alpha-L-iduronidase transport in neurites
Mol. Genet. Metab.
87
349-358
2006
Homo sapiens
brenda
Chung, S.; Ma, X.; Liu, Y.; Lee, D.; Tittiger, M.; Ponder, K.P.
Effect of neonatal administration of a retroviral vector expressing alpha-L-iduronidase upon lysosomal storage in brain and other organs in mucopolysaccharidosis I mice
Mol. Genet. Metab.
90
181-192
2007
Homo sapiens
brenda
Wraith, J.E.; Beck, M.; Lane, R.; van der Ploeg, A.; Shapiro, E.; Xue, Y.; Kakkis, E.D.; Guffon, N.
Enzyme replacement therapy in patients who have mucopolysaccharidosis I and are younger than 5 years: results of a multinational study of recombinant human alpha-L-iduronidase (laronidase)
Pediatrics
120
e37-e46
2007
Homo sapiens
brenda
Downing, W.L.; Galpin, J.D.; Clemens, S.; Lauzon, S.M.; Samuels, A.L.; Pidkowich, M.S.; Clarke, L.A.; Kermode, A.R.
Synthesis of enzymatically active human alpha-L-iduronidase in Arabidopsis cgl (complex glycan-deficient) seeds
Plant Biotechnol. J.
4
169-181
2006
Homo sapiens
brenda
Kermode, A.R.; Zeng, Y.; Hu, X.; Lauson, S.; Abrams, S.R.; He, X.
Ectopic expression of a conifer Abscisic Acid Insensitive3 transcription factor induces high-level synthesis of recombinant human alpha-L-iduronidase in transgenic tobacco leaves
Plant Mol. Biol.
63
763-776
2007
Homo sapiens (P35475), Homo sapiens
brenda
Tsukimura, T.; Tajima, Y.; Kawashima, I.; Fukushige, T.; Kanzaki, T.; Kanekura, T.; Ikekita, M.; Sugawara, K.; Suzuki, T.; Togawa, T.; Sakuraba, H.
Uptake of a recombinant human alpha-L-iduronidase (laronidase) by cultured fibroblasts and osteoblasts
Biol. Pharm. Bull.
31
1691-1695
2008
Homo sapiens
brenda
Pastores, G.M.
Laronidase (Aldurazyme): enzyme replacement therapy for mucopolysaccharidosis type I
Expert. Opin. Biol. Ther.
8
1003-1009
2008
Homo sapiens
brenda
Sugawara, K.; Saito, S.; Ohno, K.; Okuyama, T.; Sakuraba, H.
Structural study on mutant alpha-L-iduronidases: insight into mucopolysaccharidosis type I
J. Hum. Genet.
53
467-474
2008
Homo sapiens
brenda
Wynn, R.F.; Mercer, J.; Page, J.; Carr, T.F.; Jones, S.; Wraith, J.E.
Use of enzyme replacement therapy (Laronidase) before hematopoietic stem cell transplantation for mucopolysaccharidosis I: experience in 18 patients
J. Pediatr.
154
135-139
2009
Homo sapiens
brenda
Giugliani, R.; Rojas, V.M.; Martins, A.M.; Valadares, E.R.; Clarke, J.T.; Goes, J.E.; Kakkis, E.D.; Worden, M.A.; Sidman, M.; Cox, G.F.
A dose-optimization trial of laronidase (Aldurazyme) in patients with mucopolysaccharidosis I
Mol. Genet. Metab.
96
13-19
2009
Homo sapiens
brenda
Clarke, L.A.; Wraith, J.E.; Beck, M.; Kolodny, E.H.; Pastores, G.M.; Muenzer, J.; Rapoport, D.M.; Berger, K.I.; Sidman, M.; Kakkis, E.D.; Cox, G.F.
Long-term efficacy and safety of laronidase in the treatment of mucopolysaccharidosis I
Pediatrics
123
229-240
2009
Homo sapiens
brenda
Kasper, D.C.; Iqbal, F.; Dvorakova, L.; Zeman, J.; Magner, M.; Bodamer, O.; Pollak, A.; Herkner, K.R.; Item, C.B.
Rapid and accurate denaturating high performance liquid chromatography protocol for the detection of alpha-L-iduronidase mutations causing mucopolysaccharidosis type I
Clin. Chim. Acta
411
345-350
2010
Homo sapiens
brenda
Boado, R.J.; Hui, E.K.; Lu, J.Z.; Pardridge, W.M.
AGT-181: expression in CHO cells and pharmacokinetics, safety, and plasma iduronidase enzyme activity in Rhesus monkeys
J. Biotechnol.
144
135-141
2009
Homo sapiens
brenda
Tylki-Szymanska, A.; Marucha, J.; Jurecka, A.; Syczewska, M.; Czartoryska, B.
Efficacy of recombinant human alpha-L-iduronidase (laronidase) on restricted range of motion of upper extremities in mucopolysaccharidosis type I patients
J. Inherit. Metab. Dis.
33
151-157
2010
Homo sapiens
brenda
Valayannopoulos, V.; Boddaert, N.; Barbier, V.; Le Merrer, M.; Caillaud, C.; de Lonlay, P.
Cognitive and neuroradiological improvement in three patients with attenuated MPS I treated by laronidase
Mol. Genet. Metab.
100
20-23
2010
Homo sapiens
brenda
Tylki-Szymanska, A.; Rozdzynska, A.; Jurecka, A.; Marucha, J.; Czartoryska, B.
Anthropometric data of 14 patients with mucopolysaccharidosis I: retrospective analysis and efficacy of recombinant human alpha-L-iduronidase (laronidase)
Mol. Genet. Metab.
99
10-17
2010
Homo sapiens
brenda
Fu, L.; Miao, Y.; Lo, S.; Seto, T.; Sun, S.; Xu, Z.; Clemens, S.; Clarke, L.; Kermode, A.; Jiang, L.
Production and characterization of soluble human lysosomal enzyme ?-iduronidase with high activity from culture media of transgenic tobacco BY-2 cells
Plant Sci.
177
668-675
2009
Homo sapiens
brenda
Galpin, J.; Clemens, S.; Kermode, A.
The carboxy-terminal ER-retention motif, SEKDEL, influences the N-linked glycosylation of recombinant human ?-l-iduronidase but has little effect on enzyme activity in seeds of Brassica napus and Nicotiana tabacum
Plant Sci.
178
440-447
2010
Homo sapiens
brenda
Sun, L.; Li, C.; Song, X.; Zheng, N.; Zhang, H.; Dong, G.
Three novel alpha-L-iduronidase mutations in 10 unrelated Chinese mucopolysaccharidosis type I families
Genet. Mol. Biol.
34
195-200
2011
Homo sapiens
brenda
Vite, C.H.; Wang, P.; Patel, R.T.; Walton, R.M.; Walkley, S.U.; Sellers, R.S.; Ellinwood, N.M.; Cheng, A.S.; White, J.T.; ONeill, C.A.; Haskins, M.
Biodistribution and pharmacodynamics of recombinant human alpha-L-iduronidase (rhIDU) in mucopolysaccharidosis type I-affected cats following multiple intrathecal administrations
Mol. Genet. Metab.
103
268-274
2011
Felis catus, Homo sapiens
brenda
Maita, N.; Taniguchi, H.; Sakuraba, H.
Crystallization, X-ray diffraction analysis and SIRAS phasing of human alpha-L-iduronidase
Acta Crystallogr. Sect. F
68
1363-1366
2012
Homo sapiens (P35475)
brenda
Lu, F.; Lico, L.; Hung, S.
Synthesis of a fluorogenic substrate for alpha-L-iduronidase
Arkivoc
2013
13-21
2012
Homo sapiens
-
brenda
Baldo, G.; Quoos Mayer, F.; Burin, M.; Carrillo-Farga, J.; Matte, U.; Giugliani, R.
Recombinant encapsulated cells overexpressing alpha-L-iduronidase correct enzyme deficiency in human mucopolysaccharidosis type I cells
Cells Tissues Organs
195
323-329
2012
Homo sapiens
brenda
Jung, G.; Pabst, M.; Neumann, L.; Berger, A.; Lubec, G.
Characterization of alpha-L-iduronidase (Aldurazyme) and its complexes
J. Proteomics
80
26-33
2013
Homo sapiens
brenda
Oussoren, E.; Keulemans, J.; van Diggelen, O.P.; Oemardien, L.F.; Timmermans, R.G.; van der Ploeg, A.T.; Ruijter, G.J.
Residual alpha-L-iduronidase activity in fibroblasts of mild to severe mucopolysaccharidosis type I patients
Mol. Genet. Metab.
109
377-381
2013
Homo sapiens
brenda
Ou, L.; Herzog, T.L.; Wilmot, C.M.; Whitley, C.B.
Standardization of alpha-L-iduronidase enzyme assay with Michaelis-Menten kinetics
Mol. Genet. Metab.
111
113-115
2014
Mus musculus, Mus musculus C57BL/6
brenda
Maita, N.; Tsukimura, T.; Taniguchi, T.; Saito, S.; Ohno, K.; Taniguchi, H.; Sakuraba, H.
Human alpha-L-iduronidase uses its own N-glycan as a substrate-binding and catalytic module
Proc. Natl. Acad. Sci. USA
110
14628-14633
2013
Homo sapiens
brenda
Cheng, W.C.; Lin, C.K.; Li, H.Y.; Chang, Y.C.; Lu, S.J.; Chen, Y.S.; Chang, S.Y.
A combinatorial approach towards the synthesis of non-hydrolysable triazole-iduronic acid hybrid inhibitors of human alpha-L-iduronidase discovery of enzyme stabilizers for the potential treatment of MPSI
Chem. Commun. (Camb.)
54
2647-2650
2018
Homo sapiens (P35475)
brenda
Artola, M.; Kuo, C.L.; McMahon, S.A.; Oehler, V.; Hansen, T.; van der Lienden, M.; He, X.; van den Elst, H.; Florea, B.I.; Kermode, A.R.; van der Marel, G.A.; Gloster, T.M.; Codee, J.D.C.; Overkleeft, H.S.; Aerts, J.M.F.G.
New irreversible alpha-L-iduronidase inhibitors and activity-based probes
Chemistry
24
19081-19088
2018
Homo sapiens (P35475), Homo sapiens
brenda
Breier, A.C.; Ce, J.; Mezzalira, J.; Daitx, V.V.; Moraes, V.C.; Goldim, M.P.S.; Coelho, J.C.
alpha-L-iduronidase and arylsulfatase B in dried blood spots on filter paper Biochemical parameters and time stability
Clin. Biochem.
50
431-435
2017
Homo sapiens (P35475)
brenda
Cardon, F.; Pallisse, R.; Bardor, M.; Caron, A.; Vanier, J.; Ele Ekouna, J.P.; Lerouge, P.; Boitel-Conti, M.; Guillet, M.
Brassica rapa hairy root based expression system leads to the production of highly homogenous and reproducible profiles of recombinant human alpha-L-iduronidase
Plant Biotechnol. J.
17
505-516
2019
Homo sapiens (P35475), Homo sapiens
brenda