Conversion of cysteine to formylglycine in eukaryotic sulfatases occurs by a common mechanism in the endoplasmic reticulum.
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Sulfatases and sulfatase modifying factors: an exclusive and promiscuous relationshipA general binding mechanism for all human sulfatases by the formylglycine-generating enzyme.Arylsulfatase B improves locomotor function after mouse spinal cord injuryRYK, a catalytically inactive receptor tyrosine kinase, associates with EphB2 and EphB3 but does not interact with AF-6Molecular characterization of the human Calpha-formylglycine-generating enzyme.Crystal structure of human pFGE, the paralog of the Calpha-formylglycine-generating enzyme.Formylglycine, a post-translationally generated residue with unique catalytic capabilities and biotechnology applications.Phylogeny of Algal Sequences Encoding Carbohydrate Sulfotransferases, Formylglycine-Dependent Sulfatases, and Putative Sulfatase Modifying Factors.Low-scale expression and purification of an active putative iduronate 2-sulfate sulfatase-Like enzyme from Escherichia coli K12.Overexpression of inactive arylsulphatase mutants and in vitro activation by light-dependent oxidation with vanadate.Sequence determinants directing conversion of cysteine to formylglycine in eukaryotic sulfatases.Characterization of posttranslational formylglycine formation by luminal components of the endoplasmic reticulum.Posttranslational modification of serine to formylglycine in bacterial sulfatases. Recognition of the modification motif by the iron-sulfur protein AtsB.Post-translational formylglycine modification of bacterial sulfatases by the radical S-adenosylmethionine protein AtsB.Asymmetric synthesis of propargylamines as amino acid surrogates in peptidomimetics.The iron sulfur protein AtsB is required for posttranslational formation of formylglycine in the Klebsiella sulfatase.A biochemical and physicochemical comparison of two recombinant enzymes used for enzyme replacement therapies of hunter syndrome.Eukaryotic formylglycine-generating enzyme catalyses a monooxygenase type of reaction.Posttranslational formation of formylglycine in prokaryotic sulfatases by modification of either cysteine or serine
P2860
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P2860
Conversion of cysteine to formylglycine in eukaryotic sulfatases occurs by a common mechanism in the endoplasmic reticulum.
description
1998 nî lūn-bûn
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1998年の論文
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1998年学术文章
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1998年学术文章
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1998年学术文章
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1998年学术文章
@zh-my
1998年学术文章
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1998年學術文章
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1998年學術文章
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1998年學術文章
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name
Conversion of cysteine to form ...... in the endoplasmic reticulum.
@en
type
label
Conversion of cysteine to form ...... in the endoplasmic reticulum.
@en
prefLabel
Conversion of cysteine to form ...... in the endoplasmic reticulum.
@en
P2093
P2860
P1433
P1476
Conversion of cysteine to form ...... in the endoplasmic reticulum.
@en
P2093
P2860
P356
10.1016/S0014-5793(98)00065-9
P407
P577
1998-02-01T00:00:00Z