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Human IDS Protein expressed in Human Cells - ABIN2002610
Wilson, Morris, Anson, Occhiodoro, Bielicki, Clements, Hopwood: Hunter syndrome: isolation of an iduronate-2-sulfatase cDNA clone and analysis of patient DNA. in Proceedings of the National Academy of Sciences of the United States of America 1990
Show all 3 references for ABIN2002610
Data demonstrate that iduronate sulfatase plays a critical role during early vertebrate development and its downregulation may be responsible for severe developmental defects, including a misshapen trunk and abnormal craniofacial cartilages.
This study evaluated a novel mutation in the IDS gene among 8 male Hunter syndrome patients; there was a quantitative deficiency of NK and B cell with normal responses in other immune parameters.
30 novel iduronate sulfatase mutations have been identified in mucopolysaccharidosis type II Latin American patients.
Identification of a splice site mutation in the IDS gene associated with mucopolysaccharidosis type II.
a novel (p.R468P) and five known (p.R88C, p.D148V, p.G224A, p.Y348X, and p.R468Q) IDS mutations were shown to result in proteins with little or no IDS activity and altered protein processing, when expressed in COS7 cells
A report of a novel IDS nonsense mutation resulting in mucopolysaccharidosis type II in several patients from a Chinese family.
genetically analyze patients with severe Hunter syndrome that showed a total deletion of the iduronate-2-sulphatase (IDS) gene
Family members with 3 generations of X-inactivation with Hunter syndrome have 1568A>G missence mutation in the IDS gene
LCR (show CBR2 Proteins)-initiated rearrangements at the IDS locus, completed with Alu-mediated recombination or non-homologous end joining
Hunter syndrome in Thailand is caused by a diverse set of defects affecting both IDS protein production and activity.
The in vivo correction of heritable gene lesions at the RNA level operating via a correction mechanism akin to RNA-editing, was observed for IDS mutant transcript.
While the iduronate 2-sulfatase sp replacement results in increased enzyme secretion, the addition of the ApoB (show APOB Proteins)-BD allows efficient BBB transcytosis and restoration of sulphamidase (show SGSH Proteins) activity in the brain of treated mice.
Iduronate-2-sulfatase (IDS) is localized in lysosomes in pancreatic islet cells and expression is regulated by glucose. IDS has a potential role in the normal pathway of lysosomal degradation of secretory peptides.
Ids crossing the blood-brain barrier corrects CNS defects in MPSII mice.
Iduronate-2-sulfatase is required for the lysosomal degradation of heparan sulfate and dermatan sulfate. Mutations in this X-chromosome gene that result in enzymatic deficiency lead to the sex-linked Mucopolysaccharidosis Type II, also known as Hunter Syndrome. Iduronate-2-sulfatase has a strong sequence similarity with human arylsulfatases A, B, and C, and human glucosamine-6-sulfatase. Multiple alternatively spliced transcript variants that encode different protein isoforms have been described.
iduronate 2-sulfatase (Hunter syndrome)
, iduronate 2-sulfatase
, iduronate 2-sulfatase-like
, alpha-L-iduronate sulfate sulfatase
, iduronate 2-sulfatase 14 kDa chain
, iduronate 2-sulfatase 42 kDa chain
, iduronate sulfatase