About: Multiple sulfatase deficiency is caused by mutations in the gene encoding the human C(alpha)-formylglycine generating enzyme

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About: Multiple sulfatase deficiency is caused by mutations in the gene encoding the human C(alpha)-formylglycine generating enzyme Goto Sponge NotDistinct Permalink

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description	artículu científicu espublizáu en 2003 (ast) vědecký článek publikovaný v roce 2003 (cs) наукова стаття, опублікована в травні 2003 (uk) 2003 թվականի մայիսին հրատարակված գիտական հոդված (hy) 2003 թուականի Մայիսին հրատարակուած գիտական յօդուած (hyw) vedecký článok (publikovaný 2003/05/16) (sk) مقالة علمية (نشرت في 16-5-2003) (ar) im Mai 2003 veröffentlichter wissenschaftlicher Artikel (de) article scientifique publié en 2003 (fr) wetenschappelijk artikel (gepubliceerd op 2003/05/16) (nl) scientific journal article (en)
publication date	wds:Q28646260-B3666A4A-114A-4AAE-8ACA-83647BFF89DE
publication date	2003-05-16 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28646260-565A6C59-2917-433C-9863-4D3B78B8CCB6
language of work or name	English
cites work	wds:Q28646260-01CFF6F8-F154-49D9-AAA7-A482F91B6A04 wds:Q28646260-063F34CF-315E-446C-A2EE-CE9D57208D54 wds:Q28646260-12A9A955-EDB4-450D-B42A-D4BBA67E8711 wds:Q28646260-19EE9A6F-734C-431D-86F9-51CBC64F477B wds:Q28646260-1A53BB0A-177C-4A6A-9F08-54745C0D76CA wds:Q28646260-20D99C3A-366F-4C40-865D-10A9D8BF0BF7 wds:Q28646260-315AF1F3-C452-4C7F-A19F-E5F0AF39A63E wds:Q28646260-36531026-4EB8-43E8-B65D-C5A7D95773DD wds:Q28646260-41997CB7-C75E-4CD1-97C4-B002837FD43F wds:Q28646260-4623F830-1AFB-4DF3-B1A5-85AA9C4AD9BA wds:Q28646260-49957832-9652-4A67-9DAE-DD194A6CE412 wds:Q28646260-55B680D2-C5AC-49D7-B1D0-243D24CCFDC8 wds:Q28646260-5DDB2C68-4877-47FA-BC33-A996324FD75F wds:Q28646260-5F53BDDD-5AD5-4AD7-9B46-0097B857AE35 wds:Q28646260-6921FAA7-5E0C-418C-8BB4-71E02445943B wds:Q28646260-709235D7-1A95-40EE-A559-AA1C815D5134 wds:Q28646260-7183BFC6-5146-421E-AA78-D27D6F21AB51 wds:Q28646260-733A582F-493A-4DA1-9333-B83AA4D5D3A4 wds:Q28646260-7C7ED25F-6EFC-46AF-A2D5-C69C6E67547E wds:Q28646260-83ED618B-B40D-4830-AA87-98E625672F45 wds:Q28646260-8CB61196-0939-4490-AE48-14140C01747A wds:Q28646260-911C24AF-BADA-4E4E-B088-7BC1F47C8243 wds:Q28646260-A06979DD-5C5B-419F-942F-4D695A2AFA53 wds:Q28646260-AE00FC95-2A0D-4A84-8599-504C6296B9A7 wds:Q28646260-B6D266E7-7FA1-4878-A6C9-CA709BE5EC28 wds:Q28646260-BD90008B-BF35-46AB-ABA3-CC59F3E1A04E wds:Q28646260-BE79DD6A-8750-4462-9C4F-078970B45DC4 wds:Q28646260-C14B14C1-A8FE-4FB7-B4AA-7171BDD381D8 wds:Q28646260-C505B465-7A44-4E80-8867-AB8ECB7E601D wds:Q28646260-CAC1215C-F3D3-48CE-999A-E9AA6A713A45 wds:Q28646260-DA7508A9-0455-41EC-8700-DA2D42EDB9B0 wds:Q28646260-E036C309-D686-4570-8CB4-919FAC229D2F wds:Q28646260-E2ADB5E9-880C-45C6-9835-8573A4DE8ADF wds:Q28646260-F0B6E1A4-6847-4263-89C6-DA1E6072310F wds:Q28646260-F278D85F-1776-4BCA-A01E-2CCDAAC21C5E wds:Q28646260-F522C17C-FB5B-4464-88A8-CF67C9E42ED9 wds:Q28646260-F80A5CE5-ECD1-4A0B-B67C-A4D23838E136 wds:Q28646260-FA75F47A-B8B1-4024-89DA-C411F718D3DB
cites work	Crystal structure of human arylsulfatase A: the aldehyde function and the metal ion at the active site suggest a novel mechanism for sulfate ester hydrolysis Mammalian Sec61 is associated with Sec62 and Sec63 A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency Conversion of cysteine to formylglycine: a protein modification in the endoplasmic reticulum Vectors for efficient expression in mammalian fibroblastoid, myeloid and lymphoid cells via transfection or infection. EMBOSS: the European Molecular Biology Open Software Suite Pfam: multiple sequence alignments and HMM-profiles of protein domains A new method for predicting signal sequence cleavage sites Gapped BLAST and PSI-BLAST: a new generation of protein database search programs Mass Spectrometric Sequencing of Proteins from Silver-Stained Polyacrylamide Gels The iron sulfur protein AtsB is required for posttranslational formation of formylglycine in the Klebsiella sulfatase. Overexpression of N-acetylgalactosamine-4-sulphatase induces a multiple sulphatase deficiency in mucopolysaccharidosis-type-VI fibroblasts The multiple sulfatase deficiency gene encodes an essential and limiting factor for the activity of sulfatases Database resources of the National Center for Biotechnology Information: 2002 update Preparation of microsomal membranes for cotranslational protein translocation. Characterization of posttranslational formylglycine formation by luminal components of the endoplasmic reticulum Conversion of cysteine to formylglycine in eukaryotic sulfatases occurs by a common mechanism in the endoplasmic reticulum Sequence determinants directing conversion of cysteine to formylglycine in eukaryotic sulfatases Arylsulfatase from Klebsiella pneumoniae carries a formylglycine generated from a serine 1.3 A structure of arylsulfatase from Pseudomonas aeruginosa establishes the catalytic mechanism of sulfate ester cleavage in the sulfatase family Early manifestations of multiple sulfatase deficiency Crystal structure of an enzyme-substrate complex provides insight into the interaction between human arylsulfatase A and its substrates during catalysis The evolutionary conservation of a novel protein modification, the conversion of cysteine to serinesemialdehyde in arylsulfatase from Volvox carteri Multiple sulfatase deficiency: catalytically inactive sulfatases are expressed from retrovirally introduced sulfatase cDNAs A sensitive procedure for the diagnosis of N-acetyl-galactosamine-6-sulfate sulfatase deficiency in classical Morquio's disease Posttranslational formation of formylglycine in prokaryotic sulfatases by modification of either cysteine or serine Studies in metachromatic leukodystrophy. XII. Multiple sulfatase deficiency Properties of sulfatases in cultured skin fibroblasts of multiple sulfatase deficient patients Multiple Deficiency of Mucopolysaccharide Sulfatases in Mucosulfatidosis Thiosulfate-mediated increase of arylsulfatase activities in multiple sulfatase deficiency disorder fibroblasts Deficiency of UDP-galactose:N-acetylglucosamine beta-1,4-galactosyltransferase I causes the congenital disorder of glycosylation type IId. Biochemical variability of arylsulphatases‐A,‐B and‐C in cultured fibroblasts from patients with multiple sulphatase deficiency Multiple sulphatase deficiency with early onset Multiple sulphatase deficiency presenting at birth Identification of formylglycine in sulfatases by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry Synthesis and stability of steroid sulfatase in fibroblasts from multiple sulfatase deficiency Synthesis and stability of arylsulfatase A and B in fibroblasts from multiple sulfatase deficiency Deficiency of dolichyl-P-Man:Man7GlcNAc2-PP-dolichyl mannosyltransferase causes congenital disorder of glycosylation type Ig
author name string	wds:Q28646260-00E61356-C82B-4D82-9E8F-8BD38EF7A626 wds:Q28646260-3F827F8F-C914-4817-A304-47854B633A69 wds:Q28646260-52DE6CE3-5B51-49CF-86F4-D68C38C4AEF0 wds:Q28646260-6234EE19-A9A2-4730-B1AA-8D968645FC34 wds:Q28646260-99428907-24E8-4210-B4C2-163A48D89BDC wds:Q28646260-C47B60B5-E2EB-49A5-90D9-64CAB05DFF97
OpenCitations bibliographic resource ID	wds:Q28646260-3A998EAB-F1E9-454D-90E0-D4081852D124
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/247226

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