ERp44 Mediates a Thiol-independent Retention of Formylglycine-generating Enzyme in the Endoplasmic Reticulum
Authors:
- Karthikeyan RadhakrishnanKarthikeyan Radhakrishnan
- Thomas DierksTDThomas Dierks
- Bernhard SchmidtBSBernhard Schmidt
- Kurt von FiguraKFKurt von Figura
Open Access
- 1 March 2008
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 283 (10) , 6375-6383
Abstract
No abstract availableKeywords
This publication has 29 references indexed in Scilit:
- Sulfatases and sulfatase modifying factors: an exclusive and promiscuous relationshipHuman Molecular Genetics, 2005
- SULFATASES AND HUMAN DISEASEAnnual Review of Genomics and Human Genetics, 2005
- 1.3 Å Structure of Arylsulfatase from Pseudomonas aeruginosa Establishes the Catalytic Mechanism of Sulfate Ester Cleavage in the Sulfatase FamilyStructure, 2001
- Crystal Structure of an Enzyme-Substrate Complex Provides Insight into the Interaction between Human Arylsulfatase A and its Substrates During CatalysisJournal of Molecular Biology, 2001
- A novel protein modification generating an aldehyde group in sulfatases: its role in catalysis and diseaseBioEssays, 1998
- Posttranslational Formation of Formylglycine in Prokaryotic Sulfatases by Modification of Either Cysteine or SerineJournal of Biological Chemistry, 1998
- 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,Biochemistry, 1998
- Arylsulfatase from Klebsiella pneumoniae Carries a Formylglycine Generated from a SerineJournal of Biological Chemistry, 1998
- Conversion of cysteine to formylglycine: A protein modification in the endoplasmic reticulumProceedings of the National Academy of Sciences, 1997
- A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiencyCell, 1995