Identification of ERp29, an Endoplasmic Reticulum Lumenal Protein, as a New Member of the Thyroglobulin Folding Complex
Open Access
- 1 May 2002
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 277 (19), 17009-17015
- https://doi.org/10.1074/jbc.m200539200
Abstract
No abstract availableKeywords
This publication has 30 references indexed in Scilit:
- Genomic organization and promoter characterization of the gene encoding a putative endoplasmic reticulum chaperone, ERp29Gene, 2002
- Thioredoxin Fold as Homodimerization Module in the Putative Chaperone ERp29: NMR Structures of the Domains and Experimental Model of the 51 kDa DimerStructure, 2001
- Quality control in the secretory assembly linePhilosophical Transactions Of The Royal Society B-Biological Sciences, 2001
- Isolation of ERp29, a novel endoplasmic reticulum protein, from rat enamel cellsEuropean Journal of Biochemistry, 2000
- Protein folding in the ERSeminars in Cell & Developmental Biology, 1999
- ERp28, a human endoplasmic‐reticulum‐lumenal protein, is a member of the protein disulfide isomerase family but lacks a CXXC thioredoxin‐box motifEuropean Journal of Biochemistry, 1998
- windbeutel,a gene required for dorsoventral patterning inDrosophila,encodes a protein that has homologies to vertebrate proteins of the endoplasmic reticulumGenes & Development, 1998
- A stress‐inducible rat liver endoplasmic reticulum protein, ERp29European Journal of Biochemistry, 1998
- Combination of Direct DNA Sequencing with Degenerate Primer-Mediated PCR and 5′-/3′-RACE to Screen Novel cDNA SequencesBioTechniques, 1997
- Molecular cloning of ERp29, a novel and widely expressed resident of the endoplasmic reticulumFEBS Letters, 1997