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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Protein disulfide isomerase family A, member 5

Top mentioned proteins: CAN, alpha-Synuclein, PCNA, RbAp46, ACID
Papers on PDIR
Structure of the non-catalytic domain of the protein disulfide isomerase-related protein (PDIR) reveals function in protein binding.
Gehring et al., Montréal, Canada. In Plos One, 2012
Protein disulfide isomerase-related (PDIR) protein (also known as PDIA5) is a specialized member that participates in the folding of α1-antitrypsin and N-linked glycoproteins.
Unfolded protein response is not activated in the mucopolysaccharidoses but protein disulfide isomerase 5 is deregulated.
Di Natale et al., Napoli, Italy. In J Inherit Metab Dis, 2012
protein disulfide isomerase 5 is deregulated in the mucopolysaccharidoses, although the unfolded protein response is not activated
Osteogenic differentiation of marrow stromal cells on random and aligned electrospun poly(L-lactide) nanofibers.
Jabbari et al., Columbia, United States. In Ann Biomed Eng, 2011
Percent deviation from ideal randomness (PDIR) values indicated that cells seeded on the random fibers (PDIR=6.5%)
A structural overview of the PDI family of proteins.
Gehring et al., Montréal, Canada. In Febs J, 2010
Protein disulfide isomerases are enzymes that mediate oxidative protein folding in the endoplasmic reticulum.
Oxidative protein folding in the mammalian endoplasmic reticulum.
Bulleid et al., Manchester, United Kingdom. In Biochem Soc Trans, 2004
Disulphide bonds are formed, reduced and isomerized in the endoplasmic reticulum of mammalian cells by a family of oxidoreductases, which includes protein disulphide isomerase (PDI), ERp57, ERp72, P5 and PDIR.
Different contributions of the three CXXC motifs of human protein-disulfide isomerase-related protein to isomerase activity and oxidative refolding.
Kikuchi et al., Kusatsu, Japan. In J Biol Chem, 2004
Three thioredoxin motifs (CXXC) of purified PDIR were found to contribute to its isomerase activity.
Analysis of plausible downstream target genes of Hoxc8 in F9 teratocarcinoma cells. Putative downstream target genes of Hoxc8.
Kim et al., Seoul, South Korea. In Mol Biol Rep, 2003
The protein spots having differences more than 4 fold in intensity were selected, analyzed by MALDI-TOF, and grouped in terms of putative function; cytoskeleton and motility (vimentin, gamma-actin, tropomyosin, and tubulin beta-5 chain); folding, modification and degradation of protein (GRP78, proteasome subunit alpha type 5, 26S proteasome regulatory subunit p27 protein, and PDIR); metabolism (ATP synthase beta subunit, Pgam1, and CAII); transcription/translation factors and general nucleic acid binding proteins (RbAp46, PCNA, eEF-1-beta, and nucleophosmin).
Androgen-induced expression of endoplasmic reticulum (ER) stress response genes in prostate cancer cells.
Srivastava et al., Rockville, United States. In Oncogene, 2003
This study focuses on our new observations of the coordinated androgen induction of genes (NDRG1, PDIR, HERPUD1, ORP150) involved in the endoplasmic reticulum (ER) stress response pathway.
Molecular cloning of the cDNA encoding a novel protein disulfide isomerase-related protein (PDIR).
Kikuchi et al., Ōsaka, Japan. In Febs Lett, 1995
We isolated the cDNA of a novel protein disulfide isomerase (PDI)-related protein, designated PDIR, from a human placental cDNA library.
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