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


Ero1-Lalpha, Ero1alpha, ERO1-L
This gene encodes a member of the endoplasmic reticulum oxidoreductin family. The encoded protein is localized to the endoplasmic reticulum and promotes the formation of disulfide bonds by oxidizing protein disulfide isomerase. This gene may play a role in endoplasmic reticulum stress-induced apoptosis and the cellular response to hypoxia. [provided by RefSeq, Feb 2011] (from NCBI)
Top mentioned proteins: alpha-Synuclein, oxidoreductase, CAN, V1a, Thioredoxin
Papers on Ero1-Lalpha
Activation of the unfolded protein response in aged human lenses.
Yang et al., Liaocheng, China. In Mol Med Report, Jul 2015
A similar effect was observed in the protein levels, which also demonstrated a gradual increase in the levels of endoplasmic oxidoreductin-1-like (Ero1-L)-β and protein disulfide isomerase, but a lower level of Ero1-Lα.
Dynamics of unfolded protein response in recombinant CHO cells.
Mehra et al., Mumbai, India. In Cytotechnology, Mar 2015
In contrast, calreticulin and ERO1-L alpha, two of the lowest expressed genes exhibit transient time profiles, with peak induction on day 3.
Autophagy-related prognostic signature for breast cancer.
Guo et al., Harbin, China. In Mol Carcinog, Feb 2015
We identified a set of eight autophagy genes (BCL2, BIRC5, EIF4EBP1, ERO1L, FOS, GAPDH, ITPR1 and VEGFA) that were significantly associated with overall survival in breast cancer.
iTRAQ-based proteomic analysis of tetramethylpyrazine inhibition on lipopolysaccharide-induced microglial activation.
Yu et al., Chongqing, China. In Life Sci, Feb 2015
Protein annotation revealed that the differentially expressed proteins, such as inducible nitric oxide synthase (iNOS) and ERO1-like protein (ERO1L), might be involved in reducing cellular oxidation in response to stress.
The transcription factor CHOP, a central component of the transcriptional regulatory network induced upon CCl4 intoxication in mouse liver, is not a critical mediator of hepatotoxicity.
Godoy et al., Dortmund, Germany. In Arch Toxicol, 2014
Two observations indicated that CHOP may be responsible for CCl4-induced cell death: (1) Nuclear translocation of CHOP was exclusively observed in the pericentral fraction of hepatocytes that deteriorate in response to CCl4 and (2) CHOP-regulated genes with previously reported pro-apoptotic function such as GADD34, TRB3 and ERO1L were induced in the pericentral zone as well.
Exploration of potential roles of a new LOXL2 splicing variant using network knowledge in esophageal squamous cell carcinoma.
Li et al., Shantou, China. In Scientificworldjournal, 2013
Several tumor-related genes such as ERO1L, ITGA3, and MAPK8 were found closest to LOXL2-e13.
Identification of differentially expressed genes in the oviduct of two rabbit lines divergently selected for uterine capacity using suppression subtractive hybridization.
Folch et al., Barcelona, Spain. In Anim Genet, 2013
Finally, three interesting genes, PGR, HSD17B4 and ERO1L, were identified as overexpressed in the low line using RT-qPCR.
Ero1α regulates Ca(2+) fluxes at the endoplasmic reticulum-mitochondria interface (MAM).
Sitia et al., Milano, Italy. In Antioxid Redox Signal, 2012
the levels, subcellular localization, and activity of Ero1alpha coordinately regulate Ca(2+) and redox homeostasis and signaling in the early secretory compartment.
Functional in vitro analysis of the ERO1 protein and protein-disulfide isomerase pathway.
Nagata et al., Kyoto, Japan. In J Biol Chem, 2011
the intramolecular electron transfer from the a domain to the a' domain within PDI during its oxidation by ERO1alpha.
Molecular cloning and characterization of the porcine Ero1L and ERp44 genes: potential roles in controlling energy metabolism.
Yang et al., Wuhan, China. In Gen Comp Endocrinol, 2011
Here, we cloned full-length cDNA sequences of the porcine Ero1L (1448bp) and ERp44 (1361bp) genes.
The sarcoplasmic reticulum luminal thiol oxidase ERO1 regulates cardiomyocyte excitation-coupled calcium release and response to hemodynamic load.
Ron et al., New York City, United States. In Faseb J, 2011
The peak amplitude of calcium transients in homozygous Ero1alpha mutant adult cardiomyocytes was reduced to 42.0 +/- 2.2% (n=10, P </= 0.01) of values recorded in wild-type cardiomyocytes.
Molecular bases of cyclic and specific disulfide interchange between human ERO1alpha protein and protein-disulfide isomerase (PDI).
Inaba et al., Fukuoka, Japan. In J Biol Chem, 2011
Molecular bases of cyclic and specific disulfide interchange between human ERO1alpha protein and protein-disulfide isomerase (PDI).
Increased expression of Ero1L-alpha in healing fetal wounds.
Kathju et al., Pittsburgh, United States. In Bmc Res Notes, 2010
This study establishes its identity as Ero1L-alpha and confirms its elevated expression in healing fetal wounds.
Crystal structures of human Ero1α reveal the mechanisms of regulated and targeted oxidation of PDI.
Suzuki et al., Fukuoka, Japan. In Embo J, 2010
Ero1alpha limits its oxidative activity using four regulatory cysteines properly positioned within a critical loop that transfers electrons from protein disulphide isomerase to the FAD-containing active site.
Ero1alpha is expressed on blood platelets in association with protein-disulfide isomerase and contributes to redox-controlled remodeling of alphaIIbbeta3.
Cierniewski et al., Łódź, Poland. In J Biol Chem, 2010
Ero1alpha is expressed on blood platelets in association with protein-disulfide isomerase and contributes to redox-controlled remodeling of alphaIIbbeta3.
Oxidative protein folding in the endoplasmic reticulum: tight links to the mitochondria-associated membrane (MAM).
Thomas et al., Edmonton, Canada. In Biochim Biophys Acta, 2010
On the MAM, ER folding chaperones such as calnexin and calreticulin and oxidoreductases such as ERp44, ERp57 and Ero1alpha regulate calcium flux from the ER through reversible, calcium and redox-dependent interactions with IP3Rs (inositol 1,4,5-trisphophate receptors) and with SERCAs (sarcoplasmic/endoplasmic reticulum calcium ATPases).
New insights into thiol-mediated regulation of adiponectin secretion.
Wolf, Berkeley, United States. In Nutr Rev, 2008
Within adipocytes, it is retained in the lumen of the endoplasmic reticulum by binding to the thiol protein ERp44 and released by another thiol protein, Ero1-Lalpha.
Post-translational modifications of adiponectin: mechanisms and functional implications.
Xu et al., Hong Kong, Hong Kong. In Biochem J, 2008
Secretion of the adiponectin oligomers is tightly controlled by a pair of molecular chaperones in the ER (endoplasmic reticulum), including ERp44 (ER protein of 44 kDa) and Ero1-Lalpha (ER oxidoreductase 1-Lalpha).
Prognostic model of pulmonary adenocarcinoma by expression profiling of eight genes as determined by quantitative real-time reverse transcriptase polymerase chain reaction.
Mitsudomi et al., Nagoya, Japan. In J Clin Oncol, 2004
Next, we tried to identify a smaller number of genes of particular predictive value, and eight genes (PTK7, CIT, SCNN1A, PGES, ERO1L, ZWINT, and two ESTs) were selected.
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