ERO1L

ERO1-like (S. cerevisiae)
Identifiers
Symbols	ERO1L ; ERO1-alpha
External IDs	Template:MGI HomoloGene: 49392
Gene ontology Molecular function Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Biological process Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

ERO1-like (S. cerevisiae), also known as ERO1L, is a human gene.

Further reading

• Cabibbo A, Pagani M, Fabbri M; et al. (2000). "ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum". J. Biol. Chem. 275 (7): 4827–33. PMID 10671517.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Pagani M, Fabbri M, Benedetti C; et al. (2000). "Endoplasmic reticulum oxidoreductin 1-lbeta (ERO1-Lbeta), a human gene induced in the course of the unfolded protein response". J. Biol. Chem. 275 (31): 23685–92. doi:10.1074/jbc.M003061200. PMID 10818100.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Benham AM, Cabibbo A, Fassio A; et al. (2000). "The CXXCXXC motif determines the folding, structure and stability of human Ero1-Lalpha". EMBO J. 19 (17): 4493–502. doi:10.1093/emboj/19.17.4493. PMID 10970843.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Pagani M, Pilati S, Bertoli G; et al. (2001). "The C-terminal domain of yeast Ero1p mediates membrane localization and is essential for function". FEBS Lett. 508 (1): 117–20. PMID 11707280.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Mezghrani A, Fassio A, Benham A; et al. (2002). "Manipulation of oxidative protein folding and PDI redox state in mammalian cells". EMBO J. 20 (22): 6288–96. doi:10.1093/emboj/20.22.6288. PMID 11707400.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Anelli T, Alessio M, Mezghrani A; et al. (2002). "ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family". EMBO J. 21 (4): 835–44. doi:10.1093/emboj/21.4.835. PMID 11847130.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Tsai B, Rapoport TA (2002). "Unfolded cholera toxin is transferred to the ER membrane and released from protein disulfide isomerase upon oxidation by Ero1". J. Cell Biol. 159 (2): 207–16. doi:10.1083/jcb.200207120. PMID 12403808.
• Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Gess B, Hofbauer KH, Wenger RH; et al. (2003). "The cellular oxygen tension regulates expression of the endoplasmic oxidoreductase ERO1-Lalpha". Eur. J. Biochem. 270 (10): 2228–35. PMID 12752442.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Clark HF, Gurney AL, Abaya E; et al. (2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMID 12975309.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Anelli T, Alessio M, Bachi A; et al. (2003). "Thiol-mediated protein retention in the endoplasmic reticulum: the role of ERp44". EMBO J. 22 (19): 5015–22. doi:10.1093/emboj/cdg491. PMID 14517240.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Bertoli G, Simmen T, Anelli T; et al. (2004). "Two conserved cysteine triads in human Ero1alpha cooperate for efficient disulfide bond formation in the endoplasmic reticulum". J. Biol. Chem. 279 (29): 30047–52. doi:10.1074/jbc.M403192200. PMID 15136577.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Molteni SN, Fassio A, Ciriolo MR; et al. (2004). "Glutathione limits Ero1-dependent oxidation in the endoplasmic reticulum". J. Biol. Chem. 279 (31): 32667–73. doi:10.1074/jbc.M404992200. PMID 15161913.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• van Lith M, Hartigan N, Hatch J, Benham AM (2005). "PDILT, a divergent testis-specific protein disulfide isomerase with a non-classical SXXC motif that engages in disulfide-dependent interactions in the endoplasmic reticulum". J. Biol. Chem. 280 (2): 1376–83. doi:10.1074/jbc.M408651200. PMID 15475357.CS1 maint: Multiple names: authors list (link)
• Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• May D, Itin A, Gal O; et al. (2005). "Ero1-L alpha plays a key role in a HIF-1-mediated pathway to improve disulfide bond formation and VEGF secretion under hypoxia: implication for cancer". Oncogene. 24 (6): 1011–20. doi:10.1038/sj.onc.1208325. PMID 15592500.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Otsu M, Bertoli G, Fagioli C; et al. (2006). "Dynamic retention of Ero1alpha and Ero1beta in the endoplasmic reticulum by interactions with PDI and ERp44". Antioxid. Redox Signal. 8 (3–4): 274–82. doi:10.1089/ars.2006.8.274. PMID 16677073.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)