ERO1L

ERO1L

ERO1-like (S. cerevisiae), also known as ERO1L, is a human gene.cite web | title = Entrez Gene: ERO1L ERO1-like (S. cerevisiae)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=30001| accessdate = ]

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References

Further reading

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

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