ERO1L
ERO1L (ERO1-like protein alpha) هوَ بروتين يُشَفر بواسطة جين ERO1L في الإنسان.[1][2]
المراجع
- "ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum"، J Biol Chem، 275 (7): 4827–33، مارس 2000، doi:10.1074/jbc.275.7.4827، PMID 10671517.
- "Entrez Gene: ERO1L ERO1-like (S. cerevisiae)"، مؤرشف من الأصل في 05 ديسمبر 2010.
قراءة متعمقة
- "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، 2000، doi:10.1074/jbc.M003061200، PMID 10818100.
- "The CXXCXXC motif determines the folding, structure and stability of human Ero1-Lalpha."، EMBO J.، 19 (17): 4493–502، 2000، doi:10.1093/emboj/19.17.4493، PMC 302061، PMID 10970843.
- "The C-terminal domain of yeast Ero1p mediates membrane localization and is essential for function."، FEBS Lett.، 508 (1): 117–20، 2001، doi:10.1016/S0014-5793(01)03034-4، PMID 11707280.
- "Manipulation of oxidative protein folding and PDI redox state in mammalian cells."، EMBO J.، 20 (22): 6288–96، 2002، doi:10.1093/emboj/20.22.6288، PMC 125306، PMID 11707400.
- "ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family."، EMBO J.، 21 (4): 835–44، 2002، doi:10.1093/emboj/21.4.835، PMC 125352، PMID 11847130.
- "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، 2002، doi:10.1083/jcb.200207120، PMC 2173060، PMID 12403808.
- "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، 2003، Bibcode:2002PNAS...9916899M، doi:10.1073/pnas.242603899، PMC 139241، PMID 12477932.
- "The cellular oxygen tension regulates expression of the endoplasmic oxidoreductase ERO1-Lalpha."، Eur. J. Biochem.، 270 (10): 2228–35، 2003، doi:10.1046/j.1432-1033.2003.03590.x، PMID 12752442.
- "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، 2003، doi:10.1101/gr.1293003، PMC 403697، PMID 12975309.
- "Thiol-mediated protein retention in the endoplasmic reticulum: the role of ERp44."، EMBO J.، 22 (19): 5015–22، 2003، doi:10.1093/emboj/cdg491، PMC 204474، PMID 14517240.
- "Two conserved cysteine triads in human Ero1alpha cooperate for efficient disulfide bond formation in the endoplasmic reticulum."، J. Biol. Chem.، 279 (29): 30047–52، 2004، doi:10.1074/jbc.M403192200، PMID 15136577.
- "Glutathione limits Ero1-dependent oxidation in the endoplasmic reticulum."، J. Biol. Chem.، 279 (31): 32667–73، 2004، doi:10.1074/jbc.M404992200، PMID 15161913.
- "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، 2005، doi:10.1074/jbc.M408651200، PMID 15475357.
- "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."، Genome Res.، 14 (10B): 2121–7، 2004، doi:10.1101/gr.2596504، PMC 528928، PMID 15489334.
- "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، 2005، doi:10.1038/sj.onc.1208325، PMID 15592500.
- "Dynamic retention of Ero1alpha and Ero1beta in the endoplasmic reticulum by interactions with PDI and ERp44."، Antioxid. Redox Signal.، 8 (3–4): 274–82، 2006، doi:10.1089/ars.2006.8.274، PMID 16677073.
بوابة الكيمياء الحيوية
بوابة علم الأحياء الخلوي والجزيئي
بوابة طب
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