ER-resident protein
From Proteopedia
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*'''ERp27''' functions a a disulphide isomerase<ref>PMID:16940051</ref>. | *'''ERp27''' functions a a disulphide isomerase<ref>PMID:16940051</ref>. | ||
*'''ERp29''' facilitates processing and transport of proteins in the early secretary pathway<ref>PMID:20920593</ref>. | *'''ERp29''' facilitates processing and transport of proteins in the early secretary pathway<ref>PMID:20920593</ref>. | ||
| + | *'''ERp44''' may be involved in the control of oxidative protein folding<ref>PMID:11847130</ref>. | ||
For details on ERdj5 see [[Molecular Playground/ERDj5]]. | For details on ERdj5 see [[Molecular Playground/ERDj5]]. | ||
Revision as of 08:19, 19 June 2024
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3D Structures of ER-resident protein
Updated on 19-June-2024
References
- ↑ Hagiwara M, Maegawa K, Suzuki M, Ushioda R, Araki K, Matsumoto Y, Hoseki J, Nagata K, Inaba K. Structural basis of an ERAD pathway mediated by the ER-resident protein disulfide reductase ERdj5. Mol Cell. 2011 Feb 18;41(4):432-44. PMID:21329881 doi:10.1016/j.molcel.2011.01.021
- ↑ Oka OB, van Lith M, Rudolf J, Tungkum W, Pringle MA, Bulleid NJ. ERp18 regulates activation of ATF6α during unfolded protein response. EMBO J. 2019 Aug 1;38(15):e100990. PMID:31368601 doi:10.15252/embj.2018100990
- ↑ Alanen HI, Williamson RA, Howard MJ, Hatahet FS, Salo KE, Kauppila A, Kellokumpu S, Ruddock LW. ERp27, a new non-catalytic endoplasmic reticulum-located human protein disulfide isomerase family member, interacts with ERp57. J Biol Chem. 2006 Nov 3;281(44):33727-38. PMID:16940051 doi:10.1074/jbc.M604314200
- ↑ Zhang D, Richardson DR. Endoplasmic reticulum protein 29 (ERp29): An emerging role in cancer. Int J Biochem Cell Biol. 2011 Jan;43(1):33-6. PMID:20920593 doi:10.1016/j.biocel.2010.09.019
- ↑ Anelli T, Alessio M, Mezghrani A, Simmen T, Talamo F, Bachi A, Sitia R. ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family. EMBO J. 2002 Feb 15;21(4):835-44. PMID:11847130 doi:http://dx.doi.org/10.1093/emboj/21.4.835
