Primary Literature
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- Yi JK, et al. (2021) Rapid inactivation of the yeast Sec complex selectively blocks transport of post-translationally translocated proteins. J Biol Chem 297(4):101171 PMID: 34492269
- Wu X, et al. (2019) Structure of the post-translational protein translocation machinery of the ER membrane. Nature 566(7742):136-139 PMID: 30644436
- Jung SJ, et al. (2014) The Sec62-Sec63 translocon facilitates translocation of the C-terminus of membrane proteins. J Cell Sci 127(Pt 19):4270-8 PMID: 25097231
- Harada Y, et al. (2011) Structural studies and the assembly of the heptameric post-translational translocon complex. J Biol Chem 286(4):2956-65 PMID: 20826819
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- Wittke S, et al. (2000) Sec62p, a component of the endoplasmic reticulum protein translocation machinery, contains multiple binding sites for the Sec-complex. Mol Biol Cell 11(11):3859-71 PMID: 11071912
- Lyman SK and Schekman R (1997) Binding of secretory precursor polypeptides to a translocon subcomplex is regulated by BiP. Cell 88(1):85-96 PMID: 9019409
- Brodsky JL and Schekman R (1993) A Sec63p-BiP complex from yeast is required for protein translocation in a reconstituted proteoliposome. J Cell Biol 123(6 Pt 1):1355-63 PMID: 8253836
- Deshaies RJ, et al. (1991) Assembly of yeast Sec proteins involved in translocation into the endoplasmic reticulum into a membrane-bound multisubunit complex. Nature 349(6312):806-8 PMID: 2000150