SEC72/YLR292C Literature Guide Help

Other names published for SEC72: SEC67, SIM2, YLR292C

SEC72 - Primary Literature (17)

ReferenceOther Genes Addressed
Ast T, et al.  (2013) A network of cytosolic factors targets SRP-independent proteins to the endoplasmic reticulum. Cell 152(5):1134-45
Wu MJ, et al.  (2012) Delineation of the molecular mechanism for disulfide stress-induced aluminium toxicity. Biometals 25(3):553-61
Arias P, et al.  (2011) Genome-wide survey of yeast mutations leading to activation of the yeast cell integrity MAPK pathway: Novel insights into diverse MAPK outcomes. BMC Genomics 12(1):390
Harada Y, et al.  (2011) Structural Studies and the Assembly of the Heptameric Post-translational Translocon Complex. J Biol Chem 286(4):2956-65
Schlegel T, et al.  (2007) The tetratricopeptide repeats of receptors involved in protein translocation across membranes. Mol Biol Evol 24(12):2763-74
Breinig F, et al.  (2006) Dissecting toxin immunity in virus-infected killer yeast uncovers an intrinsic strategy of self-protection. Proc Natl Acad Sci U S A 103(10):3810-5
Willer M, et al.  (2003) Identification of novel protein-protein interactions at the cytosolic surface of the Sec63 complex in the yeast ER membrane. Yeast 20(2):133-48
Morrow MW and Brodsky JL  (2001) Yeast ribosomes bind to highly purified reconstituted Sec61p complex and to mammalian p180. Traffic 2(10):705-16
Young BP, et al.  (2001) Sec63p and Kar2p are required for the translocation of SRP-dependent precursors into the yeast endoplasmic reticulum in vivo. EMBO J 20(1-2):262-71
Romisch K  (1999) Surfing the Sec61 channel: bidirectional protein translocation across the ER membrane. J Cell Sci 112 ( Pt 23)():4185-91
Lyman SK and Schekman R  (1997) Binding of secretory precursor polypeptides to a translocon subcomplex is regulated by BiP. Cell 88(1):85-96
Matlack KE, et al.  (1997) Protein transport by purified yeast Sec complex and Kar2p without membranes. Science 277(5328):938-41
Dahmann C, et al.  (1995) S-phase-promoting cyclin-dependent kinases prevent re-replication by inhibiting the transition of replication origins to a pre-replicative state. Curr Biol 5(11):1257-69
Panzner S, et al.  (1995) Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p. Cell 81(4):561-70
Fang H and Green N  (1994) Nonlethal sec71-1 and sec72-1 mutations eliminate proteins associated with the Sec63p-BiP complex from S. cerevisiae. Mol Biol Cell 5(9):933-42
Feldheim D and Schekman R  (1994) Sec72p contributes to the selective recognition of signal peptides by the secretory polypeptide translocation complex. J Cell Biol 126(4):935-43
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