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The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane.
Hartl FU, Lecker S, Schiebel E, Hendrick JP, Wickner W. Hartl FU, et al. Cell. 1990 Oct 19;63(2):269-79. doi: 10.1016/0092-8674(90)90160-g. Cell. 1990. PMID: 2170023
The export of many E. coli proteins such as proOmpA requires the cytosolic chaperone SecB and the membrane-bound preprotein translocase. Translocase is a multisubunit enzyme with the SecA protein as its peripheral membrane domain and the SecY/E protein as its integr …
The export of many E. coli proteins such as proOmpA requires the cytosolic chaperone SecB and the membrane-bound preprotein transloca …
Delta mu H+ and ATP function at different steps of the catalytic cycle of preprotein translocase.
Schiebel E, Driessen AJ, Hartl FU, Wickner W. Schiebel E, et al. Cell. 1991 Mar 8;64(5):927-39. doi: 10.1016/0092-8674(91)90317-r. Cell. 1991. PMID: 1825804
Preprotein translocation in E. coli requires ATP, the membrane electrochemical potential delta mu H+, and translocase, an enzyme with an ATPase domain (SecA) and the membrane-embedded SecY/E. ...
Preprotein translocation in E. coli requires ATP, the membrane electrochemical potential delta mu H+, and translocase, an enzyme with …
Preprotein translocase of Escherichia coli: solubilization, purification, and reconstitution of the integral membrane subunits SecY/E.
Driessen AJ, Brundage L, Hendrick JP, Schiebel E, Wickner W. Driessen AJ, et al. Methods Cell Biol. 1991;34:147-65. doi: 10.1016/s0091-679x(08)61679-9. Methods Cell Biol. 1991. PMID: 1834920 Review. No abstract available.
The purified E. coli integral membrane protein SecY/E is sufficient for reconstitution of SecA-dependent precursor protein translocation.
Brundage L, Hendrick JP, Schiebel E, Driessen AJ, Wickner W. Brundage L, et al. Cell. 1990 Aug 24;62(4):649-57. doi: 10.1016/0092-8674(90)90111-q. Cell. 1990. PMID: 2167176
We now report the isolation of the SecY/E protein, the integral membrane protein component of the E. coli preprotein translocase. ...The SecY/E protein consists of SecY, SecE, and an additional polypeptide. Antiserum against SecY immunoprecipitates all three …
We now report the isolation of the SecY/E protein, the integral membrane protein component of the E. coli preprotein transloca …
Kar1 binding to Sfi1 C-terminal regions anchors the SPB bridge to the nuclear envelope.
Seybold C, Elserafy M, Rüthnick D, Ozboyaci M, Neuner A, Flottmann B, Heilemann M, Wade RC, Schiebel E. Seybold C, et al. J Cell Biol. 2015 Jun 22;209(6):843-61. doi: 10.1083/jcb.201412050. Epub 2015 Jun 15. J Cell Biol. 2015. PMID: 26076691 Free PMC article.
Cell-Intrinsic Adaptation Arising from Chronic Ablation of a Key Rho GTPase Regulator.
Cerikan B, Shaheen R, Colo GP, Gläßer C, Hata S, Knobeloch KP, Alkuraya FS, Fässler R, Schiebel E. Cerikan B, et al. Dev Cell. 2016 Oct 10;39(1):28-43. doi: 10.1016/j.devcel.2016.08.020. Epub 2016 Sep 29. Dev Cell. 2016. PMID: 27693507
Characterization of spindle pole body duplication reveals a regulatory role for nuclear pore complexes.
Rüthnick D, Neuner A, Dietrich F, Kirrmaier D, Engel U, Knop M, Schiebel E. Rüthnick D, et al. J Cell Biol. 2017 Aug 7;216(8):2425-2442. doi: 10.1083/jcb.201612129. Epub 2017 Jun 28. J Cell Biol. 2017. PMID: 28659328 Free PMC article.
The Cdc31p-binding protein Kar1p is a component of the half bridge of the yeast spindle pole body.
Spang A, Courtney I, Grein K, Matzner M, Schiebel E. Spang A, et al. J Cell Biol. 1995 Mar;128(5):863-77. doi: 10.1083/jcb.128.5.863. J Cell Biol. 1995. PMID: 7876310 Free PMC article.
Matzner, and E. Schiebel. 1993. J. Cell Biol. 123:405-416). Using an in vitro assay we demonstrate that Cdc31p specifically interacts with a short sequence within the carboxyl terminal half of Kar1p. ...
Matzner, and E. Schiebel. 1993. J. Cell Biol. 123:405-416). Using an in vitro assay we demonstrate that Cdc31p specifically in …
Subcellular location and unique secretion of the hemolysin of Serratia marcescens.
Schiebel E, Schwarz H, Braun V. Schiebel E, et al. J Biol Chem. 1989 Sep 25;264(27):16311-20. J Biol Chem. 1989. PMID: 2674128
A nonhemolytic secretion-incompetent precursor of the hemolysin, designated ShlA*, was synthesized in a shlB deletion mutant and accumulated in the periplasmic space of E. coli. ...A number of mutants carrying 3' deletions in the shlA gene secreted truncated polypeptides, …
A nonhemolytic secretion-incompetent precursor of the hemolysin, designated ShlA*, was synthesized in a shlB deletion mutant and accumulated …
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