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171 related items for PubMed ID: 8842146
1. Mini-TnhlyAs: a new tool for the construction of secreted fusion proteins. Gentschev I, Maier G, Kranig A, Goebel W. Mol Gen Genet; 1996 Sep 13; 252(3):266-74. PubMed ID: 8842146 [Abstract] [Full Text] [Related]
2. Construction of chromosomally encoded secreted hemolysin fusion proteins by use of mini-TnhlyAs transposon. Spreng S, Gentschev I. FEMS Microbiol Lett; 1998 Aug 01; 165(1):187-92. PubMed ID: 9711856 [Abstract] [Full Text] [Related]
3. Topological and functional studies on HlyB of Escherichia coli. Gentschev I, Goebel W. Mol Gen Genet; 1992 Mar 01; 232(1):40-8. PubMed ID: 1552901 [Abstract] [Full Text] [Related]
5. Analysis of the haemolysin transport process through the secretion from Escherichia coli of PCM, CAT or beta-galactosidase fused to the Hly C-terminal signal domain. Kenny B, Haigh R, Holland IB. Mol Microbiol; 1991 Oct 01; 5(10):2557-68. PubMed ID: 1791766 [Abstract] [Full Text] [Related]
6. Processing by OmpT of fusion proteins carrying the HlyA transport signal during secretion by the Escherichia coli hemolysin transport system. Hanke C, Hess J, Schumacher G, Goebel W. Mol Gen Genet; 1992 May 01; 233(1-2):42-8. PubMed ID: 1603076 [Abstract] [Full Text] [Related]
7. Analysis of the haemolysin secretion system by PhoA-HlyA fusion proteins. Hess J, Gentschev I, Goebel W, Jarchau T. Mol Gen Genet; 1990 Nov 01; 224(2):201-8. PubMed ID: 2277639 [Abstract] [Full Text] [Related]
8. A topological model for the haemolysin translocator protein HlyD. Schülein R, Gentschev I, Mollenkopf HJ, Goebel W. Mol Gen Genet; 1992 Jul 01; 234(1):155-63. PubMed ID: 1495479 [Abstract] [Full Text] [Related]
9. The Tsr chemosensory transducer of Escherichia coli assembles into the cytoplasmic membrane via a SecA-dependent process. Gebert JF, Overhoff B, Manson MD, Boos W. J Biol Chem; 1988 Nov 15; 263(32):16652-60. PubMed ID: 2846545 [Abstract] [Full Text] [Related]
10. Analysis of protein localization by use of gene fusions with complementary properties. Manoil C. J Bacteriol; 1990 Feb 15; 172(2):1035-42. PubMed ID: 2153653 [Abstract] [Full Text] [Related]
11. Improved secretory production of recombinant proteins by random mutagenesis of hlyB, an alpha-hemolysin transporter from Escherichia coli. Sugamata Y, Shiba T. Appl Environ Microbiol; 2005 Feb 15; 71(2):656-62. PubMed ID: 15691914 [Abstract] [Full Text] [Related]
12. A heterologous membrane protein domain fused to the C-terminal ATP-binding domain of HlyB can export Escherichia coli hemolysin. Thomas WD, Wagner SP, Welch RA. J Bacteriol; 1992 Nov 15; 174(21):6771-9. PubMed ID: 1400227 [Abstract] [Full Text] [Related]
13. Alkaline phosphatase which lacks its own signal sequence becomes enzymatically active when fused to N-terminal sequences of Escherichia coli haemolysin (HlyA). Erb K, Vogel M, Wagner W, Goebel W. Mol Gen Genet; 1987 Jun 15; 208(1-2):88-93. PubMed ID: 3302615 [Abstract] [Full Text] [Related]
14. Conversion of bacterial gene products to secretion-competent fusion proteins. Mollenkopf HJ, Gentschev I, Goebel W. Biotechniques; 1996 Nov 15; 21(5):854, 856-60. PubMed ID: 8922626 [Abstract] [Full Text] [Related]
15. Construction of an alkaline phosphatase fusion-generating transposon, mTn10phoA. McClain MS, Engleberg NC. Gene; 1996 Apr 17; 170(1):147-8. PubMed ID: 8621078 [Abstract] [Full Text] [Related]
17. Study of regulation and transport of hemolysin by using fusion of the beta-galactosidase gene (lacZ) to hemolysin genes. Juarez A, Härtlein M, Goebel W. J Bacteriol; 1984 Oct 17; 160(1):161-8. PubMed ID: 6434518 [Abstract] [Full Text] [Related]
18. PhoA gene fusions in Legionella pneumophila generated in vivo using a new transposon, MudphoA. Albano MA, Arroyo J, Eisenstein BI, Engleberg NC. Mol Microbiol; 1992 Jul 17; 6(13):1829-39. PubMed ID: 1321325 [Abstract] [Full Text] [Related]
19. Use of phoA and lacZ fusions to study the membrane topology of ProW, a component of the osmoregulated ProU transport system of Escherichia coli. Haardt M, Bremer E. J Bacteriol; 1996 Sep 17; 178(18):5370-81. PubMed ID: 8808924 [Abstract] [Full Text] [Related]