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Bacteriophage lambda surface display of a bacterial biotin acceptor domain reveals the minimal peptide size required for biotinylation.
Stolz J, Ludwig A, Sauer N. Stolz J, et al. FEBS Lett. 1998 Nov 27;440(1-2):213-7. doi: 10.1016/s0014-5793(98)01454-9. FEBS Lett. 1998. PMID: 9862457
Phages with a functional biotinylation domain were identified after affinity purification with immobilised avidin. All biotinylated phages isolated this way were found to have a sequence of 66 amino acids from the parental protein in common. ...The data present the …
Phages with a functional biotinylation domain were identified after affinity purification with immobilised avidin. All biotinylated p …
Analysis of the in vivo activation of hemolysin (HlyA) from Escherichia coli.
Ludwig A, Garcia F, Bauer S, Jarchau T, Benz R, Hoppe J, Goebel W. Ludwig A, et al. J Bacteriol. 1996 Sep;178(18):5422-30. doi: 10.1128/jb.178.18.5422-5430.1996. J Bacteriol. 1996. PMID: 8808931 Free PMC article.
The migration distance indicated a net loss of two positive charges in HlyA as a result of the HlyC-mediated activation (modification). ...Single modifications in mutant and truncated HlyA derivatives suggested that both lysine residues are independently fatty acid …
The migration distance indicated a net loss of two positive charges in HlyA as a result of the HlyC-mediated activation (modif …
Release of latent ClyA cytolysin from Escherichia coli mediated by a bacteriophage-associated putative holin (BlyA) from Borrelia burgdorferi.
Ludwig A, von Rhein C, Mischke A, Brade V. Ludwig A, et al. Int J Med Microbiol. 2008 Jul;298(5-6):473-81. doi: 10.1016/j.ijmm.2007.07.014. Epub 2007 Sep 25. Int J Med Microbiol. 2008. PMID: 17897882
Introduction of the Borrelia burgdorferi blyAB locus into Escherichia coli has recently been reported to cause a hemolytic phenotype that is dependent on the E. coli clyA (hlyE, sheA) gene (a cytolysin gene present in many E. coli strains, including E. coli K-12, wh …
Introduction of the Borrelia burgdorferi blyAB locus into Escherichia coli has recently been reported to cause a hemolytic phenotype …
The deletion of several amino acid stretches of Escherichia coli alpha-hemolysin (HlyA) suggests that the channel-forming domain contains beta-strands.
Benz R, Maier E, Bauer S, Ludwig A. Benz R, et al. PLoS One. 2014 Dec 2;9(12):e112248. doi: 10.1371/journal.pone.0112248. eCollection 2014. PLoS One. 2014. PMID: 25463653 Free PMC article.
Escherichia coli α-hemolysin (HlyA) is a pore-forming protein of 110 kDa belonging to the family of RTX toxins. A hydrophobic region between the amino acid residues 238 and 410 in the N-terminal half of HlyA has previously been suggested to form hydrophobic and/or a …
Escherichia coli α-hemolysin (HlyA) is a pore-forming protein of 110 kDa belonging to the family of RTX toxins. A hydrophobic …
Mutations affecting export and activity of cytolysin A from Escherichia coli.
Ludwig A, Völkerink G, von Rhein C, Bauer S, Maier E, Bergmann B, Goebel W, Benz R. Ludwig A, et al. J Bacteriol. 2010 Aug;192(15):4001-11. doi: 10.1128/JB.01283-09. Epub 2010 May 28. J Bacteriol. 2010. PMID: 20511497 Free PMC article.
Cytolysin A (known as ClyA, HlyE, and SheA) is a cytolytic pore-forming protein toxin found in several Escherichia coli and Salmonella enterica strains. ...The latter regions thus apparently promote membrane interaction without being directly required for pore forma …
Cytolysin A (known as ClyA, HlyE, and SheA) is a cytolytic pore-forming protein toxin found in several Escherichia coli and Sa …
Occurrence and characteristics of the cytolysin A gene in Shigella strains and other members of the family Enterobacteriaceae.
von Rhein C, Bauer S, Simon V, Ludwig A. von Rhein C, et al. FEMS Microbiol Lett. 2008 Oct;287(2):143-8. doi: 10.1111/j.1574-6968.2008.01290.x. Epub 2008 Aug 27. FEMS Microbiol Lett. 2008. PMID: 18754791
Cytolysin A (ClyA, HlyE, SheA) is a hemolytic pore-forming toxin found in Escherichia coli and Salmonella enterica serovars Typhi and Paratyphi A. ...According to these data, ClyA may play a role only for a rather small subset of the enteric bac …
Cytolysin A (ClyA, HlyE, SheA) is a hemolytic pore-forming toxin found in Escherichia coli and Salmonella enterica serovars Ty …
Differential regulation of multiple proteins of Escherichia coli and Salmonella enterica serovar Typhimurium by the transcriptional regulator SlyA.
Spory A, Bosserhoff A, von Rhein C, Goebel W, Ludwig A. Spory A, et al. J Bacteriol. 2002 Jul;184(13):3549-59. doi: 10.1128/jb.184.13.3549-3559.2002. J Bacteriol. 2002. PMID: 12057949 Free PMC article.
SlyA is a transcriptional regulator of Escherichia coli, Salmonella enterica, and other bacteria belonging to the ENTEROBACTERIACEAE: The SlyA protein has been shown to be involved in the virulence of S. enterica serovar Typhimurium, but its role in E. coli is unclear. ... …
SlyA is a transcriptional regulator of Escherichia coli, Salmonella enterica, and other bacteria belonging to the ENTEROBACTERIACEAE: …
Molecular analysis of cytolysin A (ClyA) in pathogenic Escherichia coli strains.
Ludwig A, von Rhein C, Bauer S, Hüttinger C, Goebel W. Ludwig A, et al. J Bacteriol. 2004 Aug;186(16):5311-20. doi: 10.1128/JB.186.16.5311-5320.2004. J Bacteriol. 2004. PMID: 15292132 Free PMC article.
Cytolysin A (ClyA) of Escherichia coli is a pore-forming hemolytic protein encoded by the clyA (hlyE, sheA) gene that was first identified in E. coli K-12. ...The presented data indicate that cytolysin A can play a role only for some of the pathogenic …
Cytolysin A (ClyA) of Escherichia coli is a pore-forming hemolytic protein encoded by the clyA (hlyE, sheA) gene that was firs …
Escherichia coli alpha-hemolysin (HlyA) is heterogeneously acylated in vivo with 14-, 15-, and 17-carbon fatty acids.
Lim KB, Walker CR, Guo L, Pellett S, Shabanowitz J, Hunt DF, Hewlett EL, Ludwig A, Goebel W, Welch RA, Hackett M. Lim KB, et al. J Biol Chem. 2000 Nov 24;275(47):36698-702. doi: 10.1074/jbc.C000544200. J Biol Chem. 2000. PMID: 10978310
alpha-Hemolysin (HlyA) is a secreted protein virulence factor observed in certain uropathogenic strains of Escherichia coli. ...Thus, HlyA activated in vivo consists of a heterogeneous family of up to nine different covalent structures, and the substrate specificity …
alpha-Hemolysin (HlyA) is a secreted protein virulence factor observed in certain uropathogenic strains of Escherichia coli. ...Thus, …
Mutations affecting activity and transport of haemolysin in Escherichia coli.
Ludwig A, Vogel M, Goebel W. Ludwig A, et al. Mol Gen Genet. 1987 Feb;206(2):238-45. doi: 10.1007/BF00333579. Mol Gen Genet. 1987. PMID: 3295483
Complementation with recombinant plasmids carrying one of the four hly genes (C, A, B or D) allowed localization of the hly(ts) mutations. A ts mutation in hlyC leads to a pro----leu exchange in amino acid position 53 of HlyC. Two ts mutations in HlyA were fo …
Complementation with recombinant plasmids carrying one of the four hly genes (C, A, B or D) allowed localization of the hly(ts) mutat …
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