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Differential expression of mal genes under cAMP and endogenous inducer control in nutrient-stressed Escherichia coli.
Notley L, Ferenci T. Notley L, et al. Among authors: ferenci t. Mol Microbiol. 1995 Apr;16(1):121-9. doi: 10.1111/j.1365-2958.1995.tb02397.x. Mol Microbiol. 1995. PMID: 7651130
Genetic mapping of starch- and lambda-receptor sites in maltoporin: identification of substitutions causing direct and indirect effects on binding sites by cysteine mutagenesis.
Francis G, Brennan L, Stretton S, Ferenci T. Francis G, et al. Among authors: ferenci t. Mol Microbiol. 1991 Sep;5(9):2293-301. doi: 10.1111/j.1365-2958.1991.tb02160.x. Mol Microbiol. 1991. PMID: 1722561
Affinity-chromatographic purification of sixteen cysteine-substituted maltoporin variants: thiol reactivity and cross-linking in an outer membrane protein of Escherichia coli.
Francis G, Brennan L, Ferenci T. Francis G, et al. Among authors: ferenci t. Biochim Biophys Acta. 1991 Aug 5;1067(1):89-96. doi: 10.1016/0005-2736(91)90029-8. Biochim Biophys Acta. 1991. PMID: 1868106
Channel architecture in maltoporin: dominance studies with lamB mutations influencing maltodextrin binding provide evidence for independent selectivity filters in each subunit.
Ferenci T, Lee KS. Ferenci T, et al. J Bacteriol. 1989 Feb;171(2):855-61. doi: 10.1128/jb.171.2.855-861.1989. J Bacteriol. 1989. PMID: 2521623 Free PMC article.
Cysteine-22 and cysteine-38 are not essential for the functions of maltoporin (LamB protein).
Ferenci T, Stretton S. Ferenci T, et al. FEMS Microbiol Lett. 1989 Oct 15;52(3):335-9. doi: 10.1016/0378-1097(89)90221-8. FEMS Microbiol Lett. 1989. PMID: 2693195
Genetic analysis of sequences in maltoporin that contribute to binding domains and pore structure.
Heine HG, Francis G, Lee KS, Ferenci T. Heine HG, et al. Among authors: ferenci t. J Bacteriol. 1988 Apr;170(4):1730-8. doi: 10.1128/jb.170.4.1730-1738.1988. J Bacteriol. 1988. PMID: 2832377 Free PMC article.
Maltose transport and starch binding in phage-resistant point mutants of maltoporin. Functional and topological implications.
Charbit A, Gehring K, Nikaido H, Ferenci T, Hofnung M. Charbit A, et al. Among authors: ferenci t. J Mol Biol. 1988 Jun 5;201(3):487-96. doi: 10.1016/0022-2836(88)90630-4. J Mol Biol. 1988. PMID: 2971116
Isolation, by affinity chromatography, of mutant escherichia coli cells with novel regulation of lamB expression.
Ferenci T, Lee KS. Ferenci T, et al. J Bacteriol. 1983 May;154(2):984-7. doi: 10.1128/JB.154.2.984-987.1983. J Bacteriol. 1983. PMID: 6302087 Free PMC article.
Epitope mapping by cysteine mutagenesis: identification of residues involved in recognition by three monoclonal antibodies directed against LamB glycoporin in the outer membrane of Escherichia coli.
Notley L, Hillier C, Ferenci T. Notley L, et al. Among authors: ferenci t. FEMS Microbiol Lett. 1994 Jul 15;120(3):341-8. doi: 10.1111/j.1574-6968.1994.tb07056.x. FEMS Microbiol Lett. 1994. PMID: 7521310
Sequence alignment and structural modelling of the LamB glycoporin family.
Lång H, Ferenci T. Lång H, et al. Among authors: ferenci t. Biochem Biophys Res Commun. 1995 Mar 28;208(3):927-34. doi: 10.1006/bbrc.1995.1423. Biochem Biophys Res Commun. 1995. PMID: 7702622
The aligned amino acid sequences permitted derivation of a model of LamB folding across the bacterial outer membrane using an approach successfully applied in the identification of structural features in other porins (Ferenci,T. (1994) Mol. ...
The aligned amino acid sequences permitted derivation of a model of LamB folding across the bacterial outer membrane using an approach succe …
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