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157 related items for PubMed ID: 2211614

  • 1. Protein secretion in gram-negative bacteria. The extracellular metalloprotease B from Erwinia chrysanthemi contains a C-terminal secretion signal analogous to that of Escherichia coli alpha-hemolysin.
    Delepelaire P, Wandersman C.
    J Biol Chem; 1990 Oct 05; 265(28):17118-25. PubMed ID: 2211614
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  • 2. Protease secretion by Erwinia chrysanthemi: the specific secretion functions are analogous to those of Escherichia coli alpha-haemolysin.
    Létoffé S, Delepelaire P, Wandersman C.
    EMBO J; 1990 May 05; 9(5):1375-82. PubMed ID: 2184029
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  • 3. Cloning and expression in Escherichia coli of the Serratia marcescens metalloprotease gene: secretion of the protease from E. coli in the presence of the Erwinia chrysanthemi protease secretion functions.
    Létoffé S, Delepelaire P, Wandersman C.
    J Bacteriol; 1991 Apr 05; 173(7):2160-6. PubMed ID: 2007544
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  • 4. Cloning, nucleotide sequence and characterization of the gene encoding the Erwinia chrysanthemi B374 PrtA metalloprotease: a third metalloprotease secreted via a C-terminal secretion signal.
    Ghigo JM, Wandersman C.
    Mol Gen Genet; 1992 Dec 05; 236(1):135-44. PubMed ID: 1494344
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  • 8. Extracellular secretion of pectate lyase by the Erwinia chrysanthemi out pathway is dependent upon Sec-mediated export across the inner membrane.
    He SY, Schoedel C, Chatterjee AK, Collmer A.
    J Bacteriol; 1991 Jul 05; 173(14):4310-7. PubMed ID: 1829728
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  • 10. The secretion genes of Pseudomonas aeruginosa alkaline protease are functionally related to those of Erwinia chrysanthemi proteases and Escherichia coli alpha-haemolysin.
    Guzzo J, Duong F, Wandersman C, Murgier M, Lazdunski A.
    Mol Microbiol; 1991 Feb 05; 5(2):447-53. PubMed ID: 1904127
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  • 11. Cloning of genes encoding extracellular metalloproteases from Erwinia chrysanthemi EC16.
    Dahler GS, Barras F, Keen NT.
    J Bacteriol; 1990 Oct 05; 172(10):5803-15. PubMed ID: 2211513
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  • 12. Secretion of the Serratia marcescens HasA protein by an ABC transporter.
    Létoffé S, Ghigo JM, Wandersman C.
    J Bacteriol; 1994 Sep 05; 176(17):5372-7. PubMed ID: 8071214
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  • 13. Analysis of eight out genes in a cluster required for pectic enzyme secretion by Erwinia chrysanthemi: sequence comparison with secretion genes from other gram-negative bacteria.
    Lindeberg M, Collmer A.
    J Bacteriol; 1992 Nov 05; 174(22):7385-97. PubMed ID: 1429461
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  • 14. Characterization of a protein inhibitor of extracellular proteases produced by Erwinia chrysanthemi.
    Létoffé S, Delepelaire P, Wandersman C.
    Mol Microbiol; 1989 Jan 05; 3(1):79-86. PubMed ID: 2654540
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  • 15. Identification of two components of the Serratia marcescens metalloprotease transporter: protease SM secretion in Escherichia coli is TolC dependent.
    Létoffé S, Ghigo JM, Wandersman C.
    J Bacteriol; 1993 Nov 05; 175(22):7321-8. PubMed ID: 8226679
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  • 16. Molecular characterization of a protease secreted by Erwinia amylovora.
    Zhang Y, Bak DD, Heid H, Geider K.
    J Mol Biol; 1999 Jun 25; 289(5):1239-51. PubMed ID: 10373365
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  • 17. Production of active Serratia marcescens metalloprotease from Escherichia coli by alpha-hemolysin HlyB and HlyD.
    Suh Y, Benedik MJ.
    J Bacteriol; 1992 Apr 25; 174(7):2361-6. PubMed ID: 1551853
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  • 18. Functional complementation between bacterial MDR-like export systems: colicin V, alpha-hemolysin, and Erwinia protease.
    Fath MJ, Skvirsky RC, Kolter R.
    J Bacteriol; 1991 Dec 25; 173(23):7549-56. PubMed ID: 1938950
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  • 19. 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 25; 5(10):2557-68. PubMed ID: 1791766
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  • 20. A carboxyl-terminal four-amino acid motif is required for secretion of the metalloprotease PrtG through the Erwinia chrysanthemi protease secretion pathway.
    Ghigo JM, Wandersman C.
    J Biol Chem; 1994 Mar 25; 269(12):8979-85. PubMed ID: 8132636
    [Abstract] [Full Text] [Related]

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