Characterization of effector proteins translocated via the SPI1 type III secretion system of Salmonella typhimurium.
暂无分享,去创建一个
[1] N. Moran,et al. Genes Lost and Genes Found: Evolution of Bacterial Pathogenesis and Symbiosis , 2001, Science.
[2] E. McGhie,et al. Cooperation between actin‐binding proteins of invasive Salmonella: SipA potentiates SipC nucleation and bundling of actin , 2001, The EMBO journal.
[3] K. Darwin,et al. Type III secretion chaperone‐dependent regulation: activation of virulence genes by SicA and InvF in Salmonella typhimurium , 2001, The EMBO journal.
[4] W. Hardt,et al. Salmonella Host Cell Invasion Emerged by Acquisition of a Mosaic of Separate Genetic Elements, IncludingSalmonella Pathogenicity Island 1 (SPI1), SPI5, and sopE2 , 2001, Journal of bacteriology.
[5] P. Majerus,et al. Overexpression of the inositol phosphatase SopB in human 293 cells stimulates cellular chloride influx and inhibits nuclear mRNA export. , 2001, Proceedings of the National Academy of Sciences of the United States of America.
[6] L. Hernandez,et al. A Salmonella inositol polyphosphatase acts in conjunction with other bacterial effectors to promote host cell actin cytoskeleton rearrangements and bacterial internalization , 2001, Molecular microbiology.
[7] L. Bossi,et al. Variable assortment of prophages provides a transferable repertoire of pathogenic determinants in Salmonella , 2001, Molecular microbiology.
[8] W. Rabsch,et al. Prevalence and polymorphism of genes encoding translocated effector proteins among clinical isolates of Salmonella enterica. , 2000, International journal of medical microbiology : IJMM.
[9] R. Rosqvist,et al. The secreted effector protein of Salmonella dublin, SopA, is translocated into eukaryotic cells and influences the induction of enteritis , 2000, Cellular microbiology.
[10] J. Galán,et al. Striking a balance: modulation of the actin cytoskeleton by Salmonella. , 2000, Proceedings of the National Academy of Sciences of the United States of America.
[11] S. Miller,et al. A conserved amino acid sequence directing intracellular type III secretion by Salmonella typhimurium. , 2000, Proceedings of the National Academy of Sciences of the United States of America.
[12] W. Hardt,et al. Identification of SopE2 from Salmonella typhimurium, a conserved guanine nucleotide exchange factor for Cdc42 of the host cell , 2000, Molecular microbiology.
[13] T S Wallis,et al. Molecular basis of Salmonella‐induced enteritis , 2000, Molecular microbiology.
[14] A. Hall,et al. Rho GTPases and their effector proteins. , 2000, The Biochemical journal.
[15] V. Singh,et al. Identification of SopE2, a SalmonellaSecreted Protein Which Is Highly Homologous to SopE and Involved in Bacterial Invasion of Epithelial Cells , 2000, Journal of bacteriology.
[16] Samuel I. Miller,et al. Identification of a Putative Salmonella enterica Serotype Typhimurium Host Range Factor with Homology to IpaH and YopM by Signature-Tagged Mutagenesis , 1999, Infection and Immunity.
[17] S. Miller,et al. Salmonella typhimurium leucine‐rich repeat proteins are targeted to the SPI1 and SPI2 type III secretion systems , 1999, Molecular microbiology.
[18] J. Galán,et al. A Salmonella protein antagonizes Rac-1 and Cdc42 to mediate host-cell recovery after bacterial invasion , 1999, Nature.
[19] R. Hayward,et al. Direct nucleation and bundling of actin by the SipC protein of invasive Salmonella , 1999, The EMBO journal.
[20] J. Galán,et al. An invasion-associated Salmonella protein modulates the actin-bundling activity of plastin. , 1999, Proceedings of the National Academy of Sciences of the United States of America.
[21] W. Rabsch,et al. Isolation of a temperate bacteriophage encoding the type III effector protein SopE from an epidemic Salmonella typhimurium strain. , 1999, Proceedings of the National Academy of Sciences of the United States of America.
[22] J. Galán,et al. Type III Secretion Machines: Bacterial Devices for Protein Delivery into Host Cells , 1999 .
[23] J. Galán,et al. Role of the S. typhimurium actin-binding protein SipA in bacterial internalization. , 1999, Science.
[24] S Falkow,et al. The Salmonella invasin SipB induces macrophage apoptosis by binding to caspase-1. , 1999, Proceedings of the National Academy of Sciences of the United States of America.
[25] J. Galán,et al. Interaction of Salmonella with host cells through the centisome 63 type III secretion system. , 1999, Current opinion in microbiology.
[26] P. Mullan,et al. Secreted Effector Proteins of Salmonella dublin Act in Concert To Induce Enteritis , 1998, Infection and Immunity.
[27] P. Majerus,et al. SopB, a protein required for virulence of Salmonella dublin, is an inositol phosphate phosphatase. , 1998, Proceedings of the National Academy of Sciences of the United States of America.
[28] M. Jones,et al. Identification of a pathogenicity island required for Salmonella enteropathogenicity , 1998, Molecular microbiology.
[29] C. Hueck,et al. Type III Protein Secretion Systems in Bacterial Pathogens of Animals and Plants , 1998, Microbiology and Molecular Biology Reviews.
[30] K. Schuebel,et al. S. typhimurium Encodes an Activator of Rho GTPases that Induces Membrane Ruffling and Nuclear Responses in Host Cells , 1998, Cell.
[31] V. L. Miller,et al. Identification of a Novel SalmonellaInvasion Locus Homologous to Shigella ipgDE , 1998, Journal of bacteriology.
[32] W. Hardt,et al. A substrate of the centisome 63 type III protein secretion system of Salmonella typhimurium is encoded by a cryptic bacteriophage. , 1998, Proceedings of the National Academy of Sciences of the United States of America.
[33] W. Hardt,et al. A secreted Salmonella protein with homology to an avirulence determinant of plant pathogenic bacteria. , 1997, Proceedings of the National Academy of Sciences of the United States of America.
[34] P. Mullan,et al. A secreted effector protein of Salmonella dublin is translocated into eukaryotic cells and mediates inflammation and fluid secretion in infected ileal mucosa , 1997, Molecular microbiology.
[35] J. Galán,et al. The invasion‐associated type III system of Salmonella typhimurium directs the translocation of Sip proteins into the host cell , 1997, Molecular microbiology.
[36] H. Ochman,et al. Comparative genetics of the inv-spa invasion gene complex of Salmonella enterica , 1997, Journal of bacteriology.
[37] J Hacker,et al. Pathogenicity islands of virulent bacteria: structure, function and impact on microbial evolution , 1997, Molecular microbiology.
[38] Howard Ochman,et al. Pathogenicity Islands: Bacterial Evolution in Quantum Leaps , 1996, Cell.
[39] P. Mullan,et al. SopE, a secreted protein of Salmonelladublin, is translocated into the target eukaryotic cell via a sip‐dependent mechanism and promotes bacterial entry , 1996, Molecular microbiology.
[40] J. Galán,et al. Requirement for exported proteins in secretion through the invasion-associated type III system of Salmonella typhimurium , 1996, Infection and immunity.
[41] T. Whittam,et al. Molecular genetic relationships of the salmonellae , 1996, Applied and environmental microbiology.
[42] J. Galán,et al. Identification of two targets of the type III protein secretion system encoded by the inv and spa loci of Salmonella typhimurium that have homology to the Shigella IpaD and IpaA proteins , 1995, Journal of bacteriology.
[43] S. Miller,et al. Salmonella typhimurium secreted invasion determinants are homologous to Shigella lpa proteins , 1995, Molecular microbiology.
[44] H. Ochman,et al. Relationship between evolutionary rate and cellular location among the Inv/Spa invasion proteins of Salmonella enterica. , 1995, Proceedings of the National Academy of Sciences of the United States of America.
[45] J. Galán,et al. Homologs of the Shigella IpaB and IpaC invasins are required for Salmonella typhimurium entry into cultured epithelial cells , 1995, Journal of bacteriology.
[46] J. Galán,et al. The Salmonella typhimurium invasion genes invF and invG encode homologues of the AraC and PulD family of proteins , 1994, Molecular microbiology.
[47] B. Stocker,et al. Aromatic-dependent Salmonella typhimurium are non-virulent and effective as live vaccines , 1981, Nature.