Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Joanne Goranson"'
Autor:
Joanne Goranson-Siekierke, Ehmke Pohl, Randall K. Holmes, Tarmo Roosild, Michael K. Choi, Wim G. J. Hol
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 57:619-627
The diphtheria toxin repressor (DtxR) from Corynebacterium diphtheriae regulates the expression of the gene on corynebacteriophages that encodes diphtheria toxin (DT). Other genes regulated by DtxR include those that encode proteins involved in sider
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d5e73f8e4ffd3f655e8f7be825aed8c
https://doi.org/10.1107/s090744490100230x
https://doi.org/10.1107/s090744490100230x
Autor:
Wim G. J. Hol, Bjarni Pàll Ingason, Randall K. Holmes, Michael D. Feese, Joanne Goranson-Siekierke
Publikováno v:
Journal of Biological Chemistry. 276:5959-5966
Iron-dependent regulators are primary transcriptional regulators of virulence factors and iron scavenging systems that are important for infection by several bacterial pathogens. Here we present the 2.0-A crystal structure of the wild type iron-depen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d5347d3f130051cedfe6b72b3f1619b6
https://doi.org/10.1074/jbc.m007531200
https://doi.org/10.1074/jbc.m007531200
Publikováno v:
Infection and Immunity. 67:1806-1811
The homodimeric diphtheria toxin repressor (DtxR) uses Fe 2+ as a corepressor, binds to iron-regulated promoters, and negatively regulates the syntheses of diphtheria toxin, corynebacterial siderophore, and several other Corynebacterium diphtheriae p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::22b777e494bdddcedf4ad4fbb493ad8e
https://doi.org/10.1128/iai.67.4.1806-1811.1999
https://doi.org/10.1128/iai.67.4.1806-1811.1999
Autor:
Liane M. Mende-Mueller, Jeanine P. Wiener-Kronish, Lei Zhu, Christine Wu, Suzanne M. J. Fleiszig, Dara W. Frank, Joanne Goranson, Viviane Finck-Barbançon, Teiji Sawa
Publikováno v:
Scopus-Elsevier
The production of exoenzyme S is correlated with the ability of Pseudomonas aeruginosa to disseminate from epithelial colonization sites and cause a fatal sepsis in burn injury and acute lung infection models. Exoenzyme S is purified from culture sup
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8d7000c6c4736cffbca9842bdffb74f9
https://doi.org/10.1046/j.1365-2958.1997.4891851.x
https://doi.org/10.1046/j.1365-2958.1997.4891851.x
Publikováno v:
Molecular Microbiology. 22:991-1003
Exoenzyme S is an extracellular ADP-ribosyltransferase of Pseudomonas aeruginosa. Transposon mutagenesis of P. aeruginosa 388 was used to identify genes required for exoenzyme S production. Five Tn5Tc insertion mutants were isolated which exhibited a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b2399d10f6f5cb2b5b2ba7d0b20d4853
https://doi.org/10.1046/j.1365-2958.1996.01554.x
https://doi.org/10.1046/j.1365-2958.1996.01554.x
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 235
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::61079bb09d021d925af645d5f8c38a94
https://pubmed.ncbi.nlm.nih.gov/12904660
https://pubmed.ncbi.nlm.nih.gov/12904660
Publikováno v:
Journal of bacteriology. 179(5)
Expression of ExsC, ExsB, and ExsA (the exoenzyme S trans-regulatory locus) of Pseudomonas aeruginosa was analyzed by using complementation, RNase protection, translational fusion, and T7-directed protein expression analyses. T7 expression analyses i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a8ee638b5737b68621089b2faa22cc82
https://pubmed.ncbi.nlm.nih.gov/9045825
https://pubmed.ncbi.nlm.nih.gov/9045825
Autor:
Joanne Goranson, Dara W. Frank
Publikováno v:
FEMS microbiology letters. 135(2-3)
The dissemination of Pseudomonas aeruginosa to the bloodstream increases the likelihood of developing fatal sepsis. In experimental models, the ability to disseminate is linked to expression of the exoenzyme S pathway. Genetic and biochemical analysi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7f535ee2878b06c14432d2e81648e709
https://pubmed.ncbi.nlm.nih.gov/8595851
https://pubmed.ncbi.nlm.nih.gov/8595851
Autor:
Jimmy B. Feix, Jun Liu, Joanne Goranson, Phillip E. Klebba, Jeanette M. Rutz, Jeri Ann Lyons, Sandra K. Armstrong, Mark A. McIntosh
Publikováno v:
Science (New York, N.Y.). 258(5081)
The ferric enterobactin receptor (FepA) is a high-affinity ligand-specific transport protein in the outer membrane of Gram-negative bacteria. Deletion of the cell-surface ligand-binding peptides of FepA generated mutant proteins that were incapable o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9ac1d66bdc7ad61c9bbad94bf5786296
https://pubmed.ncbi.nlm.nih.gov/1411544
https://pubmed.ncbi.nlm.nih.gov/1411544