Zobrazeno 1 - 10
of 240
pro vyhledávání: '"M Bagdasarian"'
Autor:
Michael Bagdasarian, Christopher M. Waters, Ashley E. Konal, Rudolph E. Sloup, Geoffrey B. Severin, Mira M. Bagdasarian, Michelle L. Korir
Publikováno v:
Journal of Bacteriology. 199
Vibrio cholerae is a human pathogen that alternates between growth in environmental reservoirs and infection of human hosts, causing severe diarrhea. The second messenger cyclic di-GMP (c-di-GMP) mediates this transition by controlling a wide range o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dd9098d832a4fcc0006bb0199509003a
https://doi.org/10.1128/jb.00106-17
https://doi.org/10.1128/jb.00106-17
Publikováno v:
Journal of Medical Entomology. 43:288-295
Whether the house fly, Musca domestica L., gut is a permissive environment for horizontal transfer of antibiotic resistance and virulence genes between strains of Escherichia coli is not known. House flies were immobilized and force fed suspensions o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a59a276fa0e52e2ed2ed7d01b483b539
https://doi.org/10.1603/0022-2585(2006)043[0288:htosta]2.0.co
https://doi.org/10.1603/0022-2585(2006)043[0288:htosta]2.0.co
Publikováno v:
Journal of Medical Entomology. 43:288-295
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4ee0daf9ce371ce96d4661f4cb6f74ed
https://doi.org/10.1093/jmedent/43.2.288
https://doi.org/10.1093/jmedent/43.2.288
Publikováno v:
Infection and Immunity. 68:4930-4937
Vibrio choleraestrain VB1 secretes a number of enzymes into the outside medium that utilize ATP as a substrate. Such enzymes are found in the outside medium during the mid-log phase of growth, when the optical density at 650 nm is about 0.4, and they
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0a47712317d9ded8de65f1a5e7598fc8
https://doi.org/10.1128/iai.68.9.4930-4937.2000
https://doi.org/10.1128/iai.68.9.4930-4937.2000
Publikováno v:
Vaccine. 16:1611-1619
In vitro gene manipulation was used to develop a novel chimeric antigen consisting of the non-toxic B subunit (EtxB) of an E. coli enterotoxin and the first 14 N-terminal amino acid residues of the carboxy-terminal portion of the α subunit of bovine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::390fba23b26efa57200d7c56c4b15b23
https://doi.org/10.1016/s0264-410x(98)00056-5
https://doi.org/10.1016/s0264-410x(98)00056-5
Publikováno v:
Journal of Bacteriology. 179:6994-7003
The general secretion pathway (GSP) of Vibrio cholerae is required for secretion of proteins including chitinase, enterotoxin, and protease through the outer membrane. In this study, we report the cloning and sequencing of a DNA fragment from V. chol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9ce9782d34159e075bc7140f73c78efd
https://doi.org/10.1128/jb.179.22.6994-7003.1997
https://doi.org/10.1128/jb.179.22.6994-7003.1997
Publikováno v:
The EMBO Journal. 14:1664-1673
Vibrio cholerae secretes a number of proteins important for virulence, including cholera toxin. This process requires the products of the eps genes which have homologues in genera such as Aeromonas, Klebsiella and Pseudomonas and are thought to form
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9391aeb3477a3359008b572d75fe2183
https://doi.org/10.1002/j.1460-2075.1995.tb07155.x
https://doi.org/10.1002/j.1460-2075.1995.tb07155.x
Autor:
Michael Bagdasarian, Mira M. Bagdasarian, Peter Scholz, Adriana Bailone, Jaime F. Angulo, R. Devoret
Publikováno v:
Molecular Microbiology. 6:885-893
Summary PsiB, an anti-SOS protein, shown previously to prevent activation of RecA protein, was purified from the crude extract of PsiB overproducing cells. PsiB is probably a tetrameric protein, whose subunit has a sequence-deduced molecular mass of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4c3b373fe5349df25aad57ccc3484e38
https://doi.org/10.1111/j.1365-2958.1992.tb01539.x
https://doi.org/10.1111/j.1365-2958.1992.tb01539.x
Publikováno v:
Proceedings of the National Academy of Sciences. 88:4015-4019
The substrate specificity of thermophilic xylose isomerase from Clostridium thermosulfurogenes was examined by using predictions from the known crystal structure of the Arthrobacter enzyme and site-directed mutagenesis of the thermophile xylA gene. T
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::94f3f264813dba230e62e5454e1c043d
https://doi.org/10.1073/pnas.88.9.4015
https://doi.org/10.1073/pnas.88.9.4015
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