Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Tasia Joy, Lightly"'
Autor:
Anna J. Hooppaw, Jenna C. McGuffey, Gisela Di Venanzio, Juan C. Ortiz-Marquez, Brent S. Weber, Tasia Joy Lightly, Tim van Opijnen, Nichollas E. Scott, Silvia T. Cardona, Mario F. Feldman
Publikováno v:
mBio, Vol 13, Iss 3 (2022)
ABSTRACT The opportunistic pathogen Acinetobacter baumannii is responsible for a wide range of infections that are becoming increasingly difficult to treat due to extremely high rates of multidrug resistance. Acinetobacter’s pathogenic potential is
Externí odkaz:
https://doaj.org/article/30f123d366be48099dc72ea13e663c47
Publikováno v:
ACS Synthetic Biology. 8:2372-2384
Genetic tools are critical to dissecting the mechanisms governing cellular processes, from fundamental physiology to pathogenesis. Members of the genus Burkholderia have potential for biotechnological applications but can also cause disease in humans
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::db8155d300437a74fb8b7be4fe06a048
https://doi.org/10.1021/acssynbio.9b00232
https://doi.org/10.1021/acssynbio.9b00232
Publikováno v:
Canadian Journal of Microbiology. 63:427-438
Phenylacetic acid (PAA), an intermediate of phenylalanine degradation, is emerging as a signal molecule in microbial interactions with the host. In this work, we explore the presence of phenylalanine and PAA catabolism in 3 microbial pathogens of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e503d4da3b12d692e03323d0a8a98e27
https://doi.org/10.1139/cjm-2016-0705
https://doi.org/10.1139/cjm-2016-0705
Autor:
Kara L. Frejuk, Cor Ras, Tasia Joy Lightly, Eric Déziel, John L. Sorensen, Laurent R. Chiarelli, Silvia T. Cardona, Marie-Christine Groleau, Silvia Buroni
Publikováno v:
Appl Environ Microbiol
During phenylalanine catabolism, phenylacetic acid (PAA) is converted to phenylacetyl coenzyme A (PAA-CoA) by a ligase, PaaK, and then PAA-CoA is epoxidized by a multicomponent monooxygenase, PaaABCDE, before further degradation through the tricarbox
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0017fbce13d8487e801356cb545a3319
https://doi.org/10.1128/aem.01594-19
https://doi.org/10.1128/aem.01594-19
Autor:
Laurent R. Chiarelli, Eric Déziel, Silvia T. Cardona, Kara L. Frejuk, Tasia Joy Lightly, Cor Ras, Silvia Buroni, Marie-Christine Groleau, John L. Sorensen
During phenylalanine catabolism, phenylacetic acid (PAA) is converted to phenylacetyl-CoA (PAA-CoA) by a ligase, PaaK, and then epoxidized by a multicomponent monooxygenase, PaaABCDE, before further degradation to the TCA cycle. In the opportunistic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d3ea56ed1a7bdf8e5e135490c5b86981
https://doi.org/10.1101/700799
https://doi.org/10.1101/700799
Autor:
Tanya Pribytkova, Brijesh Kumar, Silvia T. Cardona, John L. Sorensen, Steve P. Bernier, Michael G. Surette, Tasia Joy Lightly
Publikováno v:
Molecular Microbiology. 94:522-536
Summary The phenylacetic acid degradation pathway of Burkholderia cenocepacia is active during cystic fibrosis-like conditions and is necessary for full pathogenicity of B. cenocepacia in nematode and rat infection models; however, the reasons for su
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7dd4bfd8cf58c6d26357c0feb159fd61
https://doi.org/10.1111/mmi.12771
https://doi.org/10.1111/mmi.12771
Autor:
Tanya, Pribytkova, Tasia Joy, Lightly, Brijesh, Kumar, Steve P, Bernier, John L, Sorensen, Michael G, Surette, Silvia T, Cardona
Publikováno v:
Molecular microbiology. 94(3)
The phenylacetic acid degradation pathway of Burkholderia cenocepacia is active during cystic fibrosis-like conditions and is necessary for full pathogenicity of B. cenocepacia in nematode and rat infection models; however, the reasons for such requi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::fdea988051bdbf53d230a9b4034d3e0d
https://pubmed.ncbi.nlm.nih.gov/25155974
https://pubmed.ncbi.nlm.nih.gov/25155974