Zobrazeno 1 - 10
of 27
pro vyhledávání: '"Kurt W. Miller"'
Autor:
Li-Hong Chen, Volkan K Köseoğlu, Zehra T Güvener, Tanya Myers-Morales, Joseph M Reed, Sarah E F D'Orazio, Kurt W Miller, Mark Gomelsky
Publikováno v:
PLoS Pathogens, Vol 10, Iss 8, p e1004301 (2014)
We characterized key components and major targets of the c-di-GMP signaling pathways in the foodborne pathogen Listeria monocytogenes, identified a new c-di-GMP-inducible exopolysaccharide responsible for motility inhibition, cell aggregation, and en
Externí odkaz:
https://doaj.org/article/520c5f84accf48f09422a49585babf72
Publikováno v:
Journal of Bacteriology. 200
Elevated levels of the second messenger c-di-GMP suppress virulence in diverse pathogenic bacteria, yet mechanisms are poorly characterized. In the foodborne pathogen Listeria monocytogenes , high c-di-GMP levels inhibit mammalian cell invasion. Here
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::88b24107cb2b05837544012ee29b5191
https://doi.org/10.1128/jb.00457-17
https://doi.org/10.1128/jb.00457-17
Autor:
Volkan K. Köseoğlu, Teresa E. Lehmann, Parastoo Azadi, Elena Topchiy, Mark Gomelsky, Kurt W. Miller, Christian Heiss, Zehra Tüzün Güvener
Publikováno v:
Molecular Microbiology. 96:728-743
Summary Elevated levels of the second messenger c-di-GMP activate biosynthesis of an unknown exopolysaccharide (EPS) in the food-borne pathogen Listeria monocytogenes. This EPS strongly protects cells against disinfectants and desiccation, indicating
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eb801bc97fd1a03aa35cecbcc6963f60
https://doi.org/10.1111/mmi.12966
https://doi.org/10.1111/mmi.12966
Autor:
Kurt W. Miller, Hung Vu-Khac
Publikováno v:
Applied and Environmental Microbiology. 75:6671-6678
The EII t Man phosphotransferase system (PTS) permease encoded by the mpt operon is the principal glucose transporter in Listeria monocytogenes. EII t Man participates in glucose-mediated carbon catabolite repression (CCR) and downregulation of virul
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::553419b73613027b513ad97d442b3616
https://doi.org/10.1128/aem.01104-09
https://doi.org/10.1128/aem.01104-09
Publikováno v:
Applied and Environmental Microbiology. 74:7073-7079
1,2-Propanediol (1,2-PD) added exogenously to cultures or produced endogenously from l -rhamnose is metabolized to n -propanol and propionate in Listeria innocua Lin11. The pduD gene, which encodes a diol dehydratase ß subunit homolog, is required f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9c8efeb22fe319faceb648ce3723e866
https://doi.org/10.1128/aem.01074-08
https://doi.org/10.1128/aem.01074-08
Publikováno v:
Applied and Environmental Microbiology. 71:1283-1290
Bacteriocins are small, cationic, antimicrobial peptides produced by lactic acid bacteria (12, 16, 27, 28). These peptides are grouped into three major classes: lantibiotics (class I); small, heat-stable peptides functioning alone (class IIa) or in p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3938fce087fdd129c42460ce2ba3b3ca
https://doi.org/10.1128/aem.71.3.1283-1290.2005
https://doi.org/10.1128/aem.71.3.1283-1290.2005
Publikováno v:
Applied and Environmental Microbiology. 64:1997-2005
Pediocin AcH (same sequence as pediocin PA-1) is a ribosomally synthesized bacteriocin that is produced by certain strains of Pediococcus acidilactici (24, 27). Synthesis is conferred by the papABCD operon, which encodes the pediocin AcH structural g
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::381b9d3d1d9da227ee6f0a6b9c87fc56
https://doi.org/10.1128/aem.64.6.1997-2005.1998
https://doi.org/10.1128/aem.64.6.1997-2005.1998
Autor:
Andrea B. Kohn, Anahit V. Azaryan, Kurt W. Miller, Vivian Hook, Kim Moran, Martin R. Schiller, Mark O. Lively, Rama Kannan
Publikováno v:
Protein Expression and Purification. 10:80-88
Prohormone substrates are required for investigation of the proteolytic processing of prohormones and proproteins into active peptide hormones and neurotransmitters. However, the lack of prohormone proteins has been a limiting factor in elucidating p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6f27cc76db1f8d880f9981c995f0d2e4
https://doi.org/10.1006/prep.1996.0715
https://doi.org/10.1006/prep.1996.0715
Publikováno v:
FEBS Letters. 382:6-10
The preference of the ‘prohormone thiol protease’ (PTP), a candidate prohormone processing enzyme, for different peptide precursors was assessed in vitro with recombinant prohormones near estimated in vivo levels. Pro-neuropeptide Y (pro-NPY), pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b09311bef79926f934158add8145ccf8
https://doi.org/10.1016/0014-5793(96)00083-x
https://doi.org/10.1016/0014-5793(96)00083-x
Autor:
Jean E. Jewell, Kurt W. Miller
Publikováno v:
Archives of Biochemistry and Biophysics. 322:445-452
Two N-terminal fusion proteins combining Escherichia coli maltose-binding protein (MBP) and the 12-transmembrane-segment pBR322 tetracycline resistance protein (Tet) have been constructed to determine the strength and location of topology control sig
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a5efa20ab9c07d67c7b27186f9dc1ccf
https://doi.org/10.1006/abbi.1995.1487
https://doi.org/10.1006/abbi.1995.1487