Differential expression and transcriptional analysis of the alpha-2,3-sialyltransferase gene in pathogenic Neisseria spp - Wikidata - wikimedia - TriplyDB

Differential expression and transcriptional analysis of the alpha-2,3-sialyltransferase gene in pathogenic Neisseria spp

Differential expression and transcriptional analysis of the alpha-2,3-sialyltransferase gene in pathogenic Neisseria spp

http://www.wikidata.org/entity/Q34601796

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Meningococcal genetic variation mechanisms viewed through comparative analysis of serogroup C strain FAM18.Comparative analysis of two Neisseria gonorrhoeae genome sequences reveals evidence of mobilization of Correia Repeat Enclosed Elements and their role in regulation.Regulatory role of the MisR/S two-component system in hemoglobin utilization in Neisseria meningitidis The transposon-like Correia elements encode numerous strong promoters and provide a potential new mechanism for phase variation in the meningococcus.Meningococcal disease and the complement system.α-2,3-sialyltransferase expression level impacts the kinetics of lipooligosaccharide sialylation, complement resistance, and the ability of Neisseria gonorrhoeae to colonize the murine genital tract Neisserial Correia repeat-enclosed elements do not influence the transcription of pil genes in Neisseria gonorrhoeae and Neisseria meningitidis A strain-specific catalase mutation and mutation of the metal-binding transporter gene mntC attenuate Neisseria gonorrhoeae in vivo but not by increasing susceptibility to oxidative killing by phagocytes.Is gonococcal disease preventable? The importance of understanding immunity and pathogenesis in vaccine development.Mechanisms in Neisseria meningitidis for resistance against complement-mediated killing.Control of pili and sialyltransferase expression in Neisseria gonorrhoeae is mediated by the transcriptional regulator CrgA.Gonococcal lipooligosaccharide sialylation: virulence factor and target for novel immunotherapeutics.A novel link between Campylobacter jejuni bacteriophage defence, virulence and Guillain-Barré syndrome.

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P2860

Differential expression and transcriptional analysis of the alpha-2,3-sialyltransferase gene in pathogenic Neisseria spp

http://www.wikidata.org/entity/Q34601796

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2006 nî lūn-bûn

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2006 թուականի Մայիսին հրատարակուած գիտական յօդուած

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Differential expression and tr ...... ne in pathogenic Neisseria spp

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Differential expression and tr ...... ne in pathogenic Neisseria spp

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Differential expression and tr ...... ne in pathogenic Neisseria spp

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Differential expression and tr ...... ne in pathogenic Neisseria spp

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Differential expression and tr ...... ne in pathogenic Neisseria spp

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Differential expression and tr ...... ne in pathogenic Neisseria spp

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Differential expression and tr ...... ne in pathogenic Neisseria spp

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Differential expression and tr ...... ne in pathogenic Neisseria spp

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Differential expression and tr ...... ne in pathogenic Neisseria spp

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IAI.74.5.2637-2650.2006

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Infection and Immunity

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Differential expression and tr ...... ne in pathogenic Neisseria spp

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Dawn M Shell

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Mathanraj Packiam

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Ranjana Srivastava

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Richard F Rest

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Samar Seal

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Shi V Liu

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Yao-Bin Liu

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P2860

Regulation of gonococcal sialyltransferase, lipooligosaccharide, and serum resistance by glucose, pyruvate, and lactate

Anaerobic growth and cytidine 5'-monophospho-N-acetylneuraminic acid act synergistically to induce high-level serum resistance in Neisseria gonorrhoeae.

The contrasting mechanisms of serum resistance of Neisseria gonorrhoeae and group B Neisseria meningitidis.

Induction of the mtrCDE-encoded efflux pump system of Neisseria gonorrhoeae requires MtrA, an AraC-like protein.

Identification, characterization, and variable expression of a naturally occurring inhibitor protein of IS1106 transposase in clinical isolates of Neisseria meningitidis

Enhanced factor H binding to sialylated Gonococci is restricted to the sialylated lacto-N-neotetraose lipooligosaccharide species: implications for serum resistance and evidence for a bifunctional lipooligosaccharide sialyltransferase in Gonococci

The Neisseria lipooligosaccharide-specific alpha-2,3-sialyltransferase is a surface-exposed outer membrane protein.

Genome analysis and strain comparison of correia repeats and correia repeat-enclosed elements in pathogenic Neisseria.

Sialylation of Neisseria meningitidis lipooligosaccharide inhibits serum bactericidal activity by masking lacto-N-neotetraose

A 26-base-pair repetitive sequence specific for Neisseria gonorrhoeae and Neisseria meningitidis genomic DNA

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