Characterization of Streptococcus agalactiae CAMP factor as a pore-forming toxin. - Wikidata - awgldk - TriplyDB

Characterization of Streptococcus agalactiae CAMP factor as a pore-forming toxin.

Characterization of Streptococcus agalactiae CAMP factor as a pore-forming toxin.

http://www.wikidata.org/entity/Q44497627

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Proteomic identification of secreted proteins of Propionibacterium acnes Understanding the regulation of Group B Streptococcal virulence factors Adaptive response of Group B streptococcus to high glucose conditions: new insights on the CovRS regulation network Propionibacterium acnes CAMP factor and host acid sphingomyelinase contribute to bacterial virulence: potential targets for inflammatory acne treatment Threonine phosphorylation prevents promoter DNA binding of the Group B Streptococcus response regulator CovR.Hair sheep blood, citrated or defibrinated, fulfills all requirements of blood agar for diagnostic microbiology laboratory tests Synthetic Studies of Glycosylphosphatidylinositol (GPI) Anchors and GPI-Anchored Peptides, Glycopeptides, and Proteins High-level fluorescence labeling of gram-positive pathogens.Role of pore-forming toxins in bacterial infectious diseases.An expanded multilocus sequence typing scheme for propionibacterium acnes: investigation of 'pathogenic', 'commensal' and antibiotic resistant strains.Interaction of Streptococcus agalactiae and Cellular Innate Immunity in Colonization and Disease Characterization of a new CAMP factor carried by an integrative and conjugative element in Streptococcus agalactiae and spreading in Streptococci.Reductive evolution in Streptococcus agalactiae and the emergence of a host adapted lineage.Staphylococcus aureus hijacks a skin commensal to intensify its virulence: immunization targeting β-hemolysin and CAMP factor.Interaction of neonatal phagocytes with group B streptococcus: recognition and response.Concerted action of sphingomyelinase and non-hemolytic enterotoxin in pathogenic Bacillus cereus.SecA localization and SecA-dependent secretion occurs at new division septa in group B Streptococcus Streptococcus iniae SF1: complete genome sequence, proteomic profile, and immunoprotective antigens Mammalian reovirus, a nonfusogenic nonenveloped virus, forms size-selective pores in a model membrane.Passive immunoprotection targeting a secreted CAMP factor of Propionibacterium acnes as a novel immunotherapeutic for acne vulgaris Genome characterization and population genetic structure of the zoonotic pathogen, Streptococcus canis.Role of pore-forming toxins in neonatal sepsis Deciphering the intracellular fate of Propionibacterium acnes in macrophages.Chemical biology of glycosylphosphatidylinositol anchors.Streptococcal toxins: role in pathogenesis and disease.Cardiolipin synthetase is involved in antagonistic interaction (reverse CAMP phenomenon) of Mycoplasma species with Staphylococcus aureus beta-hemolysis.The cytotoxic fimbrial structural subunit of Xenorhabdus nematophila is a pore-forming toxin.Perinatal Group B Streptococcal Infections: Virulence Factors, Immunity, and Prevention Strategies.Peptides released from reovirus outer capsid form membrane pores that recruit virus particles.Bacterial toxins: Offensive, defensive, or something else altogether?CAMP factor is not essential for systemic virulence of Group B Streptococcus.Synthesis of biotin-labelled core glycans of GPI anchors and their application in the study of GPI interaction with pore-forming bacterial toxins.Identification of β-haemolysin-encoding genes in Streptococcus anginosus.The Composition and Structure of Biofilms Developed by Propionibacterium acnes Isolated from Cardiac Pacemaker Devices.Development of a melting-curve based multiplex real-time PCR assay for simultaneous detection of Streptococcus agalactiae and genes encoding resistance to macrolides and lincosamides.

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P2860

Characterization of Streptococcus agalactiae CAMP factor as a pore-forming toxin.

http://www.wikidata.org/entity/Q44497627

description

2003 nî lūn-bûn

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2003年の論文

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年學術文章

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2003年學術文章

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name

Characterization of Streptococcus agalactiae CAMP factor as a pore-forming toxin.

@en

Characterization of Streptococcus agalactiae CAMP factor as a pore-forming toxin.

@nl

type

label

Characterization of Streptococcus agalactiae CAMP factor as a pore-forming toxin.

@en

Characterization of Streptococcus agalactiae CAMP factor as a pore-forming toxin.

@nl

prefLabel

Characterization of Streptococcus agalactiae CAMP factor as a pore-forming toxin.

@en

Characterization of Streptococcus agalactiae CAMP factor as a pore-forming toxin.

@nl

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Journal of Biological Chemistry

P1476

Characterization of Streptococcus agalactiae CAMP factor as a pore-forming toxin.

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P2093

Michael Palmer

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Shenhui Lang

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P2860

Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase

Eukaryotic proteins expressed in Escherichia coli: an improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase

Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set

Assembly mechanism of the oligomeric streptolysin O pore: the early membrane lesion is lined by a free edge of the lipid membrane and is extended gradually during oligomerization.

Complement pore genesis observed in erythrocyte membranes by fluorescence microscopic single-channel recording.

Cloning, sequencing and expression of the CAMP factor gene of Streptococcus uberis.

Unspecific binding of group B streptococcal cocytolysin (CAMP factor) to immunoglobulins and its possible role in pathogenicity.

Evidence for intermolecular interaction as a necessary step for pore-formation activity and toxicity of Bacillus thuringiensis Cry1Ab toxin.

DICHROWEB: an interactive website for the analysis of protein secondary structure from circular dichroism spectra.

An antimicrobial peptide, magainin 2, induced rapid flip-flop of phospholipids coupled with pore formation and peptide translocation.

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38167-38173

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scholarly article

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40

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