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Membrane insertion: The strategies of toxins (review).Complicated catheter-associated urinary tract infections due to Escherichia coli and Proteus mirabilisDetection of hemolysin variants of Shiga toxin-producing Escherichia coli by PCR and culture on vancomycin-cefixime-cefsulodin blood agar.Synthetic Studies of Glycosylphosphatidylinositol (GPI) Anchors and GPI-Anchored Peptides, Glycopeptides, and ProteinsHemolytic and hemoxidative activities in Mycoplasma penetransPhylogenetic and functional gene structure shifts of the oral microbiomes in periodontitis patients.Characterization of Bacteroides fragilis hemolysins and regulation and synergistic interactions of HlyA and HlyB.A Serratia marcescens PigP homolog controls prodigiosin biosynthesis, swarming motility and hemolysis and is regulated by cAMP-CRP and HexS.A cytolysin encoded by Salmonella is required for survival within macrophages.Secretome of obligate intracellular Rickettsia.Intermedilysin, a novel cytotoxin specific for human cells secreted by Streptococcus intermedius UNS46 isolated from a human liver abscesscis Elements and trans factors are both important in strain-specific regulation of the leukotoxin gene in Actinobacillus actinomycetemcomitans.Cloning and characterization of a Prevotella melaninogenica hemolysin.Crystallization of truncated hemolysin A from Proteus mirabilisPotential virulence factors of Proteus bacilli.Expression of Bacteroides fragilis hemolysins in vivo and role of HlyBA in an intra-abdominal infection model.Vaccination with proteus toxic agglutinin, a hemolysin-independent cytotoxin in vivo, protects against Proteus mirabilis urinary tract infection.Activation of the Nlrp3 inflammasome by Streptococcus pyogenes requires streptolysin O and NF-kappa B activation but proceeds independently of TLR signaling and P2X7 receptor.Chemical biology of glycosylphosphatidylinositol anchors.YcaO-Dependent Posttranslational Amide Activation: Biosynthesis, Structure, and Function.Helicobacter pylori pore-forming cytolysin orthologue TlyA possesses in vitro hemolytic activity and has a role in colonization of the gastric mucosa.Cytotoxic action of Serratia marcescens hemolysin on human epithelial cells.Characterization of the roles of hemolysin and other toxins in enteropathy caused by alpha-hemolytic Escherichia coli linked to human diarrheaCharacterization of a pore-forming cytotoxin expressed by Salmonella enterica serovars typhi and paratyphi A.Toxin production by Campylobacter spp.An Edwardsiella tarda strain containing a mutation in a gene with homology to shlB and hpmB is defective for entry into epithelial cells in culture.Cloning, expression, and sequencing of a protease gene from Bacteroides forsythus ATCC 43037 in Escherichia coli.In vitro activation of the Serratia marcescens hemolysin through modification and complementation.Activation of Serratia marcescens hemolysin through a conformational change.Molecular analysis of the tlyA gene in Campylobacter lari.Endotoxin "priming" potentiates lung vascular abnormalities in response to Escherichia coli hemolysin: an example of synergism between endo- and exotoxin.Cloning of Prevotella intermedia loci demonstrating multiple hemolytic domains.Synthesis of biotin-labelled core glycans of GPI anchors and their application in the study of GPI interaction with pore-forming bacterial toxins.Pathogenesis of Proteus mirabilis Infection.An alternative approach for evaluating the phenotypic virulence factors of pathogenic Escherichia coli.Tannerella forsythensis prtH genotype and association with periodontal status.
P2860
Q30176580-F4C6A56E-E32D-4EB6-92DC-5528099DA591Q30491878-AD0926E5-19A3-48B7-9C3B-D79C4875EBAAQ33714771-52EF9891-8E44-4D05-A712-DAFC853960C6Q33777317-36851679-7332-4854-B3A4-120F7690E2DCQ34005043-34C1ADE5-F726-40BD-9C68-77A6D71F5F48Q34071990-F00F9922-E6BA-4EF9-AC4A-955FAA3766AEQ34492639-D20F76E8-A76C-4FBF-A5B2-17CF582EFD4DQ34613143-709F829C-5DA6-494A-AC40-416183965BD1Q34979023-2871A315-55DD-41CA-AA69-F2114571325EQ35132653-28FEBA45-D06C-431C-A271-6366B6FCBAADQ35510878-D06D9E28-E19A-49DE-8212-CA8F92D16782Q35515043-FDB4C466-05DF-43CE-AEE1-830555832B34Q35550981-5381B571-89E2-4995-B9D5-18FFDABAD07DQ35950969-07E2D590-23F6-4A96-9C32-538E2EA81D03Q36574211-DB6C5979-99B5-4A90-816B-D9C2522B2E17Q36787160-5C31D822-188D-4BCF-8429-610379E4782EQ37075483-B84EECA8-29AC-4615-965E-EF65A3CCBB79Q37395836-09EADFD1-896A-4681-8761-E9957666FFBFQ38054022-C21B52BE-AA45-4244-826A-722C1625A15CQ38751212-547577A3-4802-49BE-86D3-7F9F17AF92B1Q39219691-AA08A560-7402-4E36-84BB-AE2EC0F85F79Q39509713-18A6A2EF-D383-4104-94EE-AA046D917987Q39571101-5068D8E0-A562-41E2-BF99-12CEF871E939Q39656445-1A901082-F8C5-4146-83B9-3A4CFC053810Q39820812-79288DED-DCDA-45AA-881B-5E165450DC69Q39831028-CC4CA36D-EBAA-41DD-9C5D-BB6627771968Q39831612-F03097EA-F971-4993-8F44-1CB87D3EC0BFQ39935594-00590F7D-710D-49B2-8404-AB04067A18D7Q40582671-327CD842-1FCC-401A-9A04-820198D828A5Q41021794-E383A706-A1B1-41F5-8709-DB4B410EDE79Q41969291-0EB706D5-E0F4-4D85-9FB5-D4C261697A67Q42610467-EB5FE6D4-7252-4B13-A823-E893365E84C1Q48795459-C2F162A6-327B-4980-AC1A-938936704266Q50102491-43CC9A19-67BF-4A9D-ADC2-77E8C6262CBFQ50145974-6CD1AEEC-5440-484C-8EFE-E904F2B536E2Q54558400-EA3C5796-C8F9-45C8-9600-96463BC568CB
P2860
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on January 1991
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Pore-forming bacterial protein hemolysins (cytolysins).
@en
Pore-forming bacterial protein hemolysins
@nl
type
label
Pore-forming bacterial protein hemolysins (cytolysins).
@en
Pore-forming bacterial protein hemolysins
@nl
prefLabel
Pore-forming bacterial protein hemolysins (cytolysins).
@en
Pore-forming bacterial protein hemolysins
@nl
P2860
P1476
Pore-forming bacterial protein hemolysins (cytolysins).
@en
P2093
P2860
P304
P356
10.3109/10408419109113511
P407
P577
1991-01-01T00:00:00Z