Escherichia coli hemolysin may damage target cell membranes by generating transmembrane pores.
about
Genomic insights into an obligate epibiotic bacterial predator: Micavibrio aeruginosavorus ARL-13RTX proteins: a highly diverse family secreted by a common mechanismalpha-latrotoxin triggers transmitter release via direct insertion into the presynaptic plasma membraneThe virulence plasmid of Yersinia, an antihost genomeVirulence factors in Escherichia coli urinary tract infectionContribution of Escherichia coli alpha-hemolysin to bacterial virulence and to intraperitoneal alterations in peritonitis.Differences in purinergic amplification of osmotic cell lysis by the pore-forming RTX toxins Bordetella pertussis CyaA and Actinobacillus pleuropneumoniae ApxIA: the role of pore size.In vivo cytokine response to Escherichia coli alpha-hemolysin determined with genetically engineered hemolytic and nonhemolytic E. coli variantsAlpha-hemolysin from Escherichia coli uses endogenous amplification through P2X receptor activation to induce hemolysis.Cytotoxic activities of Leptospira interrogans hemolysin SphH as a pore-forming protein on mammalian cells.Clostridium perfringens delta toxin is sequence related to beta toxin, NetB, and Staphylococcus pore-forming toxins, but shows functional differences.Cloning and expression of a Serpula (Treponema) hyodysenteriae hemolysin gene.NetB, a new toxin that is associated with avian necrotic enteritis caused by Clostridium perfringens.Molecular analysis of the plasmid-encoded hemolysin of Escherichia coli O157:H7 strain EDL 933.Alterations of amino acid repeats in the Escherichia coli hemolysin affect cytolytic activity and secretion.TolC, an Escherichia coli outer membrane protein required for hemolysin secretion.Pseudomonas syringae phytotoxins: mode of action, regulation, and biosynthesis by peptide and polyketide synthetasesThe Yersinia deadly kiss.Insight into the salivary transcriptome and proteome of Dipetalogaster maximaEscherichia coli alpha-hemolysin triggers shrinkage of erythrocytes via K(Ca)3.1 and TMEM16A channels with subsequent phosphatidylserine exposure.Bacterial RTX toxins allow acute ATP release from human erythrocytes directly through the toxin pore.Alterations in bovine platelet function and acute phase proteins induced by Pasteurella haemolytica A1.Alpha hemolysin induces an increase of erythrocytes calcium: a FLIM 2-photon phasor analysis approachCorrelation of Pasteurella haemolytica leukotoxin binding with susceptibility to intoxication of lymphoid cells from various species.Characterization of hemolysin of Moraxella bovis using a hemolysis-neutralizing monoclonal antibodySecretion of RTX leukotoxin by Actinobacillus actinomycetemcomitans.Pyelonephritogenic diffusely adhering Escherichia coli EC7372 harboring Dr-II adhesin carries classical uropathogenic virulence genes and promotes cell lysis and apoptosis in polarized epithelial caco-2/TC7 cells.Genetic conservation of hlyA determinants and serological conservation of HlyA: basis for developing a broadly cross-reactive subunit Escherichia coli alpha-hemolysin vaccine.A cytolysin encoded by Salmonella is required for survival within macrophages.Epitopes of Escherichia coli alpha-hemolysin: identification of monoclonal antibodies that prevent hemolysisIdentification and partial characterization of a cytolytic toxin produced by Gardnerella vaginalisDifferent types of cell death induced by enterotoxins.The deletion of several amino acid stretches of Escherichia coli alpha-hemolysin (HlyA) suggests that the channel-forming domain contains beta-strands.Mitotic block and delayed lethality in HeLa epithelial cells exposed to Escherichia coli BM2-1 producing cytotoxic necrotizing factor type 1.Pasteurella haemolytica leukotoxin induces bovine leukocytes to undergo morphologic changes consistent with apoptosis in vitro.Channel-forming activity and channel size of the RTX toxins ApxI, ApxII, and ApxIII of Actinobacillus pleuropneumoniae.Hyperproduction, purification, and mechanism of action of the cytotoxic enterotoxin produced by Aeromonas hydrophilaPore forming activity of the potent RTX-toxin produced by pediatric pathogen Kingella kingae: Characterization and comparison to other RTX-family members.The UPEC pore-forming toxin α-hemolysin triggers proteolysis of host proteins to disrupt cell adhesion, inflammatory, and survival pathways.Regulation of Actinobacillus actinomycetemcomitans leukotoxin expression: analysis of the promoter regions of leukotoxic and minimally leukotoxic strains
P2860
Q21267175-D782BEE8-DC41-4C95-BE46-A251C03EA25EQ24630254-4386569C-8D1F-4052-B623-AD1A64C2980DQ26269973-C818FFFD-A7FF-456D-B32B-B493BF4EF995Q28290675-B66FCFCC-74C8-470A-A6A5-38FFDD01E283Q28468751-714AE2E5-76BB-4A0F-B0FB-7243A9E1361FQ30304556-C89863A4-44BC-49E2-97FA-37F52A8F838FQ30412779-B82363B2-1F48-406E-8B15-05CF7EE08DD4Q30452859-1849EF64-C4A9-4E94-990E-06D49EE8DF69Q30486501-F2CD5793-FA34-4590-8B32-93DCA4C3CE6CQ30780506-08D8098F-F6E2-4696-9E45-C60FD5500A3AQ30854566-0C4A6D6D-03EE-4DD0-89AD-32E154D0BE07Q33274133-EA0150DB-1D0F-46B7-B23E-E906F37B3F42Q33319276-CADE6818-E70B-42D3-B55B-76BB6369DF92Q33490539-570184E4-98EA-4842-B657-870F3D961C63Q33633119-F1ECCC75-6AE8-427C-A0E8-48A1CE90451AQ33644353-38EB8AD8-0AF9-47D3-BC00-95104AE4275FQ33652140-6B32CF87-26E3-4194-9102-8B0BF2DAA90EQ33738622-B4008FC3-D71B-47B6-963F-4DD38E61EDCEQ33740905-193A5C49-59E0-48E1-9FA8-87A5C7E1DD32Q33832565-64BCFFDC-7CA0-4AC2-A477-F83A424EFD10Q33846524-53B33BCD-8061-4980-8DB4-E7EDCE1C6A8BQ33923295-7F121E66-6444-4D09-AF38-85D4632D7E05Q33940798-B682299D-2986-4590-A330-4EAD13617F5FQ34002667-A7E3110E-3711-48E3-A132-4A55D257422DQ34004767-0BF6EEEF-D427-42DE-BA08-6AED5F78A959Q34004906-36DC771A-0380-4BA9-B492-F2ECA9B32F7EQ34005319-5F211ABA-C076-4B1D-A8B7-316E6675EB33Q34527547-E2294E49-C096-478E-A9FE-CF2D8AF4A309Q34979023-503B9E08-8A25-49E2-9848-269023E3D45DQ35104471-522CE1BA-F1A0-4078-B2CF-B6A607F196D4Q35107979-53215164-5926-4380-8832-B3F64EDDE83EQ35155921-8A4EDFB3-C194-4BF1-8366-358C53815118Q35478487-CA495ACB-1DCE-476C-A2B0-3D5B0A4A18B9Q35490054-FE70A8C1-4646-4D2C-8B2E-168414CF6892Q35505550-1BB0AF0D-6A7A-453B-9B63-936A93873DFAQ35527151-B2658094-0F36-4495-A742-843E42F1B863Q35556925-CED9749F-C55C-4D1A-ABAF-746F9D80346FQ35602763-BE753CC6-8BDD-4546-9B0B-6960E27BE6D1Q35697535-57F20CCD-81E3-43F6-9AF9-18DAC8CE9714Q35773013-CE311634-E9F9-4883-A174-207EB79952D1
P2860
Escherichia coli hemolysin may damage target cell membranes by generating transmembrane pores.
description
1986 nî lūn-bûn
@nan
1986年の論文
@ja
1986年論文
@yue
1986年論文
@zh-hant
1986年論文
@zh-hk
1986年論文
@zh-mo
1986年論文
@zh-tw
1986年论文
@wuu
1986年论文
@zh
1986年论文
@zh-cn
name
Escherichia coli hemolysin may ...... enerating transmembrane pores.
@en
type
label
Escherichia coli hemolysin may ...... enerating transmembrane pores.
@en
prefLabel
Escherichia coli hemolysin may ...... enerating transmembrane pores.
@en
P2093
P2860
P1476
Escherichia coli hemolysin may ...... enerating transmembrane pores.
@en
P2093
P2860
P407
P577
1986-04-01T00:00:00Z