RTX cytotoxins recognize beta2 integrin receptors through N-linked oligosaccharides
about
Bordetella adenylate cyclase toxin mobilizes its beta2 integrin receptor into lipid rafts to accomplish translocation across target cell membrane in two stepsPertussis toxin and adenylate cyclase toxin: key virulence factors of Bordetella pertussis and cell biology toolsRTX proteins: a highly diverse family secreted by a common mechanismReview of the neutrophil response to Bordetella pertussis infection.Bordetella adenylate cyclase toxin is a unique ligand of the integrin complement receptor 3Selective translocation of the Bordetella pertussis adenylate cyclase toxin across the basolateral membranes of polarized epithelial cellsProbing of Actinobacillus pleuropneumoniae ApxIIIA toxin-dependent cytotoxicity towards mammalian peripheral blood mononucleated cellsBacterial RTX toxins allow acute ATP release from human erythrocytes directly through the toxin pore.N-glycosylation of ß4 integrin controls the adhesion and motility of keratinocytes.Calcium-induced folding and stabilization of the intrinsically disordered RTX domain of the CyaA toxinMonoclonal antibodies against Vibrio vulnificus RtxA1 elicit protective immunity through distinct mechanisms.Aggregatibacter actinomycetemcomitans leukotoxin: from threat to therapyGangliosides block Aggregatibacter Actinomycetemcomitans leukotoxin (LtxA)-mediated hemolysisThe Bordetella pertussis adenylate cyclase toxin binds to T cells via LFA-1 and induces its disengagement from the immune synapseSialic acid associated with αvβ3 integrin mediates HIV-1 Tat protein interaction and endothelial cell proangiogenic activation.Uropathogenic Escherichia coli-Associated ExotoxinsVirulence factor secretion and translocation by Bordetella species.Mechanisms of cytolysin-induced cell damage -- a role for auto- and paracrine signalling.Adenylate cyclase toxin-hemolysin relevance for pertussis vaccines.Interaction of Bordetella adenylate cyclase toxin with complement receptor 3 involves multivalent glycan binding.Bordetella adenylate cyclase toxin: a unique combination of a pore-forming moiety with a cell-invading adenylate cyclase enzyme.Transmembrane segments of complement receptor 3 do not participate in cytotoxic activities but determine receptor structure required for action of Bordetella adenylate cyclase toxin.Sialic acid residues are essential for cell lysis mediated by leukotoxin from Aggregatibacter actinomycetemcomitans.Brief heat treatment causes a structural change and enhances cytotoxicity of the Escherichia coli α-hemolysin.Porcine CD18 mediates Actinobacillus pleuropneumoniae ApxIII species-specific toxicity.N-glycosylation of the I-like domain of beta1 integrin is essential for beta1 integrin expression and biological function: identification of the minimal N-glycosylation requirement for alpha5beta1.Cyclic AMP-Elevating Capacity of Adenylate Cyclase Toxin-Hemolysin Is Sufficient for Lung Infection but Not for Full Virulence of Bordetella pertussis.Identification of a virulence determinant that is conserved in the Jawetz and Heyl biotypes of [Pasteurella] pneumotropica.The conserved tyrosine residue 940 plays a key structural role in membrane interaction of Bordetella adenylate cyclase toxin.Identification and characterization of hemolysin-like proteins similar to RTX toxin in Pasteurella pneumotropica.Structure-Function Relationships Underlying the Capacity of Bordetella Adenylate Cyclase Toxin to Disarm Host Phagocytes.Bordetella pertussis adenylate cyclase toxin disrupts functional integrity of bronchial epithelial layers.Leukotoxin from Aggregatibacter actinomycetemcomitans causes shrinkage and P2X receptor-dependent lysis of human erythrocytes.Bordetella Pertussis Adenylate Cyclase Toxin Does Not Possess a Phospholipase A Activity; Serine 606 and Aspartate 1079 Residues Are Not Involved in Target Cell Delivery of the Adenylyl Cyclase Enzyme Domain.Immunology in the heart of the High Tatra mountains
P2860
Q21131558-373F8E71-09E9-471D-84CF-72CBFC672D5EQ24602050-ED6CB2EC-7D39-43B4-8432-9711542A626EQ24630254-4447F204-D727-4B13-9054-6C90453F4F6EQ30278579-81DDFF37-FD26-47F3-8FD2-D5BF5ADD46CAQ30360778-3C4B3C57-778A-4C2B-BD5F-E396882A7954Q30432788-18CCF232-3379-465B-85C9-9312FEFE809DQ33388553-F74DE81B-B00E-4DB3-9860-AC23FFDAE091Q33846524-E6584952-03F3-4C1A-88BD-8DA71E2F55FCQ34071779-03E87926-C28F-4B1C-BFCA-17A94ADC8220Q34388681-7405D070-2750-411A-8524-4146937CEBB9Q34596138-94316A9C-29C3-49D5-A84C-A6321FBE50A1Q35129153-C0734207-615C-4C5D-88E1-090A410CECB3Q35155672-6C93B30B-6F39-4172-895C-92D3996E0A6BQ35213542-729ACDD1-BC5E-405A-9254-7FAE9BE30565Q36016939-3B67802F-5D18-4D1E-8519-F13BFE3C93F8Q37035981-1EEAEC83-698C-48FE-8EA0-D6786AB9F9CBQ37382931-A09117B7-78B5-4C4B-9E7F-58CBD809B3CFQ38127458-08841F7F-CF16-476D-83BA-57B56B70371CQ38236718-EC757ABA-477C-4168-A8B2-0085475E80A7Q38301936-EEF871A5-EB5C-4988-8334-2613B06FFF53Q38590644-965518DC-A82D-4944-8129-8D563BF1A496Q38800261-72C0720F-DF80-4DF1-B3AA-8E1C049991F5Q39014126-B022F372-09E9-423A-8D92-2EF01115E52AQ39275077-8387F176-B43F-435C-AB16-E5B7F24D8158Q39862744-6ECDF180-4B4A-4563-9BEE-B02214ADC54CQ39877253-35B98060-2489-49B0-9B50-4E25837C7D76Q40257250-86EBD615-7193-48A3-8C79-356162D3C285Q40617425-CEAAB22A-9CA1-4DA7-9C84-5DBDE132A7C5Q41518063-16CE48FC-522C-4983-892F-6C5E59E5753BQ43127705-62DDB4C2-7840-435A-98C2-77720989CDA4Q44920994-B52AFCF0-09A5-4766-8BEA-9C12D54DEB6AQ47691335-61E0C79F-2F12-4561-94B3-5A21F5532864Q54330041-03758EA8-2B89-4E1E-987A-D947618B8D0BQ55515159-8A0D968A-B40F-498D-AA52-473E4785F791Q57100638-614CB912-6E46-4BC2-A959-45C995D6B50F
P2860
RTX cytotoxins recognize beta2 integrin receptors through N-linked oligosaccharides
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
RTX cytotoxins recognize beta2 integrin receptors through N-linked oligosaccharides
@ast
RTX cytotoxins recognize beta2 integrin receptors through N-linked oligosaccharides
@en
type
label
RTX cytotoxins recognize beta2 integrin receptors through N-linked oligosaccharides
@ast
RTX cytotoxins recognize beta2 integrin receptors through N-linked oligosaccharides
@en
prefLabel
RTX cytotoxins recognize beta2 integrin receptors through N-linked oligosaccharides
@ast
RTX cytotoxins recognize beta2 integrin receptors through N-linked oligosaccharides
@en
P2860
P356
P1476
RTX cytotoxins recognize beta2 integrin receptors through N-linked oligosaccharides
@en
P2093
Jana Morova
Jiri Masin
P2860
P304
P356
10.1073/PNAS.0711400105
P407
P577
2008-03-28T00:00:00Z