Anthrax toxin-mediated delivery of a cytotoxic T-cell epitope in vivo.
about
Binary bacterial toxins: biochemistry, biology, and applications of common Clostridium and Bacillus proteinsTumor Targeting and Drug Delivery by Anthrax ToxinCrystal structure of the anthrax lethal factorInhibition of axotomy-induced neuronal apoptosis by extracellular delivery of a Bcl-XL fusion proteinVariations in TcdB activity and the hypervirulence of emerging strains of Clostridium difficileMutational analysis of the enzymatic domain of Clostridium difficile toxin B reveals novel inhibitors of the wild-type toxinNanopore Detector based analysis of single-molecule conformational kinetics and binding interactions.Protective antigen-mediated antibody response against a heterologous protein produced in vivo by Bacillus anthracisInduction of a polarized Th1 response by insertion of multiple copies of a viral T-cell epitope into adenylate cyclase of Bordetella pertussis.Contributions of edema factor and protective antigen to the induction of protective immunity by Bacillus anthracis edema toxin as an intranasal adjuvantAnthrax toxin-mediated delivery in vivo and in vitro of a cytotoxic T-lymphocyte epitope from ovalbuminAnthrax toxin as a molecular tool for stimulation of cytotoxic T lymphocytes: disulfide-linked epitopes, multiple injections, and role of CD4(+) cells.Delivery of multiple epitopes by recombinant detoxified adenylate cyclase of Bordetella pertussis induces protective antiviral immunity.Potential use of non-classical pathways for the transport of macromolecular drugs.Enhanced delivery of exogenous peptides into the class I antigen processing and presentation pathway.A chimeric protein that functions as both an anthrax dual-target antitoxin and a trivalent vaccine.Stimulation of CD8+ T cells following diphtheria toxin-mediated antigen delivery into dendritic cellsAn anthrax subunit vaccine candidate based on protective regions of Bacillus anthracis protective antigen and lethal factor.Polylysine-mediated translocation of the diphtheria toxin catalytic domain through the anthrax protective antigen poreAntigen-specific CD8(+) T cells fail to respond to Shigella flexneri.A fragment of anthrax lethal factor delivers proteins to the cytosol without requiring protective antigen.Genetically modified anthrax lethal toxin safely delivers whole HIV protein antigens into the cytosol to induce T cell immunityAnthrax toxin: structures, functions and tumour targeting.Delivery of antibody mimics into mammalian cells via anthrax toxin protective antigenNAD+-Glycohydrolase Promotes Intracellular Survival of Group A Streptococcus.Molecular and biological characterization of Streptococcal SpyA-mediated ADP-ribosylation of intermediate filament protein vimentin.In vivo cytotoxic T lymphocyte elicitation by mycobacterial heat shock protein 70 fusion proteins maps to a discrete domain and is CD4(+) T cell independentModel of the toxic complex of anthrax: responsive conformational changes in both the lethal factor and the protective antigen heptamerAntigen delivered by anthrax lethal toxin induces the development of memory CD8+ T cells that can be rapidly boosted and display effector functions.Charge-dependent translocation of Bordetella pertussis adenylate cyclase toxin into eukaryotic cells: implication for the in vivo delivery of CD8(+) T cell epitopes into antigen-presenting cells.Identification of a His-Asp-Cys catalytic triad essential for function of the Rho inactivation domain (RID) of Vibrio cholerae MARTX toxin.Targeting HIV proteins to the major histocompatibility complex class I processing pathway with a novel gp120-anthrax toxin fusion proteinBoth CD4+ and CD8+ T cells respond to antigens fused to anthrax lethal toxin.NAIP proteins are required for cytosolic detection of specific bacterial ligands in vivo.Adjuvants in vaccines and for immunisation: current trends.Progress in the development of genetic immunization.Intracellular delivery of a cytolytic T-lymphocyte epitope peptide by pertussis toxin to major histocompatibility complex class I without involvement of the cytosolic class I antigen processing pathway.Cytotoxic T-lymphocyte epitopes fused to anthrax toxin induce protective antiviral immunity.NAIP-NLRC4 Inflammasomes Coordinate Intestinal Epithelial Cell Expulsion with Eicosanoid and IL-18 Release via Activation of Caspase-1 and -8.Trafficking of exogenous peptides into proteasome-dependent major histocompatibility complex class I pathway following enterotoxin B subunit-mediated delivery.
P2860
Q24562788-C2C673F0-ED0C-4B02-B7B5-C3A9199004F5Q26744720-590EAC0A-EAF1-492B-80B1-477445B31C9CQ27636113-928FF062-4CE9-4446-99B2-789793FE7DC9Q28189050-40447B65-AABF-4827-9063-3A0ACD88CD1CQ28475218-6CC48CE5-A604-422C-946C-91D96FC1814BQ33187111-98BDB720-4073-4007-9B52-031387A23ADAQ33264203-A05ED005-B950-4B34-9E71-2EA0AE860250Q33592070-59F850BB-5E65-4425-B2E5-638EABCCF76EQ33595975-54DA51A5-6475-4B98-A639-A6170A88E702Q33741147-4E32B6CC-5536-402F-B1E0-EB988A45027BQ33750314-91852E0B-DDA8-4659-B621-2EC56561FD48Q33764677-3F92AD20-9DB6-45D4-8E85-A88D0F3790EAQ33852549-D13B1638-7F5D-45DE-B87B-E30898B31B4DQ34075054-13A3DE70-5EC8-44A5-8CBF-1AA3167165DDQ34124112-96AB7EE1-2E34-430E-BFF8-448D1BBC1548Q34289944-46AAD3CA-6BD1-4E77-A951-4DBF7404B3D9Q34334277-3611F657-C63C-43E0-90CA-5F74DA40C5FBQ34433313-07A9019C-4EA0-4EC6-879D-5770B205C6A1Q34502790-A7B7E114-ABD8-44D6-827A-7BD0A8390ED0Q34931500-B2267625-6BEA-480F-B6CB-C9F8BC177DDAQ35143862-A0160DDE-524D-4EA8-B5CB-A562AB1AB0C1Q35174985-C3F92DCF-9BC3-4CF8-939A-8B1900661B01Q35184740-5AA97FE1-A7C5-434A-9DCF-91B44914836DQ35838335-5E0B6E98-2707-4077-B79C-05DBDB34BB8DQ35944727-9827AF5A-7135-4A33-A758-C58102225CDDQ36033302-D1DA7B64-5FDD-4DB9-BF2F-7F8FF6112ED6Q36375719-9F5F6769-CFF5-4028-9A83-2585861939C2Q36458615-53F0C204-441E-42EA-B2C3-16FBC159E4EFQ36483545-F466EED8-5D49-45E6-9459-A0641E7129C2Q36526152-8572899E-B3F4-4070-85EA-72A6F6A4ED61Q36526338-9526D4E2-BF26-4A38-9214-CFA63AAB57FDQ36635448-66371495-9944-40CC-8E60-B06CB988C69AQ36710762-46651FD6-4A2C-48F0-AAF0-68DFCC1DC3C3Q36863162-23988953-8153-462A-8306-B4D5C2297F8AQ36960502-30C140A3-776F-4DF8-BEFD-07BD6D59949AQ37316018-25F79F84-388F-42A5-BCCF-3720B3A43605Q39509568-AD8FAFA6-106D-422F-96A7-37F8EF3D0C5BQ39612918-E6108691-437F-4087-9207-FDDED5B21B8EQ40250344-A03DEA67-D71C-491E-8E2C-0E801E92898DQ40519775-B7C43558-A7BE-46C5-A1DE-039534E24ACB
P2860
Anthrax toxin-mediated delivery of a cytotoxic T-cell epitope in vivo.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on October 1996
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Anthrax toxin-mediated delivery of a cytotoxic T-cell epitope in vivo.
@en
Anthrax toxin-mediated delivery of a cytotoxic T-cell epitope in vivo.
@nl
type
label
Anthrax toxin-mediated delivery of a cytotoxic T-cell epitope in vivo.
@en
Anthrax toxin-mediated delivery of a cytotoxic T-cell epitope in vivo.
@nl
prefLabel
Anthrax toxin-mediated delivery of a cytotoxic T-cell epitope in vivo.
@en
Anthrax toxin-mediated delivery of a cytotoxic T-cell epitope in vivo.
@nl
P2860
P356
P1476
Anthrax toxin-mediated delivery of a cytotoxic T-cell epitope in vivo.
@en
P2093
J D Ballard
M N Starnbach
P2860
P304
12531-12534
P356
10.1073/PNAS.93.22.12531
P407
P577
1996-10-01T00:00:00Z