Fusions of anthrax toxin lethal factor with shiga toxin and diphtheria toxin enzymatic domains are toxic to mammalian cells.
about
Binary bacterial toxins: biochemistry, biology, and applications of common Clostridium and Bacillus proteinsTumor Targeting and Drug Delivery by Anthrax ToxinObstructing toxin pathways by targeted pore blockageStructural basis for the unfolding of anthrax lethal factor by protective antigen oligomersOverall view of chemical and biochemical weaponsInjection of Staphylococcus aureus EDIN by the Bacillus anthracis protective antigen machinery induces vascular permeability.Mutational analysis of the enzymatic domain of Clostridium difficile toxin B reveals novel inhibitors of the wild-type toxinImaging specific cell surface protease activity in living cells using reengineered bacterial cytotoxinsProtective antigen-mediated antibody response against a heterologous protein produced in vivo by Bacillus anthracisCytolethal distending toxin B as a cell-killing component of tumor-targeted anthrax toxin fusion proteins.Expression and purification of the recombinant lethal factor of Bacillus anthracisAnthrax toxin as a molecular tool for stimulation of cytotoxic T lymphocytes: disulfide-linked epitopes, multiple injections, and role of CD4(+) cells.Oligomerization of anthrax toxin protective antigen and binding of lethal factor during endocytic uptake into mammalian cells.A conserved motif in transmembrane helix 1 of diphtheria toxin mediates catalytic domain delivery to the cytosol.Prodrug applications for targeted cancer therapy.Channel-forming bacterial toxins in biosensing and macromolecule deliveryPotent antitumor activity of a urokinase-activated engineered anthrax toxin.Polylysine-mediated translocation of the diphtheria toxin catalytic domain through the anthrax protective antigen poreCisplatin inhibition of anthrax lethal toxin.Delivery of antibody mimics into mammalian cells via anthrax toxin protective antigenAn anthrax toxin variant with an improved activity in tumor targetingTranslocation of Non-Canonical Polypeptides into Cells Using Protective AntigenNAD+-Glycohydrolase Promotes Intracellular Survival of Group A Streptococcus.From structure to solutions: the role of basic research in developing anthrax countermeasures: Microbiology Graduate Program Seminar: Anthrax toxin.Internalization of a Bacillus anthracis protective antigen-c-Myc fusion protein mediated by cell surface anti-c-Myc antibodies.COPI coatomer complex proteins facilitate the translocation of anthrax lethal factor across vesicular membranes in vitro.Recombinant expression and purification of a tumor-targeted toxin in Bacillus anthracisTargeting HIV proteins to the major histocompatibility complex class I processing pathway with a novel gp120-anthrax toxin fusion proteinOrganometallic palladium reagents for cysteine bioconjugationCharacterization of the interaction between anthrax toxin and its cellular receptorsAnthrax toxin-mediated delivery of the Pseudomonas exotoxin A enzymatic domain to the cytosol of tumor cells via cleavable ubiquitin fusions.Anthrax toxin-mediated delivery of a cytotoxic T-cell epitope in vivo.Potent neutralization of anthrax edema toxin by a humanized monoclonal antibody that competes with calmodulin for edema factor binding.Novel chimpanzee/human monoclonal antibodies that neutralize anthrax lethal factor, and evidence for possible synergy with anti-protective antigen antibody.Bacterial toxins deliver the goods.Fused polycationic peptide mediates delivery of diphtheria toxin A chain to the cytosol in the presence of anthrax protective antigen.Evidence that translocation of anthrax toxin's lethal factor is initiated by entry of its N terminus into the protective antigen channel.Reductive methylation and mutation of an anthrax toxin fusion protein modulates its stability and cytotoxicity.ACTIN-DIRECTED TOXIN. ACD toxin-produced actin oligomers poison formin-controlled actin polymerization.Changing the receptor specificity of anthrax toxin.
P2860
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P2860
Fusions of anthrax toxin lethal factor with shiga toxin and diphtheria toxin enzymatic domains are toxic to mammalian cells.
description
1994 nî lūn-bûn
@nan
1994 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
Fusions of anthrax toxin letha ...... are toxic to mammalian cells.
@ast
Fusions of anthrax toxin letha ...... are toxic to mammalian cells.
@en
Fusions of anthrax toxin letha ...... are toxic to mammalian cells.
@nl
type
label
Fusions of anthrax toxin letha ...... are toxic to mammalian cells.
@ast
Fusions of anthrax toxin letha ...... are toxic to mammalian cells.
@en
Fusions of anthrax toxin letha ...... are toxic to mammalian cells.
@nl
prefLabel
Fusions of anthrax toxin letha ...... are toxic to mammalian cells.
@ast
Fusions of anthrax toxin letha ...... are toxic to mammalian cells.
@en
Fusions of anthrax toxin letha ...... are toxic to mammalian cells.
@nl
P2860
P1476
Fusions of anthrax toxin letha ...... are toxic to mammalian cells.
@en
P2093
P2860
P304
P407
P577
1994-11-01T00:00:00Z