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Structural basis for the unfolding of anthrax lethal factor by protective antigen oligomers

Structural basis for the unfolding of anthrax lethal factor by protective antigen oligomers

http://www.wikidata.org/entity/Q27665492

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Tumor Targeting and Drug Delivery by Anthrax Toxin The Ins and Outs of Anthrax Toxin Obstructing toxin pathways by targeted pore blockage Bacillus anthracis edema factor substrate specificity: evidence for new modes of action Ratcheting up protein translocation with anthrax toxin Atomic structure of anthrax protective antigen pore elucidates toxin translocation Anthrax toxin protective antigen integrates poly- -D-glutamate and pH signals to sense the optimal environment for channel formation Domain Flexibility Modulates the Heterogeneous Assembly Mechanism of Anthrax Toxin Protective Antigen Characterization of Protein-Protein Interfaces through a Protein Contact Network Approach Tailored ß-cyclodextrin blocks the translocation pores of binary exotoxins from C. botulinum and C. perfringens and protects cells from intoxication Role of N-terminal His6-Tags in binding and efficient translocation of polypeptides into cells using anthrax protective antigen (PA)CCT chaperonin complex is required for efficient delivery of anthrax toxin into the cytosol of host cells Role of the α Clamp in the Protein Translocation Mechanism of Anthrax Toxin Monitoring the kinetics of the pH-driven transition of the anthrax toxin prepore to the pore by biolayer interferometry and surface plasmon resonance.Cross-reactivity of anthrax and C2 toxin: protective antigen promotes the uptake of botulinum C2I toxin into human endothelial cells Polylysine-mediated translocation of the diphtheria toxin catalytic domain through the anthrax protective antigen pore Interactions of anthrax lethal factor with protective antigen defined by site-directed spin labeling Engineering anthrax toxin variants that exclusively form octamers and their application to targeting tumors Trapping a translocating protein within the anthrax toxin channel: implications for the secondary structure of permeating proteins Mapping the epitopes of a neutralizing antibody fragment directed against the lethal factor of Bacillus anthracis and cross-reacting with the homologous edema factor Charge requirements for proton gradient-driven translocation of anthrax toxin Automated real-space refinement of protein structures using a realistic backbone move set.Ultrasensitive detection of protein translocated through toxin pores in droplet-interface bilayers Selection of nanobodies that block the enzymatic and cytotoxic activities of the binary Clostridium difficile toxin CDT Antibodies against anthrax: mechanisms of action and clinical applications.Supercharging protein complexes from aqueous solution disrupts their native conformations.An anthrax toxin variant with an improved activity in tumor targeting Translocation of Non-Canonical Polypeptides into Cells Using Protective Antigen NAD+-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.A d-Amino Acid at the N-Terminus of a Protein Abrogates Its Degradation by the N-End Rule Pathway.Electrostatic ratchet in the protective antigen channel promotes anthrax toxin translocation.Inhibiting bacterial toxins by channel blockage.Identification of novel host-targeted compounds that protect from anthrax lethal toxin-induced cell death.Solid tumor therapy by selectively targeting stromal endothelial cells.Anthrax toxin-induced rupture of artificial lipid bilayer membranes.Peptide- and proton-driven allosteric clamps catalyze anthrax toxin translocation across membranes.Structure of anthrax lethal toxin prepore complex suggests a pathway for efficient cell entry.Anthrax lethal toxin co-complexes are stabilized by contacts between adjacent lethal factors.Peptide Probes Reveal a Hydrophobic Steric Ratchet in the Anthrax Toxin Protective Antigen Translocase.

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P2860

Structural basis for the unfolding of anthrax lethal factor by protective antigen oligomers

http://www.wikidata.org/entity/Q27665492

description

2010 nî lūn-bûn

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2010 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

@zh-hk

2010年論文

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2010年論文

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2010年论文

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name

Structural basis for the unfol ...... y protective antigen oligomers

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Structural basis for the unfol ...... y protective antigen oligomers

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Structural basis for the unfol ...... y protective antigen oligomers

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Structural basis for the unfol ...... y protective antigen oligomers

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Structural basis for the unfol ...... y protective antigen oligomers

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Structural basis for the unfol ...... y protective antigen oligomers

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Structural basis for the unfol ...... y protective antigen oligomers

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Structural basis for the unfol ...... y protective antigen oligomers

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Nature Structural & Molecular Biology

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Structural basis for the unfol ...... y protective antigen oligomers

@en

P2093

Evan R Williams

http://www.w3.org/2001/XMLSchema#string

Harry J Sterling

http://www.w3.org/2001/XMLSchema#string

Iok I Tang

http://www.w3.org/2001/XMLSchema#string

Katie L Thoren

http://www.w3.org/2001/XMLSchema#string

Shoshana G Greenberg

http://www.w3.org/2001/XMLSchema#string

P2860

Structure of heptameric protective antigen bound to an anthrax toxin receptor: a role for receptor in pH-dependent pore formation

A model of anthrax toxin lethal factor bound to protective antigen.

MolProbity: all-atom contacts and structure validation for proteins and nucleic acids

Crystal structures of the HslVU peptidase-ATPase complex reveal an ATP-dependent proteolysis mechanism

Crystal structure of the anthrax lethal factor

Nucleotide-dependent conformational changes in a protease-associated ATPase HsIU

Structure of a delivery protein for an AAA+ protease in complex with a peptide degradation tag

X-ray structure of a protein-conducting channel

Structure of a complex of the ATPase SecA and the protein-translocation channel

The Protective Antigen Component of Anthrax Toxin Forms Functional Octameric Complexes

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1383-1390

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scholarly article

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4703602

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10.1038/NSMB.1923

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11

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P478

17

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Bryan A. Krantz

Geoffrey K Feld

Alexander F Kintzer

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2010-10-31T00:00:00Z

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47636262

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1037348056

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21037566

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structural biology

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3133606

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