Unique substrate recognition by botulinum neurotoxins serotypes A and E. - Wikidata - awgldk - TriplyDB

Unique substrate recognition by botulinum neurotoxins serotypes A and E.

Unique substrate recognition by botulinum neurotoxins serotypes A and E.

http://www.wikidata.org/entity/Q53636622

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SNAP-25 Substrate Peptide (Residues 180-183) Binds to but Bypasses Cleavage by Catalytically Active Clostridium botulinum Neurotoxin E Substrate Binding Mode and Its Implication on Drug Design for Botulinum Neurotoxin A A Single-Domain Llama Antibody Potently Inhibits the Enzymatic Activity of Botulinum Neurotoxin by Binding to the Non-Catalytic α-Exosite Binding Region Structural Characterization of Three Novel Hydroxamate-Based Zinc Chelating Inhibitors of the Clostridium botulinum Serotype A Neurotoxin Light Chain Metalloprotease Reveals a Compact Binding Site Resulting from 60/70 Loop Flexibility Botulinum neurotoxin A protease: discovery of natural product exosite inhibitors Light chain separated from the rest of the type a botulinum neurotoxin molecule is the most catalytically active form.Identification of a Natural Product Antagonist against the Botulinum Neurotoxin Light Chain Protease Exocytosis at the hair cell ribbon synapse apparently operates without neuronal SNARE proteins.Improved detection of botulinum neurotoxin serotype A by Endopep-MS through peptide substrate modification.Small-molecule quinolinol inhibitor identified provides protection against BoNT/A in mice.Association of botulinum neurotoxin serotype A light chain with plasma membrane-bound SNAP-25 Cleavage of SNAP25 and its shorter versions by the protease domain of serotype A botulinum neurotoxin.In vitro detection and quantification of botulinum neurotoxin type e activity in avian blood Accelerated intoxication of GABAergic synapses by botulinum neurotoxin A disinhibits stem cell-derived neuron networks prior to network silencing.Towards new uses of botulinum toxin as a novel therapeutic tool Cargo-delivery platforms for targeted delivery of inhibitor cargos against botulism.Differential gene expression and functional analysis implicate novel mechanisms in enteric nervous system precursor migration and neuritogenesis.Comparison of the catalytic properties of the botulinum neurotoxin subtypes A1 and A5.Substrate-based inhibitors exhibiting excellent protective and therapeutic effects against Botulinum Neurotoxin A intoxication The SNARE complex from yeast is partially unstructured on the membrane.The C terminus of the catalytic domain of type A botulinum neurotoxin may facilitate product release from the active site Engineering botulinum neurotoxin to extend therapeutic intervention.Receptor and substrate interactions of clostridial neurotoxins.Toxins from bacteria.Clostridial neurotoxins: mechanism of SNARE cleavage and outlook on potential substrate specificity reengineering.The blockade of the neurotransmitter release apparatus by botulinum neurotoxins.Challenges in searching for therapeutics against Botulinum Neurotoxins.Substrate recognition mechanism of VAMP/synaptobrevin-cleaving clostridial neurotoxins.Substrate recognition of VAMP-2 by botulinum neurotoxin B and tetanus neurotoxin.Ultrasensitive detection of protease activity of anthrax and botulinum toxins by a new PCR-based assay.Further optimization of peptide substrate enhanced assay performance for BoNT/A detection by MALDI-TOF mass spectrometry.Glycine insertion at protease cleavage site of SNAP25 resists cleavage but enhances affinity for botulinum neurotoxin serotype A.Optimization of peptide substrates for botulinum neurotoxin E improves detection sensitivity in the Endopep-MS assay.Unique substrate recognition mechanism of the botulinum neurotoxin D light chain Detection and quantification of botulinum neurotoxin type a by a novel rapid in vitro fluorimetric assay.Probing BoNT/A protease exosites: implications for inhibitor design and light chain longevity Insights into the different catalytic activities of Clostridium neurotoxins Augmentation of VAMP-catalytic activity of botulinum neurotoxin serotype B does not result in increased potency in physiological systems.A label free colorimetric assay for the detection of active botulinum neurotoxin type A by SNAP-25 conjugated colloidal gold.Catalytic properties of botulinum neurotoxin subtypes A3 and A4.

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Unique substrate recognition by botulinum neurotoxins serotypes A and E.

http://www.wikidata.org/entity/Q53636622

description

2006 nî lūn-bûn

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2006年の論文

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2006年学术文章

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2006年学术文章

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2006年学术文章

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2006年学术文章

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2006年学术文章

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2006年學術文章

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2006年學術文章

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2006年學術文章

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Unique substrate recognition by botulinum neurotoxins serotypes A and E.

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Unique substrate recognition by botulinum neurotoxins serotypes A and E.

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type

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Unique substrate recognition by botulinum neurotoxins serotypes A and E.

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Unique substrate recognition by botulinum neurotoxins serotypes A and E.

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Unique substrate recognition by botulinum neurotoxins serotypes A and E.

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Unique substrate recognition by botulinum neurotoxins serotypes A and E.

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Journal of Biological Chemistry

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Unique substrate recognition by botulinum neurotoxins serotypes A and E.

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P2093

Joseph T Barbieri

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P2860

SWISS-MODEL: An automated protein homology-modeling server

Slow- and fast-binding inhibitors of thermolysin display different modes of binding: crystallographic analysis of extended phosphonamidate transition-state analogues

Mechanism of action of tetanus and botulinum neurotoxins

Proteolysis of SNAP-25 isoforms by botulinum neurotoxin types A, C, and E: domains and amino acid residues controlling the formation of enzyme-substrate complexes and cleavage

Management of botulism.

New insights into clostridial neurotoxin-SNARE interactions.

Synaptotagmins I and II mediate entry of botulinum neurotoxin B into cells.

Intestinal infection and toxin production by Clostridium botulinum as one cause of sudden infant death syndrome.

Beta-blocker-induced complications and the patient with glaucoma. Newer treatments to help reduce systemic adverse events.

[Botulism: the agent, mode of action of the botulinum neurotoxins, forms of acquisition, treatment and prevention].

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10906-10911

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10.1074/JBC.M513032200

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