T
Thomas Binz
Researcher at Hochschule Hannover
Publications - 109
Citations - 11203
Thomas Binz is an academic researcher from Hochschule Hannover. The author has contributed to research in topics: Synaptobrevin & Synaptic vesicle. The author has an hindex of 50, co-authored 107 publications receiving 10718 citations. Previous affiliations of Thomas Binz include University of Giessen & University of California, Irvine.
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Journal ArticleDOI
Neutralisation of specific surface carboxylates speeds up translocation of botulinum neurotoxin type B enzymatic domain
Marco Pirazzini,Tina Henke,Ornella Rossetto,Stefan Mahrhold,Nadja Krez,Andreas Rummel,Cesare Montecucco,Thomas Binz +7 more
TL;DR: This triple mutant showed increased neurotoxicity due to faster cytosolic delivery of the enzymatic domain; membrane translocation could take place at less acidic pH, and neutralisation of specific negative surface charges facilitates membrane contact permitting a faster initiation of the toxin membrane insertion.
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Inhibition of botulinum neurotoxins interchain disulfide bond reduction prevents the peripheral neuroparalysis of botulism.
Giulia Zanetti,Domenico Azarnia Tehran,Marcon Pirazzini,Thomas Binz,Clifford C. Shone,Silvia Fillo,Florigio Lista,Ornella Rossetto,Cesare Montecucco +8 more
TL;DR: The present data demonstrate the essential role of the thiOREDoxin-thioredoxin reductase system in reducing the interchain disulfide during the nerve intoxication mechanism of all serotypes and its inhibitors should be considered for a possible use to prevent botulism and for treating infant botulisms.
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The thioredoxin reductase – Thioredoxin redox system cleaves the interchain disulphide bond of botulinum neurotoxins on the cytosolic surface of synaptic vesicles
Marco Pirazzini,Domenico Azarnia Tehran,Giulia Zanetti,Florigio Lista,Thomas Binz,Clifford C. Shone,Ornella Rossetto,Cesare Montecucco +7 more
TL;DR: It is found that thioredoxin 1 and its reductase compose the cell redox system responsible for this reduction, and its inhibition via specific chemicals significantly reduces BoNTs activity, in vitro as well as in vivo.
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Time course and temperature dependence of the membrane translocation of tetanus and botulinum neurotoxins C and D in neurons.
Marco Pirazzini,Ornella Rossetto,Cristina Bertasio,Fulvio Bordin,Clifford C. Shone,Thomas Binz,Cesare Montecucco +6 more
TL;DR: The temperature dependence and time course of the entry of the L chain of tetanus neurotoxin and of botulinum neurotoxin type C and D across the plasma membrane of cerebellar granular neurons is studied to study the contribution of the membrane translocation step to the total time to paralysis and to the low toxicity of these neurotoxins in cold-blood vertebrates.
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Identification and Characterization of Botulinum Neurotoxin A Substrate Binding Pockets and Their Re-Engineering for Human SNAP-23
Stefan Sikorra,Christa Litschko,Carina Müller,Nadine Thiel,Thierry Galli,Timo Eichner,Thomas Binz +6 more
TL;DR: The reason for the resistance of human SNAP-23, an isoform of SNAP-25, is examined by mutational analyses and it is shown that replacement of 10 SNAP- 23 residues with their SNAP-24 counterparts effects SNAP- 25-like cleavability.