Literature DB >> 18064414

Presynaptic neurotoxins with enzymatic activities.

Ornella Rossetto1, Cesare Montecucco.   

Abstract

Toxins that alter neurotransmitter release from nerve terminals are of considerable scientific and clinical importance. Many advances were recently made in the understanding of their molecular mechanisms of action and use in human therapy. Here, we focus on presynaptic neurotoxins, which are very potent inhibitors of the neurotransmitter release because they are endowed with specific enzymatic activities: (1) clostridial neurotoxins with a metallo-proteolytic activity and (2) snake presynaptic neurotoxins with a phospholipase A2 activity.

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Year:  2008        PMID: 18064414     DOI: 10.1007/978-3-540-74805-2_6

Source DB:  PubMed          Journal:  Handb Exp Pharmacol        ISSN: 0171-2004


  18 in total

1.  Es kann die Spur von unseren Erdetagen--on pharmacologists and pharmacology.

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Review 2.  Obstructing toxin pathways by targeted pore blockage.

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3.  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.

Authors:  Aaron A Thompson; Guan-Sheng Jiao; Seongjin Kim; April Thai; Lynne Cregar-Hernandez; Stephen A Margosiak; Alan T Johnson; Gye Won Han; Sean O'Malley; Raymond C Stevens
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4.  Mitochondrial alarmins released by degenerating motor axon terminals activate perisynaptic Schwann cells.

Authors:  Elisa Duregotti; Samuele Negro; Michele Scorzeto; Irene Zornetta; Bryan C Dickinson; Christopher J Chang; Cesare Montecucco; Michela Rigoni
Journal:  Proc Natl Acad Sci U S A       Date:  2015-01-20       Impact factor: 11.205

Review 5.  Therapeutic use of botulinum toxin in migraine: mechanisms of action.

Authors:  Roshni Ramachandran; Tony L Yaksh
Journal:  Br J Pharmacol       Date:  2014-09       Impact factor: 8.739

6.  Localization of the sites and characterization of the mechanisms by which anti-light chain antibodies neutralize the actions of the botulinum holotoxin.

Authors:  Tsuyoshi Takahashi; Suresh G Joshi; Fetweh Al-Saleem; Denise Ancharski; Ajay Singh; Zidoon Nasser; Lance L Simpson
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Review 7.  Translocation of botulinum neurotoxin light chain protease by the heavy chain protein-conducting channel.

Authors:  Mauricio Montal
Journal:  Toxicon       Date:  2008-12-14       Impact factor: 3.033

8.  Snake phospholipase A2 neurotoxins enter neurons, bind specifically to mitochondria, and open their transition pores.

Authors:  Michela Rigoni; Marco Paoli; Eva Milanesi; Paola Caccin; Andrea Rasola; Paolo Bernardi; Cesare Montecucco
Journal:  J Biol Chem       Date:  2008-09-22       Impact factor: 5.157

9.  Potent neutralization of botulinum neurotoxin/B by synergistic action of antibodies recognizing protein and ganglioside receptor binding domain.

Authors:  Changchun Chen; Shuhui Wang; Huajing Wang; Xiaoyan Mao; Tiancheng Zhang; Guanghui Ji; Xin Shi; Tian Xia; Weijia Lu; Dapeng Zhang; Jianxin Dai; Yajun Guo
Journal:  PLoS One       Date:  2012-08-29       Impact factor: 3.240

10.  Botulinum neurotoxins A and E undergo retrograde axonal transport in primary motor neurons.

Authors:  Laura Restani; Francesco Giribaldi; Maria Manich; Kinga Bercsenyi; Guillermo Menendez; Ornella Rossetto; Matteo Caleo; Giampietro Schiavo
Journal:  PLoS Pathog       Date:  2012-12-27       Impact factor: 6.823

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