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Response from Facchiano, Innamorati and Luini
No full textCoffield et al. discuss three hypotheses that have been proposed recently for the mode of action of the clostridial neurotoxins. They conclude that the mechanism of toxin action suggested by Schiavo et al. ‘v2, that is, by proteolytic cleavage of essential synaptic proteins, is supported by substantial evidence and explains toxin-induced neuroparalysis elegantly. By contrast, they suggest that there are reasons to be cautious about the other two hypotheses, which implicate the enzymes transglutaminase (TGase)“,4 and phospholipase A, (PLA,)’ in the neuroparalytic effects of the toxins. We could not agree more about the power and elegance of the proteolytic mechanism first demonstrated by Cesare Montecucco and colleagues, and later confirmed by Link et aL6. Indeed, we believe that their idea that the short-term effects of clostridial toxins depend on the proteolysis of proteins essential for exocytosis’ is sound, and will be rapidly and universally accepted
Bioinformatics for Proteomics: developing new tools for the analysis of experimental data
No full textTransglutaminases: future perspectives
No full textThis is the third special issue focused on "Transglutaminases" that is now available on this journal and dedicated to one of the pioneers of these enzymes, John Edward Folk, who died December 2010 [see in this issue Beninati et al. 2012a]. The first edition, "Polyamines and Transglutaminases" was published in Amino Acids, vol 26, no. 4, 2004, with the contribution of two prestigious Guest Editors as Alberto Abbruzzese and Mauro Piacentini. This editorial initiative was followed by the second special issue published in occasion of the 50th years of the discovery of transglutaminase. Indeed, "Transglutaminase 2: 50th Anniversary of the Discovery" Amino Acids, vol 36, no. 4, 2009, was published with the valuable collaboration of Carlo Maria Bergamini and Mauro Piacentini (Beninati et al. 2009). To continue with this editorial tradition, on this occasion, an outstanding board of Guest Editors composed by Francesco Facchiano and Mauro Piacentini has also been invited to promote this initiative and recruit a selected panel of Authors, many of who participated in the first and second edition of the Gordon Conference on Transglutaminases: "Transglutaminases in Human Diseases Processes" chaired by Rickard L Eckert and Kapil Mehta on July 18-23, 2010, and by Kapil Mehta and Mauro Piacentini on July 15-20, 2012, held at Davidson College, NC, USA. In this Amino Acids special issue, the manuscripts were selected to reflect the progress and the future perspectives of transglutaminases
Regeneration of trasected cortico-spinal tract axons is promoted by the combined application of recombinant vascular endothelial growth factor (VEGF) and adenovirus coding for VEGF
No full textEffect of temperature on the propylamine transferase from Sulfolobus solfataricus, an extreme thermophilic archaebacterium. 1. Conformational behavior of the oligomeric enzyme in solution
No full textEffect of temperature on the propylamine transferase from Sulfolobus solfataricus, an extreme thermophilic archaebacterium. 2. Denaturation and structural stability
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The transglutaminase hypothesis for the action of tetanus toxin
No full textTetanus toxin potently and almost irreversibly inhibits the release of neurotransmitters from nerve terminals. The toxin binds to and activates transglutaminase, a Ca2+-dependent enzyme that can form stable crosslinks between substrate proteins. Transglutaminase is present in nerve terminals and recognizes synapsin I, an abundant synaptic vesicle phosphoprotein involved in neurotransmission, as an excellent substrate. The neuroparalytic action of tetanus toxin might be due, at least in part, to the stimulation of synaptic transglutaminase and the consequent crosslinking of synapsin I. © 1993
Thermodynamic analysis of the temperature effect on the conformational behaviour of propylaminetransferase from Sulfolobus solfataricus
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