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Articles by Fabiola Bonezzi in JoVE
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तैयारी और
Elisa Romeo1, Silvia Pontis1, Stefano Ponzano1, Fabiola Bonezzi1, Marco Migliore1, Simona Di Martino1, Maria Summa1, Daniele Piomelli1,2
1Drug Discovery and Development, Istituto Italiano di Tecnologia, 2Departments of Anatomy and Neurobiology, Pharmacology, and Biological Chemistry, University of California, Irvine School of Medicine
यहाँ, हम तैयार करने और एक गतिविधि आधारित जांच के उपयोग का वर्णन (ARN14686, undec-10-एन ynyl- - [(3 एस) -2-oxoazetidin-3-YL] carbamate) है कि पता लगाने और मात्रा का ठहराव के लिए अनुमति देता है proinflammatory एंजाइम एन -acylethanolamine एसिड amidase के सक्रिय रूप (naaa), दोनों इन विट्रो और पूर्व vivo में।
Other articles by Fabiola Bonezzi on PubMed
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A Glycosylated, Labionin-containing Lanthipeptide with Marked Antinociceptive Activity
ACS Chemical Biology.
Feb, 2014 |
Pubmed ID: 24191663 Among the growing family of ribosomally synthesized, post-translationally modified peptides, particularly intriguing are class III lanthipeptides containing the triamino acid labionin. In the course of a screening program aimed at finding bacterial cell wall inhibitors, we discovered a new lanthipeptide produced by an Actinoplanes sp. The molecule, designated NAI-112, consists of 22 amino acids and contains an N-terminal labionin and a C-terminal methyl-labionin. Unique among lanthipeptides, it carries a 6-deoxyhexose moiety N-linked to a tryptophan residue. Consistently, the corresponding gene cluster encodes, in addition to the LanKC enzyme characteristic of this lanthipeptide class, a glycosyl transferase. Despite possessing weak antibacterial activity, NAI-112 is effective in experimental models of nociceptive pain, reducing pain symptoms in mice in both the formalin and the chronic constriction injury tests. Thus, NAI-112 represents, after the labyrinthopeptins, the second example of a lanthipeptide effective against nociceptive pain.
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