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000141238 0247_ $$2doi$$a10.1016/j.bmc.2012.06.026
000141238 0247_ $$2pmid$$apmid:22795751
000141238 0247_ $$2ISSN$$a0968-0896
000141238 0247_ $$2ISSN$$a1464-3391
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000141238 037__ $$aDZNE-2020-07560
000141238 041__ $$aEnglish
000141238 082__ $$a610
000141238 1001_ $$aFiorino, Ferdinando$$b0
000141238 245__ $$aSynthesis of benzamide derivatives and their evaluation as antiprion agents.
000141238 260__ $$aAmsterdam [u.a.]$$bElsevier$$c2012
000141238 264_1 $$2Crossref$$3print$$bElsevier BV$$c2012-08-01
000141238 3367_ $$2DRIVER$$aarticle
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000141238 520__ $$aA new set of 5-(2-(pyrrolidin-1-yl)acetamido)-N-butyl-2-(substituted)benzamide and 5-(2-(piperidin-1-yl)acetamido)-N-butyl-2-(substituted) benzamide derivatives were synthesized in which as structural features the 2-(1-pyrrolidinyl)- or 2-(1-piperidyl)acetylamino group or a diphenylether moiety are associated to a benzamide scaffold. Their binding affinity for human PrP(C) and inhibition of its conversion into PrP(Sc) were determined in vitro; moreover, the antiprion activity was assayed by inhibition of PrP(Sc) accumulation in scrapie-infected mouse neuroblastoma cells (ScN2a) and scrapie mouse brain (SMB) cells. The results clearly indicate the benzamide derivatives as attractive lead compounds for the development of potential therapeutic agents against prion disease.
000141238 536__ $$0G:(DE-HGF)POF3-342$$a342 - Disease Mechanisms and Model Systems (POF3-342)$$cPOF3-342$$fPOF III$$x0
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000141238 650_7 $$2NLM Chemicals$$aBenzamides
000141238 650_7 $$2NLM Chemicals$$aPrions
000141238 650_7 $$2NLM Chemicals$$aRecombinant Proteins
000141238 650_7 $$06X80438640$$2NLM Chemicals$$abenzamide
000141238 650_2 $$2MeSH$$aAnimals
000141238 650_2 $$2MeSH$$aBenzamides: chemical synthesis
000141238 650_2 $$2MeSH$$aBenzamides: chemistry
000141238 650_2 $$2MeSH$$aBenzamides: pharmacology
000141238 650_2 $$2MeSH$$aCell Line
000141238 650_2 $$2MeSH$$aDose-Response Relationship, Drug
000141238 650_2 $$2MeSH$$aHumans
000141238 650_2 $$2MeSH$$aMice
000141238 650_2 $$2MeSH$$aMolecular Structure
000141238 650_2 $$2MeSH$$aPrions: antagonists & inhibitors
000141238 650_2 $$2MeSH$$aPrions: metabolism
000141238 650_2 $$2MeSH$$aRecombinant Proteins: antagonists & inhibitors
000141238 650_2 $$2MeSH$$aRecombinant Proteins: metabolism
000141238 650_2 $$2MeSH$$aScrapie: drug therapy
000141238 650_2 $$2MeSH$$aScrapie: metabolism
000141238 650_2 $$2MeSH$$aStructure-Activity Relationship
000141238 7001_ $$aEiden, Martin$$b1
000141238 7001_ $$0P:(DE-HGF)0$$aGiese, Armin$$b2
000141238 7001_ $$aSeverino, Beatrice$$b3
000141238 7001_ $$aEsposito, Antonella$$b4
000141238 7001_ $$aGroschup, Martin H$$b5
000141238 7001_ $$aPerissutti, Elisa$$b6
000141238 7001_ $$aMagli, Elisa$$b7
000141238 7001_ $$aIncisivo, Giuseppina Maria$$b8
000141238 7001_ $$aCiano, Antonio$$b9
000141238 7001_ $$aFrecentese, Francesco$$b10
000141238 7001_ $$0P:(DE-HGF)0$$aKretzschmar, Hans A$$b11
000141238 7001_ $$0P:(DE-2719)2662292$$aWagner, Jens$$b12$$udzne
000141238 7001_ $$aSantagada, Vincenzo$$b13
000141238 7001_ $$0P:(DE-HGF)0$$aCaliendo, Giuseppe$$b14$$eCorresponding author
000141238 77318 $$2Crossref$$3journal-article$$a10.1016/j.bmc.2012.06.026$$b : Elsevier BV, 2012-08-01$$n16$$p5001-5011$$tBioorganic & Medicinal Chemistry$$v20$$x0968-0896$$y2012
000141238 773__ $$0PERI:(DE-600)1501507-5$$a10.1016/j.bmc.2012.06.026$$gVol. 20, no. 16, p. 5001 - 5011$$n16$$p5001-5011$$q20:16<5001 - 5011$$tBioorganic & medicinal chemistry$$v20$$x0968-0896$$y2012
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