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010   $a3-030-00853-3
024 7 $a10.1007/978-3-030-00853-6
035   $a(CKB)4100000006999362
035   $a(MiAaPQ)EBC5534440
035   $a(DE-He213)978-3-030-00853-6
035   $a(PPN)231462220
035   $a(EXLCZ)994100000006999362
100   $a20181001d2018      u|         0
101 0 $aeng
135   $aurcnu||||||||
181   $ctxt$2rdacontent
182   $cc$2rdamedia
183   $acr$2rdacarrier
200 10$aGold(I,III) Complexes Designed for Selective Targeting and Inhibition of Zinc Finger Proteins /$fby Raphael Enoque Ferraz de Paiva
205   $a1st ed. 2018.
210  1$aCham :$cSpringer International Publishing :$cImprint: Springer,$d2018.
215   $a1 online resource (184 pages)
225 1 $aSpringer Theses, Recognizing Outstanding Ph.D. Research,$x2190-5053
311   $a3-030-00852-5 
327   $aAu(I)-phosphine series design -- Probing the Protein: Ion Mobility Spectrometry -- Probing Gold: X-ray Absorption Spectroscopy -- Probing Cells: Cytotoxicity Evaluation -- Au(III) series with k2C,N and k2N,N' ligands -- "Dual Probe" X-ray Absorption Spectroscopy.
330   $aThis book examines Au (I, III) complexes that selectively attack and inhibit zinc finger proteins (ZnFs) for potential therapeutic use. The author explores gold(I)-phosphine, gold(III) complexes with N^N and C^N donors as inhibitors of the HIV-1 nucleocapsid protein (NCp7), in comparison to the human transcription factor Sp1. To determine the coordination sphere of the gold adducts formed by interaction with ZnFs, two innovative approaches are used, based on Travelling-Wave Ion Mobility coupled with Mass Spectrometry (TWIM-MS), and X-ray Absorption Spectroscopy. Both approaches are proven to yield valuable structural information regarding the coordination sphere of gold in the adducts. In addition, the organometallic compound [Au (bnpy)Cl2] is evaluated. The system is shown to be capable of inhibiting ZnFs by means of C?S coupling.
410  0$aSpringer Theses, Recognizing Outstanding Ph.D. Research,$x2190-5053
606   $aInorganic chemistry
606   $aOrganometallic chemistry 
606   $aProteins 
606   $aMass spectrometry
606   $aBioorganic chemistry
606   $aImmunology
606   $aInorganic Chemistry$3https://scigraph.springernature.com/ontologies/product-market-codes/C16008
606   $aOrganometallic Chemistry$3https://scigraph.springernature.com/ontologies/product-market-codes/C19020
606   $aProtein-Ligand Interactions$3https://scigraph.springernature.com/ontologies/product-market-codes/L14060
606   $aMass Spectrometry$3https://scigraph.springernature.com/ontologies/product-market-codes/C11010
606   $aBioorganic Chemistry$3https://scigraph.springernature.com/ontologies/product-market-codes/C19010
606   $aImmunology$3https://scigraph.springernature.com/ontologies/product-market-codes/B14000
615  0$aInorganic chemistry.
615  0$aOrganometallic chemistry .
615  0$aProteins .
615  0$aMass spectrometry.
615  0$aBioorganic chemistry.
615  0$aImmunology.
615 14$aInorganic Chemistry.
615 24$aOrganometallic Chemistry.
615 24$aProtein-Ligand Interactions.
615 24$aMass Spectrometry.
615 24$aBioorganic Chemistry.
615 24$aImmunology.
676   $a571.845
700   $aFerraz de Paiva$b Raphael Enoque$4aut$4http://id.loc.gov/vocabulary/relators/aut$01059031
906   $aBOOK
912   $a9910298584603321
996   $aGold(I,III) Complexes Designed for Selective Targeting and Inhibition of Zinc Finger Proteins$92503745
997   $aUNINA