LEADER 05568nam 2200709 450 001 9910812642303321 005 20200520144314.0 010 $a1-118-32963-5 010 $a1-118-32966-X 010 $a1-118-32965-1 035 $a(CKB)3710000000215625 035 $a(EBL)1758510 035 $a(SSID)ssj0001414945 035 $a(PQKBManifestationID)11803838 035 $a(PQKBTitleCode)TC0001414945 035 $a(PQKBWorkID)11440207 035 $a(PQKB)11676145 035 $a(MiAaPQ)EBC1758510 035 $a(Au-PeEL)EBL1758510 035 $a(CaPaEBR)ebr10905962 035 $a(CaONFJC)MIL635791 035 $a(OCoLC)886112272 035 $a(PPN)189677309 035 $a(EXLCZ)993710000000215625 100 $a20140819h20142014 uy 0 101 0 $aeng 135 $aur|n|---||||| 181 $ctxt 182 $cc 183 $acr 200 00$aRecent advances in polyphenol research$hVolume 4 /$fedited by Annalisa Romani, Vincenzo Lattanzio, Stephane Quideau ; contributors Nickolas A. Anderson [and twenty eight others] 210 1$aChichester, England :$cWiley Blackwell,$d2014. 210 4$dİ2014 215 $a1 online resource (468 p.) 225 1 $aRecent Advances in Polyphenol Research 300 $aDescription based upon print version of record. 311 $a1-118-32967-8 320 $aIncludes bibliographical references at the end of each chapters and index. 327 $aCover; Title Page; Copyright; Acknowledgments; Contents; Contributors; Preface; Chapter 1 Monolignol Biosynthesis and its Genetic Manipulation: The Good, the Bad, and the Ugly; 1.1 Introduction; 1.2 Function and distribution of lignin in plants; 1.3 Targets for modification of lignin biosynthesis; 1.3.1 Gene targets 1. Biosynthetic enzymes; 1.3.1.1 L-phenylalanine ammonia-lyase (PAL); 1.3.1.2 Cinnamate 4-hydroxylase (C4H); 1.3.1.3 4-coumarate: coenzyme-A ligase (4CL); 1.3.1.4 Enzymes of the coumaroyl shikimate shunt; 1.3.1.5 Caffeoyl-CoA 3-O-methyltransferase (CCoAOMT) 327 $a1.3.1.6 Ferulate 5-hydroxylase (F5H)1.3.1.7 Caffeic acid 3-O-methyltransferase (COMT); 1.3.1.8 Cinnamoyl-CoA reductase; 1.3.1.9 Cinnamyl alcohol dehydrogenase (CAD); 1.3.2 Gene targets 2. Transcription factors; 1.4 Impacts of lignin modification through targeting of the monolignol biosynthetic pathway; 1.4.1 L-phenylalanine ammonia-lyase (PAL); 1.4.2 Cinnamate 4-hydroxylase (C4H); 1.4.3 4-coumarate: coenzyme-A ligase (4CL); 1.4.4 Hydroxycinnamoyl-CoA: shikimate hydroxycinnamoyl transferase (HCT); 1.4.5 4-coumaroyl shikimate 3'-hydroxylase (C3'H) 327 $a1.4.6 Caffeoyl CoA 3-O-methyltransferase (CCoAOMT)1.4.7 Ferulate 5-hydroxylase (F5H); 1.4.8 Caffeic acid O-methyltransferase (COMT); 1.4.9 Cinnamoyl-CoA reductase (CCR); 1.4.10 Cinnamyl alcohol dehydrogenase (CAD); 1.5 Impacts of lignin modification through targeting of TFs; 1.5.1 NAC master switches; 1.5.2 MYB repressors of monolignol biosynthesis; 1.5.3 WRKY repressors of lignification in pith; 1.6 Monolignol pathway modification and plant growth; 1.7 Conclusions: it isn't all that bad!; References 327 $aChapter 2 Perturbing Lignin Biosynthesis: Metabolic Changes in Response to Manipulation of the Phenylpropanoid Pathway2.1 Introduction; 2.1.1 Cell wall-bound phenylpropanoids; 2.1.2 Soluble phenylpropanoids; 2.2 Changes in metabolism associated with phenylpropanoid-pathway disruptions; 2.2.1 Phenylalanine ammonia-lyase (PAL); 2.2.2 Cinnamate 4-hydroxylase (C4H); 2.2.3 4-coumarate: CoA ligase (4CL); 2.2.4 Hydroxycinnamoyl-coenzyme A: shikimate/quinate hydroxycinnamoyltransferase (HCT)/p-coumaroyl shikimate 3'-hydroxylase (C3'H); 2.2.5 Cinnamoyl CoA reductase (CCR) 327 $a2.2.6 Ferulate 5-hydroxylase (F5H)2.2.7 Caffeic acid/5-hydroxyferulic acid O-methyltransferase (COMT)/caffeoyl CoA 3-O-methyltransferase (CCoAOMT); 2.2.8 Cinnamyl alcohol dehydrogenases (CAD); 2.3 Atypical lignins; 2.4 Dwarfism; 2.5 Conclusions; References; Chapter 3 Function, Structure, and Evolution of Flavonoid Glycosyltransferases in Plants; 3.1 Introduction; 3.2 UDP-dependent glycosyltransferases; 3.2.1 Functional identification of flavonoid UGTs; 3.2.1.1 Flavonoid 3-O-glycosyltransferases; 3.2.1.2 Flavonoid 7-O-glycosyltransferases 327 $a3.2.1.3 Flavonoid glycosyltransferases that glycosylate the sugar moiety attached to a flavonoid aglycone 330 $a Plant polyphenols are secondary metabolites that constitute one of the most common and widespread groups of natural products. They express a large and diverse panel of biological activities including beneficial effects on both plants and humans. Many polyphenols, from their structurally simplest representatives to their oligo/polymeric versions (also referred to as vegetable tannins) are notably known as phytoestrogens, plant pigments, potent antioxidants, and protein interacting agents. Sponsored by the scholarly society Groupe Polyphe?nols, this publication, which is the fourth volume in th 410 0$aRecent Advances in Polyphenol Research 606 $aBotanical chemistry$vCongresses 606 $aPolyphenols$vCongresses 615 0$aBotanical chemistry 615 0$aPolyphenols 676 $a581.192 702 $aRomani$b Annalisa 702 $aLattanzio$b V$g(Vincenzo), 702 $aQuideau$b Ste?phane 702 $aAnderson$b Nickolas A. 801 0$bMiAaPQ 801 1$bMiAaPQ 801 2$bMiAaPQ 906 $aBOOK 912 $a9910812642303321 996 $aRecent advances in polyphenol research$9720466 997 $aUNINA