LEADER 00974nam a22002531i 4500 001 991004198679707536 005 20020826103352.0 008 020826s1907 fr |||||||||||||||||fre 035 $ab11937270-39ule_inst 035 $aARCHE-002709$9ExL 040 $aDip.to Filologia Ling. e Lett.$bita$cA.t.i. Arché s.c.r.l. Pandora Sicilia s.r.l. 100 1 $aBedier, Joseph$0396701 245 14$aLes deux poemes de La Folie Tristan /$cpublies par Joseph Bedier 246 13$aFolie Tristan 260 $aParis :$bF. Didot,$c1907 300 $aVII, 126 p. ;$c24 cm 490 0 $aSociete des anciens textes français 650 4$aRomanzo arturiano 907 $a.b11937270$b28-04-17$c01-04-03 912 $a991004198679707536 945 $aLE008 FL.M. (f.r.) XIV 102$g1$i2008000420024$lle008$o-$pE0.00$q-$rn$so $t0$u0$v0$w0$x0$y.i12211151$z01-04-03 996 $aDeux poemes de La Folie Tristan$9913470 997 $aUNISALENTO 998 $ale008$b01-04-03$cm$da $e-$ffre$gfr $h4$i1 LEADER 05430nam 22007214a 450 001 9911018824503321 005 20200520144314.0 010 $a9786610748822 010 $a9781280748820 010 $a1280748826 010 $a9780470764275 010 $a0470764279 010 $a9780470988879 010 $a0470988878 010 $a9781405173070 010 $a1405173076 035 $a(CKB)1000000000341810 035 $a(EBL)284294 035 $a(SSID)ssj0000222365 035 $a(PQKBManifestationID)11187861 035 $a(PQKBTitleCode)TC0000222365 035 $a(PQKBWorkID)10171218 035 $a(PQKB)11000358 035 $a(MiAaPQ)EBC284294 035 $a(OCoLC)184983460 035 $a(Perlego)2751245 035 $a(EXLCZ)991000000000341810 100 $a20060320d2006 uy 0 101 0 $aeng 135 $aur|n|---||||| 181 $ctxt 182 $cc 183 $acr 200 00$aPlant proteomics /$fedited by Christine Finnie 210 $aOxford, UK ;$aAmes, Iowa $cBlackwell Pub.$d2006 215 $a1 online resource (276 p.) 225 1 $aAnnual plant reviews ;$vv. 28 300 $aDescription based upon print version of record. 311 08$a9781405144292 311 08$a1405144297 320 $aIncludes bibliographical references and index. 327 $aPlant Proteomics; Contents; Preface; Contributors; 1 Plant proteomics: challenges and resources; 1.1 Introduction; 1.2 Challenges; 1.2.1 Sample extraction; 1.2.1.1 Two-dimensional gel electrophoresis; 1.2.1.2 Direct MS analysis of samples; 1.2.2 Sample preparation and arraying; 1.2.2.1 Two-dimensional gel electrophoresis; 1.2.2.2 One-dimensional gel electrophoresis; 1.2.2.3 Blue-native gel electrophoresis; 1.2.2.4 Direct analysis of samples by MS; 1.2.3 Mass spectrometry (MALDI and ESI); 1.2.3.1 MALDI; 1.2.3.2 ESI; 1.2.4 Analysis depth; 1.2.5 Data analysis; 1.2.5.1 Peptide mass fingerprints 327 $a1.2.5.2 Peptide fragmentation data (MS/MS)1.2.5.3 Analysis options; 1.2.6 Quantitation; 1.2.6.1 Gel stains; 1.2.6.2 Chemical labelling of sample; 1.2.7 Modifications; 1.2.8 Data; 1.3 Resources; 1.3.1 Proteomic databases; 1.3.2 Online proteomic tools and resources; 1.4 Future; 2 Proteomic analysis of post-translational modifications by mass spectrometry; 2.1 Summary; 2.2 Introduction; 2.3 Considerations for the experimental design of PTM analysis by proteomics; 2.4 Analysis of PTMs by proteomic approaches; 2.4.1 Phosphorylation; 2.4.2 Protein glycosylation; 2.4.3 GPI-AP; 2.4.4 Farnesylation 327 $a2.4.5 N-terminally modified proteins2.5 Conclusions and perspectives; 3 Strategies for the investigation of protein-protein interactions in plants; 3.1 Summary; 3.2 Introduction; 3.3 Biochemical procedures to characterize protein-protein interactions; 3.3.1 Chromatographic purifications; 3.3.2 Sucrose gradient ultrafiltration; 3.3.3 Native gel electrophoresis; 3.3.4 Immunoprecipitations; 3.4 Genetic procedures to characterize protein-protein interactions; 3.4.1 Yeast two-hybrid system; 3.4.2 Yeast three-hybrid system; 3.4.3 Yeast one-hybrid system 327 $a3.4.4 Limitations of yeast two-hybrid systems3.4.5 Split-ubiquitin system; 3.4.6 Bimolecular fluorescence complementation (BiFC); 3.4.7 Fo?rster resonance energy transfer (FRET); 3.4.8 Tagging technologies for the purification of protein complexes; 3.5 Cytological procedures to characterize protein-protein interactions; 3.6 Outlook; 4 Proteomics of disulphide and cysteine oxidoreduction; 4.1 Introduction; 4.2 Control of cellular redox status; 4.2.1 Sequence and structural features of proteins catalysing cysteine redox modifications; 4.2.2 Catalytic mechanisms of Trxs and Grxs 327 $a4.3 Proteomics techniques for analysis of cysteine modifications4.3.1 Reagents for cysteine labelling; 4.3.2 Disulphide mapping; 4.3.3 S-glutathionylation; 4.3.4 Cysteine SOH, SO2H and SO3H; 4.3.5 Trxs and disulphide reduction; 4.3.6 S-nitrosylation; 4.4 Conclusions and perspectives; 5 Structural proteomics; 5.1 Introduction; 5.2 Project data handling: Sesame; 5.3 ORF cloning; 5.4 E. coli cell-based protein production pipeline; 5.4.1 Large-scale protein production and labeling; 5.4.2 Protein purification; 5.5 Wheat germ cell-free protein production 327 $a5.6 Mass spectrometry of purified proteins for quality assurance and analysis 330 $aThe proteome comprises all protein species resulting from gene expression in a cell, organelle, tissue or organism. By definition, proteomics aims to identify and characterise the expression pattern, cellular location, activity, regulation, post-translational modifications, molecular interactions, three dimensional structures and functions of each protein in a biological system.In plant science, the number of proteome studies is rapidly expanding after the completion of the Arabidopsis thaliana genome sequence, and proteome analyses of other important or emerging model systems and crop 410 0$aAnnual plant reviews ;$vv. 28. 606 $aPlant proteins 606 $aPlant proteomics 615 0$aPlant proteins. 615 0$aPlant proteomics. 676 $a572/.62 686 $a42.42$2bcl 701 $aFinnie$b Christine$0863228 801 0$bMiAaPQ 801 1$bMiAaPQ 801 2$bMiAaPQ 906 $aBOOK 912 $a9911018824503321 996 $aPlant proteomics$91926951 997 $aUNINA