LEADER 05826nam 2200697Ia 450 001 9910453096903321 005 20200520144314.0 010 $a1-299-44822-4 010 $a90-272-7212-3 035 $a(CKB)2550000001018486 035 $a(EBL)1163757 035 $a(SSID)ssj0000856570 035 $a(PQKBManifestationID)12299290 035 $a(PQKBTitleCode)TC0000856570 035 $a(PQKBWorkID)10817914 035 $a(PQKB)10022045 035 $a(MiAaPQ)EBC1163757 035 $a(Au-PeEL)EBL1163757 035 $a(CaPaEBR)ebr10685284 035 $a(CaONFJC)MIL476072 035 $a(OCoLC)839545002 035 $a(EXLCZ)992550000001018486 100 $a20130118d2013 uy 0 101 0 $aeng 135 $aur|n|---||||| 181 $ctxt 182 $cc 183 $acr 200 00$aPatterns and meanings in discourse$b[electronic resource] $etheory and practice in corpus-assisted discourse studies (CADS) /$fAlan Partington, Alison Duguid, Charlotte Taylor 210 $aAmsterdam $cJohn Benjamins Publishing Company$d2013 215 $a1 online resource (385 p.) 225 1 $aStudies in Corpus Linguistics ;$v55 300 $aDescription based upon print version of record. 311 $a90-272-0360-1 320 $aIncludes bibliographical references and index. 327 $aPatterns and Meanings in Discourse; Editorial page; Title page; LCC data; Table of contents; Acknowledgements; Introduction; 0.1 Discourse and discourse analysis; 0.2 Corpus linguistics; 0.2.1 What it is and what it does; 0.2.2 Quantity, frequency, comparison and recurrence (or patterning); 0.2.3 Serendipity; 0.3 Corpus-assisted discourse studies or CADS; 0.3.1 Definition and aims; 0.3.2 A comparison between traditional corpus linguistics and CADS; 0.4 The corpora and tools for analysing corpora; 0.4.1 The corpora; 0.4.2 Corpus annotation; 0.4.3 Tools for analysing corpora 327 $a0.5 Guide to the contents of this bookThe two principles of discourse organisation; 1.1 Introduction; 1.2 Grammatical organisation; 1.2.1 Open choice; 1.2.2 The idiom principle and coselection; 1.2.3 Issues with idioms; 1.3 Script theory; 1.3.1 Learning and memory; 1.3.2 Understanding discourse; 1.4 Inductive knowledge-driven reasoning; 1.4.1 Needs, goals and plans; 1.5 Parallels; 1.5.1 Open choice and logical induction: Rule-driven behaviour; 1.5.2 The idiom and the script principles: Lexical priming; 1.6 Conclusion; Evaluation in discourse communication 327 $a2.1 For good and for bad, for better and for worse2.2 Point of view; 2.3 Evaluation working in discourse; 2.4 Categories of evaluative lexis; 2.5 Note: The evaluator and evaluative voices; 2.6 Evaluation and cohesion; evaluative consistency or harmony; 2.7 Evaluative prosody; 2.8 Embedding and nesting; 2.9 Conclusion; Suggestions for further Research; Evaluation and control; 3.1 Control: The linguistic unit; 3.2 Control and power relations; 3.3 The control feature and evaluative prosody: Examples; 3.3.1 Set in; 3.3.2 Sit through; 3.3.3 Undergo; 3.3.4 Budge; 3.3.5 Persistence/Persistent 327 $a3.3.6 Break out3.3.7 Outbreak; 3.3.8 End up; 3.3.9 Cause; 3.3.10 Fuel; 3.3.11 Fickle and flexible; 3.3.12 Orchestrate; 3.3.13 True feelings; 3.4 Conclusions; Investigating Rhetoric in Discourse 1; Utterance irony; 4.1 Irony explicit and implicit; 4.2 Suitability of data; 4.3 Case study 1: Explicit irony; 4.3.1 What is irony? Ask the people; 4.3.2 The evaluator; 4.3.3 Reversal of evaluation; 4.4 Case study 2: Implicit irony; 4.4.1 Using corpus techniques to find episodes of implicit irony; 4.4.2 Reversal of evaluation in implicit irony; 4.4.3 Verisimilar ironies: Litotes 327 $a4.4.4 Irony in questions4.5 Conclusions on explicit and implicit irony; Phrasal irony; 4.6 Case study 3: The form, function and exploitation of phrasal irony; 4.7 Evaluative clash with the phrase; 4.8 Evaluative oxymoron; 4.9 Substitution by evaluative opposite in well-known phrases; 4.10 The "popularisation" of the ironic usage of a phrase; 4.11 Replacing an expected negative element of the template with something positive; 4.12 Replacing an expected positive element of the template with something negative; 4.13 How such ironic uses become popular 327 $a4.14 A final twist: When is evaluative reversal ironic clash and when simply a counter-instance? 330 $aThis work is designed, firstly, to both provoke theoretical discussion and serve as a practical guide for researchers and students in the field of corpus linguistics and, secondly, to offer a wide-ranging introduction to corpus techniques for practitioners of discourse studies. It delves into a wide variety of language topics and areas including metaphor, irony, evaluation, (im)politeness, stylistics, language change and sociopolitical issues. Each chapter begins with an outline of an area, followed by case studies which attempt both to shed light on particular themes in this area and to demon 410 0$aStudies in Corpus Linguistics ;$v55. 606 $aComputational linguistics 606 $aEnglish language$xResearch$xData processing 606 $aEnglish language$xDiscourse analysis$xData processing 606 $aEnglish language$xStudy an371d teaching$xData processing 608 $aElectronic books. 615 0$aComputational linguistics. 615 0$aEnglish language$xResearch$xData processing. 615 0$aEnglish language$xDiscourse analysis$xData processing. 615 0$aEnglish language$xStudy an371d teaching$xData processing. 676 $a420.1/88 701 $aPartington$b Alan$0132894 801 0$bMiAaPQ 801 1$bMiAaPQ 801 2$bMiAaPQ 906 $aBOOK 912 $a9910453096903321 996 $aPatterns and meanings in discourse$91973982 997 $aUNINA LEADER 01451nam 2200397 n 450 001 996388965103316 005 20221107143824.0 035 $a(CKB)1000000000646461 035 $a(EEBO)2240919645 035 $a(UnM)99863722 035 $a(EXLCZ)991000000000646461 100 $a19930617d1648 uy | 101 0 $aeng 135 $aurbn||||a|bb| 200 12$aA letter of vnity tending, generally to a peace$b[electronic resource] $eespecially to that betweene Presbyterian Independent opinion. 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W$01001805 801 0$bCu-RivES 801 1$bCu-RivES 801 2$bCStRLIN 801 2$bWaOLN 906 $aBOOK 912 $a996388965103316 996 $aA letter of vnity tending, generally to a peace$92299404 997 $aUNISA LEADER 07393nam 2200673Ia 450 001 9910437615103321 005 20200520144314.0 010 $a3-642-36260-5 024 7 $a10.1007/978-3-642-36260-6 035 $a(CKB)2560000000104176 035 $a(SSID)ssj0000880102 035 $a(PQKBManifestationID)11484785 035 $a(PQKBTitleCode)TC0000880102 035 $a(PQKBWorkID)10872267 035 $a(PQKB)10250461 035 $a(DE-He213)978-3-642-36260-6 035 $a(MiAaPQ)EBC1206118 035 $a(PPN)169139212 035 $a(EXLCZ)992560000000104176 100 $a20130506d2013 uy 0 101 0 $aeng 135 $aurnn|008mamaa 181 $ctxt 182 $cc 183 $acr 200 00$aSpringer handbook of enzymes$b[electronic resource] $hSupplement volume S10$iClass 3.4-6 hydrolases, lyases, isomerases, ligases $eEC 3.4-6 /$fDietmar Schomburg, Ida Schomburg (eds.) ; coedited by Antje Chang 205 $a2nd ed. 210 $aBerlin ;$aNew York $cSpringer$dc2013 215 $a1 online resource (XVIII, 691 p.) 225 1 $aSpringer handbook of enzymes ;$vSuppl. vol. S10 300 $aBibliographic Level Mode of Issuance: Monograph 311 $a3-642-43792-3 311 $a3-642-36259-1 320 $aIncludes bibliographical references. 327 $a3.4.11.24 aminopeptidase S -- 3.4.17.23 angiotensin-converting enzyme 2 -- 3.4.22.69 SARS coronavirus main proteinase -- 3.4.22.70 sortase A -- 3.4.22.71 sortase B -- 3.4.23.50 human endogenous retrovirus K Endopeptidase -- 3.4.23.51 HycI peptidase -- 3.4.24.87 ADAMTS13 endopeptidase -- 3.4.25.2 HslU-HslV peptidase -- 3.5.1.99 fatty acid amide hydrolase -- 3.5.1.100 (R)-amidase -- 3.5.1.101 L-proline amide hydrolase -- 3.5.1.102 2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5?- monophosphate deformylase -- 3.5.1.103 N-acetyl-1-D-myo-inositol-2-amino-2-deoxy-a- D-glucopyranoside deacetylase -- 3.5.1.104 peptidoglycan-N-acetylglucosamine Deacetylase -- 3.5.1.105 chitin disaccharide deacetylase -- 3.5.1.106 N-formylmaleamate deformylase -- 3.5.1.107 maleamate amidohydrolase -- 3.5.1.108 UDP-3-O-acyl-N-acetylglucosamine Deacetylase -- 3.5.2.19 streptothricin hydrolase -- 3.5.99.8 5-nitroanthranilic acid aminohydrolase -- 3.6.1.53 Mn2+-dependent ADP-ribose/CDP-alcohol Diphosphatase -- 3.6.1.54 UDP-2,3-diacylglucosamine diphosphatase -- 3.6.4.12 DNA helicase -- 3.6.4.13 RNA helicase -- 3.7.1.11 cyclohexane-1,2-dione hydrolase -- 3.7.1.12 cobalt-precorrin 5A hydrolase -- 3.7.1.13 -hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4- dienoate hydrolase -- 4.1.1.87 malonyl-S-ACP decarboxylase -- 4.1.1.88 biotin-independent malonate decarboxylase -- 4.1.1.89 biotin-dependent malonate decarboxylase -- 4.1.1.90 peptidyl-glutamate 4-carboxylase -- 4.1.2.43 3-hexulose-6-phosphate synthase -- 4.1.2.44 benzoyl-CoA-dihydrodiol lyase -- 4.1.2.45 trans-o-hydroxybenzylidenepyruvate hydratase-aldolase -- 4.1.2.46 aliphatic (R)-hydroxynitrile lyase -- 4.1.3.41 3-hydroxy-D-aspartate aldolase -- 4.1.99.13 (6-4)DNA photolyase -- 4.1.99.14 spore photoproduct lyase -- 4.1.99.15 S-specific spore photoproduct lyase -- 4.2.1.114 methanogen homoaconitase -- 4.2.1.115 UDP-N-acetylglucosamine 4,6-dehydratase (inverting) -- 4.2.1.116 3-hydroxypropionyl-CoA dehydratase -- 4.2.1.117 2-methylcitrate dehydratase (2-methyl-transaconitate forming) -- 4.2.1.118 3-dehydroshikimate dehydratase -- 4.2.1.119 enoyl-CoA hydratase 2 -- 4.2.1.120 4-hydroxybutanoyl-CoA dehydratase -- 4.2.1.121 colneleate synthase -- 4.2.3.28 ent-cassa-12,15-diene synthase -- 4.2.3.29 ent-sandaracopimaradiene synthase -- 4.2.3.30 ent-pimara-8(14),15-diene synthase -- 4.2.3.31 ent-pimara-9(11),15-diene synthase -- 4.2.3.32 levopimaradiene synthase -- 4.2.3.33 stemar-13-ene synthase -- 4.2.3.34 stemod-13(17)-ene synthase -- 4.2.3.35 syn-pimara-7,15-diene synthase -- 4.2.3.36 terpentetriene synthase -- 4.2.3.37 epi-isozizaene synthase -- 4.2.3.38 a-bisabolene synthase -- 4.2.3.39 epi-cedrol synthase -- 4.2.3.40 (Z)-g-bisabolene synthase -- 4.2.3.41 elisabethatriene synthase -- 4.2.3.42 aphidicolan-16b-ol synthase -- 4.2.3.43 fusicocca-2,10(14)-diene synthase -- 4.2.3.44 isopimara-7,15-diene synthase -- 4.2.3.45 phyllocladan-16a-ol synthase -- 4.2.3.46 a-farnesene synthase -- 4.2.3.47 b-farnesene synthase -- 4.2.3.48 (3S,6E)-nerolidol synthase -- 4.2.3.49 (3R,6E)-nerolidol synthase -- 4.2.99.20 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase -- 4.2.99.21 isochorismate lyase -- 4.3.1.26 chromopyrrolate synthase -- 4.3.1.27 threo-3-hydroxy-D-aspartate ammonia-lyase -- 4.3.99.2 carboxybiotin decarboxylase -- 4.99.1.8 heme ligase -- 5.1.99.5 hydantoin racemase -- 5.3.1.27 6-phospho-3-hexuloisomerase -- 5.3.1.28 D-sedoheptulose 7-phosphate isomerase -- 5.5.1.14 syn-copalyl-diphosphate synthase -- 5.5.1.15 terpentedienyl-diphosphate synthase -- 5.5.1.16 halimadienyl-diphosphate synthase -- 5.99.1.4 2-hydroxychromene-2-carboxylate isomerase -- 6.1.1.27 O-phospho-L-serine-tRNA ligase -- 6.2.1.35 ACP-SH:acetate ligase -- 6.2.1.36 3-hydroxypropionyl-CoA synthase -- 6.3.1.13 L-cysteine:1D-myo-inositol 2-amino-2-deoxy-a-D-glucopyranoside ligase -- 6.3.1.14 diphthine-ammonia ligase -- 6.3.2.31 coenzyme F420-0:L-glutamate ligase -- 6.3.2.32 coenzyme g-F420-2:a-L-glutamate ligase -- 6.3.2.33 coenzyme g-F420-2:a-L-glutamate ligase -- 6.3.2.33 tetrahydrosarcinapterin synthase -- 6.3.2.34 coenzyme F420-1:g-L-glutamate ligase -- 6.3.2.35 D-alanine-D-serine ligase -- 6.3.2.36 4-phosphopantoate-b-alanine ligase. 330 $aSpringer Handbook of Enzymes provides data on enzymes sufficiently well characterized. It offers concise and complete descriptions of some 5,000 enzymes and their application areas. Data sheets are arranged in their EC-Number sequence and the volumes themselves are arranged according to enzyme classes. This new, second edition reflects considerable progress in enzymology: many enzymes are newly classified or reclassified. Each entry is correlated with references and one or more source organisms. New datafields are created: application and engineering (for the properties of enzymes where the sequence has been changed). The total amount of material contained in the Handbook has more than doubled so that the complete second edition consists of 39 volumes as well as a Synonym Index. In addition, starting in 2009, all newly classified enzymes are treated in Supplement Volumes. 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