Redox signaling and regulation in biology and medicine:
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| Sprache: | English |
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Weinheim
WILEY-VCH
2009
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| Beschreibung: | XXXIII, 481 S. Ill. |
| ISBN: | 9783527319251 |
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| 245 | 1 | 0 | |a Redox signaling and regulation in biology and medicine |c ed. by Claus Jacob ... |
| 264 | 1 | |a Weinheim |b WILEY-VCH |c 2009 | |
| 300 | |a XXXIII, 481 S. |b Ill. | ||
| 336 | |b txt |2 rdacontent | ||
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| 650 | 4 | |a Cellular signal transduction | |
| 650 | 4 | |a Oxidation-Reduction | |
| 650 | 4 | |a Oxidation-reduction reaction | |
| 650 | 4 | |a Oxidative Stress |x physiology | |
| 650 | 4 | |a Reactive Oxygen Species | |
| 650 | 4 | |a Signal Transduction | |
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Datensatz im Suchindex
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Titel: Redox signaling and regulation in biology and medicine
Autor: Jacob, Claus
Jahr: 2009
V
Contents
Preface XV
The Editors XVII
List of Authors XIX
1 Introduction 1
Claus Jacob and Paul C. Winyard
2 Biological Systems Relevant for Redox Signaling and Control 13
Thomas R. Hurd and Michael P. Murphy
2.1 Introduction 13
2.2 Reactive Oxygen Species 14
2.2.1 The Superoxide Radical 14
2.2.1.1 Generation of the Superoxide Radical 14
2.2.1.2 The Superoxide Radical as a Redox Signal 16
2.2.1.3 Decomposition of the Superoxide Radical 17
2.2.2 Hydrogen Peroxide 19
2.2.2.1 Generation of Hydrogen Peroxide 19
2.2.2.2 Mechanisms of Hydrogen Peroxide Signaling 20
2.2.2.3 Decomposition of Hydrogen Peroxide 27
2.3 Reactive Nitrogen Species 31
2.3.1 Nitric Oxide 31
2.3.1.1 Generation of Nitric Oxide 32
2.3.1.2 Mechanisms of Nitric Oxide Signaling 32
2.3.1.3 Decomposition of Nitric Oxide 32
2.3.2 Peroxynitrite and Reactive Nitrogen Species 33
2.3.2.1 Generation of Peroxynitrite and Other Important Reactive
Nitrogen Species 33
2.3.2.2 Mechanisms of Peroxynitrite- and Reactive Nitrogen Species-Mediated
Redox Signaling 34
Redox Signaling and Regulation in Biology and Medicine. Edited by Claus Jacob and Paul G. Winyard
Copyright © 2009 WILEY-VCH Verlag GmbH Co. KGaA, Weinheim
ISBN: 978-3-527-31925-1
VI Contents
2.4 lipid Peroxidation Products 36
2.4.1 Generation of lipid Peroxidation Products 36
2.4.2 Mechanisms of Signaling with lipid Peroxidation Products 37
2.4.3 Decomposition of lipid Peroxides 38
2.5 Conclusions 39
References 40
3 Cellular Generation of Oxidants: Relation to Oxidative Stress 45
Lars-Oliver Klotz and Helmut Sies
3.1 Introduction 45
3.2 Molecular Oxygen and Reactive Oxygen Species: Biochemical
Relations and Endogenous Sources 45
3.2.1 Endogenous Sources of Superoxide and Superoxide-Derived
Reactive Oxygen Species 46
3.2.2 Singlet Oxygen 50
3.2.3 "Secondary" Reactive Oxygen Species Generated in Radical Chain
Reactions 51
3.3 Generation of Oxidative Stress Under the Influence of Xenobiotics
and Stressful Stimuli 53
3.3.1 Quinones and Other Redox Cyders 53
3.3.2 Antioxidant Depletion by Alkylation: Acetaminophen Toxicity 56
3.3.3 Ultraviolet Radiation 57
3.3.4 Ultrafme or Nanoparticles 57
References 61
4 The Chemical Basis of Biological Redox Control 63
Claus Jacob, Mandy Doering, and Torsten Burkholz
4.1 Introduction 63
4.2 Forms fo Elemental Oxygen as Reactive Oxygen Species 67
4.2.1 Reactive Oxygen Species and Related Cellular Oxidants 67
4.2.2 Singlet Oxygen (lO2) 67
4.2.3 Ozone (O3) 71
4.3 Reduced, Yet Oxidizing: the Chemistry of Oxygen in Oxidation
States between 0 and -2 72
4.3.1 Superoxide Radicals (O2*~) 73
4.3.2 The Superoxide to Peroxide Conversion as a Key Event in Redox
Signaling 76
4.3.3 Hydrogen Peroxide (H2O2) 77
4.3.4 Hydroxyl Radicals (HO*) 79
4.3.5 Enzymatic Reduction of Hydrogen Peroxide by Peroxiredoxins,
Catalase and Glutathione Peroxidase 81
4.4 The Role of Labile Metal Ions in Oxidative Stress 84
4.5 Follow-on Species Generated by Chemical Interactions of Reactive
Oxygen Species 85
Contents VII
4.5.1 Hypochlorous Acid (HOC1) 86
4.5.2 Peroxynitrite (ONOO") 88
4.6 Nitrogen Monoxide and Reactive Nitrogen Species 91
4.6.1 Reactive Nitrogen Species 91
4.6.2 S-Nitrosothiols 95
4.7 Sulfur as a Prime Target of Oxidative Stress 98
A.I.I Thiol Groups in Peptides and Proteins 99
A.I.2 The Concept of Reactive Sulfur Species 101
4.7.3 Sulfur-Centered Radicals 103
A.7.A Disulfide-S-Oxides (RS(O)XSR') 306
4.7.5 Sulfenic and Sulfinic Acids (RSOH and RS(O)OH) 108
4.7.6 Oxidation of Methionine: Sulfoxides (RS(O)R) and Sulfones
(RS(O)2R') 109
4.7.7 S-Thiolation as Chemical Protection 110
4.7.8 Oxidation of Disulfides 111
4.8 A Brief Overview of Hydroxylation and Nitration
Reactions 112
4.8.1 Hydroxylation and Nitration of Aromatic Residues 113
4.8.2 Fatty Acid Chemistry 116
4.9 Conclusion 117
References 118
5 Protein Clutathiolation 123
Pietro Chezzi and Paolo Di Simplicio
5.1 Introduction: Glutathione - From Antioxidant to Redox
Signal 123
5.2 Glutathiolation 124
5.3 Mechanisms of Glutathiolation 127
5.3.1 ROS-Dependent Glutathiolation by Thiol/Disulfide Exchange
Reactions 129
5.3.2 ROS-Dependent Glutathiolation via Sulfenic Acid 130
5.3.3 ROS-Dependent Glutathiolation by Radical
Reactions 132
5.3.4 ROS-Independent Glutathiolation 133
5.4 Toxicological Aspects of Glutathiolation 133
5.5 Mechanisms of Deglutathiolation 135
5.6 Enzymes Implicated in Glutathiolation 136
5.7 Specificity of Glutathiolation 136
5.8 Genetic Factors Affecting Glutathiolation 137
5.8.1 Mouse Beta-Globin 137
5.8.2 Glucose-6-Phosphate Dehydrogenase Mutations 137
5.8.3 Glutathione S-Transferase Mutations 138
5.9 Future Perspectives 138
References 139
VIII Contents
6 Structure and Function of the Human Peroxiredoxin-Based
Antioxidant System: the Interplay between Peroxiredoxins,
Thioredoxins, Thioredoxin Reductases, Sulfiredoxins and
Sestrins 143
Katalin E. Szabo, Kirsty Line, Paul Eggleton, Jennifer A. Littlechild,
and Paul C. Winyard
6.1 Introduction 143
6.2 Peroxiredoxins 147
6.3 Thioredoxins 158
6.4 Thioredoxin Reductases 159
6.5 Sulfiredoxin and Sestrins 161
6.6 Regulation of the Expression and Activity of the Peroxiredoxin-Based
System Enzymes 163
6.7 Cell Signaling and the Peroxiredoxin-Based System: Regulation of
Transcription Factors, Cell Cycle and Apoptosis 166
6.8 Peroxiredoxin-Based System in Cells and Organs of the Body 170
6.9 Summary 173
References 174
7 Hydrogen Peroxide and Cysteine Protein Signaling Pathways 181
Ewald Schroder and Philip Eaton
7.1 Introduction 181
7.2 Hydrogen Peroxide Production in Cells and Tissues 182
7.3 Sources and Concentrations of Hydrogen Peroxide 183
7.4 Hydrogen Peroxide and the Formation of Secondary Oxidants such
as Peroxynitrite 184
7.5 Exogenous Hydrogen Peroxide as an Experimental Tool 186
7.6 Hydrogen Peroxide Sensing and Cysteine Sensors 188
7.7 Low Molecular Weight Oxidized Thiols and S-Thiolated Protein
Adducts 188
7.8 Protein Thiol Modifications 189
7.9 Protein Regulation via Sulfination-Dependent Proteolysis 190
References 192
8 Protein Tyrosine Phosphatases as Mediators of Redox Signaling 197
Jeroen den Heriog
8.1 Introduction 197
8.2 Protein Tyrosine Phosphatases 198
8.3 Protein Tyrosine Phosphatases are Sensitive to Oxidation 199
8.4 Allosteric Regulation of Receptor Protein Tyrosine Phosphatases
by Oxidation 200
8.5 Activation of Sdpl by Oxidation 202
8.6 Physiological Relevance of Protein Tyrosine Phosphatase Oxidation 203
8.7 Conclusions 204
References 204
Contents IX
9 Hypoxia-Induced Gene Regulation through Hypoxia Inducible
Factor-la 207
Adam J. Case and Frederick E. Domann
9.1 Introduction 207
9.2 The Proteins and Mechanism 208
9.3 Hypoxia Inducible Factor Target Genes 213
9.4 Non-Hypoxia-Induced Activation of Hypoxia Inducible
Factor 218
9.5 Diseases Involving Hypoxia Inducible Factor 220
9.6 The Promise of Hypoxia Inducible Factor-Targeted Therapies 223
9.7 Conclusions 226
References 226
10 Eicosanoid-Based Signaling 229
Valerie B. O'Donnell
10.1 Introduction 229
10.2 Biosynthesis and Structures of Eicosanoids 231
10.2.1 Lipoxygenases 234
10.2.2 Cyclooxygenases 235
10.2.3 Cytochrome P450 237
10.3 Signaling by Eicosanoids 239
10.4 Metabolism of Eicosanoids 240
10.5 Summary 242
References 243
11 Redox-Controlled Transcription Factors and Gene Expression 245
Gregory I. Giles
11.1 Introduction 245
11.2 Redox Signaling and Gene Microarry Data: The Global
Picture 248
11.3 The Antioxidant Response Element 251
11.4 The Transcription Factor Nrf2: The Master Regulator of Antioxidant
Transcription 253
11.5 The Keapl-Nrf2 Complex: A Sensor for Cellular Stress 255
11.5.1 Reactive Oxygen Species, Reactive Nitrogen Species and Electrophile
Sensing by Keapl 256
11.5.2 Structural Basis for the Sensing Function of the Keapl-Nrf2
Complex 257
11.6 Redox Reactions of Transcription Factors 261
11.6.1 Nuclear Factor kB: Redox Control of the Immune Response 262
11.6.2 Activator Protein 1 (AP-1): Redox Control of Proliferation and
Apoptosis 264
11.6.3 The Role of the Nuclear Redox State in Gene Expression 265
11.7 Summary 266
References 267
X Contents
12 Nitric Oxide Regulation in Redox Signaling 271
Dario A. Vitturi, David M. Krzywanski, Edward M. Postlethwait, and
Rakesh P. Patel
12.1 Introduction 271
12.2 Nitric Oxide Formation 271
12.3 Factors Affecting Nitric Oxide Reactivity and Signaling 272
12.3.1 Compartmentalization and Diffusion 272
12.3.2 Interaction with Metal Centers 274
12.3.3 Nitric Oxide Reaction with Free Radicals 276
12.3.3.1 Nitric Oxide and Superoxide 276
12.3.3.2 Peroxynitrite 278
12.3.3.3 Nitrogen Dioxide/Dinitrogen Trioxide 281
12.4 Nitric Oxide Signaling Beyond Soluble Guanylate Cyclase 281
12.4.1 Nitric Oxide and Mitochondria 282
12.4.2 S-Nitrosation 282
12.4.3 Nitrated Iipids 283
12.4.4 3-Nitrotyrosine 284
12.5 Redox Derivatives of Nitric Oxide 284
12.5.1 Nitroxyl Anion 285
12.5.2 Nitrite 285
12.5.3 Nitrite - a Potential Reservoir for Nitric Oxide Bioactivity
During Hypoxia 286
12.6 Summary 287
References 287
13 Is Hydrogen Sulfide a Regulator of Nitric Oxide Bioavailability
in the Vasculature? 293
Matthew Whiteman and Philip K. Moore
13.1 Introduction 293
13.2 Reactive Nitrogen Species 293
13.3 Reactive Nitrogen Species in the Heart and Vasculature 295
13.4 Hydrogen Sulfide Biosynthesis 296
13.5 Hydrogen Sulfide Measurement, Catabolism and Removal 300
13.6 Hydrogen Sulfide in the Heart and Vasculature 305
13.7 What is the Evidence for "Crosstalk" between Nitric Oxide
and Hydrogen Sulfide 309
13.8 Nitric Oxide/Hydrogen Sulfide and Evidence for the Formation
of A Novel Intermediate 312
13.9 Concluding Remarks 313
References 314
14 Aspects of Nox/Duox Signaling 317
Masuko Ushio-Fukai
14.1 Introduction 317
14.2 The Nox/Duox Enzymes (Expression and Domain Structure) 318
Contents XI
14.2.1 NOXO1 and NOXA1 322
14.3 Mechanism of the Nox/Duox Activation 322
14.3.1 Noxl 323
14.3.2 Nox3 324
14.3.3 Nox4 324
14.3.4 Nox5 324
14.3.5 Duox 325
14.4 Redox Signaling Activated by NADPH Oxidase 325
14.4.1 Activation of Kinases and Phospholipases 326
14.4.2 Activation of Ion Channels and Calcium Signaling 327
14.4.3 Oxidative Inactivation of Protein Tyrosine Phosphatase 328
14.4.4 Specific Localization of NADPH Oxidase as Mechanism of Activation
of Specific Redox Signaling 328
14.5 Transcription Factors and Gene Expression Regulated by ROS 330
14.5.1 NF-kB 331
14.5.2 AP-1 (c-Jun and c-Fos) 331
14.5.3 HIF-1 331
USA Ets 332
14.5.5 p53 332
14.6 Functional Role of Nox/Duox in Physiological and Pathophysiological
Functions 333
14.6.1 Function of Noxl 333
14.6.2 Function of Nox2 333
14.6.3 Function of Nox3 336
14.6.4 Function of Nox4 336
14.6.5 Function of Nox5 339
14.6.6 Function of Duox 340
14.7 Summary and Conclusions 340
References 341
15 Photodynamic Therapy with Aminolevulinic Acid and Iron Chelators:
A Clinical Example of Redox Signaling 351
Andrew Pye, Yuktee Dogra, Jessica Tyrrell, Paul Winyard, and
Alison Curnow
15.1 Photodynamic Therapy 351
15.2 The Development of Photodynamic Therapy 352
15.3 Aminolevulinic Acid Photodynamic Therapy 353
15.4 Heme Biosynthesis and Regulation During ALA-PDT 354
15.5 Iron and the Enhancement of ALA-PDT 356
15.6 Redox Signaling in Photodynamic Therapy after light
Irradiation 361
15.7 Photosensitizers as Reactive Oxygen Species Generators in
Redox Research 363
15.8 Reactive Oxygen Species Generation and Signaling in Clinical
Photodynamic Therapy 364
XII Contents
15.9 Apoptosis in Photodynamic Therapy 364
15.10 Subcellular Localization of Reactive Oxygen Species
Production 365
15.11 Changes in Transcription Factor and Protein Levels Following
Photodynamic Therapy 366
15.12 Iron and Iron Chelation Post light Activation of
Photosensitizer 367
15.13 Vascular Damage, Hypoxia and Hypoxia Inducible Factor 368
15.14 Conclusion 369
References 370
16 Oxidative Stress and Apoptosis 373
Silvia Cristofanon, Mario Dicato, Una Chibelli, and Marc Diederich
16.1 Apoptosis, The Programmed Destiny of a Cell 373
16.2 Historical Overview of the Relation Between Oxidative Stress and
Apoptosis 378
16.3 Oxidative Stress as a Mediator and Inducer of Apoptosis 378
References 382
17 Redox Regulation of Apoptosis in Immune Cells 385
Edith Charlier, Jacques Piette, and Geoffrey Cloire
17.1 Apoptosis, Necrosis and Autophagy 385
17.2 Apoptosis 386
17.2.1 Morphological and Biochemical Features of Apoptosis 386
17.2.2 Molecular Mechanisms of Apoptosis 386
17.2.2.1 The Major Players in Apoptosis 386
17.2.2.2 Main Pathways of Apoptosis 392
17.3 Redox Regulation of Apoptosis in Immune Cells 395
17.3.1 Induction of Apoptosis by Exogenous Reactive Oxygen Species 396
17.3.1.1 Reactive Oxygen Species Targets 396
17.3.1.2 Reactive Oxygen Species-Induced Apoptosis in Immune Cells 397
17.3.2 Control of Apoptosis by Endogenous Reactive Oxygen Species
Production 398
17.3.2.1 Cytokine Stimulation 398
17.3.2.2 Immune Receptor Stimulation 399
17.3.2.3 Granzyme A Delivery 402
17.3.2.4 Spontaneous and Bacteria-Induced Neutrophil Apoptosis 403
References 405
18 Redox Control in Human Disease with a Special Emphasis on the
Peroxiredoxin-Based Antioxidant System 409
Katalin E. Szabd, Nicholas J. Cutowski, Janet E. Holley, Jennifer A.
Littlechild, and Paul C. Winyard
18.1 Introduction 409
18.2 Inflammatory Diseases 410
Contents XIII
18.3 Neurodegenerative Diseases 414
18.4 Diseases of the Eye 418
18.5 Blood Disorders 419
18.6 Atherosclerosis and Cardiovascular Disease 420
18.7 Infections and Parasitic Diseases 421
18.8 Cancer 422
18.9 Proteins of the Peroxiredoxin-Based System as Diagnostic
and Prognostic Tools, and Potential Drug Targets 424
18.10 Conclusions 426
References 427
19 Free Radicals and Mammalian Aging 433
Alberto Sam, Gustavo Barja, Reinald Pamplona,
and Christiaan Leeuwenburgh
19.1 Introduction 433
19.2 The Mitochondrial Free Radical Theory of Aging 434
19.3 Why are Long-lived Animals so Long-Lived? Four Correlations
to Explain Longevity 435
19.3.1 Mitochondrial Free Radical Generation 436
19.3.2 Is Complex I the Major Determinant of Aging Rate? 438
19.3.2.1 Decrease in the Concentration of Respiratory Complexes 440
19.3.2.2 Modification of the Amino Acid Composition of Respiratory
Subunits 440
19.3.2.3 Posttranslational Modification of Specific Subunits 441
19.3.2.4 Changes in mtROS Production Without Altering the Electron
Transport Chain 442
19.3.3 The Unsaturation Degree of Membrane Fatty Acids 442
19.3.4 Methionine Content in Proteins 443
19.3.5 G + C Content in mtDNA 444
19.3.6 In Summary: Why are Long-Lived Animals So Long-lived? 444
19.4 Oxidative Damage to Macromolecules 446
19.4.1 Oxidative Damage to Carbohydrates 446
19.4.2 Oxidative Damage to Iipids 447
19.4.3 Oxidative Damage to Proteins 448
19.4.4 Oxidative Damage to DNA 449
19.4.5 The Importance of Mitochondrial DNA 450
19.5 Effects of Mitochondrial DNA Mutations on Cellular Function 452
19.5.1 Are There Exponential Increases in Free Radical Production
With Age? 452
19.5.2 Apoptosis 453
19.5.3 ATP Production 454
19.6 Trying to Increase the Maximum life Span 456
19.6.1 Antioxidants: The Great Hope, The Great Deception 456
19.6.2 Dietary Restriction: The Cheapest, The Best 458
19.6.3 Dietary Restriction and Reduction in Oxidative Stress 458
XIV Contents
19.6.4 How are Mitochondrial ROS Regulated During Dietary
Restriction? 460
19.6.4.1 Hormonal Regulation 461
19.6.4.2 Regulation of Mitochondrial ROS Production by Specific Dietary
Components: The Role of the Dietary Proteins and Methionine 462
References 464
Index 473 |
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| id | DE-604.BV035421918 |
| illustrated | Illustrated |
| indexdate | 2024-07-20T10:07:12Z |
| institution | BVB |
| isbn | 9783527319251 |
| language | English |
| oai_aleph_id | oai:aleph.bib-bvb.de:BVB01-017342426 |
| oclc_num | 271775099 |
| open_access_boolean | |
| owner | DE-20 DE-526 DE-11 DE-1029 |
| owner_facet | DE-20 DE-526 DE-11 DE-1029 |
| physical | XXXIII, 481 S. Ill. |
| publishDate | 2009 |
| publishDateSearch | 2009 |
| publishDateSort | 2009 |
| publisher | WILEY-VCH |
| record_format | marc |
| spelling | Redox signaling and regulation in biology and medicine ed. by Claus Jacob ... Weinheim WILEY-VCH 2009 XXXIII, 481 S. Ill. txt rdacontent n rdamedia nc rdacarrier Cellular signal transduction Oxidation-Reduction Oxidation-reduction reaction Oxidative Stress physiology Reactive Oxygen Species Signal Transduction Reaktive Sauerstoffspezies (DE-588)4236432-2 gnd rswk-swf Signaltransduktion (DE-588)4318717-1 gnd rswk-swf Reaktive Sauerstoffspezies (DE-588)4236432-2 s Signaltransduktion (DE-588)4318717-1 s DE-604 Jacob, Claus edt text/html http://deposit.dnb.de/cgi-bin/dokserv?id=3112917&prov=M&dok_var=1&dok_ext=htm Inhaltstext HBZ Datenaustausch application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=017342426&sequence=000004&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis |
| spellingShingle | Redox signaling and regulation in biology and medicine Cellular signal transduction Oxidation-Reduction Oxidation-reduction reaction Oxidative Stress physiology Reactive Oxygen Species Signal Transduction Reaktive Sauerstoffspezies (DE-588)4236432-2 gnd Signaltransduktion (DE-588)4318717-1 gnd |
| subject_GND | (DE-588)4236432-2 (DE-588)4318717-1 |
| title | Redox signaling and regulation in biology and medicine |
| title_auth | Redox signaling and regulation in biology and medicine |
| title_exact_search | Redox signaling and regulation in biology and medicine |
| title_full | Redox signaling and regulation in biology and medicine ed. by Claus Jacob ... |
| title_fullStr | Redox signaling and regulation in biology and medicine ed. by Claus Jacob ... |
| title_full_unstemmed | Redox signaling and regulation in biology and medicine ed. by Claus Jacob ... |
| title_short | Redox signaling and regulation in biology and medicine |
| title_sort | redox signaling and regulation in biology and medicine |
| topic | Cellular signal transduction Oxidation-Reduction Oxidation-reduction reaction Oxidative Stress physiology Reactive Oxygen Species Signal Transduction Reaktive Sauerstoffspezies (DE-588)4236432-2 gnd Signaltransduktion (DE-588)4318717-1 gnd |
| topic_facet | Cellular signal transduction Oxidation-Reduction Oxidation-reduction reaction Oxidative Stress physiology Reactive Oxygen Species Signal Transduction Reaktive Sauerstoffspezies Signaltransduktion |
| url | http://deposit.dnb.de/cgi-bin/dokserv?id=3112917&prov=M&dok_var=1&dok_ext=htm http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=017342426&sequence=000004&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA |
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