Оглавление
Andrew H. Cobb. Herbicides and Plant Physiology
Table of Contents
List of Tables
List of Illustrations
Guide
Pages
Herbicides and Plant Physiology
Preface
References
Chapter 1 An Introduction to Weed Biology
1.1 Introduction
1.2 Distribution
1.3 The importance of weeds
1.4 Problems caused by weeds
1.4.1 Yield losses
1.4.2 Interference with crop management and handling
1.4.3 Reduction in crop quality
1.4.4 Weeds as reservoirs for pests and diseases
1.5 Biology of weeds
1.5.1 Growth strategies
1.5.2 Germination time
1.5.3 Germination depth
1.5.4 Method of pollination
1.5.5 Seed numbers
1.5.6 Seed dispersal
1.5.7 Dormancy and duration of viability
1.5.8 Plasticity of weed growth
1.5.9 Photosynthetic pathways
1.5.10 Vegetative reproduction
1.6 A few examples of problem weeds
1.7 Positive attributes of weeds
1.8 The ever‐changing weed spectrum
1.9 Weed control
1.9.1 Traditional methods
1.9.2 Chemical methods
1.9.3 An integrated approach
1.9.3.1 Cultural methods
1.9.3.2 Alternative methods
1.9.3.3 Precision weed control
1.9.3.4 Conservation agriculture
References
Chapter 2 Herbicide Discovery and Development
2.1 Introduction
2.2 Markets
2.3 Prospects
2.4 Environmental impact and relative toxicology
2.5 Chemophobia
2.6 The search for novel active ingredients
2.7 The search for novel target sites
2.8 Mode of action studies
2.9 The role of natural chemistry
2.10 Recent developments
2.11 A lower limit for rates of herbicide application?
References
Chapter 3 Herbicide Uptake and Movement
3.1 Introduction
3.2 The cuticle as a barrier to foliar uptake
3.3 Physicochemical aspects of foliar uptake
3.4 Herbicide formulation
3.5 Uptake by roots from soil
3.6 Herbicide translocation from roots to shoots
3.7 A case study: the formulation of acids
3.8 The formulation of glyphosate
3.9 Further developments
References
Chapter 4 Herbicide Selectivity and Metabolism
4.1 Introduction
4.2 General principles
4.2.1 Phases of herbicide metabolism
4.2.1.1 Bioactivation
4.2.1.2 Metabolic attack
4.2.1.3 Conjugation
4.2.1.4 Sequestration
4.3 Herbicide safeners and synergists
4.3.1 Safener modes of action
4.3.2 Synergists
References
Chapter 5 Herbicides that Inhibit Photosynthesis
5.1 Introduction
5.2 Photosystems
5.3 Inhibition at Photosystem II
5.4 Photodamage and repair of Photosystem II
5.5 Structures and uses of Photosystem II inhibitors
5.6 Interference with electron flow at Photosystem I
5.7 RuBisCo activase
5.8 How treated plants die
5.8.1 Active oxygen species
5.9 Chlorophyll fluorescence
5.10 Inhibition of photosynthetic carbon reduction in C4 plants
References
Chapter 6 Inhibitors of Pigment Biosynthesis
6.1 Introduction: structures and functions of photosynthetic pigments
6.2 Inhibition of chlorophyll biosynthesis
6.3 Inhibition of carotenoid biosynthesis
6.3.1 Inhibition of phytoene desaturase
6.4 Inhibition of plastoquinone biosynthesis
6.5 How treated plants die
6.6 Selectivity and metabolism
6.7 Summary
References
Chapter 7 Auxin‐type Herbicides
7.1 Introduction
7.2 Structures and uses of auxin‐type herbicides
7.3 Auxin, a natural plant growth regulator
7.4 Biosynthesis and metabolism of auxins
7.5 Auxin receptors, gene expression and herbicides
7.5.1 Auxin binding protein
7.5.2 Transport inhibitor response 1 protein
7.6 Signal transduction
7.7 Auxin transport
7.8 Resistance to auxin‐type herbicides
7.9 An ‘auxin overdose’
7.10 How treated plants die
7.11 Selectivity and metabolism
References
Chapter 8 Inhibitors of Lipid Biosynthesis
8.1 Introduction
8.2 Structures and uses of graminicides
8.3 Inhibition of lipid biosynthesis
8.4 Activity of graminicides in mixtures
8.5 How treated plants die
8.6 Plant oxylipins: lipids with key roles in plant defence and development
8.6.1 The jasmonate pathway
8.7 Selectivity
References
Chapter 9 The Inhibition of Amino Acid Biosynthesis
9.1 Introduction
9.2 Overview of amino acid biosynthesis in plants
9.3 Inhibition of glutamine synthase
9.4 Inhibition of aromatic amino acid biosynthesis. 9.4.1 Inhibition of EPSP synthase
9.4.2 How glyphosate‐treated plants die
9.4.3 Glyphosate and hormesis
9.4.4 Inhibition of dehydroquinate synthase
9.5 Inhibition of branch‐chain amino acid biosynthesis. 9.5.1 Inhibition of acetolactate synthase
9.5.2 Inhibition of threonine dehydratase
9.5.3 Inhibition of dihydroxy‐acid dehydratase
9.5.4 How treated plants die
9.5.5 Selectivity
9.6 Inhibition of histidine biosynthesis
References
Chapter 10 The Disruption of Cell Division
10.1 Introduction
10.2 The cell cycle
10.3 Control of the cell cycle
10.3.1 Transition from G2 to M phase
10.3.2 After mitosis
10.3.3 Hormones and cell division
10.4 Microtubule structure and function
10.5 Herbicidal interference with microtubules
10.5.1 Dinitroanilines
10.5.2 N‐Phenylcarbamates
10.5.3 Others
10.6 Selectivity
References
Chapter 11 The Inhibition of Cellulose Biosynthesis
11.1 Introduction
11.2 Cellulose biosynthesis
11.3 Cellulose biosynthesis inhibitors
11.4 How treated plants die
11.5 Selectivity
References
Chapter 12 Plant Kinases, Phosphatases and Stress Signalling
12.1 Introduction
12.2 Plant kinases
12.3 Plant phosphatases
12.4 Cyclin‐dependent kinases and plant stress
12.5 Post‐translational modification of proteins
References
Chapter 13 Herbicide Resistance
13.1 Introduction
13.2 Definition of herbicide resistance
13.3 How resistance occurs
13.4 A chronology of herbicide resistance
13.5 Mechanisms of herbicide resistance. 13.5.1 Target site resistance
13.5.1.1 Target site‐mediated resistance to ACCase‐inhibiting herbicides
13.5.1.2 Target site‐mediated resistance to ALS‐inhibiting herbicides
13.5.1.3 Target site‐mediated resistance to Photosystem II‐inhibiting herbicides
13.5.1.4 Target site‐mediated resistance to Photosystem I‐diverting herbicides
13.5.1.5 Target site‐mediated resistance to cell division inhibitors
13.5.1.6 Target site‐mediated resistance to glyphosate
13.5.1.7 Target site‐mediated resistance to auxin‐type herbicides
13.5.1.8 Target site‐mediated resistance to cellulose biosynthesis inhibitors
13.5.1.9 Target site resistance to phytoene‐desaturase inhibitors
13.5.1.10 Target site resistance to PROTOX inhibitors
13.5.1.11 Target site resistance to glutamine synthetase inhibitors
13.5.1.12 Target site resistance to HPPD inhibitors
13.5.2 Non‐target site resistance. 13.5.2.1 Enhanced metabolism resistance
13.5.2.2 Enhanced compartmentalisation
13.5.3 Cross‐resistance
13.5.4 Multiple resistance
13.6 Case study – black‐grass (A. myosuroides Huds)
13.7 Strategies for the control of herbicide‐resistant weeds
13.8 The future development of herbicide resistance
References
Chapter 14 Herbicide‐tolerant Crops
14.1 Introduction
14.2 History of genetically modified, herbicide‐tolerant crops
14.3 How genetically modified crops are produced
14.4 Genetically engineered herbicide tolerance to glyphosate
14.5 Genetically modified herbicide tolerance to glufosinate
14.6 Genetically modified herbicide tolerance to bromoxynil
14.7 Genetically modified herbicide tolerance to sulphonylureas
14.8 Genetically modified herbicide tolerance to 2,4‐D
14.9 Genetically modified herbicide tolerance to fops and dims
14.10 Genetically modified herbicide tolerance to phytoene desaturase inhibitors
14.11 Herbicide tolerance owing to genetic engineering of enhanced metabolism
14.12 Herbicide tolerance through means other than genetic modification
14.13 Gene editing
14.14 Economic, environmental and human health benefits from the adoption of GM technology
14.14.1 Economic
14.14.2 Environmental
14.14.3 Human health benefits
14.15 Gene stacking
14.16 Will the rise of glyphosate be inevitably followed by a fall?
14.17 Why is there so much opposition to GM technology?
14.18 Future prospects
References
Chapter 15 Further Targets for Herbicide Development
15.1 Introduction
15.2 Protein turnover. 15.2.1 Introduction
15.2.2 Proteases
15.2.3 Programmed cell death
15.2.4 The ubiquitin–proteosome pathway
15.2.5 Small plant peptides
15.3 The promotion of ageing in weeds?
15.4 Herbicide leads at the apicoplast
15.5 Control of seed germination and dormancy
15.6 Natural products as leads for new herbicides
References
Glossary
Index
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