International Review of Cell and Molecular Biology

 
 
Elsevier (Verlag)
  • 1. Auflage
  • |
  • erschienen am 8. Februar 2019
  • |
  • 308 Seiten
 
E-Book | ePUB mit Adobe DRM | Systemvoraussetzungen
E-Book | PDF mit Adobe DRM | Systemvoraussetzungen
978-0-12-816704-5 (ISBN)
 

International Review of Cell and Molecular Biology, Volume 343 reviews and details current advances in cell and molecular biology. The IRCMB series has a worldwide readership, maintaining a high standard by publishing invited articles on important and timely topics that are authored by prominent cell and molecular biologists. Sections in this new release include The Molecular and Cellular Regulation of Brassicaceae Self-Incompatibility and Self-Pollen Rejection, Regulation of Plant Immunity by the Proteasome, the Role of the Ubiquitin Proteasome System in Plant Response to Abiotic Stress, Glycosylation in Anticancer Immunity, Emerging Themes in PDZ Domain Signaling: Structure, Function and Inhibition, and more.

  • Publishes invited review articles on selected topics as authored by established and active cell and molecular biologists whose work is drawn from international sources
  • Offers a wide range of perspectives on specific subjects
  • Englisch
  • San Diego
  • |
  • USA
  • 6,21 MB
978-0-12-816704-5 (9780128167045)
weitere Ausgaben werden ermittelt
  • Front Cover
  • International Review of Cell and Molecular Biology
  • INTERNATIONAL REVIEW OF CELL AND MOLECULAR BIOLOGY
  • International Review of Cell and Molecular Biology
  • Copyright
  • Contents
  • CONTRIBUTORS
  • One - The Molecular and Cellular Regulation of Brassicaceae Self-Incompatibility and Self-Pollen Rejection
  • 1. INTRODUCTION
  • 2. ROLE OF SMALL RNAS IN DOMINANT-RECESSIVE INTERACTIONS BETWEEN S-HAPLOTYPES
  • 3. USE OF THE TRANSGENIC ARABIDOPSIS THALIANA MODEL SYSTEM TO FURTHER EXPLORE SRK FUNCTION, LOCALIZATION, AND MODIFICATION
  • 4. INVESTIGATING THE SELF-INCOMPATIBILITY SIGNALING PATHWAY: MLPK AND ARC1
  • 5. CELLULAR RESPONSES TRIGGERED BY ARC1
  • 6. CALCIUM FLUXES AND AUTOPHAGY IN SELF-INCOMPATIBILITY SIGNALING
  • 7. DIVERSITY IN BRASSICACEAE SELF-INCOMPATIBILITY AND UNILATERAL INCOMPATIBILITY
  • 8. CONCLUSIONS AND FUTURE DIRECTIONS
  • ACKNOWLEDGMENTS
  • REFERENCES
  • Two - Regulation of Plant Immunity by the Proteasome
  • 1. INTRODUCTION
  • 1.1 The Plant Immune System
  • 1.2 The Ubiquitin-Proteasome System
  • 2. E3 LIGASES WITH IMMUNE-RELATED FUNCTIONS
  • 2.1 E3s Involved in the Turnover of Immune Receptors
  • 2.2 E3 Ligases Involved in Downstream Immune Signaling
  • 3. THE ROLE OF GENERAL PROTEASOME COMPONENTS IN PLANT IMMUNITY
  • 3.1 Proteins Involved in Ubiquitination and E3 Ligase Function
  • 3.2 Proteins Downstream of Ubiquitination Steps
  • 4. CONCLUSIONS AND PERSPECTIVES
  • REFERENCES
  • Three - Role of the Ubiquitin Proteasome System in Plant Response to Abiotic Stress
  • 1. INTRODUCTION
  • 2. THE UBIQUITIN PROTEASOME SYSTEM
  • 2.1 The Ubiquitination Pathway
  • 2.2 The Ubiquitin Enzymes
  • 2.2.1 Homology to E6-Associated-Carboxyl-Terminus-Type E3s
  • 2.2.2 Really Interesting New Gene-Type E3s
  • 2.2.3 U Box-Type E3s
  • 2.3 Ubiquitin-Dependent Degradation by the 26S Proteasome
  • 3. UPS-DEPENDENT REGULATION OF ABIOTIC STRESS RESPONSE
  • 4. MODES OF E3 REGULATION OF ABIOTIC STRESS SIGNALING
  • 4.1 Regulation of DREB2A-Mediated Stress Signaling
  • 4.2 Abscisic Acid Signaling Is Regulated by a Myriad of E3s
  • 5. COMPLEXITY OF UBIUITIN-DEPENDENT REGULATION OF STRESS SIGNALING
  • REFERENCES
  • Four - Glycosylation and Antitumor Immunity
  • 1. INTRODUCTION
  • 2. GLYCOSYLATION AND PROTEIN MODIFICATION: AN OVERVIEW
  • 3. GLYCOSYLATION'S ROLE IN CANCER
  • 4. GLYCOSYLATION AND TUMOR IMMUNE EVASION
  • 5. ENDOGENOUS LECTINS AND ADAPTIVE IMMUNITY
  • 6. THE IMMUNOSUPPRESSIVE NATURE OF GLYCOSPHINGOLIPIDS
  • 7. SIALIC ACID DOMAINS AND ANTITUMOR IMMUNITY
  • 8. GLYCAN-BASED CANCER THERAPIES
  • 9. CONCLUSION
  • Conflicts of Interest
  • REFERENCES
  • Five - Emerging Themes in PDZ Domain Signaling: Structure, Function, and Inhibition
  • 1. INTRODUCTION
  • 2. CELLULAR FUNCTION OF PDZ DOMAIN-CONTAINING PROTEINS AND THEIR LINK TO DISEASE
  • 2.1 Coordination of Pre- and Postsynaptic Signaling in Neuronal Cells
  • 2.1.1 AMPA Receptor
  • 2.1.2 NMDA Receptor
  • 2.1.3 G-Protein Coupled Receptors
  • 2.2 Establishment and Maintenance of Cell-Cell Junctions and Cell-Matrix Adhesions
  • 2.2.1 Adherens and Tight Junction Proteins
  • 2.2.2 Proteoglycan Receptors
  • 2.2.3 PDZ Proteins as Targets for Pathogenic Viruses
  • 2.3 Other PDZ Domain Proteins in Cell Signaling Pathways
  • 2.3.1 Wnt Signaling
  • 2.3.2 CFTR Signaling
  • 2.4 Diseases Related to PDZ Proteins and Their Interaction Partners
  • 3. CANONICAL PDZ DOMAIN-BINDING MOTIFS AND NOVEL LIGANDS
  • 3.1 C-Terminal PDZ-Binding Motifs
  • 3.2 Internal Binding Motifs
  • 3.3 Intra- and Interprotein PDZ-PDZ Domain Interactions
  • 3.4 Phosphatidylinositol and Cholesterol Binding
  • 4. INHIBITION OF PDZ DOMAIN/LIGAND INTERACTIONS
  • 4.1 PDZ Domain Inhibitors in Neuronal Disorders
  • 4.2 PDZ Domain Inhibitors in Cancer
  • 4.3 PDZ Domain Inhibitors in Cystic Fibrosis
  • 5. REGULATION OF PDZ DOMAIN/LIGAND INTERACTIONS
  • 5.1 Phosphorylation
  • 5.1.1 Phosphorylation of the PDZ-Binding Motif
  • 5.1.2 Phosphorylation of PDZ Domains
  • 5.2 PDZ Domain Dynamics and Allostery
  • 5.2.1 Intrinsic Dynamics and Allosteric Behavior
  • 5.2.2 PDZ Domain Allostery in Larger Fragments
  • 6. CONCLUSIONS
  • ACKNOWLEDGMENTS
  • REFERENCES
  • Six - Cross Talk Networks of Mammalian Target of Rapamycin Signaling With the Ubiquitin Proteasome System and Their ...
  • 1. INTRODUCTION
  • 2. MAMMALIAN TARGET OF RAPAMYCIN SIGNALING PATHWAYS
  • 2.1 Structure of Mammalian Target of Rapamycin and Its Complexes
  • 2.2 The Mammalian Target of Rapamycin Complex 1 Signaling Pathways
  • 2.2.1 Upstream Regulators of mTORC1
  • 2.2.2 Downstream Effectors of mTORC1
  • 2.3 The Mammalian Target of Rapamycin Complex 2 Signaling Pathways
  • 2.3.1 Upstream Regulators of mTORC2
  • 2.3.2 Downstream Effectors of mTORC2
  • 2.4 Crosstalk Between mTORC1 and mTORC2
  • 3. INTERPLAY BETWEEN MAMMALIAN TARGET OF RAPAMYCIN PATHWAYS AND THE UBIQUITIN PROTEASOME SYSTEM
  • 3.1 The Ubiquitin Proteasome System
  • 3.2 mTOR-Mediated Regulation of the Ubiquitin Proteasome System
  • 3.3 Key mTORC Signaling Proteins Regulated by the Ubiquitin Proteasome System
  • 3.3.1 UPS-Mediated Regulation of mTORC Components
  • 3.3.2 UPS-Mediated Regulation of mTORC Regulators and Effectors
  • 4. TARGETING THE MTOR PATHWAY IN MM
  • 4.1 Direct Targeting of Mammalian Target of Rapamycin Pathway Protein Kinases
  • 4.1.1 Mammalian Target of Rapamycin Inhibitors
  • 4.1.1.1 Rapamycin and the Rapalogs
  • 4.1.1.2 Dual Mammalian Target of Rapamycin Inhibitors
  • 4.1.2 PI3K Inhibitors
  • 4.1.2.1 Pan-PI3K Inhibitors
  • 4.1.2.2 Isoform-Specific PI3K Inhibitors
  • 4.1.3 Dual PI3K-mTOR Inhibitors
  • 4.1.4 Akt Inhibitors
  • 4.2 Inhibiting Mammalian Target of Rapamycin Signaling by Targeting the Ubiquitin Proteasome System
  • 4.2.1 Proteasomal Inhibition
  • 4.2.2 Inhibition of Ubiquitin Ligases and Other Specific Ubiquitin Proteasome System-Associated Proteins
  • 4.2.2.1 E1 and E2 Ligase Inhibitors
  • 4.2.2.1.1 E1 Inhibitors
  • 4.2.2.1.2 E2 Inhibitors
  • 4.2.2.2 General E3 Ligase Inhibitors
  • 4.2.2.3 Specific E3 Ligase Inhibitors
  • 4.2.2.3.1 MDM2 Inhibitors
  • 4.2.2.3.2 Skp2 Inhibitors
  • 4.2.2.4 Further mTOR Signaling-Associated E3 Ligases Without Specific Inhibitors
  • 5. CONCLUSION
  • ACKNOWLEDGMENTS
  • REFERENCES
  • Back Cover

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