Ubiquitin Ligase: New Insights, Emerging Roles and Clinical Implications

Edward T. Harris (Editor)

Series: Biochemistry Research Trends
BISAC: SCI007000

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The E3 ubiquitin ligases facilitate substrate specificity and isopeptide bond formation between C-terminal glycine residue of ubiquitin (Gly 76) and a lysine residue in the target protein. This book reviews several new insights, discusses emerging roles and analyzes clinical implications of uniquitin ligases. (Imprint: Nova)

Preface

Chapter 1. The Significance of E3 Ubiquitin Ligases in Cell Cycles and Genome Stability (DNA Replication and DNA Damage)
Ota Fuchs (Institute of Hematology and Blood Transfusion, Prague, Czech Republic)

Chapter 2. E3 Ubiquitin Ligases Involved in the Pathogenesis and Treatment of del(5q) Myelodysplastic Syndrome and Other Hematologic Malignancies
Ota Fuchs (Institute of Hematology and Blood Transfusion, Prague, Czech Republic)

Chapter 3. The Targeting of Neddylation of Cullin-RING E3 Ubiquitin Ligases with an NEDD8-Activating Enzyme Inhibitor Pevonedistat (MLN4924) in Hematologic Malignancies
Ota Fuchs (Institute of Hematology and Blood Transfusion, Prague, Czech Republic)

Chapter 4. Ring Finger E3 Ubiqutin Ligase CBL Protein and Its Functional Roles and Mutations in Myeloid Malignancies
Ota Fuchs (Institute of Hematology and Blood Transfusion, Prague, Czech Republic)

Chapter 5. E3 Ubiquitin Ligases Mdm2 and MdmX Regulate the Stability, Translation, Subcellular Localization and Transcriptional Activity of p53 Protein
Ota Fuchs (Institute of Hematology and Blood Transfusion, Prague, Czech Republic)

Chapter 6. Roles of E3 Ubiquitin Ligases with a Tripartite Motif (TRIM) in Innate Immune Regulation
Ota Fuchs (Institute of Hematology and Blood Transfusion, Prague, Czech Republic)

Chapter 7. Paving the Notch Pathway with Ubiquitin Ligases
Neta Erez and Amir Orian (Rappaport Research Institute and Rappaport Faculty of Medicine, Technion Integrated Cancer Center, Technion – Israel Institute of Technology, Haifa, Israel)

Index

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