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Yi S. Cullin-RING Ligases and Protein Neddylation. Biology and Therapeutics 2020
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Textbook in PDF format

This book summarizes all the important aspects of CRLs (Cullin-RING E3 Ubiquitin Ligases), while providing details of mechanistic specifics that go beyond protein ubiquitination and neddylation. Ubiquitin ligases, including the CRLs, which are activated by neddylation, play an important role in diverse biological processes and are involved in various human diseases, particularly cancer. The book covers various topics, such as CRL structure, biology, genetics, its regulation by neddylation, its pivotal role in human disease, and its potential in drug discovery and targeted therapies. The book appeals to biochemists and biologists working in other fields, and, given the importance of CRLs in all aspects of cell biology and the great promise of targeting these complexes for therapy, is a valuable resource anyone interested in modern biology or medicine.
Introduction
Structural Biology of CRL Ubiquitin Ligases
Assembly and Regulation of CRL Ubiquitin Ligases
Cullin-RING Ligase Regulation by the COP9 Signalosome: Structural Mechanisms and New Physiologic Players
Coordinated Actions Between p97 and Cullin-RING Ubiquitin Ligases for Protein Degradation
Regulation of Stem Cells by Cullin-RING Ligase
Viral Manipulations of the Cullin-RING Ubiquitin Ligases
The Biology of F-box Proteins: The SCF Family of E3 Ubiquitin Ligases
Targeting SCF E3 Ligases for Cancer Therapies
Knockout Mouse Models Provide Insight into the Biological Functions of CRL1 Components
The Roles of Cullin-2 E3 Ubiquitin Ligase Complex in Cancer
Cullin 3 and Its Role in Tumorigenesis
CRL3s: The BTB-CUL3-RING E3 Ubiquitin Ligases
CRL4 Ubiquitin Pathway and DNA Damage Response
Cullin 4-DCAF Proteins in Tumorigenesis
Cullin RING Ligase 5 (CRL-5): Neddylation Activation and Biological Functions
Cullin-RING E3 Ubiquitin Ligase 7 in Growth Control and Cancer
Targeting Protein Neddylation for Cancer Therapy
Targeting Cullin-RING Ubiquitin Ligases and the Applications in PROTACs
Targeting DCN1-UBC12 Protein-Protein Interaction for Regulation of Neddylation Pathway