
Regulated Cell Death Part B
Necroptotic, Autophagic and other Non-apoptotic Mechanisms
- 1st Edition, Volume 545 - July 23, 2014
- Imprint: Academic Press
- Editors: Avi Ashkenazi, Jim Wells, Junying Yuan
- Language: English
- Hardback ISBN:9 7 8 - 0 - 1 2 - 8 0 1 4 3 0 - 1
- eBook ISBN:9 7 8 - 0 - 1 2 - 8 0 1 6 1 9 - 0
Regulated Cell Death Part A & Part B of Methods in Enzymology continues the legacy of this premier serial with quality chapters authored by leaders in the field. This volume c… Read more

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Request a sales quote- Continues the legacy of this premier serial with quality chapters authored by leaders in the field
- Covers research methods in biomineralization science
- Regulated Cell Death Part A & Part B contains sections on such topics as apoptosis focusing on the important areas of intrinsic pathway, extrinsic pathway, caspases, cellular assays and post-apoptotic effects and model organisms; as well as topics on necroptosis and screening approaches
- Preface
- Chapter One: Assays for Necroptosis and Activity of RIP Kinases
- Abstract
- 1 Introduction
- 2 Cellular Models of Necroptosis
- 3 Measurement of Necroptotic Cell Death
- 4 Recapitulation of RIP1 Kinase Expression in RIP1-Deficient Jurkat Cells
- 5 Analysis of Necrosome Complex Formation
- 6 Endogenous RIPK Autophosphorylation Assays (Fig. 1.9)
- 7 Analysis of Recombinant RIPK1 Kinase Activity and Inhibition by Necrostatins
- 8 Conclusions
- Acknowledgments
- Chapter Two: IAP Family of Cell Death and Signaling Regulators
- Abstract
- 1 Identification of IAPs, Structure, and Domain Function
- 2 IAP Proteins and Cell Death Pathways
- Chapter Three: Activation of the NLRP3 Inflammasome by Proteins That Signal for Necroptosis
- Abstract
- 1 Introduction
- 2 Altered Expression or Function of Enzymes That Control Induction of Necroptosis Results in Altered Generation of IL-1β and IL-18 by Mouse DCs
- 3 Signaling Proteins Controlling Necroptosis Affect Assembly of the NLRP3 Inflammasome
- 4 Does the Similarity Between the Regulation of Necroptosis and of Assembly of the NLRP3 Inflammasome Reflect Activation of the Inflammasome by Products of Necrotic Cells?
- 5 Concluding Remarks
- Acknowledgments
- Chapter Four: Characterization of the Ripoptosome and Its Components: Implications for Anti-inflammatory and Cancer Therapy
- Abstract
- 1 Introduction
- 2 The Ripoptosome: Cellular Model Systems to Study Its Formation
- 3 Biochemical Analysis of the Ripoptosome: Analysis of Ripoptosome Formation and Identification of Novel Components via Immunoprecipitation and Mass Spectrometry
- 4 Outlook: Future Implications of the Function and Regulation of the Ripoptosome
- Chapter Five: Tools and Techniques to Study Ligand–Receptor Interactions and Receptor Activation by TNF Superfamily Members
- Abstract
- 1 Introduction
- 2 Methods
- 3 Conclusions
- Acknowledgments
- Chapter Six: Necrotic Cell Death in Caenorhabditis elegans
- Abstract
- 1 Introduction
- 2 Necrotic Cell Death Paradigms During C. elegans Development
- 3 Nondevelopmental Necrotic Death
- 4 Execution of Necrosis
- 5 C. elegans as a Model for Human Diseases Entailing Necrosis
- 6 Concluding Remarks
- Acknowledgments
- Chapter Seven: Noncanonical Cell Death in the Nematode Caenorhabditis elegans
- Abstract
- 1 Introduction
- 2 Pathological Cell Death Induced by Genome Lesions and Environmental Stress
- 3 Developmental Cell Deaths That Do not Follow the Canonical Apoptotic Pathway
- 4 Nonapoptotic, Caspase-Independent Linker Cell Death
- 5 Conclusion
- Acknowledgments
- Chapter Eight: Autophagy and Cell Death in the Fly
- Abstract
- 1 Introduction
- 2 Materials and Methods
- 3 Data Analysis and Interpretation
- Acknowledgments
- Chapter Nine: Structural Studies of Death Receptors
- Abstract
- 1 Introduction. Signaling by the Tumor Necrosis Receptor Superfamily
- 2 Outline Death Ligand and DR Domain Structure
- 3 DR Ectodomain Structure
- 4 Physiological Complexes of Death Ligands with DRs
- 5 A Decoy Receptor–Ligand Complex
- 6 The DR Preligand Association Domain
- 7 Death Ligand Structure–Activity Relationships
- 8 Structural Analysis of AntiTNF Agents
- 9 Structural Analysis of the Blockade of DR Function
- 10 DR Cytoplasmic Domains
- 11 DD Structure
- 12 The DD Superfamily
- 13 DD Assembly Revealed by the Structure of the PIDDosome Core
- 14 Structural Characterization of CD95:FADD-DD Complexes
- 15 Relevance of CD95:FADD-DD Assemblies to Physiological CD95 Signaling
- 16 Unanswered Questions and Future Prospects
- Acknowledgments
- Chapter Ten: Use of E2~ Ubiquitin Conjugates for the Characterization of Ubiquitin Transfer by RING E3 Ligases Such as the Inhibitor of Apoptosis Proteins
- Abstract
- 1 Introduction
- 2 Synthesis of E2~ Ub Conjugates
- 3 Characterization of RING-E2~ Ub Complexes
- 4 Conclusion
- Acknowledgments
- Chapter Eleven: Multidimensional Profiling in the Investigation of Small-Molecule-Induced Cell Death
- Abstract
- 1 Introduction
- 2 Gene Expression Profiling
- 3 Protein Quantification
- 4 Gene–Small-Molecule Interactions
- 5 Small-Molecule Combination Interactions
- 6 Cell Line Viability Profiling
- 7 Quantitative Imaging
- 8 Modulatory Profiling
- 9 Conclusions
- Author Index
- Subject Index
- Edition: 1
- Volume: 545
- Published: July 23, 2014
- No. of pages (Hardback): 352
- No. of pages (eBook): 352
- Imprint: Academic Press
- Language: English
- Hardback ISBN: 9780128014301
- eBook ISBN: 9780128016190
AA
Avi Ashkenazi
JW
Jim Wells
James A. Wells, PhD, focuses on development of enabling technologies for engineering proteins and for identifying small molecules to aid in drug discovery for challenging targets such as allosteric regulation and protein-protein interactions. He is interested in the discovery and design of small molecules and enzymes that trigger or modulate cellular processes in inflammation and cancer. Using small molecules and engineered proteins, the Wells lab is studying how activation of particular signaling nodes involving protease, kinases, or ubiquitin ligases drives cell biology. The lab has focused much on a set of proteases, known as caspases, responsible for fate determining cellular decisions involved in apoptosis and innate inflammation among others. These enzymes act as cellular remodelers and help us understand the essential protein struts that support life. These targets also provide leads for developing new cancer therapeutics and biomarkers for cancer treatment.
Wells is a professor and chair of the Department of Pharmaceutical Chemistry in the UCSF School of Pharmacy. He holds a combined appointment as professor in the Department of Cellular & Molecular Pharmacology in the School of Medicine. He joined UCSF in 2005 as holder of the Harry Wm. and Diana V. Hind Distinguished Professorship in Pharmaceutical Sciences. Wells also founded and directs the Small Molecule Discovery Center (SMDC) located at UCSF’s Mission Bay campus. He earned a PhD degree in biochemistry from Washington State University with Professor Ralph Yount in 1979 and completed postdoctoral work at Stanford University School of Medicine with Professor George Stark in 1982. Before joining UCSF, Wells was a founding scientist in Genentech’s Protein Engineering Department and in 1998 co-founded Sunesis Pharmaceuticals.
Wells is a recipient of the Hans Neurath Award by the Protein Society, the Pfizer Award and Smissman Award given by the American Chemical Society, the Perlman Lecture Award given by the ACS Biotechnology Division, the du Vigneaud Award given by the American Peptide Society, the Merck Award from the ASBMB and in 1999 a member of the National Academy of Sciences.
JY