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Dancing Protein Clouds: Intrinsically Disordered Proteins in Health and Disease, Part B
- 1st Edition, Volume 174 - August 19, 2020
- Editor: Vladimir N Uversky
- Language: English
- Hardback ISBN:9 7 8 - 0 - 1 2 - 8 2 2 6 1 5 - 5
- eBook ISBN:9 7 8 - 0 - 1 2 - 8 2 2 6 0 4 - 9
Dancing Protein Clouds: Intrinsically Disordered Proteins in Health and Disease, Part B, represents a set of selected studies on a variety of research topics related to intrinsic… Read more
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Request a sales quoteDancing Protein Clouds: Intrinsically Disordered Proteins in Health and Disease, Part B, represents a set of selected studies on a variety of research topics related to intrinsically disordered proteins. Topics in this update include structural and functional characterization of several important intrinsically disordered proteins, such as 14-3-3 proteins and their partners, as well as proteins from muscle sarcomere; representation of intrinsic disorder-related concept of protein structure-function continuum; discussion of the role of intrinsic disorder in phenotypic switching; consideration of the role of intrinsically disordered proteins in the pathogenesis of neurodegenerative diseases and cancer; discussion of the roles of intrinsic disorder in functional amyloids; demonstration of the usefulness of the analysis of translational diffusion of unfolded and intrinsically disordered proteins; consideration of various computational tools for evaluation of functions of intrinsically disordered regions; and discussion of the role of shear stress in the amyloid formation of intrinsically disordered regions in the brain.
- Provides some recent studies on the intrinsically disordered proteins and their functions, as well as on the involvement of intrinsically disordered proteins in pthogenesis of various diseases
- Contains numerous illustrative materials (color figures, diagrams, and tables) to help the readers to delve in the information provided
- Includes contributions from recognized experts in the field
Scientists working in the fields of biochemistry, biophysics, molecular medicine, biotechnology, pharmacology and drug discovery, molecular and cellular biology, as well as students of Medical Schools, Departments of Biochemistry, Biophysics, Molecular Biology, Biotechnology, Cell Biology, etc. This book is of interest to everyone fascinated by the protein intrinsic disorder phenomenon, including graduate students, postdoctoral students, and experienced researchers studying intrinsically disordered proteins (IDPs), their structures, and functions
- Cover image
- Title page
- Table of Contents
- Copyright
- Contributors
- Preface: Looking at the clouds through kaleidoscope
- Chapter One: Intrinsically disordered proteins of viruses: Involvement in the mechanism of cell regulation and pathogenesis
- Abstract
- 1: A general introduction to intrinsically disordered proteins (IDPs) and their major properties
- 2: The dark proteomes of viruses
- 3: Involvement of IDPs in the pathogen-host mediated regulation of cell cycle
- 4: Origin of viruses and their exclusive properties
- 5: Classification of viral protein and their functions
- 6: Role of bioinformatics in divulging the dark proteome of viruses
- 7: Prevalence of IDPs in viruses in context to three distinct domains of life
- 8: Predicted IDPs pattern relation to viral transmission and host tropism
- 9: Aggregation in viral protein and its relation to intrinsic disorderness
- 10: Functional prominences of disordered viral proteins: Examples from bacteriophages, plant, and animal viruses
- 11: Summary and outlook
- Chapter Two: Transient knots in intrinsically disordered proteins and neurodegeneration
- Abstract
- 1: Introduction
- 2: Examples of topological features in proteins
- 3: Methods to study conformational dynamics of proteins
- 4: Dynamics of knots in the structured proteins in the CG model
- 5: PolyQ
- 6: Degradation of proteins by AAA+ proteases and the relevance of knots
- 7: α-Synuclein
- Chapter Three: IDPs and their complexes in GPCR and nuclear receptor signaling
- Abstract
- 1: Introduction
- 2: G protein-coupled receptors
- 3: Nuclear receptors and their transcriptional coregulators
- 4: Conclusions and perspectives
- Acknowledgments
- Chapter Four: Intrinsic disorder-based design of stable globular proteins
- Abstract
- 1: How to stabilize protein?
- 2: Analysis of literature on protein stabilization
- 3: Investigation of green fluorescent protein
- 4: L1 protein study
- 5: Comparison of spatial structure and amino acid sequences of AaeL1 and HmaL1 proteins
- 6: Mapping of disordered regions and design of disulfide bridges in AaeL1 and HmaL1
- 7: Stabilization of Gαo
- 8: Searching for stable circular permutant variants of the GroEL apical domain
- 9: Conclusions
- 10: Materials and methods
- Chapter Five: The pathophysiology of neurodegenerative disease: Disturbing the balance between phase separation and irreversible aggregation
- Abstract
- 1: Introduction
- 2: The biophysics of LLPS
- 3: Types of RNA granules
- 4: Pathological hallmarks of neurodegenerative diseases
- 5: Conclusion
- Acknowledgments
- Chapter Six: Context-dependent HOX transcription factor function in health and disease
- Abstract
- 1: Introduction
- 2: The HOX paradox
- 3: Intrinsic disorder in HOX proteins
- 4: Context-dependent function
- 5: Malfunction of HOX proteins in animal development
- 6: HOX proteins and arthritis
- 7: HOX proteins and cancer
- 8: Context-dependent HOX function in disease
- 9: Conclusions and ongoing HOX mysteries
- 10: Complications involved in solving these mysteries
- Chapter Seven: Dancing while self-eating: Protein intrinsic disorder in autophagy
- Abstract
- 1: An introduction to the autophagy pathway
- 2: Intrinsically disordered regions in autophagosome biogenesis
- 3: Protein intrinsic disorder in selective autophagy
- 4: Autophagic IDPRs in disease and aging
- 5: New post-translationally modified targets for innovative modulation of autophagy
- 6: Conclusion and perspectives
- Acknowledgments
- Chapter Eight: Intrinsic disorder in the nickel-dependent urease network
- Abstract
- 1: Introduction
- 2: The transcriptional regulation of urease genes relies on IDRs
- 3: Intrinsic disorder regulates the network of protein-protein interaction for urease maturation
- 4: Urease flexibility controls substrate accessibility into the active site
- Chapter Nine: Disorder and cysteines in proteins: A design for orchestration of conformational see-saw and modulatory functions
- Abstract
- 1: Introduction
- 2: IDPs and IDRs
- 3: Cysteines in structure–function relation of proteins
- 4: Correlations between cysteine containing protein families, disorder propensity and redox-functions
- 5: Sequences containing <5% cysteines
- 6: Sequences containing 5%–10% of cysteines
- 7: Sequences containing 10%–20% cysteines
- 8: Sequences containing >20% cysteines
- 9: Conclusions and future perspectives
- 10: Methods
- Index
- No. of pages: 402
- Language: English
- Edition: 1
- Volume: 174
- Published: August 19, 2020
- Imprint: Academic Press
- Hardback ISBN: 9780128226155
- eBook ISBN: 9780128226049
VU
Vladimir N Uversky
Prof. Vladimir N. Uversky, PhD, DSc, FRSB, FRSC, F.A.I.M.B.E., Professor at the Department of Molecular Medicine, Morsani College of Medicine, University of South Florida (USF), is a pioneer in the field of protein intrinsic disorder. He has made a number of groundbreaking contributions in the field of protein folding, misfolding, and intrinsic disorder. He obtained his academic degrees from Moscow Institute of Physics and Technology (Ph.D., in 1991) and from the Institute of Experimental and Theoretical Biophysics, Russian Academy of Sciences (D.Sc., in 1998). He spent his early career working mostly on protein folding at the Institute of Protein Research and the Institute for Biological Instrumentation (Russia). In 1998, moved to the University of California Santa Cruz. In 2004, joined the Indiana University−Purdue University Indianapolis as a Senior Research Professor. Since 2010, Professor Uversky is with USF, where he works on various aspects of protein intrinsic disorder phenomenon and on analysis of protein folding and misfolding processes. Prof. Uversky has authored over 1250 scientific publications and edited several books and book series on protein structure, function, folding, misfolding, and intrinsic disorder. He is also serving as an editor in a number of scientific journals. He was a co-founder of the Intrinsically Disordered Proteins Subgroup at the Biophysical Society and the Intrinsically Disordered Proteins Gordon Research Conference. Prof. Uversky collaborated with more than 12,500 colleagues from more than 2,750 research organizations in 89 countries/territories.
Affiliations and expertise
Department of Molecular Medicine and USF Health Byrd Alzheimer’s Research Institute, Morsani College of Medicine, University of South Florida, Tampa, FL, United StatesRead Dancing Protein Clouds: Intrinsically Disordered Proteins in Health and Disease, Part B on ScienceDirect