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E-grāmata: Dancing protein clouds: Intrinsically disordered proteins in health and disease, Part A

Volume editor (Department of Molecular Medicine and USF Health Byrd Alzheimers Research Institute, Morsani College of Medicine, University of South Florida, Tampa, FL, United States)
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Dancing protein clouds: Intrinsically disordered proteins in health and disease, Part APalielināt
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"Dancing protein clouds: Intrinsically disordered proteins in the norm and pathology" 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
Contributors ix
Preface xi
1 Protein intrinsic disorder and structure-function continuum
1(18)
Vladimir N. Uversky
1 Introduction
2(1)
2 Locks, keys, and protein functionality
3(1)
3 Intrinsic disorder, multifunctionality, and "moonlighting" vs. structure-function paradigm
4(1)
4 Proteoforms against "one gene-one enzyme" hypothesis
5(1)
5 Intrinsic disorder and proteoforms
6(3)
6 Proteoforms and structural flexibility of ordered proteins
9(1)
7 Proteoforms and protein-structure continuum
10(1)
References
11(8)
2 Intrinsic disorder associated with 14-3-3 proteins and their partners
19(44)
Nikolai N. Sluchanko
Diego M. Bustos
1 Introduction
20(1)
2 Role of protein modules, intrinsic disorder, and posttranslational modifications in protein-protein recognition
21(4)
3 14-3-3 Protein hubs: General aspects
25(2)
4 Structural features and intrinsic disorder associated with 14-3-3 proteins
27(6)
5 Multifunctionality of 14-3-3 proteins
33(3)
6 Intrinsic disorder and the 14-3-3 interactome
36(6)
7 Protein-protein interaction subnetworks of 14-3-3 paralogs
42(1)
8 The mechanism of binding of intrinsically disordered target proteins to 14-3-3
43(5)
9 Conclusions and perspectives
48(1)
Acknowledgments
49(1)
References
49(14)
3 Intrinsically disordered proteins and phenotypic switching: Implications in cancer
63(22)
Vivek Kulkarni
Prakash Kulkarni
1 Introduction
64(1)
2 Conformational noise hypothesis: The MRK model
65(3)
3 Evidence supporting the MRK hypothesis
68(3)
4 Learning and evolution
71(1)
5 Inheritance of acquired learning
72(3)
6 Therapeutic implications
75(1)
7 Conclusions
76(1)
References
76(8)
Further reading
84(1)
4 Translational diffusion of unfolded and intrinsically disordered proteins
85(24)
Irina V. Nesmelova
Daria L. Melnikova
Venkatesh Ranjan
Vladimir D. Skirda
1 Introduction
86(1)
2 Dilute solutions
87(8)
3 Concentrated solutions
95(6)
4 Conclusions and future directions
101(1)
References
102(7)
5 Intrinsically disordered proteins in the formation of functional amyloids from bacteria to humans
109(36)
Anamika Avni
Hema M. Swasthi
Anupa Majumdar
Samrat Mukhopadhyay
1 An introduction to intrinsically disordered proteins
110(2)
2 Mechanism of protein aggregation and amyloid formation
112(2)
3 Supramolecular architecture of amyloids
114(2)
4 Amyloids as functional workhorses
116(1)
5 Bacterial functional amyloids
117(5)
6 Functional amyloids in yeast
122(3)
7 Functional amyloids in long-term memory in Aplysia and Drosophila
125(1)
8 Amyloid fibers in spider silk
126(1)
9 Functional amyloids in vertebrates and higher organisms
126(1)
10 Functional amyloids in mammals and humans
127(6)
11 Functional amyloids in the plant kingdom
133(1)
12 Conclusions and future directions
133(1)
Acknowledgments
134(1)
References
134(11)
6 Intrinsically disordered proteins in various hypotheses on the pathogenesis of Alzheimer's and Parkinson's diseases
145(80)
Orkid Coskuner
Vladimir N. Uversky
1 Introduction
146(18)
2 A brief summary of techniques currently used for in vivo, in vitro, and in silico AD and PD analysis
164(10)
3 Some insights from computational biology and computational chemistry
174(34)
4 Disorder and aggregation propensity analysis using bioinformatics
208(4)
5 Conclusion
212(1)
References
212(13)
7 Shear-induced amyloid formation of IDPs in the brain
225(86)
Conrad N. Trumbore
1 Introduction
227(2)
2 What is liquid shear?
229(6)
3 Aβ shear within the brain?
235(3)
4 Previous, current, and future research in sheared Aβ and amyloid monomers
238(3)
5 General properties of IDPs and their application to Aβ
241(4)
6 The free energy folding Aβ landscape
245(2)
7 Aβ aggregation, oligomer structures, and drug intervention
247(1)
8 Brain environmental effects: Aβ flow paths and possible shear events
248(18)
9 The role of shear energy: What does Aβ * really mean?
266(6)
10 Mechanisms for Aβ aggregation: Thermal vs. shear activation
272(1)
11 Proposed Alzheimer's disease model with shear included
273(13)
12 In vivo and in vitro experiments
286(7)
13 Other amyloid diseases and participants in AD
293(1)
14 The shear extremes: Concussion and traumatic brain injury
293(1)
15 Extrapolations to non-amyloid diseases?
294(1)
16 Conclusions
294(3)
17 Suggested future directions in shear research
297(8)
Acknowledgments
305(1)
References
306(5)
8 Role of intrinsic disorder in muscle sarcomeres
311(30)
Dmitri Tolkatchev
Garry E. Smith Jr.
Alia S. Kostyukova
1 Introduction
312(1)
2 Myosin-binding protein C (MyBP-C)
313(8)
3 Proteins of tropomodulin family
321(13)
4 Concluding remarks
334(1)
Acknowledgment
335(1)
References
335(6)
9 Computational prediction of functions of intrinsically disordered regions
341(30)
Akila Katuwawala
Sina Ghadermarzi
Lukasz Kurgan
1 Introduction
342(1)
2 Functional annotations of intrinsically disordered regions
343(5)
3 Prediction of functions of intrinsically disordered regions
348(9)
4 Case studies
357(3)
5 Summary and prospective advances
360(2)
Acknowledgment
362(1)
References
362(9)
10 The dark proteome of cancer: Intrinsic disorderedness and functionality of HIF-1α along with its interacting proteins
371(34)
Neha Garg
Prateek Kumar
Kundlik Gadhave
Rajanish Giri
1 Introduction
373(2)
2 Methods
375(1)
3 Results
376(19)
4 Discussion
395(3)
Author contributions
398(1)
Competing interests
398(1)
References
398(7)
Index 405
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 PhD from Moscow Institute of Physics and Technology and D.Sc. from the Institute of Experimental and Theoretical Biophysics, Russian Academy of Sciences. Since 2010, Professor Uversky has worked at University of South Florida, where he works on various aspects of protein intrinsic disorder phenomenon and analysis of protein folding and misfolding processes. He has authored over 1250 scientific publications and edited several books and book series on protein structure, function, folding, misfolding, and intrinsic disorder. He also servs as an editor in a number of scientific journals.
Biežāk uzdotie jautājumi par e-grāmatām Biežāk uzdotie jautājumi par e-grāmatām
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