Role of Molecular Chaperones on Structural Folding, Biological Functions, and Drug Interactions of Client Proteins

 
 
Frontiers in Structural Biology (Verlag)
  • 1. Auflage
  • |
  • erschienen am 26. April 2018
  • |
  • 250 Seiten
 
E-Book | ePUB mit Adobe DRM | Systemvoraussetzungen
978-1-68108-615-6 (ISBN)
 

The book provides an updated panorama of the functional relevance of molecular chaperones in the proper folding of client factors, protein-protein interactions, the regulation of key biological functions, the development of ligand-based structural complex

  • Englisch
  • Sharjah
  • |
  • Vereinigte Arabische Emirate
PublishDrive
  • 7,07 MB
978-1-68108-615-6 (9781681086156)
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  • Intro
  • CONTENTS
  • PREFACE
  • List of Contributors
  • Regulatory Roles for Hsp70 in Cancer Incidence and Tumor Progression
  • Taka Eguchi1, Benjamin J. Lang1, Ayesha Murshid1, Thomas Prince2, Jianlin Gong3 and Stuart K Calderwood1,*
  • 1. INTRODUCTION
  • 2. HSP70 PROTEINS IN THE CYTOPLASM AND NUCLEUS
  • 3. MUTATION AND OVEREXPRESSION OF HSP72 IN CANCER
  • 4. HSP72 AND THE HALLMARKS OF CANCER
  • 4A. HSP72 Suppresses Apoptotic Cell Death in Cancer
  • 4B. HSP72 and Senescence
  • 4C. HSP72 in Tumor Initiation and Metastasis
  • 4D. HsSP72 in Sustained Angiogenesis
  • 5. DRUGGING HSP70 IN CANCER: ISOFORMS AND DRUGGABLE DOMAINS
  • 5A. Targeting the HSP70 Substrate-Binding Domain (SBD)
  • 5B. Targeting the HSP70 Nucleotide-Binding Domain
  • 5C. Perturbation of HSP70-Protein Interactions
  • CONCLUSIONS
  • CONSENT FOR PUBLICATION
  • CONFLICT OF INTEREST
  • ACKNOWLEDGEMENTS
  • REFERENCES
  • Use of Coarse-Grained and All-Atom Molecular Dynamics to Study Hsp70 and Hsp40 Chaperone Action
  • Ewa I. Golas1,2,¶, Magdalena A. Mozolewska1,2,¶, Pawel Krupa1,2, Cezary Czaplewski1, Harold A. Scheraga2 and Adam Liwo1,*
  • INTRODUCTION
  • METHODS
  • RESULTS
  • Mechanism of Chaperone Cycle
  • Modeling Iron-sulfur Cluster Biogenesis
  • Modeling the Structure of Isu1 from Yeast
  • Modeling the Structure of the Binary Isu1-Jac1 Complex and Assessing the Stability of its Interactions
  • Preliminary Molecular-modeling Study of the Structure of the Isu1-Jac1-Ssq1 Ternary Complex
  • CONCLUSIONS AND OUTLOOK
  • CONSENT FOR PUBLICATION
  • CONFLICT OF INTEREST
  • ACKNOWLEDGEMENTS
  • REFERENCES
  • Quaternary Structure of Chaperones from the Hsp70 System Determined by Small Angle X-Ray Scattering (SAXS) and Analytical Ultra-centrifugation
  • Júlio C. Borges1 and Carlos H.I. Ramos2,*
  • INTRODUCTION
  • Protein Folding and Molecular Chaperones
  • Small Angle X-ray Scattering (SAXS)
  • Analytical Ultracentrifugation
  • The Hsp70-folding System
  • Human Mitochondrial GrpE, Conformational Modification upon Hsp70 Binding
  • Eukaryotic Hsp40s Types I and II, on the Position of the J Domain
  • FINAL REMARKS
  • CONSENT FOR PUBLICATION
  • CONFLICT OF INTEREST
  • ACKNOWLEDGMENTS
  • REFERENCES
  • Structural Characteristics of the TPR Protein-Hsp90 Interaction: A New Target in Biotechnology
  • Ana Cauerhff1,* and Mario D. Galigniana1,2
  • INTRODUCTION
  • TPR PROTEIN CHARACTERISTICS
  • Definition and Prediction of the Sequence and Basic Structure of TPR Motifs
  • Three Dimensional Structure
  • Curvature and Shape of the TPR Domain
  • Examples of TPR Protein Structures
  • Ligand Binding
  • Folding and Stability of TPR Proteins
  • Oligomerization, Stability and Biological Functions
  • Novel TPR Protein Design
  • SEQUENCE, FUNCTION, AND BASIC STRUCTURE OF HSP90 PROTEINS: HSP90 ALPHA AND BETA
  • Introduction
  • Hsp90 Isoforms
  • Sequence and Basic Structure of Hsp90 Proteins: Hsp90 a and ß
  • Difference in Structure of Hsp90 a-and ß-isoforms
  • Conformational Changes in Hsp90
  • Sequence of Conformational Changes Induced by ATP Binding to Hsp90
  • HSP90-TPR PROTEIN INTERACTIONS
  • Introduction
  • Chaperone Cycle in SHRs
  • Hop/Sti1
  • Overall Structure
  • Hop-Hsp90 Interaction: Structural and Biophysical Aspects
  • CyP40, FKBP51 and FKBP52
  • Function
  • CyP40 Overall Structure
  • Cyp40-Hsp90 Interaction: Structural Studies
  • FKBP51: Overall Structure and Implications
  • FKBP-like Domains
  • TPR Domain
  • FKBP51-Hsp90 Interaction: Structural Studies
  • FKBP52 Structure
  • FKBP-like Domains
  • TPR Domain
  • Comparison Between FKBP51 and FKBP52
  • FKBP52-Hsp90 Complex
  • FKBP52-FK506 Complex
  • Binding Studies of Immunophilins
  • CyP40, FKBP51 and FKBP52 Interaction with Hsp90: Physico-chemical Binding Studies
  • Secondary Structure and Stability of CyP40, FKBP51 and FKBP52
  • Stability of the CyP40, FKBP51 and FKBP52
  • PP5
  • Introduction
  • PP5 Overall Structure
  • TPR Domain
  • Catalytic Phosphatase Domain
  • Relationship Between Phosphatase Activity and Hsp90 Binding
  • Structural Aspects of PP5-Hsp90 Interaction
  • PP5-Hsp90 Binding Studies
  • Structural Considerations
  • PP5 Folding Biophysical Studies
  • CHIP
  • Introduction
  • Structure
  • Hsp90 C-Terminal Binding to the CHIP TPR Domain
  • Folding and Degradation Balance Mechanism
  • TARGETING HSP90 INTERACTIONS FOR BIOTECHNOLOGICAL APPLICATIONS
  • Introduction
  • Hsp90 and Cancer
  • Inhibitors of the N-terminal Domain of Hsp90
  • Inhibitors of the C-terminal Domain of Hsp90
  • Inhibitors of the Hsp90-TPR Interactions
  • FINAL CONSIDERATIONS
  • CONSENT FOR PUBLICATION
  • CONFLICT OF INTEREST
  • ACKNOWLEDGEMENTS
  • REFERENCES
  • GroEL Chaperonin: Interaction with Polypeptides Lacking a Rigid Tertiary Structure
  • Victor V. Marchenkov, Natalia Yu Marchenko and Gennady V. Semisotnov*
  • INTRODUCTION
  • Driving Forces of GroEL Interaction with Substrate Polypeptides
  • Location of Substrate Polypeptides within a GroEL Particle and Stoichiometry of this Complex
  • The Role of Ligands in GroEL Functioning
  • Biotechnological Applications of GroEL Interaction with Substrate Polypeptides
  • CONCLUSION
  • CONSENT FOR PUBLICATION
  • CONFLICT OF INTEREST
  • ACKNOWLEDGEMENTS
  • REFERENCES
  • Mechanisms of Protein Folding by Type II Chaperonins
  • Rebecca L. Plimpton1, José M. Valpuesta2 and Barry M. Willardson1,*
  • INTRODUCTION
  • Molecular Chaperones and Proteostasis
  • THE CHAPERONINS
  • CCT STRUCTURE
  • General Features
  • Subunit Arrangement
  • SUBSTRATE RECOGNITION
  • Substrate Binding Sites on CCT
  • CCT Binding Sites on Substrates
  • MECHANISM OF FOLDING
  • CCT CO-CHAPERONES
  • Hsc70
  • PFD
  • PhLP1
  • Pdcd5
  • CONCLUDING REMARKS
  • CONSENT FOR PUBLICATION
  • CONFLICT OF INTEREST
  • ACKNOWLEDGEMENTS
  • REFERENCES
  • Mechanisms and Functions of the Cytosolic DNAJ-Hsp70 Chaperone System
  • Imad Baaklini and Jason C. Young*
  • INTRODUCTION
  • HSP70
  • Hsp70 Structure
  • ATPase Cycle
  • HSP40/DNAJ CO-CHAPERONES
  • Classification
  • Domains of DNAJs
  • J Domain
  • G/F-rich Linker
  • Substrate Binding and Cys(Zn) Regions
  • Quaternary Structure
  • NUCLEOTIDE EXCHANGE FACTORS (NEF)
  • CHAPERONE FUNCTION
  • FUNCTIONS IN CELLS AND TISSUES
  • Neurological Diseases
  • Cancer
  • Mitochondrial Import
  • Ion Channels
  • Androgen Receptor
  • Activation-Induced Cytidine Deaminase
  • Viruses
  • OUTLOOK
  • CONSENT FOR PUBLICATION
  • CONFLICT OF INTEREST
  • ACKNOWLEDGEMENTS
  • REFERENCES

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