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Dendritic cell interactions with bacteria 1st Edition by Maria Rescigno ISBN B000SEI712 9780521855860

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Dendritic cell interactions with bacteria 1st Edition Maria Rescigno Digital Instant Download

Author(s): Maria Rescigno
ISBN(s): 9780521815253, 0521809401
Edition: 1
File Details: PDF, 2.88 MB
Year: 2007
Language: english
SKU: EB-1355632 Category: Tag:

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Product details:
ISBN 10: B000SEI712
ISBN 13: 9780521855860
Author: Maria Rescigno

Emerging evidence suggests that dendritic cells play a major role in the orchestration of the immune response to bacteria. This volume introduces the reader to the complex world of dendritic cells and describes how the intimate interplay between dendritic cells, bacteria and the environment dictates either the induction of immunity or tolerance to the encountered microorganisms. It discusses how this can allow organisms to tolerate beneficial bacteria and to react against pathogens, as well as the strategies pathogenic bacteria have evolved to escape dendritic cell patrolling. Expert contributors discuss everything from bacterial capture and recognition to their killing, processing and the induction of adaptive immunity. Particular focus is on the tissue context in which bacteria are handled by dendritic cells and on possible defects therein, which may potentially lead to chronic infection or inflammation. Graduate students and researchers will find this an invaluable overview of current dendritic cell biology research.

Dendritic cell interactions with bacteria 1st Edition Table of contents:

1 Fundamentals of Protein Folding

1.1 Folding–misfolding–nonfolding crossroads

1.2 Protein folding

1.2.1 Protein-Folding Code

1.2.2 Protein-Folding Models

1.2.3 Polymer Aspects of Protein Folding

1.2.4 Different Conformations Seen in Protein Folding

1.3 Nonfolding

1.3.1 Intrinsically Disordered Proteins and Their Abundance

1.3.2 Some Functional Advantages of IDPs

1.3.3 Function-Induced Folding of IDPs

1.3.4 IDPs and Human Diseases

1.3.5 How Does an Amino Acid Sequence Encode Intrinsic Disorder?

1.3.6 Polymer Aspects of Nonfolding

1.4 Misfolding

1.4.1 Molecular Mechanisms of Protein Misfolding

1.4.2 Fibrillogenesis of Globular Proteins: Requirement for Partial Unfolding

1.4.3 Fibrillogenesis of IDPs: Requirement for Partial Folding

1.4.4 Conformational Prerequisites for Amyloidogenesis

1.4.5 Multiple Pathways of Protein Misfolding

1.4.6 Polymer Aspects of Protein Misfolding

References

2 Recruiting Unfolding Chaperones to Solubilize Misfolded Recombinant Proteins

2.1 Introduction

2.2 Chemical Chaperones

2.3 PPIs and PDIs are folding enzymes

2.4 Molecular Chaperones

2.5 The small Hsps

2.6 Hsp90

2.7 Hsp70/Hsp40

2.8 GroEL Chaperonins

2.9 Conclusions

References

3 Osmolytes as Chemical Chaperones to Use in Protein Biotechnology

3.1 Introduction

3.2 Protein-destabilizing conditions and counteracting mechanisms: shared or independent routes?

3.3 Proposed molecular mechanisms for osmolyte activities

3.4 Osmolytes and expression of recombinant proteins

3.5 Biotechnological relevance of osmolytes for preserving purified proteins

3.6 Conclusions

References

4 Inclusion Bodies in the Study of Amyloid Aggregation

4.1 Introduction

4.2 Structure of IBs

4.2.1 Amyloid-like Nature of IBs

4.2.2 Detection and Characterization of Amyloid Conformations Inside IBs

4.3 Formation of IBs

4.3.1 In Vivo Formation Kinetics

4.3.2 Molecular Determinants of IB Aggregation

4.3.3 Sequence Specificity in IB Formation

4.4 IBs as the simplest model for in vivo amyloid toxicity

4.4.1 The Fitness Cost of Amyloid Aggregation

4.4.2 Citotoxicity of Amyloid IBs

4.4.3 Infectious Properties of IBs

4.5 Using IBs to screen for amyloid inhibitors

4.6 Conclusions

References

5 Protein Aggregation in Unicellular Eukaryotes

5.1 Introduction

5.2 UPR: Unfolded protein response in the ER

5.3 Removing persistent misfolded proteins with the proteasome

5.4 Lysosomal/vacuolar proteolysis (overload UPS)

5.4.1 Autophagy

5.4.2 Selective Types of Autophagy

5.5 Refolding of protein aggregates in cytosol and nucleus

5.6 JUNQ and IPOD

5.7 Segregation of aggregates in yeast

5.8 Proteins forming nonpathological amyloid-like fibrils in unicellular eukaryotes

5.9 Humanized yeast models

5.10 Concluding remarks

Acknowledgments

References

6 Structural Properties of Bacterial Inclusion Bodies

6.1 Introduction

6.2 Intermediate species in inclusion body formation

6.3 Structural characterization of inclusion bodies

6.3.1 Composition, Overall Structure, Shape, and Morphology

6.3.2 Native-like and Amyloid-like Structures

6.4 Appendix: experimental methods Used in IB structural characterization

References

7 Residue-Specific Structural Studies of Inclusion Bodies

7.1 Introduction

7.2 Molecular structure of amyloid fibrils

7.2.1 Structure of Peptide Amyloid Fibrils as Determined by X-ray Crystallography

7.2.2 Structure of HET-s Amyloid Fibrils as Determined by Solid -State NMR Spectroscopy

7.2.3 Cross- β -Sheet Core of HET-s Amyloid Fibrils as Determined by Solution-tate NMR and the H /D

7.3 Structural study of inclusion bodies with solution-state NMR and the H/D-exchange method

7.3.1 Experimental Mechanism of Solution-State NMR and the H/D-Exchange Method

7.3.2 Example: Structural Study of BMP2 (13–74) Inclusion Bodies

7.4 Structural study of inclusion bodies with solid-state NMR spectroscopy

7.4.1 Structural Study of HET-s(218–289) Inclusion Bodies

7.4.2 Structural Study of FHA2 Inclusion Bodies

7.5 Summary

References

8 Biomedical Applications of Bacterial Inclusion Bodies

8.1 Biology of IB proteins

8.2 IB protein quality

8.3 IB architecture

8.4 IBs as biomaterials

8.5 Purification of IBs

8.6 IBs in tissue engineering

8.7 Slow drug release from bacterial IBs used as Nanopills

8.8 Conclusions

References

9 Aggregation of Recombinant Proteins: Understanding Basic Issues to Overcome Production Bottlenecks

9.1 Introduction

9.2 How do cells react to the overproduction of a recombinant protein?

9.2.1 Physiological Responses to Protein Overproduction

9.2.2 Stress Response to Protein Overproduction

9.2.3 Effects of Protein Overproduction on the Cell Membrane

9.3 Structure, composition, and mechanism of deposition of inclusion bodies

9.4 From knowledge to application

9.4.1 Growth Conditions

9.4.2 Coexpression with Chaperones and Folding Modulators

9.4.3 Expressivity Tags

9.4.4 Protein Engineering as a Tool to Improve Protein Solubility

9.4.5 What Have We Learned? Lessons from Directed Evolution

9.5 Advantages of using inclusion bodies

References

10 Fusion to a Pull-Down Module : Designing Enzymes to Form BioCatalytically Active Insoluble Aggreg

10.1 Introduction

10.2 A short glance at CLEAs

10.3 Pull-down modules and their use in inducing selective protein aggregation

10.4 Self-aggregating tags as pull-down modules

10.5 Pull-down modules undergoing ordered self-assembly

10.6 Auto-encapsulation

10.7 Even simpler enzymatically active inclusion bodies derived from recombinant proteins as such

10.8 Conclusions

References

Index

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