Kooperativer Bibliotheksverbund

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Format: 1 Online-Ressource (xxix, 656 pages) , digital, PDF file(s)

ISBN: 9781139164665

Content: Antibiotic resistance and our consequent inability to treat many bacterial infections had fuelled an urgent need to understand the means by which bacteria cause disease. This has lead to a renaissance in research into bacterial disease mechanisms and the birth of a new discipline - cellular microbiology. The fruits of such research and how they have lead to an alternative perspective on bacteria-host interactions are described in this introductory textbook. The central premise is that bacteria have evolved means of manipulating normal host cell functions and overcoming host defence systems to ensure their survival. As well as offering an interesting perspective on the classical bacterial virulence mechanisms, this book outlines the molecular techniques developed to unravel the complexity of bacteria-host interactions. Research may lead not only to a better understanding of disease mechanisms, but also to alternative means of preventing and/or treating bacterial infections

Content: An introduction to bacterial diseases -- Bacterial cell biology -- Molecular analysis of bacterial virulence mechanisms -- Communication in infection -- The mucosal surface: the front line of antibacterial defence -- Immune defences against bacteria -- Bacterial adhesion as a virulence mechanism -- Bacterial invasion as a virulence mechanism -- Bacterial exotoxins -- Bacterial evasion of host defence mechanisms -- Bacteria in human health and disease: the future?

Note: Title from publisher's bibliographic system (viewed on 05 Oct 2015)

Additional Edition: ISBN 9780521792509

Additional Edition: ISBN 9780521796897

Additional Edition: Print version ISBN 9780521792509

Language: English

DOI: 10.1017/CBO9781139164665

URL: Volltext

URL: Inhaltsverzeichnis

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Format: 1 Online-Ressource (xiv, 330 pages) , digital, PDF file(s)

ISBN: 9780511546310

Content: Originally published in 2005, this book reviews understanding of the biological roles of extracellular molecular chaperones. It provides an overview of the structure and function of molecular chaperones, their role in the cellular response to stress and their disposition within the cell. It also questions the basic paradigm of molecular chaperone biology - that these proteins are first and foremost protein-folding molecules. Paradigms of protein secretion are reviewed and the evolving concept of proteins (such as molecular chaperones) as multi-functional molecules for which the term 'moonlighting proteins' has been introduced is discussed. The role of exogenous molecular chaperones as cell regulators is examined and the physiological and pathophysiological role that molecular chaperones play is described. In the final section, the potential therapeutic use of molecular chaperones is described and the final chapter asks the question - what does the future hold for the extracellular biology of molecular chaperones?

Content: Chaperone function / R.J. Ellis -- Intracellular disposition of mitochondrial molecular chaperones / R.S. Gupta [and others] -- Novel pathways of protein secretion / G. Chimini, A. Rubartelli -- Moonlighting proteins / C.J. Jeffery -- Molecular chaperones / B. Henderson, A. Shamaei-Tousi -- Cell-cell signalling properties of the chaperonins / A.R.M. Coates -- Toll-like receptor-dependent activation of antigen presenting cells by Hsp60, Hsp70 and Gp96 / R.M. Vabulas, H. Wagner -- Regulation of signal transduction by intracellular and extracellular Hsp70 / A. Asea, S. Calderwood -- Hsp72 and cell signalling / M.Y. Sherman -- Heat shock proteins, their cell surface receptors and effect on the immune system / T. Lehner [and others] -- Molecular chaperone-cytokine interactions at the transcriptional level / A. Stephanou, D.S. Latchman -- Heat shock protein release and naturally-occurring exogenous heat shock proteins / J. Frostegård, A.G. Pockley -- Hsp27 as an anti-inflammatory protein / K. Laudanski, A. De, C. Miller-Graziano -- Bip, a negative immune regulator involved in rheumatoid arthritis / V.M. Corrigal, G.S. Panayi -- Neuroendocrine aspects of the molecular chaperones ADNF and ADNP / I. Gozes [and others] -- Heat shock proteins regulate by both molecular and network cross-reactivity / F.J. Quintana, I.R. Cohen -- Heat shock protein fusions / L. Mizzen, J. Neefe -- Molecular chaperones as inducers of tumour immunity / P.P. Banerjee, Z. Li -- Gazing into the crystal ball / L. Hightower

Note: Title from publisher's bibliographic system (viewed on 05 Oct 2015)

Additional Edition: ISBN 9780521836548

Additional Edition: ISBN 9780521177474

Additional Edition: Print version ISBN 9780521836548

Language: English

DOI: 10.1017/CBO9780511546310

URL: Volltext

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Format: 1 Online-Ressource (xvi, 304 pages) , digital, PDF file(s)

ISBN: 9780511546266

Series Statement: Advances in molecular and cellular microbiology 2

Content: Our survival as multicellular organisms requires the constant surveillance of our internal and external (mucosal) environments by the multifarious elements of the innate and acquired systems of immunity. The objective of this surveillance, expensive as it is to the organisms, is to recognise and kill invading microorganisms. Over the past fifty years the cells and mediators involved in our immune defences have been painstakingly identified. However, it is only relatively recently that the ability of microorganisms to evade immunity has been recognised and investigated. Bacterial Evasion of Host Immune Responses introduces the reader to the mechanisms used by bacteria to evade both humoral and cellular immune responses, using systems ranging in complexity from the simple quorum sensing molecules - acyl homoserine lactones - to the supramolecular syringe-like devices of type III secretion systems. This book will be of interest to researchers and graduate students in microbiology, immunology, pharmacology and molecular medicine

Content: Part I. Recognition of bacteria: [Ch.] 1. The dendritic cell in bacterial infection : sentinel or Trojan horse? / Benjamin M. Chain and Janusz Marcinkiewicz -- [ch.] 2. CD1 and nonpeptide antigen recognition systems in microbial immunity / Kayvan R. Niazi, Steven A. Pocelli, and Robert L. Modlin -- [ch.] 3. The NRAMP family : co-evolution of a host/pathogen defence system -- Part II. Evasion of humoral immunity: [ch.] 4. Evasion of complement system pathwas by bacteria / Michael A. Kerr and Brian Henderson -- [ch.] 5. Bacterial immunoglobulin-evading mechanisms : lg-dregrading and lg-binding proteins / Mogen Kilian -- [ch.] 6. Evasion of antibody responses : bacterial phase variation / Nigel J. Saunders -- Part III. Evasion of cellular immunity: [ch.] 7. Type III protein secretion and resistance to phagocytosis / Ake Forsberg, Roland Rosqvist and Maria Fallman -- [ch.] 8. Bacterial superantigens and immune evasion / John Fraser, Thomas Proft, Vickery Arcus and Edward Baker -- [ch.] 9. Bacterial quorum sensing signalling molecules as immune modulators / David Pritchard, Doreen Hooi, Eleanor Watson, Sek Chow, Gary Telford, Barrie Bycroft, Siri Ram Chhabra, Christopher Harty, Miguel Camara, Stephen Diggle and Paul Williams -- [ch.] 10. Microbial modulation of cytokine networks / B. Henderson and Rob M. Seymour -- [ch.] 11. Enterotoxins : adjuvants and immune inhibitors / Jan-Michael Klapproth and Michael S. Donnenberg -- [ch.]. 12. Type III protein secretion and inhibition of NF-kB / Klaus Ruckdeschel, Bruno Rouot and Jü̈rgen Heesemann

Note: Title from publisher's bibliographic system (viewed on 05 Oct 2015)

Additional Edition: ISBN 9780521801737

Additional Edition: Print version ISBN 9780521801737

Language: English

DOI: 10.1017/CBO9780511546266

URL: Volltext

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Format: Online-Ressource (XIII, 297 p. 28 illus., 13 illus. in color, digital)

ISBN: 9789400747401

Series Statement: Heat Shock Proteins 6

Content: Since the beginning of the 21st Century there has been a rapid increase in our understanding of the cellular trafficking mechanisms of molecular chaperones in eukaryotes and in prokaryotes. In the former, molecular chaperone trafficking can occur between the various cellular compartments, with concomitant movement of other proteins. Such events can also result in the release of molecular chaperones from cells. In bacteria, molecular chaperones are involved in the trafficking of other proteins and are themselves released into the external milieu. The increasing appreciation of the role of molecular chaperones and Protein-Folding Catalysts in the interplay between bacteria and the cells of their hosts is now an important area of research for understanding the mechanisms of infectious diseases. This volume brings together experts in the biochemistry, cellular biology, immunology and molecular biology of molecular chaperones and Protein-Folding Catalysts with a focus on the mechanisms of cellular trafficking of these proteins and the role of these variegated trafficking mechanisms in both human and animal health and disease.

Note: Description based upon print version of record , Preface; Contents; Contributors; Note on Nomenclature; Chapter1 Discovery of the Cellular Secretion of Cell Stress Proteins; 1.1 Introduction; 1.2 The Path to a New Discovery; 1.3 Hsps are Released from Mammalian Cells by an Active Process Other than the ER-Golgi Pathway: The Odyssey of Peer Review; 1.3.1 Hightower and Guidon 1989; 1.4 Extracellular Hsps-Still Hot; 1.5 Mechanism of Extracellular Hsp Release; 1.6 Hsps on the Cell Surface; References; Chapter 2 Discovery of the Extracellular AgonistActions of Molecular Chaperonesand Protein-Folding Catalysts; 2.1 Introduction , 2.2 Secretion of Molecular Chaperones2.3 Identification of the Cell Signalling Agonist Actionsof Cell Stress Proteins; 2.3.1 Chaperonin 10 (HSPE1); 2.3.2 Macrophage Migration Inhibitory Factor (MIF); 2.3.3 Thioredoxin; 2.3.4 Peptidylprolyl Isomerases; 2.3.5 Chaperonin (Hsp)60 (HSPD1); 2.3.6 Hsp70; 2.3.7 Hsp27; 2.4 Conclusions; References; Chapter3 Molecular Chaperones and Protein-Folding Catalysts in Biological Fluids; References; Chapter4 Hsp27 Phosphorylation Patterns and Cellular Consequences; 4.1 Introduction; 4.2 Phosphorylation/Dephosphorylation of HSP27 , 4.3 Function of HSP27 Phosphorylation4.3.1 HSP27 Phosphorylation and Oligomerization; 4.3.2 HSP27 Phosphorylation and Chaperone Function; 4.3.3 HSP27 Phosphorylation and F-actin Dynamics and F-actin-Dependent Processes; 4.3.4 HSP27 Phosphorylation and Cytoprotection/Anti-Apoptotic Function; 4.3.5 HSP27 Phosphorylation and Differentiation; 4.3.6 HSP27 Phosphorylation and Bone Metabolism; 4.3.7 HSP27 Phosphorylation and Ageing; 4.3.8 HSP27 Phosphorylation and Cell Proliferation; 4.3.9 HSP27 Phosphorylation and DNA Repair; 4.3.10 HSP27 Phosphorylation and Subcellular Localization , 4.3.11 HSP27 Phosphorylation and Vascular Functions4.3.12 HSP27 Phosphorylation and Gene Expression; 4.4 Aberrant HSP27 Phosphorylation and Diseases; 4.4.1 Cancer; 4.4.2 Cardiovascular Diseases; 4.4.3 Hypoxia-Induced Injury; 4.4.4 HSP27 Phosphorylation and Viral Infection; 4.4.5 Hsp27 Phosphorylation and the Autoimmune Disease Pemphigus; 4.4.6 Hsp27 Phosphorylation in Kidney Diseases; 4.4.7 HSP27 Phosphorylation and Neurodegenerative Diseases; 4.5 Modulating HSP27 Phosphorylation and Therapy; 4.6 Conclusion and Future Perspective; References , Chapter 5 Evidence on Cholesterol-Controlled Lipid RaftInteraction of the Small Heat Shock ProteinHSPB11Abbreviation; 5.1 Introduction; 5.2 Membrane-Association of sHSPs: Overview; 5.3 HSPB11 is a Novel Molecular Chaperone; 5.3.1 HSPB11 Protects the Mitochondrial Membrane System; 5.3.2 Role of HSPB11 in Lipid Raft Formation; 5.3.3 Regulation of Kinase Cascades by HSPB11; 5.3.4 Covalent Modification of HSPB11; 5.3.5 HSPB11 Binds to a Lipid Monolayerin a Cholesterol-Dependent Manner; 5.4 Concluding Remarks; References; Chapter6 Hsp70 Chaperone Systems in Vesicular Trafficking , 6.1 The Hsp70 Chaperone System , Preface -- Contents -- Note on Nomenclature -- Author Addresses -- Section 1 Historical Introduction to Secreted Cell Stress Proteins as Signalling Proteins -- Discovery of the Cellular Secretion of Cell Stress Proteins -- Discovery of the Agonist Activities of Molecular Chaperones and Protein-Folding Catalysts -- Identification of Cell Stress Proteins in Biological Fluids -- Section 2 Intracellular Trafficking of Molecular Chaperones and its Consequences -- Hsp27 Phosphorylation Patterns and Cellular Consequences -- Evidence on Cholesterol-Controlled Lipid Raft Interaction of the Small Heat Shock Protein HSPB11 -- Hsp70 Chaperone Systems in Vesicular Trafficking -- Pathways of Hsp70 Release: Lessons from Cytokine Secretion -- Nucleolin: A Novel Intracellular Transporter of HSPA1A -- The Hsp90-Based Protein Trafficking System and Linkage to Protein Quality Control -- Section 3 Molecular Chaperones as Cell Surface Receptors and Receptor Ligands -- Cell Surface Molecular Chaperones and the LPS Receptor -- Hsp60: An Unexpected Cell Surface Receptor in Prokaryotes and Eukaryotes -- Pathophysiological Barriers Impeding the Delivery of Heat Shock Protein (HSP)-based Macromolecules and Nanotherapeutics to Solid Tumors -- The Chaperokine Activity of HSPA1A -- Molecular Chaperones and Scavenger Receptors: Binding and Trafficking of Molecular Chaperones by Class F and Class H Scavenger Receptors -- Grp78 (BiP): A Multifunctional Cell Surface Receptor -- Section 4 Extracellular Secretion of Molecular Chaperones in Prokaryotes and Eukaryotes -- Mycobacterium Tuberculosis Hsp60 as a Key Virulence Factor in Tuberculosis -- Hsp90 vs Conventional Growth Factors in Acute and Diabetic Wound Healing -- Circulating Molecular Chaperones in Health and Disease -- Index.

Additional Edition: ISBN 9789400747395

Additional Edition: Buchausg. u.d.T. ISBN 978-94-007-4739-5

Language: English

DOI: 10.1007/978-94-007-4740-1

URL: Volltext

URL: Volltext  (lizenzpflichtig)

URL: Cover

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Format: Online-Ressource (XVII, 406 p. 55 illus., 33 illus. in color, online resource)

ISBN: 9789400767874

Series Statement: Heat Shock Proteins 7

Content: Microbial infection is increasingly seen as a problem as we begin to run out of antibiotics. Understanding how microbes cause disease is essential. In recent years it has begun to emerge that bacteria, fungi, protozoa and viruses can use their cell stress proteins to cause infection. This volume brings together the world's leading experts in the study of the microbial and human cell stress proteins that are involved in enabling microorganisms to infect humans and cause serious disease

Note: Description based upon print version of record , Bacterial Cell Stress ResponsesA Brief Introduction to Eukaryotic Cell Stress Proteins -- New Thoughts on Protein Moonlighting -- Chaperonin 10 a Pro- and Anti-inflammatory Host Modulator -- Helicobacter pylori peptidyl prolyl cis, trans isomerase: a modulator of the host immune response -- Macrophage Infectivity Promoter: An FK506-Binding Peptidylprolyl Isomerase with Collagen-Binding and Transmigrating Activity -- Evolution of Bacterial Chaperonin 60 Paralogues and Moonlighting Activity -- Mycobacterium tuberculosis Chaperonins as Novel Virulence Factors -- Legionella pneumophila Chaperonin 60: A Multifunctional Virulence Protein -- Chaperonin 60.1 of the Chlamydiae (cHSP60) as a Major Virulence Determinant -- Symbiotic Bacterial Chaperonin 60 and Plant Virus Transmission -- Histoplasma capsulatum Chaperonin 60: A Novel Adhesin and Vaccine Candidate -- The role of stress-induced activation of HSP70 in dendritic cells, CD4+ T cell memory and adjuvanticity -- Candida albicans Ssa: A Hsp70 Homologue and Virulence Factor -- Hsp90 plays a role in host-bacterial interactions: Insight gained from Acanthamoeba castellanii -- Role of Peptidyl-Prolyl cis/trans Isomerases in Cellular Uptake of Bacterial Protein Toxins -- Listeria monocytogenes and Host Hsp60 - an Invasive Pairing -- Cell Surface Stress Proteins and the Receptor for Lipopolysaccharide -- Grp78 (BiP) a Cell Surface Receptor for Viruses -- BiP (Grp78): a Target for Escherichia coli Subtilase Cytotoxin -- Cholera Toxin Interactions with Host Cell Stress Proteins -- Endoplasmic reticulum stress-associated Gp96 chaperone is a host receptor for Adherent-Invasive E. coli -- Escherichia coli K1 Meningitis and Heat Shock Protein, Gp96 -- Bacterial Cell Stress Protein Clp: A Novel Antibiotic Target -- Host Neuroendocrine Stress Hormones Driving Bacterial Behaviour and Virulence.

Additional Edition: ISBN 9789400767867

Additional Edition: Druckausg. Moonlighting cell stress proteins in microbial infections Dordrecht : Springer, 2013 ISBN 9789400767867

Language: English

Subjects: Biology

DOI: 10.1007/978-94-007-6787-4

URL: Volltext

URL: Volltext  (lizenzpflichtig)

URL: Cover