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Cellular trafficking of cell stress proteins in health and disease[electronic resource] /

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
杜威分類號:	572.645
書名/作者:	Cellular trafficking of cell stress proteins in health and disease/ edited by Brian Henderson, A. Graham Pockley.
其他作者:	Henderson, Brian.
出版者:	Dordrecht : : Springer Netherlands :, 2012.
面頁冊數:	281 p. : : ill., digital ;; 24 cm.
Contained By:	Springer eBooks
標題:	Molecular chaperones.
標題:	Proteins - Physiological transport.
標題:	Biomedicine.
標題:	Human Physiology.
標題:	Life Sciences, general.
標題:	Neurosciences.
標題:	Molecular Medicine.
ISBN:	9789400747401 (electronic bk.)
ISBN:	9789400747395 (paper)
內容註:	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.
摘要、提要註:	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.
電子資源:	http://dx.doi.org/10.1007/978-94-007-4740-1

Cellular trafficking of cell stress proteins in health and disease[electronic resource] /
Cellular trafficking of cell stress proteins in health and disease[electronic resource] /edited by Brian Henderson, A. Graham Pockley. - Dordrecht :Springer Netherlands :2012. - 281 p. :ill., digital ;24 cm. - Heat shock proteins,v.61877-1246 ;. - Heat shock proteins ;v.6..

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.

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.

ISBN: 9789400747401 (electronic bk.)Subjects--Topical Terms:

490511
Molecular chaperones.

LC Class. No.: QP552.M64 / C45 2012

Dewey Class. No.: 572.645

Cellular trafficking of cell stress proteins in health and disease[electronic resource] /
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