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  • Book
    Robert J. Binder, Pramod K. Srivastava, editors.
    Summary: Experts from around the world review the current field of the immunobiology of heat shock proteins, and provide a comprehensive account of how these molecules are spearheading efforts in the understanding of various pathways of the immune system. This one-stop resource contains numerous images to both help illustrate the research on heat shock proteins, and better clarify the field for the non-expert. Heat shock proteins (HSPs) were discovered in 1962 and were quickly recognized for their role in protecting cells from stress. Twenty years later, the immunogenicity of a select few HSPs was described, and for the past 30 years, these findings have been applied to numerous branches of immunology, including tumor immunology and immunosurveillance, immunotherapy, etiology of autoimmunity, immunotherapy of infectious diseases, and expression of innate receptors. While HSPs can be used to manipulate immune responses by exogenous administration, they appear to be involved in initiation of de novo immune responses to cancer and likely in the maintenance of immune homeostasis.

    Contents:
    Intro; Introduction and History; Contents; Part I: Structure of the HSPs in Relation to Chaperoning Peptides and Proteins;
    Chapter 1: Hsp70-Substrate Interactions; 1.1 Introduction; 1.2 Hsp70 Functional Cycle; 1.3 Structural Basis for Hsp70-Substrate Interactions; 1.4 Mechanism of Action of Hsp70 Chaperones; 1.5 Interactions of Hsp70 Chaperones with Protein Substrates; 1.6 Role of Co-Chaperones; 1.7 Concluding Remarks; References;
    Chapter 2: Molecular Chaperone Inhibitors; 2.1 The Hsp70 and Hsp90 Chaperone Cycle; 2.2 Hsp90 Inhibitors and Their Binding Sites; 2.2.1 Hsp90 N-Terminal Inhibitors. 2.2.2 Benzoquinone Ansamycin Inhibitors2.2.3 Radicicol and Analogous Inhibitors; 2.2.4 Additional Hsp90 Second-Generation Inhibitors; 2.2.5 Consequences of Different N-Terminal Inhibitors for Hsp90 Specificity and Conformation; 2.2.6 Hsp90 C-Terminal Inhibitors; 2.3 Grp94; 2.3.1 Allosteric Inhibitors of Grp94; 2.4 Hsp90 Co-Chaperone Inhibitors; 2.5 Hsp70/Hsc70; 2.6 Hsp70/Hsc70 Inhibitors and Their Binding Sites; 2.6.1 ATP-Competitive Inhibitors of Hsp70/Hsc70; 2.6.2 Allosteric Inhibitors of Hsp70/Hsc70; 2.6.3 Peptide Mimetics Targeting Hsp70/Hsc70; 2.7 Hsp40; 2.8 Small Hsps-Hsp27. 2.8.1 Antisense Oligonucleotides Targeting Hsp272.9 Small Hsps: Clusterin; 2.9.1 Antisense Oligonucleotides Targeting Clusterin; References; Part II: Exposure of HSPs to Immune Cells;
    Chapter 3: Extracellular Heat Shock Proteins as Stress Communication Signals; 3.1 Introduction; 3.2 Types of Cellular Communication; 3.3 Extracellular HSP as Communication Signals; 3.4 Extracellular HSP in Pathological Conditions; 3.5 Mechanisms of HSP Export; 3.6 The Stress Observation System; 3.7 Conclusions; References; Part III: Regulation of Immune Responses by Extracellular HSPs. 5.2 The Visionary Work of Dr. Eckhard Podack and Development of the State-of-the-Art Secreted gp96-Ig Vaccine Approach5.2.1 Construction of gp96-Ig; 5.2.2 Principles of Secreted gp96-Ig Vaccine Approach; 5.3 The State of the Knowledge of Antitumor Vaccination with gp96-Ig; 5.3.1 Allogeneic gp96 Vaccine; 5.3.2 Combined Therapeutic Approach; 5.4 The State of Knowledge of Anti-Infectious Vaccination with gp96-Ig; 5.4.1 Secreted SIV/HIV gp96-Ig Vaccine; 5.4.1.1 Gp96SIVIg as a Novel Adjuvant for Antibody Production.
    Chapter 4: The Heat Shock Protein-CD91 Pathway and Tumor Immunosurveillance4.1 Heat Shock Proteins as Chaperones of Macromolecules; 4.2 Immune Responses Elicited by Extracellular HSPs; 4.3 Extracellular HSPs as the Molecular Signature for Immunological Responsiveness; 4.4 The Role of Extracellular HSPs in Tumor Immunosurveillance; 4.5 Conclusion; References;
    Chapter 5: Bridging the Gaps in the Vaccine Development: Avant-Garde Vaccine Approach with Secreted Heat Shock Protein gp96-Ig; 5.1 Introduction.
    Digital Access Springer 2018
  • Article
    Papermaster DS, Schneider BG, Zorn MA, Kraehenbuhl JP.
    J Cell Biol. 1978 Apr;77(1):196-210.
    Adult vertebrate retinal cells (rod and cones) continuously synthesize membrane proteins and transport them to the organelle specialized for photon capture, the outer segment. The cell structures involved in the synthesis of opsin have been identified by means of immunocytochemistry at the electron microscope level. Two indirect detection systems were used: (a) rabbit antibodies to frog opsin were localized with ferritin conjugated F(ab')2 of sheep antibodies to rabbit F(ab')2 and (b) sheep antibodies to cattle opsin were coupled to biotin and visualized by means of avidin-ferritin conjugates (AvF). The reagents were applied directly to the surface of thin sections of frog retinal tissues embedded in glutaraldehyde cross-linked bovine serum albumin (BSA). Specific binding of anti-opsin antibodies indicates that opsin is localized in the disks of rod outer segments (ROS), as expected, and in the Golgi zone of the rod cell inner segments. In addition, we observed quantitatively different labeling patterns of outer segments of rods and cones with each of the sera employed. These reactions may indicate immunological homology of rod and cone photopigments. Because these quantitiative variations of labeling density extend along the entire length of the outer segment, they also serve to identify the cell which has shed its disks into adjacent pigment ipithelial cell phagosomes.
    Digital Access Access Options
  • Journal
    Print Began publication with the issue for 1950.