000838539 000__ 05716cam\a2200529Ii\4500 000838539 001__ 838539 000838539 005__ 20230306144547.0 000838539 006__ m\\\\\o\\d\\\\\\\\ 000838539 007__ cr\un\nnnunnun 000838539 008__ 180412s2018\\\\sz\\\\\\ob\\\\001\0\eng\d 000838539 019__ $$a1031344048$$a1031361837$$a1034547470$$a1038429709 000838539 020__ $$a9783319690421$$q(electronic book) 000838539 020__ $$a3319690426$$q(electronic book) 000838539 020__ $$z9783319690407 000838539 020__ $$z331969040X 000838539 0247_ $$a10.1007/978-3-319-69042-1$$2doi 000838539 035__ $$aSP(OCoLC)on1031090405 000838539 035__ $$aSP(OCoLC)1031090405$$z(OCoLC)1031344048$$z(OCoLC)1031361837$$z(OCoLC)1034547470$$z(OCoLC)1038429709 000838539 040__ $$aN$T$$beng$$erda$$epn$$cN$T$$dN$T$$dGW5XE$$dEBLCP$$dYDX$$dOCLCF$$dAZU$$dCOO$$dUPM$$dUAB$$dOCLCQ 000838539 049__ $$aISEA 000838539 050_4 $$aQP552.H43 000838539 08204 $$a572.6$$223 000838539 24500 $$aHeat shock proteins in the immune system /$$cRobert J. Binder, Pramod K. Srivastava, editors. 000838539 264_1 $$aCham :$$bSpringer,$$c2018. 000838539 300__ $$a1 online resource. 000838539 336__ $$atext$$btxt$$2rdacontent 000838539 337__ $$acomputer$$bc$$2rdamedia 000838539 338__ $$aonline resource$$bcr$$2rdacarrier 000838539 347__ $$atext file$$bPDF$$2rda 000838539 504__ $$aIncludes bibliographical references and index. 000838539 5050_ $$aIntro; Introduction and History; Contents; Part I: Structure of the HSPs in Relation to Chaperoning Peptides and Proteins; Chapter 1: Hsp70-Substrate Interactions; 1.1 Introduction; 1.2 Hsp70 Functional Cycle; 1.3 Structural Basis for Hsp70-Substrate Interactions; 1.4 Mechanism of Action of Hsp70 Chaperones; 1.5 Interactions of Hsp70 Chaperones with Protein Substrates; 1.6 Role of Co-Chaperones; 1.7 Concluding Remarks; References; Chapter 2: Molecular Chaperone Inhibitors; 2.1 The Hsp70 and Hsp90 Chaperone Cycle; 2.2 Hsp90 Inhibitors and Their Binding Sites; 2.2.1 Hsp90 N-Terminal Inhibitors 000838539 5058_ $$a2.2.2 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 000838539 5058_ $$a2.8.1 Antisense Oligonucleotides Targeting Hsp272.9 Small Hsps: Clusterin; 2.9.1 Antisense Oligonucleotides Targeting Clusterin; References; Part II: Exposure of HSPs to Immune Cells; Chapter 3: Extracellular Heat Shock Proteins as Stress Communication Signals; 3.1 Introduction; 3.2 Types of Cellular Communication; 3.3 Extracellular HSP as Communication Signals; 3.4 Extracellular HSP in Pathological Conditions; 3.5 Mechanisms of HSP Export; 3.6 The Stress Observation System; 3.7 Conclusions; References; Part III: Regulation of Immune Responses by Extracellular HSPs 000838539 5058_ $$aChapter 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 000838539 5058_ $$a5.2 The Visionary Work of Dr. Eckhard Podack and Development of the State-of-the-Art Secreted gp96-Ig Vaccine Approach5.2.1 Construction of gp96-Ig; 5.2.2 Principles of Secreted gp96-Ig Vaccine Approach; 5.3 The State of the Knowledge of Antitumor Vaccination with gp96-Ig; 5.3.1 Allogeneic gp96 Vaccine; 5.3.2 Combined Therapeutic Approach; 5.4 The State of Knowledge of Anti-Infectious Vaccination with gp96-Ig; 5.4.1 Secreted SIV/HIV gp96-Ig Vaccine; 5.4.1.1 Gp96SIVIg as a Novel Adjuvant for Antibody Production 000838539 506__ $$aAccess limited to authorized users. 000838539 520__ $$aExperts from around the world review the current field of the immunobiology of heat shock proteins, and provide a comprehensive account of how these molecules are spearheading efforts in the understanding of various pathways of the immune system. This one-stop resource contains numerous images to both help illustrate the research on heat shock proteins, and better clarify the field for the non-expert. Heat shock proteins (HSPs) were discovered in 1962 and were quickly recognized for their role in protecting cells from stress. Twenty years later, the immunogenicity of a select few HSPs was described, and for the past 30 years, these findings have been applied to numerous branches of immunology, including tumor immunology and immunosurveillance, immunotherapy, etiology of autoimmunity, immunotherapy of infectious diseases, and expression of innate receptors. While HSPs can be used to manipulate immune responses by exogenous administration, they appear to be involved in initiation of de novo immune responses to cancer and likely in the maintenance of immune homeostasis. . 000838539 588__ $$aOnline resource; title from PDF title page (viewed April 16, 2018). 000838539 650_0 $$aHeat shock proteins. 000838539 650_0 $$aImmune system. 000838539 7001_ $$aBinder, Robert J.,$$eeditor. 000838539 7001_ $$aSrivastava, Pramod K.,$$eeditor. 000838539 77608 $$iPrint version: $$z331969040X$$z9783319690407$$w(OCoLC)1004183449 000838539 852__ $$bebk 000838539 85640 $$3SpringerLink$$uhttps://univsouthin.idm.oclc.org/login?url=http://link.springer.com/10.1007/978-3-319-69042-1$$zOnline Access$$91397441.1 000838539 909CO $$ooai:library.usi.edu:838539$$pGLOBAL_SET 000838539 980__ $$aEBOOK 000838539 980__ $$aBIB 000838539 982__ $$aEbook 000838539 983__ $$aOnline 000838539 994__ $$a92$$bISE