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  • 1
    Keywords: Biochemistry ; Protein Science ; Springer eBooks
    Description / Table of Contents: Chapter 1. Chaperokine Activity of Heat Shock Protein -- Chapter 2. Extracellular HSP70, Neuroinflammation and Protection against Viral Virulence -- Chapter 3. The Biology of Extracellular HSP60 -- Chapter 4. Heat Shock Protein 60: A Mediator of Atherosclerosis and its Potential Therapeutic Role -- Chapter 5. Role of Heat Shock Protein 90 in Autoimmune Inflammatory Rheumatic Diseases -- Chapter 6. Upregulation of Cytoprotective Chaperones Mediate Better Tolerance to High Altitude -- Chapter 7. Role of Chaperone Mediated Autophagy in Viral Infections -- Chapter 8. Chaperones in Sterile Inflammation and Injury -- Chapter 9. Chaperone in Inflammation and Immunomodulation: Resistin and PPlases -- Chapter 10. Exercise-induced Chaperokine Activity of Hsp70: Possible Role in Chronic Diseases -- Chapter 11. Physical Exercise and Heat Shock Proteins -- Chapter 12. Extracellular Hsp90 Governs Spatio-temporal Regulation of Biological Responses -- Chapter 13. HSP47 and its Involvement in Fibrotic Disorders -- Chapter 14. Therapeutic Implications of Heat Shock Proteins in Cancer -- Chapter 15. Targeting Heat Shock Proteins for Immunotherapy -- Chapter 16. Modulation of Heat Shock Proteins by Natural Products
    Abstract: Chaperokine is a term that describes the unique function of extracellular heat shock protein (eHsp) as both chaperone and cytokine. The cellular consequence of binding and signaling of eHsp is the stimulation of a potent and long lasting immune response. eHsp induces a plethora of immune responses including the release of bioactive mediators such as cytokines, chemokines, nitric oxide, apotogenic mediators, stimulation of the innate and adaptive immune response, migration and maturation of dendritic cells (DC) and the enhancement of natural killer cell-mediated cellular cytotoxicity. This edited book provides the most comprehensive review of contemporary knowledge of the chaperokine activity of heat shock proteins (HSP) in biology and medicine. Using an integrative approach to understanding the chaperokine activity of HSP, the contributors provide an overview of novel mechanisms, signal transduction pathways and a concise understanding of how the principles of the chaperokine activity of HSP has been harnessed for therapeutic gain. Key basic and clinical research laboratories from major universities, academic medical hospitals, biotechnology and pharmaceutical laboratories around the world have contributed chapters that review present cutting-edge research activities and importantly, the future direction of chaperokine research. The book is a must read for researchers, postdoctoral fellows and graduate students in the fields of Translational Medicine, Clinical Psychology, Human Physiology, Zoology, Botany, Biotechnology, Molecular Medicine, Infectious Disease, Pathology and Pharmaceutical Sciences, as well as for researchers involved in Drug Discovery
    Pages: IX, 320 p. 49 illus., 28 illus. in color. : online resource.
    ISBN: 9783030022549
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  • 2
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    Cham : Springer International Publishing
    Keywords: Medicine ; Human Genetics ; Pharmaceutical technology ; Biomedicine ; Pharmaceutical Sciences/Technology ; Human Genetics ; Springer eBooks
    Abstract: The book Regulation of Heat Shock Protein Responses provides the most comprehensive review on contemporary knowledge on the regulation of HSP responses and its consequences to human diseases and disorders. Using an integrative approach to understanding the regulation of HSP responses, the contributors provide a synopsis of novel mechanisms by which HSP responses are regulated under normal physiological and pathophysiological conditions. Key basic and clinical research laboratories from major universities and academic medical hospitals around the world contribute chapters that review present research activity and importantly project the field into the future. The book is a must read for researchers, postdoctoral fellows and graduate students in the fields of Translational Medicine, Human Physiology, Biotechnology, Molecular Medicine, Infectious Diseases and Pathology
    Pages: IX, 472 p. 99 illus., 79 illus. in color. : online resource.
    ISBN: 9783319747156
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  • 3
    Keywords: Biochemistry ; Protein Science ; Springer eBooks
    Description / Table of Contents: Molecular Chaperones and the Nuclear Response to Stress -- Extracellular Hsp70 and Low-grade Inflammation- and Stress-related Pathologies -- Heat Shock Proteins and Endoplasmic Reticulum Stress -- Features of Stress-induced Changes of HSP70 Expression in Populations of Immunocompetent Cells -- Relationship between Oxidative Stress-induced Effects and Physical Exercise -- Role of Heat Shock Proteins in Oxidative Stress and Stress Tolerance -- Heat Shock Proteins in Oxidative and Nitrosative Stress -- High Content Screening of Small Molecule Modulators Targeting Heat Shock Response Pathway -- Regulation of Autophagy by the Heat Shock Factor 1-mediated Stress Response Pathway -- Involvement of Heat Shock Proteins in Invertebrate Anhydrobiosis -- Molecular Stress Responses against Trace Metal Contamination in Aquatic Invertebrates -- Heat Shock-induced Transcriptional and Translational Arrest in Mammalian Cells -- HSP70 Mediated Stress Modulation in Plants -- Small Heat Shock Proteins in Stress Response of Higher Eukaryotes
    Abstract: The book Heat Shock Proteins and Stress provides the most comprehensive review on contemporary knowledge on the role of HSP in Stress. Using an integrative approach to understanding the regulation of HSP responses, the contributors provide a synopsis of novel mechanisms by which HSP responses are regulated under normal physiological and pathophysiological conditions. Key basic and clinical research laboratories from major universities and academic medical hospitals around the world contribute chapters that review present research activity and importantly project the field into the future. The book is a must read for researchers, postdoctoral fellows and graduate students in the fields of Translational Medicine, Clinical Psychologists, Human Physiology, Zoologists, Botanists, Biotechnology, Molecular Medicine, Infectious Diseases Experts and Pathologists
    Pages: IX, 315 p. 41 illus., 28 illus. in color. : online resource.
    ISBN: 9783319907253
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  • 4
    Keywords: Medicine ; Immunology ; Laboratory Medicine ; Neurosciences ; Neurology ; Biomedicine ; Neurosciences ; Neurology ; Immunology ; Laboratory Medicine ; Springer eBooks
    Description / Table of Contents: Preface -- Section I: Basic Science Aspects of Multiple Sclerosis -- 1 Extracellular Vesicles in Multiple Sclerosis as Possible Biomarkers: Dream or Reality?, Maria Magdalena Barreca, Emanuele Aliotta and Fabiana Geracii -- 2 Manipulation of Oxygen and Endoplasmic Reticulum Stress Factors as Possible Interventions for Treatment of Multiple Sclerosis: Evidence For and Against, Paul Eggleton, Gary R. Smerdon, Janet Holley and Nick Gutowski -- 3 Heat Shock Proteins in Multiple Sclerosis, Ortan Pinar, Yildirim Akan Ozden, Erkizan Omur and Gedizlioglu Muhtesem -- 4 Meaning of Self in Multiple Sclerosis: Implications for Treatment and Rehabilitation, Maciej Wilski and Tomasz Tasiemski -- 5 Multiple Sclerosis and EIF2B5: A Paradox or a Missing Link, Insha Zahoor, Ehtishamul Haq and Ravouf Asimi -- 6 Molecular Genetic and Epigenetic Basis of Multiple Sclerosis, Zohreh Hojati -- 7 Role of Olygodendrocyte Dysfunction in Demyelination, Remyelination and Neurodegeneration in Multiple Sclerosis, Adriana Octaviana Dulamea -- Section II: Clinical and Epidemiological Aspects of Multiple Sclerosis -- 8 Clinical Neurophysiology of Multiple Sclerosis, Mario Habek, Ivan Adamec, Barbara Barun, Luka Crnošija, Tereza Gabelić and Magdalena Krbot Skorić -- 9 Multiple Sclerosis Epidemiology in Europe, Daiana Bezzini and Mario A. Battaglia -- 10 Timing of Future Remyelination Therapies and Their Potential to Stop Multiple Sclerosis Progression, Burcu Zeydan, Moses Rodriguez and Orhun Kantarci -- 11 Neuroplasticity-Based Technologies and Interventions for Restoring Motor Function in Multiple Sclerosis, Sofia Straudi and Nino Basaglia -- Index
    Abstract: Multiple Sclerosis (MS) is one of the main causes of disability in young adult population. The estimated burden of the disease worldwide is about three million people. The pathogenic mechanism of MS involves both auto immune and degenerative processes. These two mechanisms are thought to determine a combination of events leading to several clinical pattern of disease onset and course. Multiple Sclerosis: Global Perspectives on a Silent Killer provides the most up-to-date and concise reviews on the critical issues of multiple sclerosis from around the world. This book is written by leaders and experts in the field of multiple sclerosis research and is divided into easy to read sections. Section I focuses on basic science aspects of Multiple Sclerosis, including potential biomarkers, molecular biology, heat shock proteins, oxidative stress, genetic and epigenetics. Section II focuses on clinical and epidemiological aspects of Multiple Sclerosis, including remyelination therapy, neuroplasticity-based technologies and interventions. This is an important reference book and a must-read for Undergraduate and Postgraduate Medical Scholars, Basic Science Researchers, Neurology Fellows, Neurology Residents and Neurologists in Clinical Practice
    Pages: VIII, 188 p. 28 illus., 18 illus. in color. : online resource.
    ISBN: 9783319478616
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  • 5
    Keywords: Medicine ; Science (General) ; Life sciences ; Biomedicine ; Biomedicine general ; Life Sciences, general ; Science, general ; Medicine/Public Health, general ; Springer eBooks
    Description / Table of Contents: Contributors -- Preface -- 1 HSP27 as a Therapeutic Target of Novel Inhibitors and Dietary Phytochemicals in Cancer -- 2 Heat Shock Protein 27 (HSP27, HSPB1) is Up-Regulated by Targeted Agents and Confers Resistance to Both Targeted Drugs and Chemotherapeutics -- 3 Heat Shock Proteins and Cancer: Plant Based Therapy -- 4 Chaperonotherapy for Alzheimer’s Disease: Focusing on HSP60 -- 5 Secreted and Circulating Cell Stress Proteins in the Periodontal Diseases -- 6 The Role of Heat Shock Protein 70 in Infection and Immunity -- 7 Potential Cytoprotective Effects of Heat Shock Proteins to Skeletal Muscle -- 8 Heat Shock Proteins in Triple-Negative Breast Cancer (TNBC) Treatment -- 9 Heat Shock Proteins in Multiple Sclerosis Pathogenesis: Friend or Foe? -- 10 New Indications for HSP90 and HSP70 Inhibitors as Antiviral Drugs -- 11 Potential Applications of Nanoparticles for Hyperthermia -- 12 Gene Therapy Against HSP90: Glucocorticoid Receptor-Assisted Cancer Treatment -- 13 Potential of HSP90 Inhibitors to Treat Neurofibromatosis-Related Tumors -- 14 Role of Heat Shock Protein 90 in the Cause of Various Diseases: A Potential Therapeutic Target -- 15 HSP90 Inhibitor-Based Strategies for Cancer Therapy: Advancing Toward Clinical Impact -- 16 Molecular Survival Strategies of Organisms: HSP and Small Molecules for Diagnostics and Drug Development.-17 Targeting Heat Shock Proteins in Colorectal Cancer -- Index
    Abstract: ℗ The book Heat Shock Protein-Based Therapies provides the most up-to-date review on new heat shock protein-based mechanisms used in the therapy and treatment of various human disorders and diseases, including cancer, muscular atrophy, neurodegenerative disorders (Alzheimer's Disease, Multiple Sclerosis) and infectious diseases (HIV, periodontal disease). Written by leaders in the field of heat shock protein research, the chapters systematically and in a step wise fashion takes the reader through the fascinating sequence of events by which mechanisms dependent on heat shock proteins are targeted. The chapters also provide answers as to HSP biological significance to the host. This book is a must read for graduate and postgraduates in the field of Drug Development, Biotechnology, Pharmaceutical Industry, Phytomedicine, Biology (plant and mammal), Biochemistry (pro- and eukaryotic), Oncology, Immunology, Microbiology, Exercise Medicine, Physiology, Inflammatory diseases, Autoimmunity, Pharmacology and Pathology
    Pages: XVII, 385 p. 47 illus., 22 illus. in color. : online resource.
    Edition: 1st ed. 2015.
    ISBN: 9783319172118
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  • 6
    Keywords: Biochemistry ; Protein Science ; Springer eBooks
    Description / Table of Contents: Thiol-based Redox Signaling: Impacts on Molecular Chaperones and Cellular Proteostasis -- Heat Shock Proteins (HSP) in Stress-Related Inflammatory Diseases -- Heat Shock Response and Metabolism in Skeletal Muscle -- Temperature Stress and Redox Homeostasis: The Synergistic Network of Redox and Chaperone System in Response to Stress in Plants -- Dynamics of Heat Shock Proteins in Immunity and Aging -- Heat Shock Proteins, Exercise and Inflammation -- Heat Shock Proteins and Alarmins in Autoimmunity -- HO-1/Hsp32 and Cardiac Stress Signaling -- Targeting Heat Shock Proteins in Multiple Myeloma -- IER5 is a p53-Reguated Activator of HSF1 that Contributes to Promotion of Cancer -- Heat Shock Proteins in Digestive Tract Cancer: Molecular Mechanism and Therapeutic Potential -- The Role of Heat Shock Protein 90 in Regulating Downstream Signal Transduction Cascades -- Extracellular Hsp90a versus Intracellular Hsp90b in Wound Healing and Cancer -- Regulation of Calcineurin Signaling through Blocking of the Chaperone Function of Hsp90 by HDAC Inhibitors -- Signaling Functions of Extracellular Hsp90 (eHsp90) in Cancer Metastasis -- The Role of the Molecular Chaperones Hsp70 and Hsp90 in the DNA Damage Response -- Heat Shock Protein 90 Inhibitors in Lung Cancer Therapy -- Hsp90 Inhibitors Blocking Multiple Oncogenic Signaling Pathways for the Treatment of Cancer -- Diverse Roles of Heat Shock Proteins in Immune Activation and Tolerance: A Comprehensive Review of Mechanisms and Therapeutic Relevance -- The Role of Heat Shock Proteins on Neuromuscular Disorders/Neuronal Differentiation -- Heat Shock Proteins in Neural Signaling: Implications in Health and Disease -- Cytosolic Heat Shock Protein 90 in Plant Hormone and Environmental Stress Response
    Abstract: This edited volume offers an insightful overview of contemporary research on signaling pathways. These signaling processes are the comprehensive mechanisms by which all cellular organisms communicate internally and externally with their microenvironment. The volume is focused on heat shock proteins (HSP), which are uniquely involved in a number of critical signaling pathways. Errors in signaling pathways and in the processing of cellular information are known to be responsible for the majority of diseases including cancer, inflammatory and neurological disorders. The knowledge gained from better understanding these mechanisms can help in elucidating disease processes and will assist in development and design of novel targeted treatment therapies to combat human diseases and disorders. Key basic and clinical research laboratories from major universities, academic medical hospitals, biotechnology and pharmaceutical laboratories around the world have contributed chapters that review present research activity and importantly project the field into the future. The book is a must read for graduate students. medical students, basic science researchers and postdoctoral scholars in the fields of Translational Medicine, Clinical Research, Human Physiology, Biotechnology, Cell & Molecular Medicine, Pharmaceutical Scientists and Researchers involved in Drug Discovery
    Pages: XI, 482 p. 63 illus., 41 illus. in color. : online resource.
    Edition: 1st ed. 2019.
    ISBN: 9783030039523
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  • 7
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    Cham : Springer International Publishing
    Keywords: Medicine ; Laboratory Medicine ; Pharmaceutical technology ; Biomedicine ; Laboratory Medicine ; Biological and Medical Physics, Biophysics ; Pharmaceutical Sciences/Technology ; Springer eBooks
    Description / Table of Contents: Heat Shock Protein 70 and Molecular Confession during Neurodegeneration -- Hsp70-Family Proteins and Neurodegenerative Diseases -- Heat Shock Protein70 in Neurological Disease -- Involvement of Heat Shock Protein 70 (Hsp70) in Gastrointestinal Cancers -- Heat Shock Protein 70 and Cancer -- Implication of HSP70 in the Pathogenesis of Gastric Cancer -- Double Face of eHsp70 in Front of Different Situations -- HSP70 is a Major Contributor to the MHCII Ligandome and Inducer of Regulatory T Cells -- Immune Properties of HSP70 -- Molecular Chaperones Regulating the Dynamics, Composition and Functionality of RNP Granules: Implications for Age-related Diseases -- Heat Shock Proteins in Cardiovascular Diseases: From Bench to Bedside -- Clinical Implication of Heat Shock Protein 70 in Kidney Disease -- Heat Shock Proteins in the Kidney - What is Known About their Role in Kidney Disease -- Heat Shock Protein 70 and Other Heat Shock Proteins in Diseased Retina -- Emerging Role of HSP70 in Human Diseases -- Intranasal Administration of Hsp70: Molecular and Therapeutic Consequences -- The Effectiveness of Antitumor Vaccine Enriched with a Heat Shock Protein 70 -- Mammalian Heat Shock Protein Hsp105: The Hsp70 Inducer and a Potent Target for Cancer Therapy -- Suppression of HSP70 Expression by Quercetin and its Therapeutic Potential against Cancer -- Hsp70 in Fungi: Evolution, Function and Vaccine Candidate
    Abstract: The book HSP70 in Human Diseases and Disorders provides the most comprehensive review on contemporary knowledge on the role of HSP70 family - one of the most studied HSP - in human diseases and disorders. Using an integrative approach to expand our current understanding of HSP70 functions, the contributors provide a synopsis of novel mechanisms by which HSP70 is involved in the regulation of human diseases and disorders. Key basic and clinical research laboratories from major universities and academic medical hospitals around the world contribute chapters that review present research activity and importantly project the field into the future. The book is a must read for medical students and residents, clinical and basic science researchers, postdoctoral fellows and graduate students in the fields of Medicine, Physiology, Clinical Trials, Biotechnology, Molecular Medicine and Pathology
    Pages: IX, 403 p. 39 illus., 31 illus. in color. : online resource.
    ISBN: 9783319895512
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  • 8
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The crystal structure of phospholipase A2 from the venom of Daboia russelli pulchella has been refined to an R factor of 0.216 using 17 922 reflections to 1.9 Å resolution. The structure contains two crystallographically independent molecules in the asymmetric unit. The overall conformations of the two molecules are essentially the same except for three regions, namely the calcium-binding loop including Trp31, the β-wing and the C-terminal residues 119–131. Although these differences have apparently been caused by molecular packing, they seem to have functional relevance. Particularly noteworthy is the conformation of Trp31, which is favourable for substrate binding in one molecule as it is aligned with one of the side walls of the hydrophobic channel, whereas in the other molecule it is located at the mouth of the channel, thereby blocking the entry of substrates leading to loss of activity. This feature is unique to the present structure and does not occur in the dimers and trimers of other PLA2s.
    Type of Medium: Electronic Resource
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  • 9
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: A novel complex of phospholipase A2 complexed with another venom protein has been isolated and purified from saw-scaled viper (Echis carinatus) venom. The molecular weights of the two components are 16 and 14 kDa, respectively. The complex was purified using an Affigel blue column and an anion-exchange (DEAE Sephacel) column. Long diamond-shaped crystals were obtained by hanging-drop vapour diffusion. The protein complex was dissolved at a concentration of 10 mg ml−1 in 20 mM sodium cacodylate, 1 mM CaCl2 and 2% dioxane at pH 6.0. The reservoir contained the same buffer with 7%(w/v) PEG 4000. Crystals appeared within 2–3 weeks. Native data to 2.9 Å resolution have been obtained at 291 K. The crystals belong to the monoclinic space group P21 with unit-cell parameters a = 74.47, b = 47.87, c = 106.39 Å, β = 104.5° and contain two molecules per asymmetric unit. Structure determination by molecular replacement is in progress.
    Type of Medium: Electronic Resource
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  • 10
    ISSN: 1075-2617
    Keywords: β-turns ; folded conformation ; dehydro-residue ; X-ray diffraction ; consecutive dehydro-residue ; Chemistry ; Biochemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: To obtain general rules of peptide design using α,β-dehydro-residues, a sequence with two consecutive ΔPhe-residues, Boc-L-Val-ΔPhe-ΔPhe- L-Ala-OCH3, was synthesized by azlactone method in solution phase. The peptide was crystallized from its solution in an acetone/water mixture (70:30) in space group P61 with a=b=14.912(3)  Å, c= 25.548(5)  Å, V=4912.0(6)  Å3. The structure was determined by direct methods and refined by a full matrix least-squares procedure to an R value of 0.079 for 2891 observed [I≥3σ(I)] reflections. The backbone torsion angles φ1=-54(1)°, ψ1= 129(1)°, ω1=-177(1)°, φ2 =57(1)°, ψ2=15(1)°, ω2 =-170(1)°, φ3=80(1)°, ψ3 =7(2)°, ω3=-177(1)°, φ4 =-108(1)° and ψT4=-34 (1)° suggest that the peptide adopts a folded conformation with two overlapping β-turns of types II and III′. These turns are stabilized by two intramolecular hydrogen bonds between the CO of the Boc group and the NH of ΔPhe3 and the CO of Val1 and the NH of Ala4. The torsion angles of ΔPhe2 and ΔPhe3 side chains are similar and indicate that the two ΔPhe residues are essentially planar. The folded molecules form head-to- tail intermolecular hydrogen bonds giving rise to continuous helical columns which run parallel to the c-axis. This structure established the formation of two β-turns of types II and III′ respectively for sequences containing two consecutive ΔPhe residues at (i+2) and (i+3) positions with a branched β-carbon residue at one end of the tetrapeptide.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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