Role of Molecular Chaperones on Structural Folding, Biological Functions, and Drug Interactions of Client Proteins.

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Detalles Bibliográficos
Clasificación:Libro Electrónico
Autor principal: Galigniana, Mario D.
Formato: Electrónico eBook
Idioma:Inglés
Publicado: Sharjah : Bentham Science Publishers, 2018.
Colección:Frontiers in Structural Biology Ser.
Temas:
Molecular chaperones.
Molécules chaperonnes.
Molecular chaperones
Acceso en línea:Texto completo
Tabla de Contenidos:
  • Intro; CONTENTS; PREFACE; List of Contributors; Regulatory Roles for Hsp70 in Cancer Incidence and Tumor Progression; Taka Eguchi1, Benjamin J. Lang1, Ayesha Murshid1, Thomas Prince2, Jianlin Gong3 and Stuart K Calderwood1,*; 1. INTRODUCTION; 2. HSP70 PROTEINS IN THE CYTOPLASM AND NUCLEUS; 3. MUTATION AND OVEREXPRESSION OF HSP72 IN CANCER; 4. HSP72 AND THE HALLMARKS OF CANCER; 4A. HSP72 Suppresses Apoptotic Cell Death in Cancer; 4B. HSP72 and Senescence; 4C. HSP72 in Tumor Initiation and Metastasis; 4D. HsSP72 in Sustained Angiogenesis.
  • 5. DRUGGING HSP70 IN CANCER: ISOFORMS AND DRUGGABLE DOMAINS5A. Targeting the HSP70 Substrate-Binding Domain (SBD); 5B. Targeting the HSP70 Nucleotide-Binding Domain; 5C. Perturbation of HSP70-Protein Interactions; CONCLUSIONS; CONSENT FOR PUBLICATION; CONFLICT OF INTEREST; ACKNOWLEDGEMENTS; REFERENCES; Use of Coarse-Grained and All-Atom Molecular Dynamics to Study Hsp70 and Hsp40 Chaperone Action; Ewa I. Gołaś1,2,œ, Magdalena A. Mozolewska1,2,œ, Paweł Krupa1,2, Cezary Czaplewski1, Harold A. Scheraga2 and Adam Liwo1,*; INTRODUCTION; METHODS; RESULTS; Mechanism of Chaperone Cycle.
  • Modeling Iron-sulfur Cluster BiogenesisModeling the Structure of Isu1 from Yeast; Modeling the Structure of the Binary Isu1-Jac1 Complex and Assessing the Stability of its Interactions; Preliminary Molecular-modeling Study of the Structure of the Isu1-Jac1-Ssq1 Ternary Complex; CONCLUSIONS AND OUTLOOK; CONSENT FOR PUBLICATION; CONFLICT OF INTEREST; ACKNOWLEDGEMENTS; REFERENCES; Quaternary Structure of Chaperones from the Hsp70 System Determined by Small Angle X-Ray Scattering (SAXS) and Analytical Ultra-centrifugation; Júlio C. Borges1 and Carlos H.I. Ramos2,*; INTRODUCTION.
  • Protein Folding and Molecular ChaperonesSmall Angle X-ray Scattering (SAXS); Analytical Ultracentrifugation; The Hsp70-folding System; Human Mitochondrial GrpE, Conformational Modification upon Hsp70 Binding; Eukaryotic Hsp40s Types I and II, on the Position of the J Domain; FINAL REMARKS; CONSENT FOR PUBLICATION; CONFLICT OF INTEREST; ACKNOWLEDGMENTS; REFERENCES; Structural Characteristics of the TPR Protein-Hsp90 Interaction: A New Target in Biotechnology; Ana Cauerhff1,* and Mario D. Galigniana1,2; INTRODUCTION; TPR PROTEIN CHARACTERISTICS.

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