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|a 1264884896
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|a 1681086158
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|a 9781681086156
|q (electronic bk.)
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|b R65 2018
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|a 572/.633
|2 23
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|a UAMI
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|a Galigniana, Mario D.
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|a Role of Molecular Chaperones on Structural Folding, Biological Functions, and Drug Interactions of Client Proteins.
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| 260 |
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|a Sharjah :
|b Bentham Science Publishers,
|c 2018.
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| 300 |
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|a 1 online resource (279 pages)
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| 336 |
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|a text
|b txt
|2 rdacontent
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|a computer
|b c
|2 rdamedia
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| 338 |
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|a online resource
|b cr
|2 rdacarrier
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| 490 |
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|a Frontiers in Structural Biology Ser. ;
|v v. 1
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|a Print version record.
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|6 880-01
|a 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.
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| 505 |
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|a 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.
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| 505 |
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|a 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.
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|a 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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| 500 |
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|a Sequence of Conformational Changes Induced by ATP Binding to Hsp90.
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| 504 |
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|a Includes bibliographical references and index.
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| 590 |
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|a ProQuest Ebook Central
|b Ebook Central Academic Complete
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| 590 |
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|a eBooks on EBSCOhost
|b EBSCO eBook Subscription Academic Collection - Worldwide
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|a Molecular chaperones.
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|a Molécules chaperonnes.
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| 650 |
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|a Molecular chaperones
|2 fast
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|i has work:
|a Role of Molecular Chaperones on Structural Folding, Biological Functions, and Drug Interactions of Client Proteins (Text)
|1 https://id.oclc.org/worldcat/entity/E39PCXgdypfKPJQBJxmgtWkRXb
|4 https://id.oclc.org/worldcat/ontology/hasWork
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| 776 |
0 |
8 |
|i Print version:
|a Galigniana, Mario D.
|t Role of Molecular Chaperones on Structural Folding, Biological Functions, and Drug Interactions of Client Proteins.
|d Sharjah : Bentham Science Publishers, ©2018
|z 9781681086163
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| 830 |
|
0 |
|a Frontiers in Structural Biology Ser.
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| 856 |
4 |
0 |
|u https://ebookcentral.uam.elogim.com/lib/uam-ebooks/detail.action?docID=5392652
|z Texto completo
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| 880 |
8 |
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|6 505-01/(S
|a Definition and Prediction of the Sequence and Basic Structure of TPR MotifsThree Dimensional Structure; Curvature and Shape of the TPR Domain; Examples of TPR Protein Structures; Ligand Binding; Folding and Stability of TPR Proteins; Oligomerization, Stability and Biological Functions; Novel TPR Protein Design; SEQUENCE, FUNCTION, AND BASIC STRUCTURE OF HSP90 PROTEINS: HSP90 ALPHA AND BETA; Introduction; Hsp90 Isoforms; Sequence and Basic Structure of Hsp90 Proteins: Hsp90 α and β; Difference in Structure of Hsp90 α−and β−isoforms; Conformational Changes in Hsp90.
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