The Molecular Chaperones Interaction Networks in Protein Folding and Degradation:
Molecular chaperones are a fundamental group of proteins that have been identified only relatively recently. They are key components of a protein quality machinery in the cell which insures that the folding process of any newly-synthesized polypeptide chain results in the formation of a properly fol...
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Format: | Elektronisch E-Book |
Sprache: | English |
Veröffentlicht: |
New York, NY [u.a.]
Springer
2014
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Schriftenreihe: | Interactomics and Systems Biology
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Schlagworte: | |
Online-Zugang: | TUM01 UBT01 Volltext Inhaltsverzeichnis Abstract |
Zusammenfassung: | Molecular chaperones are a fundamental group of proteins that have been identified only relatively recently. They are key components of a protein quality machinery in the cell which insures that the folding process of any newly-synthesized polypeptide chain results in the formation of a properly folded protein and that the folded protein is maintained in an active conformation throughout its functional lifetime. Molecular chaperones have been shown to play essential roles in cell viability under both normal and stress conditions. Chaperones can also assist in the unfolding and degradation of misfolded proteins and in disaggregating preformed protein aggregates. Chaperones are also involved in other cellular functions including protein translocation across membranes, vesicle fusion events, and protein secretion. In recent years, tremendous advances have been made in our understanding of the biology, biochemistry, and biophysics of function of molecular chaperones. In addition, recent technical developments in the fields of proteomics and genomics allowed us to obtain a global view of chaperone interaction networks. Finally, there is now a growing interest in the role of molecular chaperones in diseases. This book will provide a comprehensive analysis of the structure and function of the diverse systems of molecular chaperones and their role in cell stress responses and in diseases from a global network perspective |
Beschreibung: | 1 Online-Ressource |
ISBN: | 9781493911301 |
DOI: | 10.1007/978-1-4939-1130-1 |
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520 | 1 | |a Molecular chaperones are a fundamental group of proteins that have been identified only relatively recently. They are key components of a protein quality machinery in the cell which insures that the folding process of any newly-synthesized polypeptide chain results in the formation of a properly folded protein and that the folded protein is maintained in an active conformation throughout its functional lifetime. Molecular chaperones have been shown to play essential roles in cell viability under both normal and stress conditions. Chaperones can also assist in the unfolding and degradation of misfolded proteins and in disaggregating preformed protein aggregates. Chaperones are also involved in other cellular functions including protein translocation across membranes, vesicle fusion events, and protein secretion. In recent years, tremendous advances have been made in our understanding of the biology, biochemistry, and biophysics of function of molecular chaperones. In addition, recent technical developments in the fields of proteomics and genomics allowed us to obtain a global view of chaperone interaction networks. Finally, there is now a growing interest in the role of molecular chaperones in diseases. This book will provide a comprehensive analysis of the structure and function of the diverse systems of molecular chaperones and their role in cell stress responses and in diseases from a global network perspective | |
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Datensatz im Suchindex
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adam_text | THE MOLECULAR CHAPERONES INTERACTION NETWORKS IN PROTEIN FOLDING AND
DEGRADATION
/
: 2014
TABLE OF CONTENTS / INHALTSVERZEICHNIS
PART I: GLOBAL VIEW OF THE CHAPERONE NETWORK
ANALYSIS OF CHAPERONE NETWORK THROUGHPUT
PART II: CHAPERONES AT THE RIBOSOME
FUNCTIONS OF RIBOSOME-ASSOCIATED CHAPERONES AND THEIR INTERACTION
NETWORK
PART III: THE HSP 70 AND HSP40 CHAPERONE NETWORKS
YEAST HSP70 AND J-PROTEIN CHAPERONES: FUNCTION AND INTERACTION NETWORK
THE CHAPERONE NETWORKS: AN HSP70 PERSPECTIVE
PART IV: THE HSP90 CHAPERONE NETWORK
THE INTERACTION NETWORK OF THE HSP90 MOLECULAR CHAPERONE
A GLOBAL VIEW OF THE PROTEOME PERTURBATIONS BY HSP90 INHIBITORS
DESIGNING DRUGS AGAINST HSP90 FOR CANCER THERAPY
THE CANDIDA ALBICANS HSP90 CHAPERONE NETWORK IS ENVIRONMENTALLY FLEXIBLE
AND EVOLUTIONARILY DIVERGENT
PART V: THE P23 CHAPERONE NETWORK
EMERGENCE AND CHARACTERIZATION OF THE P23 MOLECULAR CHAPERONE
PART VI: CHAPERONES IN THE ER: FUNCTION AND INTERACTION NETWORK
CHAPERONES OF THE ERAD PATHWAY
CHAPERONES AND PROTEASES OF MITOCHONDRIA: FROM PROTEIN FOLDING AND
DEGRADATION TO MITOPHAGY
PART VII: THE UBIQUITIN-PROTEASOME SYSTEM NETWORK
THE BIOGENESIS OF THE EUKARYOTIC PROTEASOME
SYSTEMS-WIDE ANALYSIS OF PROTEIN UBIQUITYLATION: WE FINALLY HAVE THE
TIGER BY THE TAIL
PART VIII: THE CHAPERONE AND PROTEASE NETWORKS IN MODEL BACTERIA AND
PARASITES
THE INTERACTION NETWORKS OF E. COLI CHAPERONES
CHAPERONE-PROTEASES OF MYCOBACTERIA
THE INTERACTION NETWORKS OF HSP70 AND HSP90 IN THE PLASMODIUM AND
LEISHMANIA PARASITES
INDEX
DIESES SCHRIFTSTUECK WURDE MASCHINELL ERZEUGT.
THE MOLECULAR CHAPERONES INTERACTION NETWORKS IN PROTEIN FOLDING AND
DEGRADATION
/
: 2014
ABSTRACT / INHALTSTEXT
MOLECULAR CHAPERONES ARE A FUNDAMENTAL GROUP OF PROTEINS THAT HAVE BEEN
IDENTIFIED ONLY RELATIVELY RECENTLY. THEY ARE KEY COMPONENTS OF A
PROTEIN QUALITY MACHINERY IN THE CELL WHICH INSURES THAT THE FOLDING
PROCESS OF ANY NEWLY-SYNTHESIZED POLYPEPTIDE CHAIN RESULTS IN THE
FORMATION OF A PROPERLY FOLDED PROTEIN AND THAT THE FOLDED PROTEIN IS
MAINTAINED IN AN ACTIVE CONFORMATION THROUGHOUT ITS FUNCTIONAL LIFETIME.
MOLECULAR CHAPERONES HAVE BEEN SHOWN TO PLAY ESSENTIAL ROLES IN CELL
VIABILITY UNDER BOTH NORMAL AND STRESS CONDITIONS. CHAPERONES CAN ALSO
ASSIST IN THE UNFOLDING AND DEGRADATION OF MISFOLDED PROTEINS AND IN
DISAGGREGATING PREFORMED PROTEIN AGGREGATES. CHAPERONES ARE ALSO
INVOLVED IN OTHER CELLULAR FUNCTIONS INCLUDING PROTEIN TRANSLOCATION
ACROSS MEMBRANES, VESICLE FUSION EVENTS, AND PROTEIN SECRETION. IN
RECENT YEARS, TREMENDOUS ADVANCES HAVE BEEN MADE IN OUR UNDERSTANDING OF
THE BIOLOGY, BIOCHEMISTRY, AND BIOPHYSICS OF FUNCTION OF MOLECULAR
CHAPERONES. IN ADDITION, RECENT TECHNICAL DEVELOPMENTS IN THE FIELDS OF
PROTEOMICS AND GENOMICS ALLOWED US TO OBTAIN A GLOBAL VIEW OF CHAPERONE
INTERACTION NETWORKS. FINALLY, THERE IS NOW A GROWING INTEREST IN THE
ROLE OF MOLECULAR CHAPERONES IN DISEASES. THIS BOOK WILL PROVIDE A
COMPREHENSIVE ANALYSIS OF THE STRUCTURE AND FUNCTION OF THE DIVERSE
SYSTEMS OF MOLECULAR CHAPERONES AND THEIR ROLE IN CELL STRESS RESPONSES
AND IN DISEASES FROM A GLOBAL NETWORK PERSPECTIVE
DIESES SCHRIFTSTUECK WURDE MASCHINELL ERZEUGT.
|
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spelling | Houry, Walid A. Verfasser aut The Molecular Chaperones Interaction Networks in Protein Folding and Degradation Walid A. Houry, ed. New York, NY [u.a.] Springer 2014 1 Online-Ressource txt rdacontent c rdamedia cr rdacarrier Interactomics and Systems Biology Molecular chaperones are a fundamental group of proteins that have been identified only relatively recently. They are key components of a protein quality machinery in the cell which insures that the folding process of any newly-synthesized polypeptide chain results in the formation of a properly folded protein and that the folded protein is maintained in an active conformation throughout its functional lifetime. Molecular chaperones have been shown to play essential roles in cell viability under both normal and stress conditions. Chaperones can also assist in the unfolding and degradation of misfolded proteins and in disaggregating preformed protein aggregates. Chaperones are also involved in other cellular functions including protein translocation across membranes, vesicle fusion events, and protein secretion. In recent years, tremendous advances have been made in our understanding of the biology, biochemistry, and biophysics of function of molecular chaperones. In addition, recent technical developments in the fields of proteomics and genomics allowed us to obtain a global view of chaperone interaction networks. Finally, there is now a growing interest in the role of molecular chaperones in diseases. This book will provide a comprehensive analysis of the structure and function of the diverse systems of molecular chaperones and their role in cell stress responses and in diseases from a global network perspective Biowissenschaften Medizin Life sciences Medicine Biochemistry Biological models Erscheint auch als Druckausgabe 978-1-4939-1129-5 https://doi.org/10.1007/978-1-4939-1130-1 Verlag Volltext Springer Fremddatenuebernahme application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=027554340&sequence=000001&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis Springer Fremddatenuebernahme application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=027554340&sequence=000003&line_number=0002&func_code=DB_RECORDS&service_type=MEDIA Abstract |
spellingShingle | Houry, Walid A. The Molecular Chaperones Interaction Networks in Protein Folding and Degradation Biowissenschaften Medizin Life sciences Medicine Biochemistry Biological models |
title | The Molecular Chaperones Interaction Networks in Protein Folding and Degradation |
title_auth | The Molecular Chaperones Interaction Networks in Protein Folding and Degradation |
title_exact_search | The Molecular Chaperones Interaction Networks in Protein Folding and Degradation |
title_full | The Molecular Chaperones Interaction Networks in Protein Folding and Degradation Walid A. Houry, ed. |
title_fullStr | The Molecular Chaperones Interaction Networks in Protein Folding and Degradation Walid A. Houry, ed. |
title_full_unstemmed | The Molecular Chaperones Interaction Networks in Protein Folding and Degradation Walid A. Houry, ed. |
title_short | The Molecular Chaperones Interaction Networks in Protein Folding and Degradation |
title_sort | the molecular chaperones interaction networks in protein folding and degradation |
topic | Biowissenschaften Medizin Life sciences Medicine Biochemistry Biological models |
topic_facet | Biowissenschaften Medizin Life sciences Medicine Biochemistry Biological models |
url | https://doi.org/10.1007/978-1-4939-1130-1 http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=027554340&sequence=000001&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=027554340&sequence=000003&line_number=0002&func_code=DB_RECORDS&service_type=MEDIA |
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