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Telomerases : chemistry, biology and clinical applications / edited by Neal F. Lue and Chantal Autexier

Contributor(s): Resource type: Ressourcentyp: Buch (Online)Book (Online)Language: English Publisher: Hoboken : John Wiley & Sons, 2012Edition: Online-AusgDescription: Online-Ressource (1 online resource (336 p.))ISBN:
  • 9781118268506
  • 9781280768736
  • 1280768738
Subject(s): Additional physical formats: 9781118268667 | 9780470592045 | Erscheint auch als: 9780470592045 Druck-Ausgabe | Erscheint auch als: Telomerases : Chemistry, Biology and Clinical Applications Druck-AusgabeDDC classification:
  • 572.7
  • 572.7 572.8 572.86
  • 572.8/6 23
  • 572.86
LOC classification:
  • QP606 .T44
Online resources: Summary: Explores the structure, function, and emerging applications of telomerases With contributions from leading experts and pioneers in the field, this book offers a comprehensive review of telomerase structure and function in a variety of organisms, including yeasts, ciliates, plants, and mammals. Chapters provide integrated discussions that examine the connections between the chemistry, biology, and emerging clinical applications of the telomerase enzyme. In particular, readers will gain new insights into the role of telomerases in cellular senescence, aging, and cancer. Telomerases begins with an overview of the telomerase complex, followed by in-depth discussions of the chemistry of its two critical components: TERT and TER. Next, the book brings readers up to date with our current understanding of telomerases, including: Biological regulatory mechanisms that control the synthesis and assembly of the telomerase complex Regulations imposed by the nucleoprotein complex at chromosome ends Studies underscoring the role of the telomerase enzyme as a promising target and a useful tool in medical interventions The book concludes with an essay that places the telomerase enzyme in an evolutionary context, illustrating its place within the highly diverse family of reverse transcriptases. Telomerases is recommended for biochemists, enzymologists, protein scientists, cancer researchers, biophysicists, geneticists, and cell, molecular, and chromosome biologists. Explaining what the latest research in the field reveals about the structure and function of telomerases and how this research has informed investigations into their clinical applications, the book points to future avenues of research that will enable us to better understand the chemistry, biology, and clinical applications of telomerases.Summary: TELOMERASES: Chemistry, Biology, and Clinical Applications -- CONTENTS -- Preface -- Contributors -- 1 The Telomerase Complex: An Overview -- 1.1 CONSERVATION OF TELOMERE FUNCTION AND THE DISCOVERY OF TELOMERASE -- 1.2 THE DISCOVERY OF THE TWO MINIMAL TELOMERASE COMPONENTS -- 1.3 TELOMERASE BEYOND THE MINIMAL COMPONENTS: ASSOCIATED PROTEINS -- 1.4 REGULATION OF TELOMERASE BY TELOMERIC PROTEINS AND RNAS -- 1.5 TELOMERASE, TELOMERE MAINTENANCE, CANCER, AND AGING -- 1.6 TELOMERASE BEYOND TELOMERE SYNTHESIS -- 1.7 TELOMERE MAINTENANCE WITHOUT TELOMERASE -- 1.8 CONCLUSION -- ACKNOWLEDGMENT -- REFERENCES -- 2 Telomerase RNA: Structure, Function, and Molecular Mechanisms -- 2.1 INTRODUCTION-TELOMERASE RNA: AN ESSENTIAL COMPONENT OF TELOMERASE -- 2.2 THE UNUSUAL DIVERSITY OF TELOMERASE RNA -- 2.2.1 Size, Sequence, and Secondary Structure -- 2.2.2 Transcription and Biogenesis -- 2.3 THE COMMON CORE OF TER -- 2.3.1 Template Boundary Definition -- 2.3.2 Pseudoknot -- 2.3.2.1 Ciliate -- 2.3.2.2 Vertebrate -- 2.3.2.3 Yeast -- 2.3.2.4 The Function of the Triple Helix -- 2.3.3 Core-Enclosing Helix -- 2.4 THE ASSEMBLY/ACTIVATION STEM-LOOP ELEMENT -- 2.4.1 The Ciliate Stem-Loop IV -- 2.4.1.1 Identification of a Conserved Structural Element -- 2.4.1.2 The Role of Stem-Loop IV in the Binding of TERT to TER -- 2.4.1.3 The Assembly Role of Stem-Loop IV is Facilitated by the Protein p65 -- 2.4.1.4 The Role of Stem-Loop IV in Telomerase Action -- 2.4.2 The Vertebrate CR4-CR5 Domain -- 2.4.3 The Yeast Three-Way Junction -- 2.4.3.1 Do the Ciliate Stem-Loop IV, the Vertebrate p6.1 and the Yeast Stem 3 Represent Homologous Elements? -- 2.5 BINDING SITES FOR TELOMERASE ACCESSORY/REGULATORY PROTEINS -- 2.5.1 Vertebrate -- 2.5.1.1 Dyskerin Protein Complex -- 2.5.1.2 TCAB1/WDR79 -- 2.5.2 Budding Yeast -- 2.5.2.1 Est1 Binding Domain.PPN: PPN: 809703378Package identifier: Produktsigel: ZDB-26-MYL | ZDB-30-PAD | ZDB-30-PQE
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