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Author: Laura Moriarty
Publisher: Penguin
ISBN: 110158565X
Category : Fiction
Languages : en
Pages : 421
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Book Description
Soon to be a feature film from the creators of Downton Abbey starring Elizabeth McGovern, The Chaperone is a New York Times-bestselling novel about the woman who chaperoned an irreverent Louise Brooks to New York City in the 1920s and the summer that would change them both. Only a few years before becoming a famous silent-film star and an icon of her generation, a fifteen-year-old Louise Brooks leaves Wichita, Kansas, to study with the prestigious Denishawn School of Dancing in New York. Much to her annoyance, she is accompanied by a thirty-six-year-old chaperone, who is neither mother nor friend. Cora Carlisle, a complicated but traditional woman with her own reasons for making the trip, has no idea what she’s in for. Young Louise, already stunningly beautiful and sporting her famous black bob with blunt bangs, is known for her arrogance and her lack of respect for convention. Ultimately, the five weeks they spend together will transform their lives forever. For Cora, the city holds the promise of discovery that might answer the question at the core of her being, and even as she does her best to watch over Louise in this strange and bustling place she embarks on a mission of her own. And while what she finds isn’t what she anticipated, she is liberated in a way she could not have imagined. Over the course of Cora’s relationship with Louise, her eyes are opened to the promise of the twentieth century and a new understanding of the possibilities for being fully alive. Drawing on the rich history of the 1920s, ’30s, and beyond—from the orphan trains to Prohibition, flappers, and the onset of the Great Depression to the burgeoning movement for equal rights and new opportunities for women—Laura Moriarty’s The Chaperone illustrates how rapidly everything, from fashion and hemlines to values and attitudes, was changing at this time and what a vast difference it all made for Louise Brooks, Cora Carlisle, and others like them.
Author: Laura Moriarty
Publisher: Penguin
ISBN: 110158565X
Category : Fiction
Languages : en
Pages : 421
Get Book
Book Description
Soon to be a feature film from the creators of Downton Abbey starring Elizabeth McGovern, The Chaperone is a New York Times-bestselling novel about the woman who chaperoned an irreverent Louise Brooks to New York City in the 1920s and the summer that would change them both. Only a few years before becoming a famous silent-film star and an icon of her generation, a fifteen-year-old Louise Brooks leaves Wichita, Kansas, to study with the prestigious Denishawn School of Dancing in New York. Much to her annoyance, she is accompanied by a thirty-six-year-old chaperone, who is neither mother nor friend. Cora Carlisle, a complicated but traditional woman with her own reasons for making the trip, has no idea what she’s in for. Young Louise, already stunningly beautiful and sporting her famous black bob with blunt bangs, is known for her arrogance and her lack of respect for convention. Ultimately, the five weeks they spend together will transform their lives forever. For Cora, the city holds the promise of discovery that might answer the question at the core of her being, and even as she does her best to watch over Louise in this strange and bustling place she embarks on a mission of her own. And while what she finds isn’t what she anticipated, she is liberated in a way she could not have imagined. Over the course of Cora’s relationship with Louise, her eyes are opened to the promise of the twentieth century and a new understanding of the possibilities for being fully alive. Drawing on the rich history of the 1920s, ’30s, and beyond—from the orphan trains to Prohibition, flappers, and the onset of the Great Depression to the burgeoning movement for equal rights and new opportunities for women—Laura Moriarty’s The Chaperone illustrates how rapidly everything, from fashion and hemlines to values and attitudes, was changing at this time and what a vast difference it all made for Louise Brooks, Cora Carlisle, and others like them.
Author: Mary-Jane Gething
Publisher: OUP Oxford
ISBN: 0191547271
Category : Medical
Languages : en
Pages : 586
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Book Description
The precise shape of a protein is a crucial factor in its function. How do proteins become folded into the right conformation? Molecular chaperones and protein folding catalysts bind to developing polypeptides in the cytoplasm and ensure correct folding and transport. This Guidebook catalogues the latest information on nearly 200 of these molecules, including the important class of heat shock proteins; each entry is written by leading researchers in the field.
Author: Matthias Gaestel
Publisher: Springer Science & Business Media
ISBN: 9783540258759
Category : Science
Languages : en
Pages : 464
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Book Description
Molecular chaperones are involved in a wide variety of essential cellular processes in living cells. A subset of molecular chaperones have been initially described as heat shock proteins protecting cells from stress damage by keeping cellular proteins in a folding competent state and preventing them from irreversible aggregation. Later it became obvious that molecular chaperones are also expressed constitutively in the cell and are involved in complex processes such as protein synthesis, intracellular protein transport, post-translational modification and secretion of proteins as well as receptor signalling. Hence, it is not surprising that molecular chaperones are implicated in the pathogenesis of many relevant diseases and could be regarded as potential pharmacological targets. Starting with the analysis of the mode of action of chaperones at the molecular, cellular and organismic level, this book will then describe specific aspects where modulation of chaperone action could be of pharmacological and therapeutic interest.
Author: Peter A. Lund
Publisher: Oxford University Press, USA
ISBN: 9780199638673
Category : Science
Languages : en
Pages : 308
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Book Description
In this text, leading experts synthesise our body of knowledge , and the reader gains not only a fuller understanding of the roles of chaperones in the context of cellular processes, but also an insight into the nature of these proteins.
Author: Gregory Lloyd Blatch
Publisher: Springer
ISBN: 3319117319
Category : Medical
Languages : en
Pages : 286
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Book Description
Co-chaperones are important mediators of the outcome of chaperone assisted protein homeostasis, which is a dynamic balance between the integrated processes of protein folding, degradation and translocation. The Networking of Chaperones by Co-chaperones describes how the function of the major molecular chaperones is regulated by a cohort of diverse non-client proteins, known as co-chaperones. The second edition includes the current status of the field and descriptions of a number of novel co-chaperones that have been recently identified. This new edition has a strong focus on the role of co-chaperones in human disease and as putative drug targets. The book will be a resource for both newcomers and established researchers in the field of cell stress and chaperones, as well as those interested in cross-cutting disciplines such as cellular networks and systems biology.
Author: R.J. Ellis
Publisher: Springer Science & Business Media
ISBN: 9401121087
Category : Science
Languages : en
Pages : 121
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Book Description
Currently one of the hottest topics in biochemistry, the concept of molecular chaperones has challenged the paradigm of protein self-assembly. Key figures in many disciplines review all aspects of molecular chaperones in this volume, which arises from a Royal Society discussion meeting. Overview chapters discuss the significance of chaperones in biochemistry, molecular genetics and cell biology. Each chapter is well referenced providing access to the literature.
Author: Bernd Bakau
Publisher: CRC Press
ISBN: 020330375X
Category : Science
Languages : en
Pages : 784
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Book Description
One of the most intriguing discoveries in molecular biology in the last decade is the existence of an evolutionary conserved and essential system, consisting of molecular chaperones and folding catalysts, which promotes the folding of the proteins in the cell. This text summarizes our current knowledge of the cellular roles, the regulation and the mechanism of action of this system. It has a broad scope, covering cell biological, genetic and biochemical aspects of protein folding in cells from bacteria to man. Particularly appropriate to researchers working in basic and applied aspects of molecular medicine, this volume should also prove useful as an up-to-date reference book and as a textbook for specialized university courses.
Author: Sophie Jackson
Publisher: Springer
ISBN: 3642345522
Category : Science
Languages : en
Pages : 281
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Book Description
Assisting Oxidative Protein Folding: How Do Protein Disulphide-Isomerases Couple Conformational and Chemical Processes in Protein Folding?, by A. Katrine Wallis and Robert B. Freedman Peptide Bond cis/trans Isomerases: A Biocatalysis Perspective of Conformational Dynamics in Proteins, by Cordelia Schiene-Fischer, Tobias Aumüller and Gunter Fischer Small Heat-Shock Proteins: Paramedics of the Cell, by Gillian R. Hilton, Hadi Lioe, Florian Stengel, Andrew J. Baldwin und Justin L. P. Benesch Allostery in the Hsp70 Chaperone Proteins, by Erik R. P. Zuiderweg, Eric B. Bertelsen, Aikaterini Rousaki, Matthias P. Mayer, Jason E. Gestwicki and Atta Ahmad Hsp90: Structure and Function, by Sophie E. Jackson Extracellular Chaperones, by Rebecca A. Dabbs, Amy R. Wyatt, Justin J. Yerbury, Heath Ecroyd and Mark R. Wilson
Author: Derek J. Chadwick
Publisher: John Wiley & Sons
ISBN: 9780470754023
Category : Science
Languages : en
Pages : 248
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Book Description
The heat shock, or cell stress, response was first identified in the polytene chromosomes of Drosophila. This was later related to the appearance of novel proteins within stressed cells, and the key signal stimulating this appearance was identified as the presence of unfolded proteins within the cell. It is now known that this is a key mechanism enabling cells to survive a multitude of physical, chemical and biological stresses. Since the promulgation of the ‘molecular chaperone’ concept as a general cellular function to control the process of correct protein folding, a large number of molecular chaperones and protein folding catalysts have been identified, and it has been recognized that not all molecular chaperones are stress proteins and vice versa. The discovery of molecular chaperones as folding proteins went hand-in-hand with their recognition as potent immunogens in microbial infection. It was subsequently shown that administration of molecular chaperones such as Hsp60, Hsp70 or Hsp90 could inhibit experimental autoimmune diseases and cancer. More recently evidence has accumulated to show that certain molecular chaperones are also present on the surface of cells or in extracellular fluids. A new paradigm is emerging: at least some molecular chaperones are secreted proteins with pro- or anti-inflammatory actions, regulating the immune response in human diseases such as coronary heart disease, diabetes and rheumatoid arthritis. In addition to having direct effects on cells, molecular chaperones can bind peptides and present them to T cells to modulate immune responses. This may be significant in the treatment of cancer. This is the first book bringing leading researchers in this field together to review and discuss: our current knowledge of cell stress response and molecular chaperones the changing paradigms of protein trafficking and function cell stress proteins as immunomodulators and pro- and anti-inflammatory signalling molecules the role of these proteins in various chronic diseases and their potential as preventative or therapeutic agents. The Biology of Extracellular Molecular Chaperones is of particular interest to immunologists, cell and molecular biologists, microbiologists and virologists, as well as clinical researchers working in cardiology, diabetes, rheumatoid arthritis and other inflammatory diseases.
Author: Stephan N. Witt
Publisher: John Wiley & Sons
ISBN: 1118063899
Category : Science
Languages : en
Pages : 516
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Book Description
How protein chaperones protect cells from neurodegenerative diseases Including contributions from leading experts, Protein Chaperones and Protection from Neurodegenerative Diseases provides an in-depth exploration of how protein chaperones are involved in shielding cells from toxic aggregated or misfolded protein states that cause ALS, Parkinson's, and related diseases. Examining how different protein chaperones ameliorate the toxicity of proteins that are known to cause neurodegenerative damage, the book addresses both research and clinical perspectives on chaperone and anti-chaperone properties. The intersection of molecular chaperones and neurodegeneration is an intensely studied area, partly because of the potential for manipulating the expression of molecular chaperones to thwart the progression of debilitating diseases, and partly because of the ever-aging global population. Discussing the potential to harness the power of protein chaperones, and future directions for research, discovery, and therapeutics, this book is essential reading for scientists working in the fields of biochemistry, molecular medicine, pharmacology and drug discovery, biotechnology and pharmaceutical companies, advanced students, and anyone interested in this cutting-edge topic.
