Protein homeostasis: a subject collection from Cold Spring Harbor perspectives in biology
Gespeichert in:
| 1. Verfasser: | |
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| Weitere Verfasser: | , |
| Format: | Buch |
| Sprache: | English |
| Veröffentlicht: |
Cold Spring Harbor, New York
Cold Spring Harbor Laboratory Press
[2019]
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| Ausgabe: | Second edition |
| Schriftenreihe: | Cold Spring Harbor perspectives in biology
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| Schlagworte: | |
| Online-Zugang: | Inhaltsverzeichnis Klappentext Inhaltsverzeichnis Klappentext |
| Beschreibung: | x, 552 Seiten 27 cm |
| ISBN: | 9781621822967 1621822966 |
Internformat
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| 245 | 1 | 0 | |a Protein homeostasis |b a subject collection from Cold Spring Harbor perspectives in biology |c edited by Richard I. Morimoto, Northwestern University, F. Ulrich Hartl, Max Planck Institute of Biochemistry, Jeffery W. Kelly, The Scripps Research Institute |
| 250 | |a Second edition | ||
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| 650 | 4 | |a Homeostasis | |
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Datensatz im Suchindex
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|---|---|
| adam_text | Contents Preface, ix Protein Solubility Predictions Using the CamSol Method in the Study of Protein Homeostasis, 1 Pietro Sormanni and Michele Vendruscolo Functional Amyloids, 13 Daniel Otzen and Roland Riek The Amyloid Phenomenon and Its Significance in Biology and Medicine, 41 Christopher M. Dobson, Tuomas PJ. Knowles, and Michele Vendruscolo The Unfolded Protein Response: Detecting and Responding to Fluctuations in the Protein-Folding Capacity of the Endoplasmic Reticulum, 59 G. Elif Karagöz, Diego Acosta-Alvear, and Peter Walter Early Events in the Endoplasmic Reticulum Unfolded Protein Response, 77 Steffen Preissler and David Ron Recognition and Degradation of Mislocalized Proteins in Health and Disease, 95 Ramanujan S. Hegde and Eszter Zavodszky Redox-Mediated Regulatory Mechanisms of Endoplasmic Reticulum Homeostasis, 113 Ryo Ushioda and Kazuhiro Nagata Chaperoning Endoplasmic Reticulum-Associated Degradation (ERAD) and Protein Conformational Diseases, 127 Patrick G. Needham, Christopher J. Guerriero, and Jeffrey L. Brodsky Mitochondrial Proteolysis and Metabolic Control, 157 Sofia Ahola, Thomas Langer, and Thomas MacVicar Signaling and Regulation of the Mitochondrial Unfolded Protein Response, 177 Nandhitha Urna Naresh and Cole M. Haynes Functional Modules of the Proteostasis Network, 195 Gopal G. Jayaraj, Mark S. Hipp, and E Ulrich Hartl
Contents Modulation of Amyloid States by Molecular Chaperones, 213 Anne Wentink, Carmen Nussbaum-Krammer, and Bernd Bukau Chaperone Interactions at the Ribosome, 239 Elke Deuerling, Martin Gamerdinger, and Stefan G. Kreft The Proteasome and Its Network: Engineering for Adaptability, 259 Daniel Finley and Miguel A. Prado The Autophagy Lysosomal Pathway and Neurodegeneration, 285 Steven Finkbeiner The Nuclear and DNA-Associated Molecular Chaperone Network, 305 Zlata Gvozdenov, Janhavi Kolhe, and Brian C. Freeman Structure, Function, and Regulation of the Hsp90 Machinery, 321 Maximilian M. Biebl and Johannes Buchner Mechanisms of Small Heat Shock Proteins, 353 Maria K. Janowska, Hannah E.R. Baughman, Christopher N. Woods, and Rachel E. Kievit Spiraling in Control: Structures and Mechanisms of the Hsp104 Disaggregase, 373 James Shorter and Daniel R. Southworth Role of Polyphosphate in Amyloidogenic Processes, 391 Justine Lempart and Ursula Jakob Protein Phase Separation as a Stress Survival Strategy, 403 Titus M. Franzmann and Simon Alberti Tailoring of Proteostasis Networks with Heat Shock Factors, 421 Jenny Joutsen and Lea Sistonen Cell-Nonautonomous Regulation of Proteostasis in Aging and Disease, 439 Richard I. Morimoto Proteostasis in Viral Infection: Unfolding the Complex Virus-Chaperone Interplay, 459 Ranen Aviner and Judith Frydman Pharmacologic Approaches for Adapting Proteostasis in the Secretory Pathway to Ameliorate Protein Conformational Diseases, 479 Jeffery W. Kelly VI
Contents A Chemical Biology Approach to the Chaperonne in Cancer—HSP90 and Beyond, 495 Tony Taldone, Tai Wang, Anna Rodina, Naga Vara Kishore Pillarsetty, Chander S. Digwal, Sahil Sharma, Pengrong Yan, Suhasini Joshi, Piyusha P. Pagare, Alexander Bolaender, Gail ]. Roboz, Monica L. Guzman, and Gabriela Chiosis Proteome-Scale Mapping of Perturbed Proteostasis in Living Cells, 519 Isabel Lam, Erine Hallacli, and Vikram Khurana Index, 545 VII
Protein Homeostasis S I: C O D EDITION The entire life cycle of a protein—from synthesis and folding to transport and degradation—is carefully controlled by the proteostasis network. This network, consisting of many interconnected pathways and processes, manages protein homeostasis by dynamically responding to the needs of the cell. Stress and aging can challenge the proteostasis network, resulting in the aggregation of misfolded proteins—a feature of numerous neurodegenerative conditions. Written and edited by experts in the field, this collection from Cold Spring Harbor Perspectives in Biology provides a comprehensive update on how the proteostasis network functions in healthy cells and the diseases that result when protein quality control goes awry. The contributors examine the relevant biochemical attributes of proteins (e.g., solubility), the func tions of normal protein aggregates (e.g., biofilm formation in bacteria), and the various heat shock proteins, chaperones, translocation machineries, proteasomes, signaling factors, and transcriptional programs involved in proteostasis. The roles of specific subcellular structures—the endoplasmic reticulum, mitochondria, ribosomes, lysosomes, and cytoplasm—in pro tein quality control are covered, as is the regulation of proteostasis at the organismal level (e.g., via neuronal activity). Discussions of the responses by cells when errors in protein quality con trol occur, the medical disorders that can result (e.g., Alzheimer disease), and pharmacologic approaches to ameliorate protein conformational disorders arc also
included. This book is therefore an essential reference for biochemists, cell biologists, and all biomedical scientists wishing to understand the pathological consequences of and potential therapies for proteostasis deficiencies in common human diseases.
Contents Preface, ix Protein Solubility Predictions Using the CamSol Method in the Study of Protein Homeostasis, 1 Pietro Sormanni and Michele Vendruscolo Functional Amyloids, 13 Daniel Otzen and Roland Riek The Amyloid Phenomenon and Its Significance in Biology and Medicine, 41 Christopher M. Dobson, Tuomas PJ. Knowles, and Michele Vendruscolo The Unfolded Protein Response: Detecting and Responding to Fluctuations in the Protein-Folding Capacity of the Endoplasmic Reticulum, 59 G. Elif Karagöz, Diego Acosta-Alvear, and Peter Walter Early Events in the Endoplasmic Reticulum Unfolded Protein Response, 77 Steffen Preissler and David Ron Recognition and Degradation of Mislocalized Proteins in Health and Disease, 95 Ramanujan S. Hegde and Eszter Zavodszky Redox-Mediated Regulatory Mechanisms of Endoplasmic Reticulum Homeostasis, 113 Ryo Ushioda and Kazuhiro Nagata Chaperoning Endoplasmic Reticulum-Associated Degradation (ERAD) and Protein Conformational Diseases, 127 Patrick G. Needham, Christopher J. Guerriero, and Jeffrey L. Brodsky Mitochondrial Proteolysis and Metabolic Control, 157 Sofia Ahola, Thomas Langer, and Thomas MacVicar Signaling and Regulation of the Mitochondrial Unfolded Protein Response, 177 Nandhitha Urna Naresh and Cole M. Haynes Functional Modules of the Proteostasis Network, 195 Gopal G. Jayaraj, Mark S. Hipp, and E Ulrich Hartl
Contents Modulation of Amyloid States by Molecular Chaperones, 213 Anne Wentink, Carmen Nussbaum-Krammer, and Bernd Bukau Chaperone Interactions at the Ribosome, 239 Elke Deuerling, Martin Gamerdinger, and Stefan G. Kreft The Proteasome and Its Network: Engineering for Adaptability, 259 Daniel Finley and Miguel A. Prado The Autophagy Lysosomal Pathway and Neurodegeneration, 285 Steven Finkbeiner The Nuclear and DNA-Associated Molecular Chaperone Network, 305 Zlata Gvozdenov, Janhavi Kolhe, and Brian C. Freeman Structure, Function, and Regulation of the Hsp90 Machinery, 321 Maximilian M. Biebl and Johannes Buchner Mechanisms of Small Heat Shock Proteins, 353 Maria K. Janowska, Hannah E.R. Baughman, Christopher N. Woods, and Rachel E. Kievit Spiraling in Control: Structures and Mechanisms of the Hsp104 Disaggregase, 373 James Shorter and Daniel R. Southworth Role of Polyphosphate in Amyloidogenic Processes, 391 Justine Lempart and Ursula Jakob Protein Phase Separation as a Stress Survival Strategy, 403 Titus M. Franzmann and Simon Alberti Tailoring of Proteostasis Networks with Heat Shock Factors, 421 Jenny Joutsen and Lea Sistonen Cell-Nonautonomous Regulation of Proteostasis in Aging and Disease, 439 Richard I. Morimoto Proteostasis in Viral Infection: Unfolding the Complex Virus-Chaperone Interplay, 459 Ranen Aviner and Judith Frydman Pharmacologic Approaches for Adapting Proteostasis in the Secretory Pathway to Ameliorate Protein Conformational Diseases, 479 Jeffery W. Kelly VI
Contents A Chemical Biology Approach to the Chaperonne in Cancer—HSP90 and Beyond, 495 Tony Taldone, Tai Wang, Anna Rodina, Naga Vara Kishore Pillarsetty, Chander S. Digwal, Sahil Sharma, Pengrong Yan, Suhasini Joshi, Piyusha P. Pagare, Alexander Bolaender, Gail ]. Roboz, Monica L. Guzman, and Gabriela Chiosis Proteome-Scale Mapping of Perturbed Proteostasis in Living Cells, 519 Isabel Lam, Erine Hallacli, and Vikram Khurana Index, 545 VII
Protein Homeostasis S I: C O D EDITION The entire life cycle of a protein—from synthesis and folding to transport and degradation—is carefully controlled by the proteostasis network. This network, consisting of many interconnected pathways and processes, manages protein homeostasis by dynamically responding to the needs of the cell. Stress and aging can challenge the proteostasis network, resulting in the aggregation of misfolded proteins—a feature of numerous neurodegenerative conditions. Written and edited by experts in the field, this collection from Cold Spring Harbor Perspectives in Biology provides a comprehensive update on how the proteostasis network functions in healthy cells and the diseases that result when protein quality control goes awry. The contributors examine the relevant biochemical attributes of proteins (e.g., solubility), the func tions of normal protein aggregates (e.g., biofilm formation in bacteria), and the various heat shock proteins, chaperones, translocation machineries, proteasomes, signaling factors, and transcriptional programs involved in proteostasis. The roles of specific subcellular structures—the endoplasmic reticulum, mitochondria, ribosomes, lysosomes, and cytoplasm—in pro tein quality control are covered, as is the regulation of proteostasis at the organismal level (e.g., via neuronal activity). Discussions of the responses by cells when errors in protein quality con trol occur, the medical disorders that can result (e.g., Alzheimer disease), and pharmacologic approaches to ameliorate protein conformational disorders arc also
included. This book is therefore an essential reference for biochemists, cell biologists, and all biomedical scientists wishing to understand the pathological consequences of and potential therapies for proteostasis deficiencies in common human diseases.
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| indexdate | 2024-07-10T08:38:30Z |
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| spelling | Protein homeostasis a subject collection from Cold Spring Harbor perspectives in biology edited by Richard I. Morimoto, Northwestern University, F. Ulrich Hartl, Max Planck Institute of Biochemistry, Jeffery W. Kelly, The Scripps Research Institute Second edition Cold Spring Harbor, New York Cold Spring Harbor Laboratory Press [2019] © 2019 x, 552 Seiten 27 cm txt rdacontent n rdamedia nc rdacarrier Cold Spring Harbor perspectives in biology Proteins Metabolism Homeostasis Biological transport (DE-588)4143413-4 Aufsatzsammlung gnd-content Morimoto, Richard I. 1952- (DE-588)172264006 edt wpr Hartl, Franz-Ulrich 1957- (DE-588)111021065 edt wpr aut Kelly, Jeffery W. 1960- (DE-588)120059133X edt wpr Erscheint auch als Online-Ausgabe, EPUB 978-1-621823-00-1 Erscheint auch als Online-Ausgabe, MOBI 978-1-621823-01-8 Digitalisierung UB Regensburg - ADAM Catalogue Enrichment application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=031593481&sequence=000001&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis Digitalisierung UB Regensburg - ADAM Catalogue Enrichment application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=031593481&sequence=000003&line_number=0002&func_code=DB_RECORDS&service_type=MEDIA Klappentext Digitalisierung UB Regensburg - ADAM Catalogue Enrichment application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=031593481&sequence=000005&line_number=0003&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis Digitalisierung UB Regensburg - ADAM Catalogue Enrichment application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=031593481&sequence=000007&line_number=0004&func_code=DB_RECORDS&service_type=MEDIA Klappentext |
| spellingShingle | Hartl, Franz-Ulrich 1957- Protein homeostasis a subject collection from Cold Spring Harbor perspectives in biology Proteins Metabolism Homeostasis Biological transport |
| subject_GND | (DE-588)4143413-4 |
| title | Protein homeostasis a subject collection from Cold Spring Harbor perspectives in biology |
| title_auth | Protein homeostasis a subject collection from Cold Spring Harbor perspectives in biology |
| title_exact_search | Protein homeostasis a subject collection from Cold Spring Harbor perspectives in biology |
| title_full | Protein homeostasis a subject collection from Cold Spring Harbor perspectives in biology edited by Richard I. Morimoto, Northwestern University, F. Ulrich Hartl, Max Planck Institute of Biochemistry, Jeffery W. Kelly, The Scripps Research Institute |
| title_fullStr | Protein homeostasis a subject collection from Cold Spring Harbor perspectives in biology edited by Richard I. Morimoto, Northwestern University, F. Ulrich Hartl, Max Planck Institute of Biochemistry, Jeffery W. Kelly, The Scripps Research Institute |
| title_full_unstemmed | Protein homeostasis a subject collection from Cold Spring Harbor perspectives in biology edited by Richard I. Morimoto, Northwestern University, F. Ulrich Hartl, Max Planck Institute of Biochemistry, Jeffery W. Kelly, The Scripps Research Institute |
| title_short | Protein homeostasis |
| title_sort | protein homeostasis a subject collection from cold spring harbor perspectives in biology |
| title_sub | a subject collection from Cold Spring Harbor perspectives in biology |
| topic | Proteins Metabolism Homeostasis Biological transport |
| topic_facet | Proteins Metabolism Homeostasis Biological transport Aufsatzsammlung |
| url | http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=031593481&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=031593481&sequence=000003&line_number=0002&func_code=DB_RECORDS&service_type=MEDIA http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=031593481&sequence=000005&line_number=0003&func_code=DB_RECORDS&service_type=MEDIA http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=031593481&sequence=000007&line_number=0004&func_code=DB_RECORDS&service_type=MEDIA |
| work_keys_str_mv | AT morimotorichardi proteinhomeostasisasubjectcollectionfromcoldspringharborperspectivesinbiology AT hartlfranzulrich proteinhomeostasisasubjectcollectionfromcoldspringharborperspectivesinbiology AT kellyjefferyw proteinhomeostasisasubjectcollectionfromcoldspringharborperspectivesinbiology |
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