Cellular osmolytes : from chaperoning protein folding to clinical perspectives
This book provides essential insights into improving protein folding/stability, which is a result of the balance between the intra-molecular interactions of protein functional groups and their interactions with the solvent environment. Even a subtle change in the composition of the solvent environme...
Saved in:
| Other Authors: | , |
|---|---|
| Format: | eBook |
| Language: | English |
| Published: |
Singapore :
Springer,
2017.
|
| Subjects: | |
| ISBN: | 9789811037078 9789811037061 |
| Physical Description: | 1 online resource (vii, 249 pages) : illustrations (some color) |
Cover
Table of contents
| LEADER | 05898cam a2200469Ii 4500 | ||
|---|---|---|---|
| 001 | 97315 | ||
| 003 | CZ-ZlUTB | ||
| 005 | 20240914110502.0 | ||
| 006 | m o d | ||
| 007 | cr cnu|||unuuu | ||
| 008 | 170518s2017 si a ob 000 0 eng d | ||
| 040 | |a N$T |b eng |e rda |e pn |c N$T |d EBLCP |d GW5XE |d N$T |d YDX |d OCLCF |d UAB |d ESU |d AZU |d UPM |d IOG |d COO |d MERER |d OCLCQ |d OHI |d U3W |d OCLCQ |d CAUOI |d KSU |d VT2 |d WYU |d AUD |d UKMGB |d UKAHL |d OCLCQ |d ERF |d OCLCQ |d SRU | ||
| 020 | |a 9789811037078 |q (electronic bk.) | ||
| 020 | |z 9789811037061 |q (print) | ||
| 024 | 7 | |a 10.1007/978-981-10-3707-8 |2 doi | |
| 035 | |a (OCoLC)987438988 |z (OCoLC)987686247 |z (OCoLC)992518824 |z (OCoLC)992826513 |z (OCoLC)999414564 |z (OCoLC)1005794872 |z (OCoLC)1011849538 |z (OCoLC)1048141994 |z (OCoLC)1066443101 |z (OCoLC)1066649778 | ||
| 245 | 0 | 0 | |a Cellular osmolytes : |b from chaperoning protein folding to clinical perspectives / |c Laishram Rajendrakumar Singh, Tanveer Ali Dar, editors. |
| 264 | 1 | |a Singapore : |b Springer, |c 2017. | |
| 300 | |a 1 online resource (vii, 249 pages) : |b illustrations (some color) | ||
| 336 | |a text |b txt |2 rdacontent | ||
| 337 | |a počítač |b c |2 rdamedia | ||
| 338 | |a online zdroj |b cr |2 rdacarrier | ||
| 504 | |a Includes bibliographical references. | ||
| 505 | 0 | |a About the Editors; 1: Osmolyte System and Its Biological Significance; 1.1 Introduction; 1.2 Production, Enhancement and Expression of Osmolytes; 1.2.1 Bacteria and Archaea; 1.2.2 Yeast; 1.2.3 Plants; 1.2.4 Marine Animals; 1.2.5 Mammals; 1.3 Mechanism of Interaction of Osmolytes with Proteins; 1.3.1 Role of Naturally Occurring Osmolytes in Destabilizing Proteins; 1.3.2 Role of Osmolytes in Maintaining Protein Homeostasis; 1.4 Role of Osmolytes in Protein Aggregation and Amyloidosis; 1.4.1 Mechanism of Aggregation; 1.4.2 Hypothesis. | |
| 505 | 8 | |a 1.5 Role of Osmolytes in Cellular Functions; 1.5.1 Role of Osmolytes in Maintenance of Cell Volume; 1.5.2 Cellular Functions of Osmolytes; 1.5.3 Protective Effect of Osmolytes on Metabolism; 1.5.4 Antioxidation; 1.5.5 Maintenance of Reduction and Oxidation Reactions and Protection Against Hypoxia; 1.5.6 Sulfide/Sulfate Detoxification; 1.5.7 Miscellaneous Roles of Osmolytes in Metabolism; 1.5.8 Stabilization and Counteraction; 1.5.9 Anhydrobiosis; 1.5.10 Freezing; 1.5.11 High Temperature; 1.5.12 Hydrostatic Pressure in the Deep Sea. | |
| 505 | 8 | |a 1.5.13 The "Yin and Yang" Theory of Cytoprotection; 1.6 Role of Osmolytes in Circumventing Stress; 1.6.1 Amaranthaceae; 1.6.2 Plumbaginaceae; 1.6.3 Plantaginaceae; 1.6.4 Aizoaceae; 1.6.5 Poaceae; 1.6.6 Brassicaceae; 1.6.7 Other Families; 1.6.8 Role of Osmolytes in Scavenging Hydroxyl Radicals; 1.7 Conclusion and Future Directions; References; 2: Protein-Osmolyte Interactions: Molecular Insights; 2.1 Introduction; 2.1.1 Organic Osmolytes Are Evolutionarily Restricted; 2.1.2 Osmolyte Can Induce Proper Protein Folding; 2.2 Forces Involved in Osmolyte-Induced Protein Folding. | |
| 505 | 8 | |a 2.2.1 Osmophobic Effect; 2.2.2 Molecular Crowding Effect; 2.2.3 Surface Tension Effect; 2.2.4 Preferential Hydration Effect; 2.2.5 Solvophobic Effect; 2.3 Models Used to Explain Osmolyte-Protein Interaction; 2.4 Summary and Perspectives; References; 3: Crosstalk Between Osmolytes and Cellular Chaperones: Examples in Saccharomyces cerevisiae; 3.1 Introduction; 3.2 Cellular Chaperones; 3.3 Chaperonins; 3.3.1 Hsp40; 3.3.2 GroEL-GroES (Hsp60-Hsp10); 3.3.3 Hsp70; 3.3.4 Hsp90; 3.3.5 Hsp100; 3.3.5.1 Small Heat Shock Proteins; 3.3.6 Peptidylprolyl Isomerase; 3.4 Osmolytes. | |
| 505 | 8 | |a 3.5 Osmolytes Synthesized in Yeast; 3.6 Cellular Stress Response Machinery; 3.6.1 Heat Shock Response; 3.6.1.1 Heat Shock Factor (Hsf); 3.6.1.2 Msn2/Msn4; 3.6.2 Unfolded Protein Response; 3.7 Crosstalk Between Chaperones and Osmolytes in Stressed Yeast; References; 4: Osmolytes Offset the Urea's Effect on Protein Structure and Function; 4.1 Introduction; 4.2 Molecular Mechanism of Counteraction Phenomenon; 4.3 Is Counteraction System Perfect?; 4.4 Methylamines Fail to Counter Urea's Effects on Some Proteins; 4.5 Factors Affecting 2:1 (Urea-Methylamine) Ratio. | |
| 506 | |a Plný text je dostupný pouze z IP adres počítačů Univerzity Tomáše Bati ve Zlíně nebo vzdáleným přístupem pro zaměstnance a studenty | ||
| 520 | |a This book provides essential insights into improving protein folding/stability, which is a result of the balance between the intra-molecular interactions of protein functional groups and their interactions with the solvent environment. Even a subtle change in the composition of the solvent environment will alter the fidelity of the protein folding process, and hostile environmental stresses represent one of the basic causes of challenges in protein folding or misfolding. Among the strategies employed in a wide range of species and cell types to circumvent the hostile environmental conditions is the elaboration of small organic molecules called osmolytes, and recent advances have revealed that certain specific osmolytes might be key biomarkers of cancer, infectious diseases and are useful in heterologous protein expression and vaccine flocculation. As such a large pool of data has been collected regarding their potential for therapeutic intervention in neurodegenerative diseases and other metabolic disorders caused by protein aggregation or proteiostasis failure. | ||
| 590 | |a SpringerLink |b Springer Complete eBooks | ||
| 650 | 0 | |a Molecular chaperones. | |
| 650 | 0 | |a Protein folding. | |
| 655 | 7 | |a elektronické knihy |7 fd186907 |2 czenas | |
| 655 | 9 | |a electronic books |2 eczenas | |
| 700 | 1 | |a Singh, Laishram Rajendrakumar, |e editor. | |
| 700 | 1 | |a Dar, Tanveer Ali, |e editor. | |
| 776 | 0 | 8 | |i Printed edition: |z 9789811037061 |
| 856 | 4 | 0 | |u https://proxy.k.utb.cz/login?url=https://link.springer.com/10.1007/978-981-10-3707-8 |y Plný text |
| 992 | |c NTK-SpringerBLS | ||
| 999 | |c 97315 |d 97315 | ||
| 993 | |x NEPOSILAT |y EIZ | ||
Save to List
Cite this
Export Record
Email this