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Books on the topic 'Folding system'

Author: Grafiati

Published: 4 June 2021

Last updated: 7 February 2022

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1

Kuwajima, Kunihiro. Water and biomolecules: Physical chemistry of life phenomena. Berlin: Springer, 2009.

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2

Fuzziness: Structural disorder in protein complexes. Austin, TX: Landes Bioscience, 2011.

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3

Frontiers of engineering: Reports on leading-edge engineering from the 2008 symposium. Washington: National Academies Press, 2009.

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4

Symposium on Frontiers of Engineering (2008 New Mexico). Frontiers of engineering: Reports on leading-edge engineering from the 2008 symposium. Washington: National Academies Press, 2009.

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5

Symposium on Frontiers of Engineering (2008 New Mexico). Frontiers of engineering: Reports on leading-edge engineering from the 2008 symposium. Washington: National Academies Press, 2009.

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6

Ghiso, Jorge, and Agueda Rostagno. Protein Folding Disorders of the Central Nervous System. WORLD SCIENTIFIC, 2017. http://dx.doi.org/10.1142/10517.

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7

Seneci, Pierfausto. Chemical Modulators of Protein Misfolding and Neurodegenerative Disease. Elsevier Science & Technology Books, 2015.

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8

Kuwajima, Kunihiro, Fumio Hirata, Mikio Kataoka, Yuji Goto, and Masahide Terazima. Water and Biomolecules: Physical Chemistry of Life Phenomena. Springer, 2010.

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9

Autonomous folding of transmembrane helices: Characterization of M13 coat protein dimerization motifs in a peptide system. Ottawa: National Library of Canada, 1999.

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10

(Editor), H. John Smith, Claire Simons (Editor), and Robert D. E. Sewell (Editor), eds. Protein Misfolding in Neurodegenerative Diseases: Mechanisms and Therapeutic Strategies (Enzyme Inhibitors). CRC, 2007.

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11

1930-, Smith H. J., Simons Claire, and Sewell Robert D. E, eds. Protein misfolding in neurodegenerative diseases: Mechanisms and therapeutic strategies. Boca Raton: Taylor & Francis, 2008.

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12

(Editor), J. Cummings, J. Hardy (Editor), M. Poncet (Editor), and Yves Christen (Editor), eds. Genotype - Proteotype - Phenotype Relationships in Neurodegenerative Diseases (Research and Perspectives in Alzheimer's Disease). Springer, 2005.

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13

Sigel, Helmut, Astrid Sigel, and Roland K. O. Sigel. Neurodegenerative Diseases and Metal Ions. Wiley & Sons, Incorporated, John, 2006.

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14

Astrid, Sigel, Sigel Helmut, and Sigel Roland K. O, eds. Neurodegenerative diseases and metal ions. Chichester, West Sussex, England: Wiley, 2006.

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15

(Editor), Astrid Sigel, Helmut Sigel (Editor), and Roland K. O. Sigel (Editor), eds. Neurodegenerative Diseases and Metal Ions: Metal Ions in Life Sciences. Wiley, 2006.

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16

Strodel, Birgit, and Bogdan Barz. Computational Approaches for Understanding Dynamical Systems: Protein Folding and Assembly. Elsevier Science & Technology Books, 2020.

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17

Computational Approaches for Understanding Dynamical Systems: Protein Folding and Assembly. Elsevier, 2020. http://dx.doi.org/10.1016/s1877-1173(20)x0003-2.

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18

Teplow, David B. Computational Approaches for Understanding Dynamical Systems: Protein Folding and Assembly. Elsevier Science & Technology, 2020.

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19

W.F. Van Gunsteren (Editor), P. K. Weiner (Editor), and A. J. Wilkinson (Editor), eds. Computer Simulation of Biomolecular Systems: Theoretical and Experimental Applications Volume 3 (Computer Simulations of Biomolecular Systems). Springer, 1997.

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20

Nakamura, Tomohiro, and Stuart A. Lipton. Neurodegenerative Diseases as Protein Misfolding Disorders. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780190233563.003.0002.

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Neurodegenerative diseases (NDDs) often represent disorders of protein folding. Rather than large aggregates, recent evidence suggests that soluble oligomers of misfolded proteins are the most neurotoxic species. Emerging evidence points to small, soluble oligomers of misfolded proteins as the cause of synaptic dysfunction and loss, the major pathological correlate to disease progression in many NDDs including Alzheimer’s disease. The protein quality control machinery of the cell, which includes molecular chaperones as found in the endoplasmic reticulum (ER), the ubiquitin-proteasome system (UPS), and various forms of autophagy, can counterbalance the accumulation of misfolded proteins to some extent. Their ability to eliminate the neurotoxic effects of misfolded proteins, however, declines with age. A plausible explanation for the age-dependent deterioration of the quality control machinery involves compromise of these systems by excessive generation of reactive oxygen species (ROS), such as superoxide anion (O2-), and reactive nitrogen species (RNS), such as nitric oxide (NO). The resulting redox stress contributes to the accumulation of misfolded proteins. Here, we focus on aberrantly increased generation of NO-related species since this process appears to accelerate the manifestation of key neuropathological features, including protein misfolding. We review the chemical mechanisms of posttranslational modification by RNS such as protein S-nitrosylation of critical cysteine thiol groups and nitration of tyrosine residues, showing how they contribute to the pathogenesis of NDDs.

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21

J, Wilkinson Anthony, Gunsteren Wilfred F. van, and Weiner Paul K, eds. Computer simulation of biomolecular systems: Theoretical and experimental applications. Dordrecht: Kluwer, 1997.

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22

Ignazio, Licata, and Sakaji Ammar, eds. Crossing in complexity: Interdisciplinary application of physics in biological and social systems. Hauppauge, N.Y: Nova Science Publishers, 2009.

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23

Gay, Steffen, and Michel Neidhart. Epigenetics. Oxford University Press, 2013. http://dx.doi.org/10.1093/med/9780199642489.003.0039.

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In higher eukaryotic organisms epigenetic modifications are crucial for proper chromatin folding and thereby proper regulation of gene expression. Epigenetics include DNA methylation, histone modifications, and microRNAs. First described in tumors, the involvement of aberrant epigenetic modifications has been reported also in other diseases, i.e. metabolic, psychiatric, inflammatory, and autoimmune. Deregulation of epigenetic mechanisms occurred in patients with rheumatoid arthritis, systemic lupus erythematosus, and scleroderma. Many questions remain: e.g. what is the cause of these epigenetic changes and how can we interfere in the pathological process? Here we discuss whether supplementation with methyl donors could represent a novel therapeutic concept for such diseases.

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24

Uversky, Vladimir, and Yuri Lyubchenko. Bio-Nanoimaging: Protein Misfolding and Aggregation. Elsevier Science & Technology Books, 2013.

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25

Lachmann, Helen J., and Giampaolo Merlini. The patient with amyloidosis. Edited by Giuseppe Remuzzi. Oxford University Press, 2015. http://dx.doi.org/10.1093/med/9780199592548.003.0152.

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Amyloidosis is a disorder of protein folding in which normally soluble plasma proteins are deposited in the extracellular space in an abnormal insoluble fibrillar form. The process of amyloid formation and deposition causes cytotoxicity and progressive organ dysfunction. Amyloid is remarkably diverse and can be hereditary or acquired, localized or systemic, and lethal or merely an incidental finding. The most important numerically are AL amyloidosis, in which the fibrils are composed of monoclonal immunoglobulin light chains, and AA amyloidosis, in which the acute phase reactant Serum Amyloid A component forms the fibrils.The kidney is involved in 75% of patients with systemic amyloidosis. Heavy proteinuria or nephrotic syndrome is characteristic of most amyloid variants.Without treatment, systemic disease is usually fatal but measures that reduce the supply of amyloid fibril precursor proteins can result in regression of amyloid deposits, prevention of organ failure, and improved quality of life and survival. Early diagnosis, before irreversible organ damage has occurred, is the key to effective treatment. Recent advances in diagnosis and therapy have much improved the outlook of patients with AL amyloidosis, but agents with broader promise are under investigation.

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26

Sherwood, Dennis, and Paul Dalby. Modern Thermodynamics for Chemists and Biochemists. Oxford University Press, 2018. http://dx.doi.org/10.1093/oso/9780198782957.001.0001.

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This book will equip a student of any physical or biological science with a sound understanding of thermodynamics, and will build confidence in using thermodynamics in practice. The emphasis is towards chemical thermodynamics, but the principles of the First, Second and Third Laws apply to all sciences. Importantly, the final four chapters show how thermodynamics can be applied to biological systems, discussing the biochemical standard state, bioenergetics, protein folding, and the self-assembly of smaller components to form higher-level structures. The book has not been written to support a particular curriculum; rather, it covers all the fundamental principles, so providing a comprehensive grounding, as well as a strong foundation for further study. It is therefore likely that there will be more material in this book than is required for any one particular curriculum, but we trust there is sufficient material for almost every curriculum. A key feature of the book is the style. It has been written so that ‘you can hear our voices’, and with the overarching intent of being logical, clear and comprehensible. The style will therefore be perceived as less formal than many other texts – and we trust more readable. Furthermore, we have sought to avoid phrases such as ‘it may be shown that...’, and ‘clearly, it follows that...’. If ‘it may be shown’, we show it; and we don’t use ‘clearly’ when things aren’t clear at all. Thermodynamics is notoriously difficult. This book does not make an intrinsically deep science ‘easy’. But it does make it intelligible.

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