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Books on the topic 'Système redox'

Author: Grafiati

Published: 4 June 2021

Last updated: 18 February 2022

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1

Hirao, Toshikazu, ed. Functionalized Redox Systems. Springer Japan, 2015. http://dx.doi.org/10.1007/978-4-431-55306-9.

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2

Nishinaga, Tohru, ed. Organic Redox Systems. John Wiley & Sons, Inc, 2016. http://dx.doi.org/10.1002/9781118858981.

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3

Hirao, Toshikazu, ed. Redox Systems Under Nano-Space Control. Springer-Verlag, 2006. http://dx.doi.org/10.1007/3-540-29580-1.

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4

Organic redox systems: Synthesis, properties, and applications. John Wiley & Sons, 2016.

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5

Genesis redux: Experiments creating artificial life. Windcrest/McGraw-Hill, 1994.

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6

1916-, King Tsoo E., Mason Howard S, and Morrison Martin, eds. Oxidases and related redox systems: Proceedings of the 4th International Symposium on Oxidases and Related Redox Systems held in Portland, Oregon, October 4-8, 1987. A.R. Liss, 1988.

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7

Asard, Han, Alajos Bérczi, and Roland J. Caubergs, eds. Plasma Membrane Redox Systems and their Role in Biological Stress and Disease. Springer Netherlands, 1998. http://dx.doi.org/10.1007/978-94-017-2695-5.

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8

Hirao, Toshikazu, and Various. Redox Systems Under Nano-Space Control. Springer, 2010.

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9

Redox Systems Under Nano-Space Control. Springer, 2006.

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10

Nishinaga, Tohru. Organic Redox Systems: Synthesis, Properties, and Applications. Wiley & Sons, Incorporated, John, 2015.

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11

Nishinaga, Tohru. Organic Redox Systems: Synthesis, Properties, and Applications. Wiley & Sons, Incorporated, John, 2015.

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12

M, LeVine Steven, Connor James R, and Schipper Hyman M. 1954-, eds. Redox-active metals in neurological disorders. New York Academy of Sciences, 2004.

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13

Redox-active metals in neurological disorders. New York Academy of Sciences, 2004.

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14

King, TE. King: Oxidases & Related Redox Systems (Pro Portland Oregon 1987). John Wiley & Sons Inc, 1988.

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15

(undifferentiated), King. Oxidases and related redox systems: Proceedings of the 4th International Symposium on Oxidases and Related Redox Systems held in Portland, Oregon, October 4-8, 1987. Wiley-Liss, 1988.

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16

Asard, Han. Plasma Membrane Redox Systems and their role in Biological Stress and Disease. Springer, 2010.

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17

Hirao, Toshikazu. Functionalized Redox Systems: Synthetic Reactions and Design of π- and Bio-Conjugates. Springer, 2015.

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18

Redox Systems Under Nano-Space Control: Nano-Space Control and Its Applications. Springer, 2006.

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19

Hirao, Toshikazu. Functionalized Redox Systems: Synthetic Reactions and Design of π- and Bio-Conjugates. Springer, 2016.

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20

Han, Asard, Bérczi Alajos, and Caubergs Roland J, eds. Plasma membrane redox systems and their role in biological stress and disease. Kluwer, 1998.

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21

Oxidases and related redox systems: Proceedings of the 4th International Symposium on Oxidases and Related Redox Systems held in Portland, Oregon, October ... in clinical and biological research). A.R. Liss, 1988.

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22

(Editor), Steven M. Levine, James R. Connor (Editor), and Hyman M. Schipper (Editor), eds. Redox-Active Metals in Neurological Disorders (Annals of the New York Academy of Sciences). New York Academy of Sciences, 2004.

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23

Chance, Britton. Non-Destructive Assays of Tissue Redox Systems (Distinguished Lecture Series of the Society of General Physiologists). Raven Pr, 1988.

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24

(Editor), Steven M. Levine, James R. Connor (Editor), and Hyman M. Schipper (Editor), eds. Redox-Active Metals in Neurological Disorders (Annals of the New York Academy of Sciences, V. 1012). New York Academy of Sciences, 2004.

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25

Banks, Alex, and Eve Porcello. Learning React: Functional Web Development with React and Redux. O'Reilly Media, 2017.

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26

React Quickly: Painless web apps with React, JSX, Redux, and GraphQL. Manning Publications, 2017.

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27

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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28

Learning React: A Hands-On Guide to Building Web Applications Using React and Redux (2nd Edition). Addison-Wesley Professional, 2018.

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29

Deegan, Patrick. Porphyria. Edited by Patrick Davey and David Sprigings. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780199568741.003.0179.

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This chapter discusses six diseases caused by inborn errors of metabolism affecting the biosynthesis of haem. Haem is a tetracyclic metal-binding compound involved in oxygen transport (in haemoglobin and myoglobin) and redox reactions (e.g. in the cytochrome P450 system). Each of these conditions is caused by a single gene defect in one of the enzymes involved in the biosynthesis of haem. Inheritance is usually autosomal dominant with incomplete penetrance. The enzyme defect results in disease, not as a result of deficiency of the reaction product, but as a result of accumulation of precursors. Early, soluble precursors, 5-aminolaevulinic acid, and porphobilinogen (not porphyrins as such) are neurotoxic and, when present in great excess, as occurs when flux through the haem synthetic pathway is increased in response to particular medications or hormones, lead to acute neurovisceral crises. Later cyclical precursors (porphyrins) in the pathway are also water soluble and excreted in urine, but are susceptible to activation by electromagnetic radiation in the visible spectrum and are converted to free-radical metabolites that cause pain, inflammation, and tissue damage in the skin. The final haem precursors (also porphyrins) are hydrophobic and excreted in the bile and faeces and are also activated by light to toxic metabolites.

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