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Books on the topic 'Proteins thiol'

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Author: Grafiati

Published: 9 March 2023

Last updated: 10 March 2023

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1

Kosuri, Pallav. Mechanochemical Methods for Single Molecule Biochemistry and Studies of Thiol-Disulfide Exchange in Proteins. [New York, N.Y.?]: [publisher not identified], 2012.

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2

service), ScienceDirect (Online, ed. Thiol redox transitions in cell signaling: Cellular localization and signaling. San Diego, Calif: Elsevier, 2010.

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3

1942-, Sies H., and Packer Lester, eds. Protein sensors and reactive oxygen species. San Diego, Calif: Academic Press, 2002.

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4

Murricane, Christopher. Correlation between ribosome breakdown and activity of a lysosomal thiol proteinase in tetrahymena pyriformis. Birmingham: University of Birmingham, 1988.

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5

Principe, Paola Domenica Luiga. Quantitative studies of cellular protein thiol groups in relation to the growth behavior of rat livercell lines: Comparative estimations by computer microdensitometry, biochemistry and flow cytometry. Uxbridge: Brunel University, 1988.

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6

Protein Sensors and Reactive Oxygen Species - Part B: Thiol Enzymes and Proteins. Elsevier, 2002. http://dx.doi.org/10.1016/s0076-6879(00)x0020-1.

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7

Packer, Lester, and Helmut Sies. Protein Sensors and Reactive Oxygen Species, Part B: Thiol Enzymes and Proteins Pt. B. Elsevier Science & Technology Books, 2002.

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8

(Editor), Helmut Sies, and Lester Packer (Editor), eds. Methods in Enzymology, Volume 348: Protein Sensors and Reactive Oxygen Species, Part B: Thiol Enzymes and Proteins (Methods in Enzymology). Academic Press, 2002.

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9

(Editor), Helmut Sies, and Lester Packer (Editor), eds. Methods in Enzymology, Volume 348: Protein Sensors and Reactive Oxygen Species, Part B: Thiol Enzymes and Proteins (Methods in Enzymology). Academic Press, 2002.

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10

Thiol Redox Transitions in Cell Signaling Pt. A,Vol.473: Chemistry and Biochemistry of Low Molecular Weight and Protein Thiols. Elsevier Science & Technology Books, 2010.

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11

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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12

Biothiols Part A Monothiols and Dithiols, Protein Thiols, and Thiyl Radicals. Elsevier, 1995. http://dx.doi.org/10.1016/s0076-6879(00)x0154-1.

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13

Abelson, John N., Helmut Sies, and Melvin I. Simon. Biothiols, Part a: Monothiols and Dithiols, Protein Thiols, and Thiyl Radicals. Elsevier Science & Technology Books, 1995.

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14

(Editor), John N. Abelson, Melvin I. Simon (Editor), and Helmut Sies (Editor), eds. Biothiols, Part A: Monothiols and Dithiols, Protein Thiols, and Thiyl Radicals (Methods in Enzymology). Academic Press, 1995.

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15

(Editor), John N. Abelson, Melvin I. Simon (Editor), and Helmut Sies (Editor), eds. Biothiols, Part A: Monothiols and Dithiols, Protein Thiols, and Thiyl Radicals (Methods in Enzymology). Academic Press, 1995.

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16

Thiol Redox Transitions in Cell Signaling, Part A: Chemistry and Biochemistry of Low Molecular Weight and Protein Thiols. Elsevier, 2010. http://dx.doi.org/10.1016/c2009-0-01955-2.

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17

Packer, Lester, and Enrique Cadenas. Thiol Redox Transitions in Cell Signaling, Part A Pt. A, Vol. 473: Chemistry and Biochemistry of Low Molecular Weight and Protein Thiols. Elsevier Science & Technology Books, 2010.

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18

Methods in Enzymology, Volume 347: Protein Sensors and Reactive Oxygen Species, Part A: Selenoproteins and Thioredoxin (Methods in Enzymology). Academic Press, 2002.

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19

(Editor), Lester Packer, and Helmut Sies (Editor), eds. Methods in Enzymology, Volume 347: Protein Sensors and Reactive Oxygen Species, Part A: Selenoproteins and Thioredoxin (Methods in Enzymology). Academic Press, 2002.

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20

Daudon, Michel, and Paul Jungers. Cystine stones. Edited by Mark E. De Broe. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780199592548.003.0203_update_001.

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Cystinuria, an autosomal recessive disease (estimated at 1:7000 births worldwide), results from the defective reabsorption of cystine and dibasic amino acids (also ornithine, arginine, lysine, COAL) by epithelial cells of renal proximal tubules, leading to an abnormally high urinary excretion of these amino acids. Due to the poor solubility of cystine at the usual urine pH, formation of cystine crystals and stones ensues. Incidence of homozygotes is estimated at 1 in 7000 births worldwide, but is lower in European countries and much higher in populations with frequent consanguinity. Cystine stones represent 1–2% of all stones in adults and 5–8% in paediatric patients, with an equal distribution between males and females.Cystinuria is caused by inactivating mutations in the gene SLC3A1 or SLC7A9, both encoding proteins contributing to the function of the heterodimeric transport system of cystine.Cystine nephrolithiasis may present in infants, most frequently in adolescents or young adults, sometimes later. Cystine calculi are weakly radio-opaque. Stone analysis using infrared spectroscopy (or X-ray diffraction) allows immediate and accurate diagnosis. Urinary amino acid chromatography quantifies urinary cystine excretion, needed to define the therapeutic strategy.Urological treatment of cystine stones currently uses extracorporeal stone wave lithotripsy or flexible ureterorenoscopy with Holmium laser, that is, minimally invasive techniques. However, as cystine stones are highly recurrent, preventive therapy is essential.Medical treatment combines reduced methionine and sodium intake, to lower cystine excretion; hyperdiuresis (> 3 L/day) to reduce cystine concentration; and active alkalinization preferably using potassium citrate (40–80 mEq/day) to increase cystine solubility by rising urine pH up to 7.5–8. If these measures are insufficient to prevent recurrent stone formation, a thiol derivative (D-penicillamine or tiopronin), which converts cystine into a more soluble disulphide, should be added. Close monitoring and adherence of the patient to the therapeutic programme are needed to ensure life-long compliance, the key for successful prevention in the long term.

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21

Schultz, Caroline Luise. The role of sulphur and thiol-rich copper-binding protein in the copper tolerance of "Deschampsia cespitosa"(L.) Beauv. 1986.

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22

Foong, Louise Yuli. Thiol reactive chemical probes for studying protein ion channel structure and the application of chemical probes to the study of U2AF, an essential RNA splicing factor. 2001.

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