Biothiols, Part A: Monothiols and Dithiols, Protein Thiols, and Thiyl Radicals
Author: ABELSON John N.Language: Anglais
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482 p. · 22.9x15.2 cm
* Prevention of oxidative stress
* Redox regulation of metabolism
A. Meister, Glutathione Metabolism.
H.F. Gilbert, Thiol/Disulfide Exchange Equilibria and Disulfide Bond Stability.
P. Wardman and C. von Sonntag, Kinetic Factors That Control the Fate of Thiyl Radicals in Cells.
C. Schineich, Kinetics of Thiol Reactions.
S.A. Everett and P. Wardman, Perthiols as Antioxidants: Radical-Scavenging and Pro-oxidative Mechanisms.
S.C. Kundu and R.L. Willson, Thiyl (Sulfhydryl/Thiol) Free Radical Reactions, Vitamins, Beta-Carotene, and Superoxide Dismutase in Oxidative Stress: Design and Interpretation of Enzymatic Studies.
C.C. Winterbourn and D. Metodiewa, Reaction of Superoxide with Glutathione and Other Thiols.
L.M. Weiner, Quantitative Determination of Thiol Groups in Low and High Molecular Weight Compounds by Electron Paramagnetic Resonance.
E. Cadenas, Thiyl Radical Formation during Thiol Oxidation by Ferrylmyoglobin.
R. Munday, In Vivo Toxicity of Thiols: Relationship to Rate of One-Electron Oxidation by Oxyhemoglobin.
Chemical Basis of Thiol/Disulfide Measurements:
N.S. Kosower and E.M. Kosower, Diamide: An Oxidant Probe for Thiols.
E.M. Kosower and N.S. Kosower, Bromobimane Probes for Thiols.
G.L. Newton and R.C. Fahey, Determination of Biothiols by Bromobimane Labeling and High-Performance Liquid Chromatography.
R. Singh, G.V. Lamoureux, W.J. Lees, and G.M. Whitesides, Reagents for Rapid Reduction of Disulfide Bonds.
K. Becker and R.H. Schirmer, 1,3-Bis(2-chloroethyl)-1-nitrosourea as Thiol-Carbamoylating Agent in Biological Systems.
Monothiols: Measurement in Organs, Cells, Organelles, and Body Fluids:
H. Nohl, K. Stolze, and L.M. Weiner, Noninvasive Measurement of Thiol Levels in Cells and Isolated Organs.
J.A. Cook and J.B. Mitchell, Measurement of Thiols in Cell Populations from Tumor and Normal Tissue.
C. Hwang, H.F. Lodish, and A.J. Sinskey, Measurement of Glutathione Redox State in Cytosol and Secretory Pathway of Cultured Cells.
T.Y. Aw, Assay of Thiols and Disulfides in Intestinal Lymph.
R. Singh, W.A. Blattler, and A.R. Collinson, Assay for Thiols Based on Reactivation of Papain.
J. Vita, J. Sastre, M. Asensi,and L. Packer, Assay of Blood Glutathione Oxidation during Physical Exercise.
P. Reinemer, H.W. Dirr, and R. Huber, X-Ray Structure Methods for Glutathione Binding.
W. Drige, R. Kinscherf, S. Mihm, D. Galter, S. Roth, H. Gmander, T. Fischbach, and M. Bockstette, Thiols and the Immune System: Effect of N-Acetylcysteine on T Cell System in Human Subjects.
R. Olivier, Flow Cytometry Technique for Assessing Effects of N-Acetylcysteine on Apoptosis and Cell Viability of Human Immunodeficiency Virus-Infected Lymphocytes.
C. Gitler and M. Londner, Use of p-Nitrophenyl Disulfide to Measure Reductive Capacity of Intact Cells.
R.L. Krauth-Siegel, E.M. Jacoby, and R.H. Schirmer, Trypanothione and N1-Glutathionylspermidine: Isolation and Determination.
D.M. Ziegler and L.L. Poulsen, Estimation of Tissue Cysteamine by Quantitative Thin-Layer Chromatography.
Dithiols: Alpha-Lipoic Acid:
G.P. Biewenga and A. Bast, Reaction of Lipoic Acid with Ebselen and Hypochlorous Acid.
D. Han, G.J. Handelman, and L. Packer, Analysis of Reduced and Oxidized Lipoic Acid in Biological Samples by High-Performance Liquid Chromatography.
T. Kawabata, H.-J. Tritschler, and L. Packer, Reaction of(R,S)-Dihydrolipoic Acid and Homologs with Iron.
G. Zimmer, L. Mainka, and H. Ulrich, ATP Synthesis and ATPase Activities in Heart Mitoplasts under Influence of R- and S-Enantiomers of Lipoic Acid.
K. Fujiwara, K. Okamura-Ikeda, and Y. Motokawa, Assay for Protein Lipoylation Reaction.
Protein Thiols and Sulfides:
R. Wynn and F.M. Richards, Chemical Modification of Protein Thiols: Formation of Mixed Disulfides.
H. Faulstich and D. Heintz, Reversible Introduction of Thiol Compounds into Proteins by Use of Activated Mixed Disulfides.
C. Gitler, B. Zarmi, and E. Kalef, Use of Cationic Detergents to Enhance Reactivity of Protein Sulfhydryls.
R. Wynn and F.M. Richards, Measuring Thiol-Disulfide Exchange Equilibrium Constants for Single Cysteine-Containing Proteins.
N. Katunuma and E. Kominami, Structure, Properties, Mechanisms, and Assays of Cysteine Protease Inhibitors: Cystatins and E-64 Derivatives.
R.B. Freedman, H.C. Hawkins, and S.H. McLaughlin, Protein Disulfide-Isomerase.
S.S. Simons, Jr., and W.B. Pratt, Glucocorticoid Receptor Thiols and Steroid Binding Activity.
J.A. Thomas, W. Zhao, S. Hendrich, and P. Haddock, Analysis of Cells and Tissues for S-Thiolation of Proteins.
M. Kussmann and M. Przybylski, Tertiary Structure-Selective Characterization of Protein Dithiol Groups by Phenylarsine Oxide Modification and Mass Spectrometric Peptide Mapping.
R.N. Perham, Structure and Posttranslational Modification of Lipoyl Domain of 2-Oxo-Acid Dehydrogenase Multienzyme Complexes.
A. van der Vliet, C.E. Cross, B. Halliwell, and C.A. O'Neill, Plasma Protein Sulfhydryl Oxidation: Effect of Low Molecular Weight Thiols.
K.L. Maier, A.-G.Lenz, I. Beck-Speier,and U. Costabel, Analysis of Methionine Sulfoxide in Proteins.
N. Brot, M.A. Rahman, J. Moskovitz, H. Weissbach, J. Strassman, S.O. Yancey, and S.R. Kushner, Escherichia coli Peptide Methionine Sulfoxide Reductase: Cloning, High Expression, andPurification.
K.M. Noll, Thiol Coenzymes of Methanogens.
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