Diverse functional roles of reactive cysteines

ACS Chemical Biology

Volumn 8, Issue 2, 2013, Pages 283-296

  Pace, Nicholas J ^a   Weerapana, Eranthie ^a  

^a BOSTON COLLEGE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

APOPTOSIS SIGNAL REGULATING KINASE 1; CYSTEINE; CYSTEINE PROTEINASE; INITIATOR CASPASE; KELCH LIKE ECH ASSOCIATED PROTEIN 1; METHIONINE SULFOXIDE REDUCTASE; NUCLEOPHILE; PHOSPHOTRANSFERASE; PROTEIN KINASE; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; THIOREDOXIN; THIOREDOXIN REDUCTASE; UBIQUITIN PROTEIN LIGASE;

ALLOSTERISM; CANCER CELL; CELL CYCLE PROGRESSION; CELL CYCLE REGULATION; CELL DEATH; CELL FUNCTION; CELL METABOLISM; CELL PROLIFERATION; CELLULAR DISTRIBUTION; CHEMOPROPHYLAXIS; GENE TARGETING; HUMAN; ISOMERIZATION; METAL BINDING; NUCLEOPHILICITY; PENTOSE PHOSPHATE CYCLE; PRIORITY JOURNAL; PROTEIN DEGRADATION; REVIEW; UBIQUITINATION; ANALOGS AND DERIVATIVES; CHEMICAL STRUCTURE; CHEMISTRY; METABOLISM;

CYSTEINE; HUMANS; MODELS, MOLECULAR; MOLECULAR STRUCTURE;

EID: 84874081337     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb3005269     Document Type: Review

References (134)

1. Pe'er, I., Felder, C. E., Man, O., Silman, I., Sussman, J. L., and Beckmann, J. S. (2004) Proteomic signatures: amino acid and oligopeptide compositions differentiate among phyla Proteins 54, 20-40
2. Marino, S. M. and Gladyshev, V. N. (2010) Cysteine function governs its conservation and degeneration and restricts its utilization on protein surfaces J. Mol. Biol. 404, 902-916
3. Jordan, I. K., Kondrashov, F. A., Adzhubei, I. A., Wolf, Y. I., Koonin, E. V., Kondrashov, A. S., and Sunyaev, S. (2005) A universal trend of amino acid gain and loss in protein evolution Nature 433, 633-638
4. Wu, H., Ma, B. G., Zhao, J. T., and Zhang, H. Y. (2007) How similar are amino acid mutations in human genetic diseases and evolution Biochem. Biophys. Res. Commun. 362, 233-237
5. Bulaj, G., Kortemme, T., and Goldenberg, D. P. (1998) Ionization-reactivity relationships for cysteine thiols in polypeptides Biochemistry 37, 8965-8972
6. Harris, T. K. and Turner, G. J. (2002) Structural basis of perturbed pKa values of catalytic groups in enzyme active sites IUBMB Life 53, 85-98
7. Giles, N. M., Giles, G. I., and Jacob, C. (2003) Multiple roles of cysteine in biocatalysis Biochem. Biophys. Res. Commun. 300, 1-4
8. Paulsen, C. E. and Carroll, K. S. (2010) Orchestrating redox signaling networks through regulatory cysteine switches ACS Chem. Biol. 5, 47-62
9. Klomsiri, C., Karplus, P. A., and Poole, L. B. (2011) Cysteine-based redox switches in enzymes Antioxid. Redox Signaling 14, 1065-1077
10. Reddie, K. G., Seo, Y. H., Muse Iii, W. B., Leonard, S. E., and Carroll, K. S. (2008) A chemical approach for detecting sulfenic acid-modified proteins in living cells Mol. Biosyst. 4, 521-531
11. Hess, D. T., Matsumoto, A., Kim, S. O., Marshall, H. E., and Stamler, J. S. (2005) Protein S-nitrosylation: purview and parameters Nat. Rev. Mol. Cell. Biol. 6, 150-166
12. Linder, M. E. and Deschenes, R. J. (2007) Palmitoylation: policing protein stability and traffic Nat. Rev. Mol. Cell. Biol. 8, 74-84
13. Zhang, F. L. and Casey, P. J. (1996) Protein prenylation: molecular mechanisms and functional consequences Annu. Rev. Biochem. 65, 241-269
14. Higdon, A., Diers, A. R., Oh, J. Y., Landar, A., and Darley-Usmar, V. M. (2012) Cell signalling by reactive lipid species: new concepts and molecular mechanisms Biochem. J. 442, 453-464
15. Leonard, S. E. and Carroll, K. S. (2010) Chemical 'omics' approaches for understanding protein cysteine oxidation in biology Curr. Opin. Chem. Biol. 15, 88-102
16. Leichert, L. I., Gehrke, F., Gudiseva, H. V., Blackwell, T., Ilbert, M., Walker, A. K., Strahler, J. R., Andrews, P. C., and Jakob, U. (2008) Quantifying changes in the thiol redox proteome upon oxidative stress in vivo Proc. Natl. Acad. Sci. U.S.A. 105, 8197-8202
17. Jaffrey, S. R. and Snyder, S. H. (2001) The biotin switch method for the detection of S-nitrosylated proteins Sci. STKE 2001, pl1
18. Poole, L. B., Klomsiri, C., Knaggs, S. A., Furdui, C. M., Nelson, K. J., Thomas, M. J., Fetrow, J. S., Daniel, L. W., and King, S. B. (2007) Fluorescent and affinity-based tools to detect cysteine sulfenic acid formation in proteins Bioconjugate Chem. 18, 2004-2017
19. Leonard, S. E., Reddie, K. G., and Carroll, K. S. (2009) Mining the thiol proteome for sulfenic acid modifications reveals new targets for oxidation in cells ACS Chem. Biol. 4, 783-799
20. Vila, A., Tallman, K. A., Jacobs, A. T., Liebler, D. C., Porter, N. A., and Marnett, L. J. (2008) Identification of protein targets of 4-hydroxynonenal using click chemistry for ex vivo biotinylation of azido and alkynyl derivatives Chem. Res. Toxicol. 21, 432-444
21. Martin, B. R. and Cravatt, B. F. (2009) Large-scale profiling of protein palmitoylation in mammalian cells Nat. Methods 6, 135-138
22. Hang, H. C. and Linder, M. E. (2011) Exploring protein lipidation with chemical biology Chem. Rev. 111, 6341-6358
23. Lindahl, M., Mata-Cabana, A., and Kieselbach, T. (2011) The disulfide proteome and other reactive cysteine proteomes: analysis and functional significance Antioxid. Redox Signaling 14, 2581-2642
24. Pinitglang, S., Watts, A. B., Patel, M., Reid, J. D., Noble, M. A., Gul, S., Bokth, A., Naeem, A., Patel, H., Thomas, E. W., Sreedharan, S. K., Verma, C., and Brocklehurst, K. (1997) A classical enzyme active center motif lacks catalytic competence until modulated electrostatically Biochemistry 36, 9968-9982
25. Zhang, Z. Y. and Dixon, J. E. (1993) Active site labeling of the Yersinia protein tyrosine phosphatase: the determination of the pKa of the active site cysteine and the function of the conserved histidine 402 Biochemistry 32, 9340-9345
26. Marino, S. M. and Gladyshev, V. N. (2011) Redox biology: computational approaches to the investigation of functional cysteine residues Antioxid. Redox Signaling 15, 135-146
27. Marino, S. M. and Gladyshev, V. N. (2012) Analysis and functional prediction of reactive cysteine residues J. Biol. Chem. 287, 4419-4425
28. Fomenko, D. E., Xing, W., Adair, B. M., Thomas, D. J., and Gladyshev, V. N. (2007) High-throughput identification of catalytic redox-active cysteine residues Science 315, 387-389
29. Hill, B. G., Reily, C., Oh, J. Y., Johnson, M. S., and Landar, A. (2009) Methods for the determination and quantification of the reactive thiol proteome Free Radicals Biol. Med. 47, 675-683
30. Dennehy, M. K., Richards, K. A., Wernke, G. R., Shyr, Y., and Liebler, D. C. (2006) Cytosolic and nuclear protein targets of thiol-reactive electrophiles Chem. Res. Toxicol. 19, 20-29
31. Shin, N. Y., Liu, Q., Stamer, S. L., and Liebler, D. C. (2007) Protein targets of reactive electrophiles in human liver microsomes Chem. Res. Toxicol. 20, 859-867
32. Weerapana, E., Wang, C., Simon, G. M., Richter, F., Khare, S., Dillon, M. B., Bachovchin, D. A., Mowen, K., Baker, D., and Cravatt, B. F. (2010) Quantitative reactivity profiling predicts functional cysteines in proteomes Nature 468, 790-795
33. Weerapana, E., Speers, A. E., and Cravatt, B. F. (2007) Tandem orthogonal proteolysis-activity-based protein profiling (TOP-ABPP)-a general method for mapping sites of probe modification in proteomes Nat. Protoc. 2, 1414-1425
34. Sato, Y. and Inaba, K. (2012) Disulfide bond formation network in the three biological kingdoms, bacteria, fungi and mammals FEBS J. 279, 2262-2271
35. Woycechowsky, K. J. and Raines, R. T. (2000) Native disulfide bond formation in proteins Curr. Opin. Chem. Biol. 4, 533-539
36. Fomenko, D. E., Marino, S. M., and Gladyshev, V. N. (2008) Functional diversity of cysteine residues in proteins and unique features of catalytic redox-active cysteines in thiol oxidoreductases Mol. Cells 26, 228-235
37. Chivers, P. T., Prehoda, K. E., and Raines, R. T. (1997) The CXXC motif: a rheostat in the active site Biochemistry 36, 4061-4066
38. Martin, J. L. (1995) Thioredoxin-a fold for all reasons Structure 3, 245-250
39. Luthman, M. and Holmgren, A. (1982) Rat liver thioredoxin and thioredoxin reductase: purification and characterization Biochemistry 21, 6628-6633
40. Arner, E. S. (2009) Focus on mammalian thioredoxin reductases - important selenoproteins with versatile functions Biochim. Biophys. Acta 1790, 495-526
41. Nordberg, J. and Arner, E. S. (2001) Reactive oxygen species, antioxidants, and the mammalian thioredoxin system Free Radicals Biol. Med. 31, 1287-1312
42. Holmgren, A. and Lu, J. (2010) Thioredoxin and thioredoxin reductase: current research with special reference to human disease Biochem. Biophys. Res. Commun. 396, 120-124
43. Soini, Y., Kahlos, K., Napankangas, U., Kaarteenaho-Wiik, R., Saily, M., Koistinen, P., Paaakko, P., Holmgren, A., and Kinnula, V. L. (2001) Widespread expression of thioredoxin and thioredoxin reductase in non-small cell lung carcinoma Clin. Cancer Res. 7, 1750-1757
44. Iwasawa, S., Yamano, Y., Takiguchi, Y., Tanzawa, H., Tatsumi, K., and Uzawa, K. (2011) Upregulation of thioredoxin reductase 1 in human oral squamous cell carcinoma Oncol. Rep. 25, 637-644
45. Powis, G., Mustacich, D., and Coon, A. (2000) The role of the redox protein thioredoxin in cell growth and cancer Free Radicals Biol. Med. 29, 312-322
46. Yamada, M., Tomida, A., Yoshikawa, H., Taketani, Y., and Tsuruo, T. (1996) Increased expression of thioredoxin/adult T-cell leukemia-derived factor in cisplatin-resistant human cancer cell lines Clin. Cancer Res. 2, 427-432
47. Kim, S. J., Miyoshi, Y., Taguchi, T., Tamaki, Y., Nakamura, H., Yodoi, J., Kato, K., and Noguchi, S. (2005) High thioredoxin expression is associated with resistance to docetaxel in primary breast cancer Clin. Cancer Res. 11, 8425-8430
48. Holmgren, A. (1981) Regulation of ribonucleotide reductase Curr. Top. Cell. Regul. 19, 47-76
49. Stadtman, E. R. (2004) Cyclic oxidation and reduction of methionine residues of proteins in antioxidant defense and cellular regulation Arch. Biochem. Biophys. 423, 2-5
50. Rhee, S. G., Chae, H. Z., and Kim, K. (2005) Peroxiredoxins: a historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling Free Radicals Biol. Med. 38, 1543-1552
51. Matthews, J. R., Wakasugi, N., Virelizier, J. L., Yodoi, J., and Hay, R. T. (1992) Thioredoxin regulates the DNA binding activity of NF-kappa B by reduction of a disulphide bond involving cysteine 62 Nucleic Acids Res. 20, 3821-3830
52. Saitoh, M., Nishitoh, H., Fujii, M., Takeda, K., Tobiume, K., Sawada, Y., Kawabata, M., Miyazono, K., and Ichijo, H. (1998) Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1 EMBO J. 17, 2596-2606
53. Liu, Y. and Min, W. (2002) Thioredoxin promotes ASK1 ubiquitination and degradation to inhibit ASK1-mediated apoptosis in a redox activity-independent manner Circ. Res. 90, 1259-1266
54. Nadeau, P. J., Charette, S. J., and Landry, J. (2009) REDOX reaction at ASK1-Cys250 is essential for activation of JNK and induction of apoptosis Mol. Biol. Cell 20, 3628-3637
55. Nadeau, P. J., Charette, S. J., Toledano, M. B., and Landry, J. (2007) Disulfide Bond-mediated multimerization of Ask1 and its reduction by thioredoxin-1 regulate H(2)O(2)-induced c-Jun NH(2)-terminal kinase activation and apoptosis Mol. Biol. Cell 18, 3903-3913
56. Mitchell, D. A., Morton, S. U., Fernhoff, N. B., and Marletta, M. A. (2007) Thioredoxin is required for S-nitrosation of procaspase-3 and the inhibition of apoptosis in Jurkat cells Proc. Natl. Acad. Sci. U.S.A. 104, 11609-11614
57. Kim, J. E. and Tannenbaum, S. R. (2004) S-Nitrosation regulates the activation of endogenous procaspase-9 in HT-29 human colon carcinoma cells J. Biol. Chem. 279, 9758-9764
58. Tonissen, K. F. and Di Trapani, G. (2009) Thioredoxin system inhibitors as mediators of apoptosis for cancer therapy Mol. Nutr. Food Res. 53, 87-103
59. Kirkpatrick, D. L., Kuperus, M., Dowdeswell, M., Potier, N., Donald, L. J., Kunkel, M., Berggren, M., Angulo, M., and Powis, G. (1998) Mechanisms of inhibition of the thioredoxin growth factor system by antitumor 2-imidazolyl disulfides Biochem. Pharmacol. 55, 987-994
60. Baker, A. F., Dragovich, T., Tate, W. R., Ramanathan, R. K., Roe, D., Hsu, C. H., Kirkpatrick, D. L., and Powis, G. (2006) The antitumor thioredoxin-1 inhibitor PX-12 (1-methylpropyl 2-imidazolyl disulfide) decreases thioredoxin-1 and VEGF levels in cancer patient plasma J. Lab. Clin. Med. 147, 83-90
61. Ramanathan, R. K., Kirkpatrick, D. L., Belani, C. P., Friedland, D., Green, S. B., Chow, H. H., Cordova, C. A., Stratton, S. P., Sharlow, E. R., Baker, A., and Dragovich, T. (2007) A Phase I pharmacokinetic and pharmacodynamic study of PX-12, a novel inhibitor of thioredoxin-1, in patients with advanced solid tumors Clin. Cancer Res. 13, 2109-2114
62. Welsh, S. J., Williams, R. R., Birmingham, A., Newman, D. J., Kirkpatrick, D. L., and Powis, G. (2003) The thioredoxin redox inhibitors 1-methylpropyl 2-imidazolyl disulfide and pleurotin inhibit hypoxia-induced factor 1alpha and vascular endothelial growth factor formation Mol. Cancer Ther. 2, 235-243
63. Chapman, H. A., Riese, R. J., and Shi, G. P. (1997) Emerging roles for cysteine proteases in human biology Annu. Rev. Physiol. 59, 63-88
64. Amerik, A. Y. and Hochstrasser, M. (2004) Mechanism and function of deubiquitinating enzymes Biochim. Biophys. Acta 1695, 189-207
65. Tonks, N. K. (2006) Protein tyrosine phosphatases: from genes, to function, to disease Nat. Rev. Mol. Cell. Biol. 7, 833-846
66. Sirover, M. A. (1997) Role of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in normal cell function and in cell pathology J. Cell. Biochem. 66, 133-140
67. Jones, J. E., Causey, C. P., Knuckley, B., Slack-Noyes, J. L., and Thompson, P. R. (2009) Protein arginine deiminase 4 (PAD4): Current understanding and future therapeutic potential Curr. Opin. Drug Discovery Dev. 12, 616-627
68. Denault, J.-B. and Salvesen, G. S. (2002) Caspases: Keys in the Ignition of Cell Death Chem. Rev. 102, 4489-4499
69. Kerr, J. F., Wyllie, A. H., and Currie, A. R. (1972) Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics Br. J. Cancer 26, 239-257
70. Hanahan, D. and Weinberg, R. A. (2000) The hallmarks of cancer Cell Cycle 100, 57-70
71. Fischer, U., Janssen, K., and Schulze-Osthoff, K. (2007) Does caspase inhibition promote clonogenic tumor growth? Cell Cycle 6, 3048-3053
72. Ghavami, S., Hashemi, M., Ange, S. R., Yeganeh, B., Xiao, W., Eshraghi, M., Bus, C. J., Kadkhoda, K., Wiechec, E., Halayko, A. J., and Los, M. (2009) Apoptosis and cancer: mutations within caspase genes J. Med. Genet. 46, 497-510
73. Olsson, M. and Zhivotovsky, B. (2011) Caspases and cancer Cell Death Differ. 18, 1441-1449
74. Boatright, K. M., Renatus, M., Scott, F. L., Sperandio, S., Shin, H., Pederson, I. M., Ricci, J.-E., Edris, W. A., Sutherlin, D. P., Green, D. R., and Salvesen, G. S. (2003) A unified model for apical caspase activation Mol. Cell 11, 529-541
75. Woo, E. J., Kim, Y. G., Kim, M. S., Han, W. D., Shin, S., Robinson, H., Park, S. Y., and Oh, B. H. (2004) Structural mechanism for inactivation and activation of CAD/DFF40 in the apoptotic pathway Mol. Cell 14, 531-539
76. Fulda, S. and Vucic, D. (2012) Targeting IAP proteins for therapeutic intervention in cancer Nat. Rev. Drug Discovery 11, 109-124
77. Ahmed, K., Zhao, Q. L., Matsuya, Y., Yu, D. Y., Feril, L. B., Jr., Nemoto, H., and Kondo, T. (2007) Rapid and transient intracellular oxidative stress due to novel macrosphelides trigger apoptosis via Fas/caspase-8-dependent pathway in human lymphoma U937 cells Chem.-Biol. Interact. 170, 86-99
78. Smith, G., Nguyen, Q. D., and Aboagye, E. O. (2009) Translational imaging of apoptosis Anticancer Agents Med. Chem. 9, 958-967
79. Edgington, L. E., Berger, A. B., Blum, G., Albrow, V. E., Paulick, M. G., Lineberry, N., and Bogyo, M. (2009) Noninvasive optical imaging of apoptosis by caspase-targeted activity-based probes Nat. Med. 15, 967-973
80. Zhou, D., Chu, W., Rothfuss, J., Zeng, C., Xu, J., Jones, L., Welch, M. J., and Mach, R. H. (2006) Synthesis, radiolabeling, and in vivo evaluation of an 18F-labeled isatin analog for imaging caspase-3 activation in apoptosis Bioorg. Med. Chem. Lett. 16, 5041-5046
81. Bedner, E., Smolewski, P., Amstad, P., and Darzynkiewicz, Z. (2000) Activation of caspases measured in situ by binding of fluorochrome-labeled inhibitors of caspases (FLICA): correlation with DNA fragmentation Exp. Cell Res. 259, 308-313
82. Nalepa, G., Rolfe, M., and Harper, J. W. (2006) Durg discovery in the ubiquitin-proteasome system Nat. Rev. Drug Discovery 5, 596-613
83. Vucic, D., Dixit, V. M., and Wertz, I. E. (2011) Ubiquitylation in apoptosis: a post-translational modification at the edge of life and death Nat. Rev. Mol. Cell Biol. 12, 439-452
84. Pickart, C. M. (2001) Mechanism underlying ubiquitination Annu. Rev. Biochem. 70, 503-533
85. Haas, A. L. and Rose, I. A. (1982) The mechanism of ubiquitin activating enzyme J. Biol. Chem. 257, 10329-10337
86. Tong, H., Hateboer, G., Perrakis, A., Bernards, R., and Sixma, T. K. (1997) Crystal structure of murine/human Ubc9 provides insight into the variability of the ubiquitin-conjugating System J. Biol. Chem. 272, 21381-21387
87. Reyes-Turcu, F. E., Ventii, K. H., and Wilkinson, K. D. (2009) Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes Annu. Rev. Biochem. 78, 363-397
88. Santarius, T., Shipley, J., Brewer, D., Stratton, M. R., and Cooper, C. S. (2010) A census of amplified and overexpressed human cancer genes Nat. Rev. Cancer 10, 59-64
89. Bedford, L., Lowe, J., Dick, L. R., Mayer, R. J., and Brownell, J. E. (2011) Ubiquitin-like protein conjugation and the ubiquitin-proteasome system as drug targets Nat. Rev. Drug Discovery 10, 29-46
90. Frezza, M., Schmitt, S., and Dou, Q. P. (2011) Targeting the ubiquitin-proteasome pathway: an emerging concept in cancer therapy Curr. Top. Med. Chem. 11, 2888-2905
91. Edelmann, M. J., Nicholson, B., and Kessler, B. M. (2011) Pharmacological targets in the ubiquitin system offer new ways of treating cancer, neurodegenerative disorders and infectious diseases Expert. Rev. Mol. Med. 13, e35
92. Yang, Y., Kitagaki, J., Dai, R. M., Tsai, Y. C., Lorick, K. L., Ludwig, R. L., Pierre, S. A., Jensen, J. P., Davydov, I. V., Oberoi, P., Li, C. C., Kenten, J. H., Beutler, J. A., Vousden, K. H., and Weissman, A. M. (2007) Inhibitors of ubiquitin-activating enzyme (E1), a new class of potential cancer therapeutics Cancer Res. 67, 9472-9481
93. Xu, G. W., Ali, M., Wood, T. E., Wong, D., Maclean, N., Wang, X., Gronda, M., Skrtic, M., Li, X., Hurren, R., Mao, X., Venkatesan, M., Beheshti Zavareh, R., Ketela, T., Reed, J. C., Rose, D., Moffat, J., Batey, R. A., Dhe-Paganon, S., and Schimmer, A. D. (2010) The ubiquitin-activating enzyme E1 as a therapeutic target for the treatment of leukemia and multiple myeloma Blood 115, 2251-2259
94. Tainer, J. A., Roberts, V. A., and Getzoff, E. D. (1991) Metal-binding sites in proteins Curr. Opin. Biotechnol. 2, 582-591
95. Giles, N. M., Watts, A. B., Giles, G. I., Fry, F. H., Littlechild, J. A., and Jacob, C. (2003) Metal and redox modulation of cysteine protein function Chem. Biol. 10, 677-693
96. Lill, R. (2009) Function and biogenesis of iron-sulphur proteins Nature 460, 831-838
97. Ye, H. and Rouault, T. A. (2010) Human iron-sulfur cluster assembly, cellular iron homeostasis, and disease Biochemistry 49, 4945-4956
98. Gari, K., Leon Ortiz, A. M., Borel, V., Flynn, H., Skehel, J. M., and Boulton, S. J. (2012) MMS19 links cytoplasmic iron-sulfur cluster assembly to DNA metabolism Science 337, 243-245
99. Stehling, O., Vashisht, A. A., Mascarenhas, J., Jonsson, Z. O., Sharma, T., Netz, D. J., Pierik, A. J., Wohlschlegel, J. A., and Lill, R. (2012) MMS19 assembles iron-sulfur proteins required for DNA metabolism and genomic integrity Science 337, 195-199
100. Rouault, T. A. (2012) Biogenesis of iron-sulfur clusters in mammalian cells: new insights and relevance to human disease Dis Model Mech 5, 155-164
101. Barf, T. and Kaptein, A. (2012) Irreversible protein kinase inhibitors: balancing the benefits and risks J. Med. Chem. 55, 6243-6262
102. Zhang, J., Yang, P. L., and Gray, N. S. (2009) Targeting cancer with small molecule kinase inhibitors Nat. Rev. Cancer 9, 28-39
103. Schirmer, A., Kennedy, J., Murli, S., Reid, R., and Santi, D. V. (2006) Targeted covalent inactivation of protein kinases by resorcylic acid lactone polyketides Proc. Natl. Acad. Sci. U.S.A. 103, 4234-4239
104. Cohen, M. S., Zhang, C., Shokat, K. M., and Taunton, J. (2005) Structural bioinformatics-based design of selective, irreversible kinase inhibitors Science 308, 1318-1321
105. Leproult, E., Barluenga, S., Moras, D., Wurtz, J. M., and Winssinger, N. (2011) Cysteine mapping in conformationally distinct kinase nucleotide binding sites: application to the design of selective covalent inhibitors J. Med. Chem. 54, 1347-1355
106. Seshacharyulu, P., Ponnusamy, M. P., Haridas, D., Jain, M., Ganti, A. K., and Batra, S. K. (2012) Targeting the EGFR signaling pathway in cancer therapy Expert Opin Ther Targets 16, 15-31
107. Han, W. and Lo, H. W. (2012) Landscape of EGFR signaling network in human cancers: biology and therapeutic response in relation to receptor subcellular locations Cancer Lett 318, 124-134
108. Paulsen, C. E., Truong, T. H., Garcia, F. J., Homann, A., Gupta, V., Leonard, S. E., and Carroll, K. S. (2012) Peroxide-dependent sulfenylation of the EGFR catalytic site enhances kinase activity Nat. Chem. Biol. 8, 57-64
109. Singh, J., Petter, R. C., and Kluge, A. F. (2010) Targeted covalent drugs of the kinase family Curr. Opin. Chem. Biol. 14, 475-480
110. Carmi, C., Lodola, A., Rivara, S., Vacondio, F., Cavazzoni, A., Alfieri, R. R., Ardizzoni, A., Petronini, P. G., and Mor, M. (2011) Epidermal growth factor receptor irreversible inhibitors: chemical exploration of the cysteine-trap portion Mini-Rev. Med. Chem. 11, 1019-1030
111. Serafimova, I. M., Pufall, M. A., Krishnan, S., Duda, K., Cohen, M. S., Maglathlin, R. L., McFarland, J. M., Miller, R. M., Frodin, M., and Taunton, J. (2012) Reversible targeting of noncatalytic cysteines with chemically tuned electrophiles Nat. Chem. Biol. 8, 471-476
112. Kwak, E. L., Sordella, R., Bell, D. W., Godin-Heymann, N., Okimoto, R. A., Brannigan, B. W., Harris, P. L., Driscoll, D. R., Fidias, P., Lynch, T. J., Rabindran, S. K., McGinnis, J. P., Wissner, A., Sharma, S. V., Isselbacher, K. J., Settleman, J., and Haber, D. A. (2005) Irreversible inhibitors of the EGF receptor may circumvent acquired resistance to gefitinib Proc. Natl. Acad. Sci. U.S.A. 102, 7665-7670
113. Aslund, F., Zheng, M., Beckwith, J., and Storz, G. (1999) Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status Proc. Natl. Acad. Sci. U.S.A. 96, 6161-6165
114. Matthews, J. R., Botting, C. H., Panico, M., Morris, H. R., and Hay, R. T. (1996) Inhibition of NF-kappaB DNA binding by nitric oxide Nucleic Acids Res. 24, 2236-2242
115. Klatt, P., Molina, E. P., De Lacoba, M. G., Padilla, C. A., Martinez-Galesteo, E., Barcena, J. A., and Lamas, S. (1999) Redox regulation of c-Jun DNA binding by reversible S-glutathiolation FASEB J. 13, 1481-1490
116. Lambert, J. M., Gorzov, P., Veprintsev, D. B., Soderqvist, M., Segerback, D., Bergman, J., Fersht, A. R., Hainaut, P., Wiman, K. G., and Bykov, V. J. (2009) PRIMA-1 reactivates mutant p53 by covalent binding to the core domain Cancer Cell 15, 376-388
117. Kobayashi, M. and Yamamoto, M. (2005) Molecular mechanisms activating the Nrf2-Keap1 pathway of antioxidant gene regulation Antioxid. Redox Signaling 7, 385-394
118. Na, H. K. and Surh, Y. J. (2006) Transcriptional regulation via cysteine thiol modification: a novel molecular strategy for chemoprevention and cytoprotection Mol. Carcinog. 45, 368-380
119. Brigelius-Flohe, R. and Flohe, L. (2011) Basic principles and emerging concepts in the redox control of transcription factors Antioxid. Redox Signaling 15, 2335-2381
120. Lau, A., Villeneuve, N. F., Sun, Z., Wong, P. K., and Zhang, D. D. (2008) Dual roles of Nrf2 in cancer Pharmacol. Res. 58, 262-270
121. Holland, R. and Fishbein, J. C. (2010) Chemistry of the cysteine sensors in Kelch-like ECH-associated protein 1 Antioxid. Redox Signaling 13, 1749-1761
122. Taguchi, K., Motohashi, H., and Yamamoto, M. (2011) Molecular mechanisms of the Keap1-Nrf2 pathway in stress response and cancer evolution Genes Cells 16, 123-140
123. Kundu, J. K. and Surh, Y. J. (2010) Nrf2-Keap1 signaling as a potential target for chemoprevention of inflammation-associated carcinogenesis Pharm. Res. 27, 999-1013
124. Hur, W. and Gray, N. S. (2011) Small molecule modulators of antioxidant response pathway Curr. Opin. Chem. Biol. 15, 162-173
125. Ahn, Y. H., Hwang, Y., Liu, H., Wang, X. J., Zhang, Y., Stephenson, K. K., Boronina, T. N., Cole, R. N., Dinkova-Kostova, A. T., Talalay, P., and Cole, P. A. (2010) Electrophilic tuning of the chemoprotective natural product sulforaphane Proc. Natl. Acad. Sci. U.S.A. 107, 9590-9595
126. Hur, W., Sun, Z., Jiang, T., Mason, D. E., Peters, E. C., Zhang, D. D., Luesch, H., Schultz, P. G., and Gray, N. S. (2010) A small-molecule inducer of the antioxidant response element Chem. Biol. 17, 537-547
127. Anastasiou, D., Poulogiannis, G., Asara, J. M., Boxer, M. B., Jiang, J. K., Shen, M., Bellinger, G., Sasaki, A. T., Locasale, J. W., Auld, D. S., Thomas, C. J., Vander Heiden, M. G., and Cantley, L. C. (2011) Inhibition of pyruvate kinase M2 by reactive oxygen species contributes to cellular antioxidant responses Science 334, 1278-1283
128. Wellen, K. E. and Thompson, C. B. (2010) Cellular metabolic stress: considering how cells respond to nutrient excess Mol. Cell 40, 323-332
129. Filosa, S., Fico, A., Paglialunga, F., Balestrieri, M., Crooke, A., Verde, P., Abrescia, P., Bautista, J. M., and Martini, G. (2003) Failure to increase glucose consumption through the pentose-phosphate pathway results in the death of glucose-6-phosphate dehydrogenase gene-deleted mouse embryonic stem cells subjected to oxidative stress Biochem. J. 370, 935-943
130. Christofk, H. R., Vander Heiden, M. G., Harris, M. H., Ramanathan, A., Gerszten, R. E., Wei, R., Fleming, M. D., Schreiber, S. L., and Cantley, L. C. (2008) The M2 splice isoform of pyruvate kinase is important for cancer metabolism and tumour growth Nature 452, 230-233
131. Christofk, H. R., Vander Heiden, M. G., Wu, N., Asara, J. M., and Cantley, L. C. (2008) Pyruvate kinase M2 is a phosphotyrosine-binding protein Nature 452, 181-186
132. Singh, J., Petter, R. C., Baillie, T. A., and Whitty, A. (2011) The resurgence of covalent drugs Nat. Rev. Drug Discovery 10, 307-317
133. Johnson, D. S., Weerapana, E., and Cravatt, B. F. (2010) Strategies for discovering and derisking covalent, irreversible enzyme inhibitors Future Med. Chem. 2, 949-964
134. Marino, S. M. and Gladyshev, V. N. (2011) Proteomics: mapping reactive cysteines Nat. Chem. Biol. 7, 72-73