Covalent Modifiers: A Chemical Perspective on the Reactivity of α,β-Unsaturated Carbonyls with Thiols via Hetero-Michael Addition Reactions

Hard and Soft Acids and Bases

Pearson, R. G. (1963) · Journal of the American Chemical Society · doi:10.1021/ja00905a001 · Cited by 10,475

Absolute hardness: companion parameter to absolute electronegativity

Parr, R. G., & Pearson, R. G. (1983) · Journal of the American Chemical Society · doi:10.1021/ja00364a005 · Cited by 7,998

Electrophilicity Index

Parr, R. G., von Szentpály, L., & Liu, S. (1999) · Journal of the American Chemical Society · doi:10.1021/ja983494x · Cited by 7,564

New Substructure Filters for Removal of Pan Assay Interference Compounds (PAINS) from Screening Libraries and for Their Exclusion in Bioassays

Baell, J. B., & Holloway, G. A. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm901137j · Cited by 4,196

Therapeutic potential of resveratrol: the in vivo evidence

Baur, J. A., & Sinclair, D. A. (2006) · Nature Reviews Drug Discovery · doi:10.1038/nrd2060 · Cited by 3,958

Density functional approach to the frontier-electron theory of chemical reactivity

Parr, R. G., & Yang, W. (1984) · Journal of the American Chemical Society · doi:10.1021/ja00326a036 · Cited by 3,672

Hard and soft acids and bases, HSAB, part 1: Fundamental principles

Pearson, R. G. (1968) · Journal of Chemical Education · doi:10.1021/ed045p581 · Cited by 2,566

AZD9291, an Irreversible EGFR TKI, Overcomes T790M-Mediated Resistance to EGFR Inhibitors in Lung Cancer

Cross, D. A. E., Ashton, S. E., Ghiorghiu, S., Eberlein, C., Nebhan, C. A., Spitzler, P. J., Orme, J. P., Finlay, M. R. V., Ward, R. A., Mellor, M. J., et al. (2014) · Cancer Discovery · doi:10.1158/2159-8290.cd-14-0337 · Cited by 2,246

The resurgence of covalent drugs

Singh, J., Petter, R. C., Baillie, T. A., & Whitty, A. (2011) · Nature Reviews Drug Discovery · doi:10.1038/nrd3410 · Cited by 1,873

Prodrugs: design and clinical applications

Rautio, J., Kumpulainen, H., Heimbach, T., Oliyai, R., Oh, D.-M., Järvinen, T., & Savolainen, J. (2008) · Nature Reviews Drug Discovery · doi:10.1038/nrd2468 · Cited by 1,681

Acquired EGFR C797S mutation mediates resistance to AZD9291 in non–small cell lung cancer harboring EGFR T790M

Thress, K. S., Paweletz, C. P., Felip, E., Cho, B. C., Stetson, D., Dougherty, B., Lai, Z., Markovets, A., Vivancos, A., Kuang, Y., et al. (2015) · Nature Medicine · doi:10.1038/nm.3854 · Cited by 1,589

Esters of Methanesulfonic Acid as Irreversible Inhibitors of Acetylcholinesterase

Kitz, R. J., & Wilson, I. B. (1962) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)50153-8 · Cited by 1,520

Resistance Mechanisms for the Bruton's Tyrosine Kinase Inhibitor Ibrutinib

Woyach, J. A., Furman, R. R., Liu, T.-M., Ozer, H. G., Zapatka, M., Ruppert, A. S., Xue, L., Li, D. H.-H., Steggerda, S. M., Versele, M., et al. (2014) · New England Journal of Medicine · doi:10.1056/nejmoa1400029 · Cited by 1,275

Activity-Based Protein Profiling: From Enzyme Chemistry to Proteomic Chemistry

Cravatt, B. F., Wright, A. T., & Kozarich, J. W. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.101304.124125 · Cited by 1,270

Structural Determinants of Phosphoinositide 3-Kinase Inhibition by Wortmannin, LY294002, Quercetin, Myricetin, and Staurosporine

Walker, E. H., Pacold, M. E., Perišić, O., Stephens, L., Hawkins, P. T., Wymann, M. P., & Williams, R. L. (2000) · Molecular Cell · doi:10.1016/s1097-2765(05)00089-4 · Cited by 1,211

Hard and soft acids and bases, HSAB, part II: Underlying theories

Pearson, R. G. (1968) · Journal of Chemical Education · doi:10.1021/ed045p643 · Cited by 1,081

Chemistry: Chemical con artists foil drug discovery

Baell, J. B., & Walters, M. A. (2014) · Nature · doi:10.1038/513481a · Cited by 1,048

Leptomycin B inactivates CRM1/exportin 1 by covalent modification at a cysteine residue in the central conserved region

Kudo, N. R., Matsumori, N., Taoka, H., Fujiwara, D., Schreiner, E. P., Wolff, B., Yoshida, M., & Horinouchi, S. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.16.9112 · Cited by 1,033

Irreversible inhibitors of the EGF receptor may circumvent acquired resistance to gefitinib

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. M., Lynch, T. J., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0502860102 · Cited by 966

Afatinib versus placebo for patients with advanced, metastatic non-small-cell lung cancer after failure of erlotinib, gefitinib, or both, and one or two lines of chemotherapy (LUX-Lung 1): a phase 2b/3 randomised trial

Miller, V. A., Hirsh, V., Cadranel, J., Chen, Y.-M., Park, K., Kim, S.-W., Zhou, C., Su, W.-C., Wang, M., Sun, Y., et al. (2012) · The Lancet Oncology · doi:10.1016/s1470-2045(12)70087-6 · Cited by 961

Target Binding Properties and Cellular Activity of Afatinib (BIBW 2992), an Irreversible ErbB Family Blocker

Solca, F., Dahl, G., Zoephel, A., Bader, G., Sanderson, M., Klein, C., Kraemer, O., Himmelsbach, F., Haaksma, E., & Adolf, G. R. (2012) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.112.197756 · Cited by 865

Targeting transcription regulation in cancer with a covalent CDK7 inhibitor

Kwiatkowski, N. P., Zhang, T., Rahl, P. B., Abraham, B. J., Reddy, J., Ficarro, S. B., Dastur, A., Amzallag, A., Ramaswamy, S., Tesar, B. M., et al. (2014) · Nature · doi:10.1038/nature13393 · Cited by 865

Leptomycin B Inhibition of Signal-Mediated Nuclear Export by Direct Binding to CRM1

Kudo, N. R., Wolff, B., Sekimoto, T., Schreiner, E. P., Yoneda, Y., Yanagida, M., Horinouchi, S., & Yoshida, M. (1998) · Experimental Cell Research · doi:10.1006/excr.1998.4136 · Cited by 812

Aldehyde Sources, Metabolism, Molecular Toxicity Mechanisms, and Possible Effects on Human Health

O'Brien, P. J., Siraki, A. G., & Shangari, N. (2005) · Critical Reviews in Toxicology · doi:10.1080/10408440591002183 · Cited by 738

Discovery of Selective Irreversible Inhibitors for Bruton’s Tyrosine Kinase

Pan, Z., Scheerens, H., Li, S., Schultz, B. E., Sprengeler, P. A., Burrill, L. C., Mendonca, R. V., Sweeney, M. D., Scott, K. C. K., Grothaus, P. G., et al. (2006) · ChemMedChem · doi:10.1002/cmdc.200600221 · Cited by 690

Wortmannin Inactivates Phosphoinositide 3-Kinase by Covalent Modification of Lys-802, a Residue Involved in the Phosphate Transfer Reaction

Wymann, M. P., Bulgarelli-Leva, G., Zvelebil, M., Pirola, L., Vanhaesebroeck, B., Waterfield, M. D., & Panayotou, G. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.4.1722 · Cited by 679

Developing Irreversible Inhibitors of the Protein Kinase Cysteinome

Liu, Q., Sabnis, Y. A., Zhao, Z., Zhang, T., Buhrlage, S. J., Jones, L. H., & Gray, N. S. (2013) · Chemistry & Biology · doi:10.1016/j.chembiol.2012.12.006 · Cited by 670

Rociletinib in EGFR-Mutated Non–Small-Cell Lung Cancer

Sequist, L. V., Soria, J.-C., Goldman, J. W., Wakelee, H. A., Gadgeel, S. M., Varga, A., Papadimitrakopoulou, V., Solomon, B. J., Oxnard, G. R., Dziadziuszko, R., et al. (2015) · New England Journal of Medicine · doi:10.1056/nejmoa1413654 · Cited by 665

The Antioxidant Defense System Keap1-Nrf2 Comprises a Multiple Sensing Mechanism for Responding to a Wide Range of Chemical Compounds

Kobayashi, M., Li, L., Iwamoto, N., Nakajima‐Takagi, Y., Kaneko, H., Nakayama, Y., Eguchi, M., Wada, Y., Kumagai, Y., & Yamamoto, M. P. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01080-08 · Cited by 641

Discovery of a Mutant-Selective Covalent Inhibitor of EGFR that Overcomes T790M-Mediated Resistance in NSCLC

Walter, A. O., Sjin, R. T. T., Haringsma, H. J., Ohashi, K., Sun, J., Lee, K., Dubrovskiy, A., Labenski, M., Zhu, Z., Wang, Z., et al. (2013) · Cancer Discovery · doi:10.1158/2159-8290.cd-13-0314 · Cited by 620

What made sesquiterpene lactones reach cancer clinical trials?

Ghantous, A., Gali‐Muhtasib, H. U., Vuorela, H. J., Saliba, N. A., & Darwiche, N. (2010) · Drug Discovery Today · doi:10.1016/j.drudis.2010.06.002 · Cited by 618

Potency of Michael reaction acceptors as inducers of enzymes that protect against carcinogenesis depends on their reactivity with sulfhydryl groups

Dinkova‐Kostova, A. T., Massiah, M. A., Bozak, R. E., Hicks, R. J., & Talalay, P. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.051632198 · Cited by 594

Mechanism-Based Profiling of Enzyme Families

Evans, M. J., & Cravatt, B. F. (2006) · Chemical Reviews · doi:10.1021/cr050288g · Cited by 574

Cyclopentenone prostaglandins: New insights on biological activities and cellular targets

Straus, D. S., & Glass, C. K. (2001) · Medicinal Research Reviews · doi:10.1002/med.1006 · Cited by 569

Diterpenoids from Isodon species and their biological activities

Sun, H., Huang, S., & Han, Q. (2006) · Natural Product Reports · doi:10.1039/b604174d · Cited by 552

Progress in the chemistry of organic natural products

Habermehl, G. (1983) · Toxicon · doi:10.1016/0041-0101(83)90119-8 · Cited by 541

Covalent inhibitors in drug discovery: from accidental discoveries to avoided liabilities and designed therapies

Bauer, R. A. (2015) · Drug Discovery Today · doi:10.1016/j.drudis.2015.05.005 · Cited by 534

Thioredoxin Reductase Is Irreversibly Modified by Curcumin

Fang, J., Lu, J., & Holmgren, A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414645200 · Cited by 521

Cyclopentenone prostaglandins: New insights on biological activities and cellular targets

Straus, D. S., & Glass, C. K. (2001) · Medicinal Research Reviews · doi:10.1002/med.1006.abs · Cited by 518

Protective and toxic roles of dopamine in Parkinson's disease

Segura‐Aguilar, J., Paris, I. B., Muñoz, P., Ferrari, E., Zecca, L., & Zucca, F. A. (2014) · Journal of Neurochemistry · doi:10.1111/jnc.12686 · Cited by 517

The anti-inflammatory natural product parthenolide from the medicinal herb Feverfew directly binds to and inhibits IκB kinase

Kwok, B. H. B., Koh, B. D., Ndubuisi, M. I., Elofsson, M., & Crews, C. M. (2001) · Chemistry & Biology · doi:10.1016/s1074-5521(01)00049-7 · Cited by 516

Reversible targeting of noncatalytic cysteines with chemically tuned electrophiles

Serafimova, I. M., Pufall, M. A., Krishnan, S., Duda, K., Cohen, M. S., Maglathlin, R. L., McFarland, J. M., Miller, R. M., Frödin, M., & Taunton, J. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.925 · Cited by 505

Molecular Mechanisms of Aldehyde Toxicity: A Chemical Perspective

LoPachin, R. M., & Gavin, T. (2014) · Chemical Research in Toxicology · doi:10.1021/tx5001046 · Cited by 499

The Renaissance of α‐Methylene‐γ‐butyrolactones: New Synthetic Approaches

Kitson, R. R. A., Millemaggi, A., & Taylor, R. J. K. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200903108 · Cited by 459

Strategies for Discovering and Derisking Covalent, Irreversible Enzyme Inhibitors

Johnson, D. S., Weerapana, E., & Cravatt, B. F. (2010) · Future Medicinal Chemistry · doi:10.4155/fmc.10.21 · Cited by 387

Long-Term Clinical Effects of Epalrestat, an Aldose Reductase Inhibitor, on Diabetic Peripheral Neuropathy

Hotta, N., Akanuma, Y., Kawamori, R., Matsuoka, K., Oka, Y., Shichiri, M., Toyota, T., Nakashima, M., Yoshimura, I., Sakamoto, N., et al. (2006) · Diabetes Care · doi:10.2337/dc05-2370 · Cited by 367

Discovery of Potent and Selective Covalent Inhibitors of JNK

Zhang, T., Iñesta-Vaquera, F., Niepel, M., Zhang, J., Ficarro, S. B., Machleidt, T., Xie, T., Marto, J. A., Kim, N., Sim, T., et al. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2011.11.010 · Cited by 361

Covalent Modifiers: An Orthogonal Approach to Drug Design

Potashman, M. H., & Duggan, M. E. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm8008597 · Cited by 348

Direct evidence that oncogenic tyrosine kinases and cyclic AMP-dependent protein kinase have homologous ATP-binding sites

Kamps, M. P., Taylor, S. S., & Sefton, B. M. (1984) · Nature · doi:10.1038/310589a0 · Cited by 345

Biological interactions of α,β-unsaturated aldehydes

Witz, G. (1989) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(89)90137-8 · Cited by 337

Chemical and Computational Methods for the Characterization of Covalent Reactive Groups for the Prospective Design of Irreversible Inhibitors

Flanagan, M. E., Abramite, J. A., Anderson, D. P., AULABAUGH, A. E., Dahal, U. P., Gilbert, A. M., Li, C., Montgomery, J. I., Oppenheimer, S. R., Ryder, T. F., et al. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm501412a · Cited by 337

Irreversible Protein Kinase Inhibitors: Balancing the Benefits and Risks

Barf, T., & Kaptein, A. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm3003203 · Cited by 331

Structure-assisted design of mechanism-based irreversible inhibitors of human rhinovirus 3C protease with potent antiviral activity against multiple rhinovirus serotypes

Matthews, D. A., Dragovich, P. S., Webber, S. E., Fuhrman, S. A., Patick, A. K., Zalman, L. S., Hendrickson, T. F., Love, R. A., Prins, T. J., Marakovits, J. T., et al. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.20.11000 · Cited by 319

Benchmarking Quantum Chemical Methods for the Calculation of Molecular Dipole Moments and Polarizabilities

Hickey, A. L., & Rowley, C. N. (2014) · The Journal of Physical Chemistry A · doi:10.1021/jp502475e · Cited by 319

Epalrestat: An Aldose Reductase Inhibitor for the Treatment of Diabetic Neuropathy

Ramirez, M. A., & Borja‐Hart, N. (2008) · Pharmacotherapy The Journal of Human Pharmacology and Drug Therapy · doi:10.1592/phco.28.5.646 · Cited by 308

The Proto-oncometabolite Fumarate Binds Glutathione to Amplify ROS-Dependent Signaling

Sullivan, L. B., Martinez-Garcia, E., Nguyen, H., Mullen, A. R., Dufour, E., Sudarshan, S., Licht, J. D., Deberardinis, R. J., & Chandel, N. S. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.05.003 · Cited by 304

Reactions of Alpha Methylene Lactone Tumor Inhibitors with Model Biological Nucleophiles

Kupchan, S. M., Fessler, D. C., Eakin, M. A., & Giacobbe, T. J. (1970) · Science · doi:10.1126/science.168.3929.376 · Cited by 301

Privileged Scaffolds or Promiscuous Binders: A Comparative Study on Rhodanines and Related Heterocycles in Medicinal Chemistry

Mendgen, T., Steuer, C., & Klein, C. D. P. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm201243p · Cited by 292

Activity-based protein profiling for the functional annotation of enzymes

Barglow, K. T., & Cravatt, B. F. (2007) · Nature Methods · doi:10.1038/nmeth1092 · Cited by 281

Rhodanine as a Privileged Scaffold in Drug Discovery

Tomašič, T., & Masic, L. (2009) · Current Medicinal Chemistry · doi:10.2174/092986709788186200 · Cited by 277

Local softness and chemical reactivity in the molecules CO, SCN− and H2CO

Lee, C., Yang, W., & Parr, R. G. (1988) · Journal of Molecular Structure THEOCHEM · doi:10.1016/0166-1280(88)80397-x · Cited by 276

Design of Reversible, Cysteine-Targeted Michael Acceptors Guided by Kinetic and Computational Analysis

Krishnan, S., Miller, R. M., Tian, B., Mullins, R. D., Jacobson, M. P., & Taunton, J. (2014) · Journal of the American Chemical Society · doi:10.1021/ja505194w · Cited by 270

Synthesis and Structure−Activity Relationships of 6,7-Disubstituted 4-Anilinoquinoline-3-carbonitriles. The Design of an Orally Active, Irreversible Inhibitor of the Tyrosine Kinase Activity of the Epidermal Growth Factor Receptor (EGFR) and the Human Epidermal Growth Factor Receptor-2 (HER-2)

Wissner, A., Overbeek, E., Reich, M. F., Floyd, M. B., Johnson, B. D., Mamuya, N. N., Rosfjord, E. C., Discafani, C. M., Davis, R. E., Shi, X., et al. (2002) · Journal of Medicinal Chemistry · doi:10.1021/jm020241c · Cited by 270

6-Substituted-4-(3-bromophenylamino)quinazolines as Putative Irreversible Inhibitors of the Epidermal Growth Factor Receptor (EGFR) and Human Epidermal Growth Factor Receptor (HER-2) Tyrosine Kinases with Enhanced Antitumor Activity

Tsou, H., Mamuya, N. N., Johnson, B. D., Reich, M. F., Gruber, B. C., Ye, F., Nilakantan, R., Shen, R., Discafani, C. M., DeBlanc, R., et al. (2001) · Journal of Medicinal Chemistry · doi:10.1021/jm0005555 · Cited by 269

Reaction of Glutathione with Conjugated Carbonyls

Esterbauer, H., Zöllner, H., & Scholz, N. (1975) · Zeitschrift für Naturforschung C · doi:10.1515/znc-1975-7-808 · Cited by 265

Chemical Strategies for Activity‐Based Proteomics

Speers, A. E., & Cravatt, B. F. (2003) · ChemBioChem · doi:10.1002/cbic.200300721 · Cited by 259

Chemistry and biology of resorcylic acid lactones

Winssinger, N., & Barluenga, S. (2006) · Chemical Communications · doi:10.1039/b610344h · Cited by 256

Protein‐Reactive Natural Products

DRAHL, C., Cravatt, B. F., & Sorensen, E. J. (2005) · Angewandte Chemie International Edition · doi:10.1002/anie.200500900 · Cited by 251

The Emerging Role of Human Esterases

Fukami, T., & Yokoi, T. (2012) · Drug Metabolism and Pharmacokinetics · doi:10.2133/dmpk.dmpk-12-rv-042 · Cited by 246

Activity-Based Proteome Profiling of Potential Cellular Targets of Orlistat − An FDA-Approved Drug with Anti-Tumor Activities

Yang, P., Liu, K., Ngai, M. H., Lear, M. J., Wenk, M. R., & Yao, S. Q. (2009) · Journal of the American Chemical Society · doi:10.1021/ja907716f · Cited by 235

In Vivo and in Vitro Binding of Microcystin to Protein Phosphatase 1 and 2A

Runnegar, M. T. C., Berndt, N., Kong, S., Lee, E. Y., & Zhang, L. F. (1995) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1995.2605 · Cited by 235

A cysteine-selective fluorescent probe for the cellular detection of cysteine

Jung, H. S., Han, J. H., Pradhan, T., Kim, S., Lee, S. W., Sessler, J. L., Kim, T. W., Kang, C., & Kim, J. S. (2011) · Biomaterials · doi:10.1016/j.biomaterials.2011.10.040 · Cited by 233

ALARM NMR: A Rapid and Robust Experimental Method To Detect Reactive False Positives in Biochemical Screens

Huth, J. R., Mendoza, R. R., Olejniczak, E. T., Johnson, R. W., Cothron, D. A., Liu, Y., Lerner, C. G., Chen, J., & Hajduk, P. J. (2004) · Journal of the American Chemical Society · doi:10.1021/ja0455547 · Cited by 232

The development and application of methods for activity-based protein profiling

Jessani, N., & Cravatt, B. F. (2003) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2003.11.004 · Cited by 218

Measurement and Estimation of Electrophilic Reactivity for Predictive Toxicology

Schwöbel, J. A. H., Koleva, Y. K., Enoch, S. J., Bajot, F., Hewitt, M., Madden, J. C., Roberts, D. W., Schultz, T. W., & Cronin, M. (2011) · Chemical Reviews · doi:10.1021/cr100098n · Cited by 213

Formation, characterization, and toxicity of the glutathione and cysteine conjugates of toxic heptapeptide microcystins

Kondo, F., Ikai, Y., Oka, H., Okumura, M., Ishikawa, N., Harada, K., Matsuura, K., Murata, H., & Suzuki, M. (1992) · Chemical Research in Toxicology · doi:10.1021/tx00029a002 · Cited by 212

Wortmannin, a Widely Used Phosphoinositide 3-Kinase Inhibitor, also Potently Inhibits Mammalian Polo-like Kinase

Liu, Y., Shreder, K. R., Gai, W. Z., Corral, S., Ferris, D. K., & Rosenblum, J. S. (2005) · Chemistry & Biology · doi:10.1016/j.chembiol.2004.11.009 · Cited by 210

Targeting Aberrant Glutathione Metabolism to Eradicate Human Acute Myelogenous Leukemia Cells

Pei, S., Minhajuddin, M., Callahan, K. P., Balys, M. M., Ashton, J. M., Neering, S. J., Lagadinou, E. D., Corbett, C. A., Ye, H., Liesveld, J. L., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.511170 · Cited by 208

Activity‐based kinase profiling of approved tyrosine kinase inhibitors

Kitagawa, D., Yokota, K., Gouda, M., Narumi, Y., Ohmoto, H., Nishiwaki, E., Akita, K., & Kirii, Y. (2012) · Genes to Cells · doi:10.1111/gtc.12022 · Cited by 206

The Tunable Functionality of α,β‐Unsaturated Carbonyl Compounds Enables Their Differential Application in Biological Systems

Amslinger, S. (2010) · ChemMedChem · doi:10.1002/cmdc.200900499 · Cited by 204

Drug discovery considerations in the development of covalent inhibitors

Mah, R., Thomas, J. R., & Shafer, C. M. (2013) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2013.10.003 · Cited by 203

Cytotoxic pigments from new zealand sponges of the genus latrunculia : discorhabdins a, b and c

Perry, N. B., Blunt, J. W., & Munro, M. H. G. (1988) · Tetrahedron · doi:10.1016/s0040-4020(01)86737-5 · Cited by 199

Nuclear export inhibition through covalent conjugation and hydrolysis of Leptomycin B by CRM1

Sun, Q., Carrasco, Y. P., Hu, Y., Guo, X., Mirzaei, H., MacMillan, J. B., & Chook, Y. M. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1217203110 · Cited by 198

Electrophilic Fragment-Based Design of Reversible Covalent Kinase Inhibitors

Miller, R. M., Paavilainen, V. O., Krishnan, S., Serafimova, I. M., & Taunton, J. (2013) · Journal of the American Chemical Society · doi:10.1021/ja401221b · Cited by 196

Aminoparthenolides as novel anti-leukemic agents: Discovery of the NF-κB inhibitor, DMAPT (LC-1)

Neelakantan, S., Nasim, S., Guzmán, M. L., Jordan, C. T., & Crooks, P. A. (2009) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2009.05.092 · Cited by 193

Chemistry of Butenolides

Rao, Y. S. (1964) · Chemical Reviews · doi:10.1021/cr60230a002 · Cited by 193

Rhodanine derivatives as inhibitors of JSP-1

Cutshall, N. S., O'Day, C. L., & Prezhdo, M. (2005) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2005.05.034 · Cited by 193

Affinity labeling of cAMP-dependent protein kinase with p-fluorosulfonylbenzoyl adenosine. Covalent modification of lysine 71.

Zoller, M. J., Nelson, N. C., & Taylor, S. S. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)68519-4 · Cited by 186

Observations on Screening-Based Research and Some Concerning Trends in the Literature

Baell, J. B. (2010) · Future Medicinal Chemistry · doi:10.4155/fmc.10.237 · Cited by 184

Chemoprotective Properties of Phenylpropenoids, Bis(benzylidene)cycloalkanones, and Related Michael Reaction Acceptors: Correlation of Potencies as Phase 2 Enzyme Inducers and Radical Scavengers

Dinkova‐Kostova, A. T., Abeygunawardana, C., & Talalay, P. (1998) · Journal of Medicinal Chemistry · doi:10.1021/jm980424s · Cited by 183

Protein Modification by Acrolein: Formation and Stability of Cysteine Adducts

Cai, J., Bhatnagar, A., & Pierce, W. M. J. (2009) · Chemical Research in Toxicology · doi:10.1021/tx800465m · Cited by 183

Targeted covalent inactivation of protein kinases by resorcylic acid lactone polyketides

Schirmer, A., Kennedy, J., Murli, S., Reid, R. C., & Santi, D. V. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0600445103 · Cited by 177

Chemical Strategies for Functional Proteomics

Adam, G. C., Sorensen, E. J., & Cravatt, B. F. (2002) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r200006-mcp200 · Cited by 176

Rhodanine as a scaffold in drug discovery: a critical review of its biological activities and mechanisms of target modulation

Tomašič, T., & Mašič, L. P. (2012) · Expert Opinion on Drug Discovery · doi:10.1517/17460441.2012.688743 · Cited by 172

A Fragment-Based Method to Discover Irreversible Covalent Inhibitors of Cysteine Proteases

Kathman, S. G., Xu, Z., & Statsyuk, A. V. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm500345q · Cited by 172

Drug discovery for a new generation of covalent drugs

Kalgutkar, A. S. S., & Dalvie, D. (2012) · Expert Opinion on Drug Discovery · doi:10.1517/17460441.2012.688744 · Cited by 169

Molecular mechanisms underlying the interaction of motuporin and microcystins with type-1 and type-2A protein phosphatases

Craig, M. M., Luu, H. A., McCready, T., Holmes, C. F. B., Williams, D. E., & Andersen, R. J. (1996) · Biochemistry and Cell Biology · doi:10.1139/o96-061 · Cited by 166

A Cell-permeable, Activity-based Probe for Protein and Lipid Kinases

Yee, M., Fas, S. C., Stohlmeyer, M. M., Wandless, T. J., & Cimprich, K. A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504730200 · Cited by 165

Systematic Study of the Glutathione (GSH) Reactivity ofN-Arylacrylamides: 1. Effects of Aryl Substitution

Cee, V. J., Volak, L. P., Chen, Y., Bartberger, M. D., Tegley, C. M., Arvedson, T., McCarter, J. D., Tasker, A. S., & Fotsch, C. H. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b01018 · Cited by 165

The reaction of cysteine with α,β-unsaturated aldehydes

Esterbauer, H., Ertl, A., & Scholz, N. (1976) · Tetrahedron · doi:10.1016/0040-4020(76)87015-9 · Cited by 161

An NMR Spectroscopic Method to Identify and Classify Thiol‐Trapping Agents: Revival of Michael Acceptors for Drug Discovery?

Avonto, C., Taglialatela‐Scafati, O., Pollastro, F., Minassi, A., Marzo, V. D., PETROCELLIS, L. D., & Appendino, G. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.201005959 · Cited by 158

Exploring the Active‐Site of a Rationally Redesigned Lipase for Catalysis of Michael‐Type Additions

Carlqvist, P., Humble, M. S., Branneby, C., Hult, K., Brinck, T., & Berglund, P. (2004) · ChemBioChem · doi:10.1002/cbic.200400213 · Cited by 145

Antitumor agents. 21. A proposed mechanism for inhibition of cancer growth by tenulin and helenalin and related cyclopentenones

Hall, I. H., Lee, K., Mar, E., Starnes, C. O., & Waddell, T. G. (1977) · Journal of Medicinal Chemistry · doi:10.1021/jm00213a003 · Cited by 144

A novel dicyanotriterpenoid, 2-cyano-3,12-dioxooleana-1,9(11)-dien-28-onitrile, active at picomolar concentrations for inhibition of nitric oxide production

Honda, T., Honda, Y., Favaloro, F. G., Gribble, G. W., Suh, N., Place, A. E., Rendi, M. H., & Sporn, M. B. (2002) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(02)00105-1 · Cited by 143

Helenanolide-type sesquiterpene lactones—III. Rates and stereochemistry in the reaction of helenalin and related helenanolides with sulfhydryl containing biomolecules

Schmidt, T. J. (1997) · Bioorganic & Medicinal Chemistry · doi:10.1016/s0968-0896(97)00003-5 · Cited by 141

Affinity labeling of the nucleotide binding site of the catalytic subunit of cAMP-dependent protein kinase using p-fluorosulfonyl-[14C]benzoyl 5'-adenosine. Identification of a modified lysine residue.

Zoller, M. J., & Taylor, S. S. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)86899-0 · Cited by 140

Reactivity of dimethyl fumarate and methylhydrogen fumarate towards glutathione and N-acetyl-l-cysteine—Preparation of S-substituted thiosuccinic acid esters

Schmidt, T. J., Ak, M., & Mrowietz, U. (2006) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2006.09.053 · Cited by 139

Affinity labeling of the inhibitory DPNH site of bovine liver glutamate dehydrogenase by 5'-fluorosulfonylbenzoyl adenosine.

Pal, P., Wechter, W. J., & Colman, R. W. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)40827-2 · Cited by 137

Prediction of Michael-Type Acceptor Reactivity toward Glutathione

Schwöbel, J. A. H., Wondrousch, D., Koleva, Y. K., Madden, J. C., Cronin, M., & Schüürmann, G. (2010) · Chemical Research in Toxicology · doi:10.1021/tx100172x · Cited by 136

A Structure-Guided Approach to Creating Covalent FGFR Inhibitors

Zhou, W., Hur, W., McDermott, U., Dutt, A., Xian, W., Ficarro, S. B., Zhang, J., Sharma, S. V., Brugge, J. S., Meyerson, M. M., et al. (2010) · Chemistry & Biology · doi:10.1016/j.chembiol.2010.02.007 · Cited by 135

Kaurane Diterpene, Kamebakaurin, Inhibits NF-κB by Directly Targeting the DNA-binding Activity of p50 and Blocks the Expression of Antiapoptotic NF-κB Target Genes

Lee, J.-H., Koo, T. H., Hwang, B. Y., & Lee, J. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201368200 · Cited by 135

Chemical Implications for Antitumor and Antiviral Prostaglandins: Reaction of Δ7-Prostaglandin A1 and Prostaglandin A1 Methyl Esters with Thiols

Suzuki, M., Mori, M., Niwa, T., Hirata, R., Furuta, K., Ishikawa, T., & Noyori, R. (1997) · Journal of the American Chemical Society · doi:10.1021/ja9628359 · Cited by 131

SAR and Mode of Action of Novel Non-Nucleoside Inhibitors of Hepatitis C NS5b RNA Polymerase

Powers, J. P., Piper, D. E., Li, Y., Mayorga, V., Anzola, J. V., Chen, J., Jaén, J. C., Lee, G., Liu, J., Peterson, M. G., et al. (2006) · Journal of Medicinal Chemistry · doi:10.1021/jm050859x · Cited by 131

Recent Advances in the Synthesis of α‐Alkylidene‐Substituted δ‐Lactones, γ‐Lactams and δ‐Lactams

Albrecht, A., Albrecht, Ł., & Janecki, T. (2011) · European Journal of Organic Chemistry · doi:10.1002/ejoc.201001486 · Cited by 129

Curcumin–glutathione interactions and the role of human glutathione S-transferase P1-1

Awasthi, S., Pandya, U., Singhal, S. S., Lin, J. T., Thiviyanathan, V., Seifert, W. E., Awasthi, S., & Ansari, G. A. S. (2000) · Chemico-Biological Interactions · doi:10.1016/s0009-2797(00)00185-x · Cited by 128

Chemical Probes of UDP-Galactopyranose Mutase

Carlson, E. E., May, J. F., & Kiessling, L. L. (2006) · Chemistry & Biology · doi:10.1016/j.chembiol.2006.06.007 · Cited by 126

Kinetic Glutathione Chemoassay To Quantify Thiol Reactivity of Organic Electrophiles—Application to α,β-Unsaturated Ketones, Acrylates, and Propiolates

Böhme, A., Thaens, D., Paschke, A., & Schüürmann, G. (2009) · Chemical Research in Toxicology · doi:10.1021/tx800492x · Cited by 125

Studies on the Mechanism of Phosphatidylinositol 3-Kinase Inhibition by Wortmannin and Related Analogs

Norman, B. H., Shih, C., Toth, J. E., Ray, J. E., Dodge, J. A., Johnson, D. W., Rutherford, P., Schultz, R. M., Worzalla, J. F., & Vlahos, C. J. (1996) · Journal of Medicinal Chemistry · doi:10.1021/jm950619p · Cited by 123

The antitumor and antibacterial activity of the Isodon diterpenoids.

Fujita, E., Nagao, Y., Kaneko, K., NAKAZAWA, S., & KURODA, H. (1976) · Chemical and Pharmaceutical Bulletin · doi:10.1248/cpb.24.2118 · Cited by 121

Structure−Cytotoxicity Relationships of Some Helenanolide-Type Sesquiterpene Lactones

Beekman, A. C., Woerdenbag, H. J., van Uden, W., Pras, N., Konings, A. W. T., Wikström, H., & Schmidt, T. J. (1997) · Journal of Natural Products · doi:10.1021/np960517h · Cited by 120

Photochemical activation of TRPA1 channels in neurons and animals

Kokel, D., Cheung, C. Y., Mills, R. W., Coutinho‐Budd, J., Huang, L., Setola, V., Sprague, J. M., Jin, S., Jin, Y. N., Huang, X., et al. (2013) · Nature Chemical Biology · doi:10.1038/nchembio.1183 · Cited by 119

Covalent binding of catechols to proteins through the sulphydryl group

Ito, S., Kato, T., & Fujita, K. (1988) · Biochemical Pharmacology · doi:10.1016/0006-2952(88)90432-7 · Cited by 114

Structure-Based Design, Synthesis, and Biological Evaluation of Irreversible Human Rhinovirus 3C Protease Inhibitors. 2. Peptide Structure−Activity Studies

Dragovich, P. S., Webber, S. E., Babine, R. E., Fuhrman, S. A., Patick, A. K., Matthews, D. A., Reich, S., Marakovits, J. T., Prins, T. J., Zhou, R., et al. (1998) · Journal of Medicinal Chemistry · doi:10.1021/jm9800696 · Cited by 112

Intracellular Glutathione Depletion by Oridonin Leads to Apoptosis in Hepatic Stellate Cells

Kuo, L. M., Kuo, C., Lin, C. Y., Hung, M.-F., Shen, J. J., & Hwang, T. (2014) · Molecules · doi:10.3390/molecules19033327 · Cited by 111

The Selective Sphingosine 1-Phosphate Receptor 1 Agonist Ponesimod Protects against Lymphocyte-Mediated Tissue Inflammation

Piali, L., Froidevaux, S., Hess, P., Nayler, O., Bolli, M. H., Schlosser, E., Kohl, C., Steiner, B., & Clozel, M. (2011) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.110.176487 · Cited by 110

Anguinomycins and Derivatives: Total Syntheses, Modeling, and Biological Evaluation of the Inhibition of Nucleocytoplasmic Transport

Bonazzi, S., Eidam, O., Güttinger, S., Wach, J., Zemp, I., Kutay, U., & Gademann, K. (2010) · Journal of the American Chemical Society · doi:10.1021/ja9097093 · Cited by 109

Novel Synthesis, Cytotoxic Evaluation, and Structure−Activity Relationship Studies of a Series of α-Alkylidene-γ-lactones and Lactams

Janecki, T., Błaszczyk, E., Studzian, K., Janecka, A. E., Krajewska, U., & Różalski, M. (2005) · Journal of Medicinal Chemistry · doi:10.1021/jm048970a · Cited by 109

Discovery and structure–activity relationship analysis of Staphylococcus aureus sortase A inhibitors

Suree, N., Yi, S. W., Thieu, W., Marohn, M., Damoiseaux, R. D., Chan, A. H., Jung, M. E., & Clubb, R. (2009) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2009.08.067 · Cited by 108

An Exceptionally Potent Inducer of Cytoprotective Enzymes

Dinkova‐Kostova, A. T., Talalay, P., Sharkey, J., Zhang, Y., Holtzclaw, W. D., Wang, X. J., David, E., Schiavoni, K. H., Finlayson, S. D., Mierke, D. F., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.163485 · Cited by 106

Reactivity of the carbon–carbon double bond towards nucleophilic additions. A DFT analysis

Domingo, L. R., Pérez, P., & Contreras, R. R. (2004) · Tetrahedron · doi:10.1016/j.tet.2004.06.003 · Cited by 105

Studies on the reactivity of CDDO, a promising new chemopreventive and chemotherapeutic agent: implications for a molecular mechanism of action

Couch, R. D., Browning, R. G., Honda, T., Gribble, G. W., Wright, D. L., Sporn, M. B., & Anderson, A. C. (2005) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2005.03.031 · Cited by 105

Palladium-Catalyzed Asymmetric Allylic Alkylation of meso- and dl-1,2-Divinylethylene Carbonate

Trost, B. M., & Aponick, A. (2006) · Journal of the American Chemical Society · doi:10.1021/ja0578348 · Cited by 103

Selective Targeting of Distinct Active Site Nucleophiles by Irreversible Src-Family Kinase Inhibitors

Gushwa, N. N., Kang, S., Chen, J., & Taunton, J. (2012) · Journal of the American Chemical Society · doi:10.1021/ja310659j · Cited by 101

Chemistry and Biology of Acylfulvenes: Sesquiterpene-Derived Antitumor Agents

Tanasova, M., & Sturla, S. J. (2012) · Chemical Reviews · doi:10.1021/cr2001367 · Cited by 101

Rupintrivir is a promising candidate for treating severe cases of enterovirus-71 infection: Evaluation of antiviral efficacy in a murine infection model

Zhang, X., Song, Z., Qin, B., Zhang, X., Chen, L., Hu, Y., & Yuan, Z. (2013) · Antiviral Research · doi:10.1016/j.antiviral.2012.12.029 · Cited by 99

Structure-activity relationships of illudins: analogs with improved therapeutic index.

McMorris, T. C., Kelner, M. J., Wang, W., Estes, L. A., Montoya, M. A., & Taetle, R. (1992) · The Journal of Organic Chemistry · doi:10.1021/jo00051a037 · Cited by 99

Neurotoxic Mechanisms of Electrophilic Type-2 Alkenes: Soft Soft Interactions Described by Quantum Mechanical Parameters

LoPachin, R. M., Gavin, T., Geohagen, B. C., & Das, S. (2007) · Toxicological Sciences · doi:10.1093/toxsci/kfm127 · Cited by 99

Antileukemic activity of aminoparthenolide analogs

Nasim, S., & Crooks, P. A. (2008) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2008.06.050 · Cited by 98

Practical synthesis of maleimides and coumarin-linked probes for protein and antibody labelling via reduction of native disulfides

Song, H. Y., Ngai, M. H., Song, Z. Y., MacAry, P. A., Hobley, J., & Lear, M. J. (2009) · Organic & Biomolecular Chemistry · doi:10.1039/b904060a · Cited by 97

Amino-derivatives of the sesquiterpene lactone class of natural products as prodrugs

Woods, J. R., Mo, H., Bieberich, A. A., Alavanja, T., & Colby, D. A. (2012) · MedChemComm · doi:10.1039/c2md20172k · Cited by 96

Irreversible Nek2 Kinase Inhibitors with Cellular Activity

Henise, J., & Taunton, J. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm200222m · Cited by 95

Selective irreversible inhibition of a protease by targeting a noncatalytic cysteine

Hagel, M., Niu, D., St Martin, T., Sheets, M. P., Qiao, L., Bernard, H., Karp, R. M., Zhu, Z., Labenski, M. T., Chaturvedi, P., et al. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.492 · Cited by 95

Synthesis and anticancer activity of novel spiro-isoxazoline and spiro-isoxazolidine derivatives of α-santonin

Khazir, J., Singh, P. P., Reddy, D. M., Hyder, I., Shafi, S., Sawant, S. D., Chashoo, G., Mahajan, A., Alam, M. S., Saxena, A. K., et al. (2013) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2013.01.003 · Cited by 95

Afatinib, Erlotinib and Gefitinib in the First-Line Therapy of EGFR Mutation-Positive Lung Adenocarcinoma: A Review

Köhler, J., & Schüler, M. (2013) · Oncology Research and Treatment · doi:10.1159/000354627 · Cited by 93

1-p-Chlorophenyl-4,4-dimethyl-5-diethylamino-1-penten-3-one hydrobromide, a sulfhydryl-specific compound which reacts irreversibly with protein thiols but reversibly with small molecular weight thiols

Mutus, B., Wagner, J. D., Talpas, C. J., Dimmock, J. R., Phillips, O. A., & Reid, R. S. (1989) · Analytical Biochemistry · doi:10.1016/0003-2697(89)90045-6 · Cited by 93

Antibiotic and Cytotoxic Activity of Brominated Compounds from the Marine Sponge Verongia aerophoba

Teeyapant, R., Woerdenbag, H. J., Kreis, P., Hacker, J. H., Wray, V., Witte, L., & Proksch, P. (1993) · Zeitschrift für Naturforschung C · doi:10.1515/znc-1993-11-1218 · Cited by 93

Structure-Based Design, Synthesis, and Biological Evaluation of Irreversible Human Rhinovirus 3C Protease Inhibitors. 1. Michael Acceptor Structure−Activity Studies

Dragovich, P. S., Webber, S. E., Babine, R. E., Fuhrman, S. A., Patick, A. K., Matthews, D. A., Lee, C. A., Reich, S., Prins, T. J., Marakovits, J. T., et al. (1998) · Journal of Medicinal Chemistry · doi:10.1021/jm980068d · Cited by 92

Acrolein scavengers: Reactivity, mechanism and impact on health

Zhu, Q. Y., Sun, Z., Jiang, Y., Chen, F., & Wang, M. (2011) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201100149 · Cited by 91

Structural insights into how irreversible inhibitors can overcome drug resistance in EGFR

Michalczyk, A., Klüter, S., Rode, H. B., Simard, J. R., Grütter, C., Rabiller, M., & Rauh, D. (2008) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2008.02.053 · Cited by 91

Discovery of a Potent and Isoform-Selective Targeted Covalent Inhibitor of the Lipid Kinase PI3Kα

Nacht, M., Qiao, L., Sheets, M. P., Martin, T. S., Labenski, M., Mazdiyasni, H., Karp, R., Zhu, Z., Chaturvedi, P., Bhavsar, D., et al. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm3008745 · Cited by 90

Conjugation of 9-deoxy-delta 9,delta 12(E)-prostaglandin D2 with intracellular glutathione and enhancement of its antiproliferative activity by glutathione depletion.

Atsmon, J., Freeman, M. L., Meredith, M. J., Sweetman, B. J., & Roberts, L. J. (1990) · PubMed · Cited by 90

Hope and Disappointment: Covalent Inhibitors to Overcome Drug Resistance in Non-Small Cell Lung Cancer

Engel, J., Lategahn, J., & Rauh, D. (2015) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.5b00475 · Cited by 90

Tripeptide Aldehyde Inhibitors of Human Rhinovirus 3C Protease: Design, Synthesis, Biological Evaluation, and Cocrystal Structure Solution of P1 Glutamine Isosteric Replacements

Webber, S. E., Okano, K., Little, T. L., Reich, S., Xin, Y., Fuhrman, S. A., Matthews, D. A., Love, R. A., Hendrickson, T. F., Patick, A. K., et al. (1998) · Journal of Medicinal Chemistry · doi:10.1021/jm980071x · Cited by 89

Formation of thiol conjugates of 9-deoxy-.DELTA.9,.DELTA.12(E)-prostaglandin D2 and .DELTA.12(E)-prostaglandin D2

Atsmon, J., Sweetman, B. J., Baertschi, S. W., Harris, T. M., & Roberts, L. J. (1990) · Biochemistry · doi:10.1021/bi00467a023 · Cited by 88

Longikaurin A, a natural ent-kaurane, induces G2/M phase arrest via downregulation of Skp2 and apoptosis induction through ROS/JNK/c-Jun pathway in hepatocellular carcinoma cells

Liao, Y.-J., Bai, H.-Y., Li, Z. H., Zou, J., Chen, J.-W., Zheng, F., Zhang, J. X., Mai, S.-J., Zeng, M.-S., Sun, H., et al. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.66 · Cited by 88

Bruton’s Tyrosine Kinase Inhibitors: Approaches to Potent and Selective Inhibition, Preclinical and Clinical Evaluation for Inflammatory Diseases and B Cell Malignancies

Lou, Y. C., Owens, T. D., Kuglstatter, A., Kondru, R. K., & GOLDSTEIN, D. M. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm300035p · Cited by 88

Helenanolide type sesquiterpene lactones. Part 5: The role of glutathione addition under physiological conditions

Schmidt, T. J., Lyß, G., Pahl, H. L., & Merfort, I. (1999) · Bioorganic & Medicinal Chemistry · doi:10.1016/s0968-0896(99)00234-5 · Cited by 87

Resorcylic Acid Lactones with Cytotoxic and NF-κB Inhibitory Activities and Their Structure–Activity Relationships

Ayers, S., Graf, T. N., Adcock, A. F., Kroll, D. J., Matthew, S., de Blanco, E. J. C., Shen, Q., Swanson, S. M., Wani, M. C., Pearce, C. J., et al. (2011) · Journal of Natural Products · doi:10.1021/np200062x · Cited by 87

Transition States and Energetics of Nucleophilic Additions of Thiols to Substituted α,β-Unsaturated Ketones: Substituent Effects Involve Enone Stabilization, Product Branching, and Solvation

Krenske, E. H., Petter, R. C., Zhu, Z., & Houk, K. N. (2011) · The Journal of Organic Chemistry · doi:10.1021/jo200761w · Cited by 86

Covalent tethering of fragments for covalent probe discovery

Kathman, S. G., & Statsyuk, A. V. (2016) · MedChemComm · doi:10.1039/c5md00518c · Cited by 85

The potency of inducers of NAD(P)H:(quinone-acceptor) oxidoreductase parallels their efficiency as substrates for glutathione transferases. Structural and electronic correlations

Spencer, S. R., Xue, L. A., Klenz, E. M., & Talalay, P. (1991) · Biochemical Journal · doi:10.1042/bj2730711 · Cited by 83

Predicting Michael-acceptor reactivity and toxicity through quantum chemical transition-state calculations

Mulliner, D., Wondrousch, D., & Schüürmann, G. (2011) · Organic & Biomolecular Chemistry · doi:10.1039/c1ob06065a · Cited by 83

Hepatoprotective effect of lucidone against alcohol-induced oxidative stress in human hepatic HepG2 cells through the up-regulation of HO-1/Nrf-2 antioxidant genes

Kumar, K. J. S., Liao, J., Xiao, J., Vani, M. G., & Wang, S. (2012) · Toxicology in Vitro · doi:10.1016/j.tiv.2012.03.012 · Cited by 80

Synthesis and biological evaluation of synthetic viridins derived from C(20)-heteroalkylation of the steroidal PI-3-kinase inhibitor wortmannin

Wipf, P., Minion, D. J., Halter, R. J., Berggren, M. I., Ho, C., Chiang, G. G., Kirkpatrick, L., Abraham, R. T., & Powis, G. (2004) · Organic & Biomolecular Chemistry · doi:10.1039/b405431h · Cited by 78

A randomized, phase 2 trial of docetaxel with or without PX-866, an irreversible oral phosphatidylinositol 3-kinase inhibitor, in patients with relapsed or metastatic head and neck squamous cell cancer

Jimeno, A., Bauman, J. E., Weissman, C., Adkins, D. R., Schnadig, I. D., Beauregard, P., Bowles, D. W., Spira, A. I., Levy, B. P., Seetharamu, N., et al. (2015) · Oral Oncology · doi:10.1016/j.oraloncology.2014.12.013 · Cited by 78

Synthesis of 2-Oxindole Derivatives via the Intramolecular Heck Reaction on Solid Support

Arumugam, V., Routledge, A., Abell, C., & Balasubramanian, S. (1997) · Tetrahedron Letters · doi:10.1016/s0040-4039(97)01481-0 · Cited by 77

Range-Separated DFT Functionals are Necessary to Model Thio-Michael Additions

Smith, J. M. B., Jami‐Alahmadi, Y., & Rowley, C. N. (2013) · Journal of Chemical Theory and Computation · doi:10.1021/ct400773k · Cited by 77

Dual irreversible kinase inhibitors: Quinazoline-based inhibitors incorporating two independent reactive centers with each targeting different cysteine residues in the kinase domains of EGFR and VEGFR-2

Wissner, A., Fraser, H. L., Ingalls, C. L., Dushin, R. G., Floyd, M. B., Cheung, K., Nittoli, T., Ravi, M., Tan, X., & Loganzo, F. (2007) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2007.03.055 · Cited by 76

Punaglandins, Chlorinated Prostaglandins, Function as Potent Michael Receptors To Inhibit Ubiquitin Isopeptidase Activity

Verbitski, S. M., Mullally, J. E., Fitzpatrick, F. A., & Ireland, C. M. (2004) · Journal of Medicinal Chemistry · doi:10.1021/jm030448l · Cited by 75

Irreversible Protein Kinase Inhibitors

Garuti, L., Roberti, M., & Bottegoni, G. (2011) · Current Medicinal Chemistry · doi:10.2174/092986711796391705 · Cited by 74

Chemical proteomics reveals HSP70 1A as a target for the anticancer diterpene oridonin in Jurkat cells

Piaz, F. D., Cotugno, R., Lepore, L., Vassallo, A., Malafronte, N., Lauro, G., Bifulco, G., Belisario, M. A., & Tommasi, N. D. (2013) · Journal of Proteomics · doi:10.1016/j.jprot.2013.01.030 · Cited by 73

Thiol Reactivity and Its Impact on the Ciliate Toxicity of α,β-Unsaturated Aldehydes, Ketones, and Esters

Böhme, A., Thaens, D., Schramm, F., Paschke, A., & Schüürmann, G. (2010) · Chemical Research in Toxicology · doi:10.1021/tx100226n · Cited by 72

A Study of the Reaction of Calicheamicin .gamma.1 with Glutathione in the Presence of Double-Stranded DNA

Myers, A. G., Cohen, S. B., & Kwon, B. M. (1994) · Journal of the American Chemical Society · doi:10.1021/ja00083a012 · Cited by 70

Synthesis and Antibacterial Activity of Peptide Deformylase Inhibitors

Huntington, K. M., Tian, Y., Wei, Y., & Pei, D. (2000) · Biochemistry · doi:10.1021/bi992452y · Cited by 68

On the mechanism of toxicity of illudins: the role of glutathione

McMorris, T. C., Kelner, M. J., Wang, W., Moon, S., & Taetle, R. (1990) · Chemical Research in Toxicology · doi:10.1021/tx00018a013 · Cited by 68

Eriocalyxin B Inhibits Nuclear Factor-κB Activation by Interfering with the Binding of Both p65 and p50 to the Response Element in a Noncompetitive Manner

Leung, C., Grill, S. P., Lam, W., Gao, W., Sun, H., & Cheng, Y.-C. (2006) · Molecular Pharmacology · doi:10.1124/mol.106.028480 · Cited by 66

Stereospecific nucleophilic addition reactions to olefins. Addition of thiols to .alpha.,.beta.-unsaturated carboxylic acid derivatives

Miyata, O., Shinada, T., Ninomiya, I., Naito, T., Date, T., Okamura, K., & Inagaki, S. (1991) · The Journal of Organic Chemistry · doi:10.1021/jo00023a021 · Cited by 66

Local Electrophilicity Predicts the Toxicity-Relevant Reactivity of Michael Acceptors

Wondrousch, D., Böhme, A., Thaens, D., Ost, N., & Schüürmann, G. (2010) · The Journal of Physical Chemistry Letters · doi:10.1021/jz100247x · Cited by 65

Recent Progress in the Development of Natural ent-Kaurane Diterpenoids with Anti-tumor Activity

Wang, L., Li, D., Wang, C., Zhang, Y., & Xu, J. (2011) · Mini-Reviews in Medicinal Chemistry · doi:10.2174/138955711796575416 · Cited by 65

Synthesis, Chemical Reactivity as Michael Acceptors, and Biological Potency of Monocyclic Cyanoenones, Novel and Highly Potent Anti-inflammatory and Cytoprotective Agents

Zheng, S., Laxmi, Y. R. S., David, E., Dinkova‐Kostova, A. T., Shiavoni, K. H., Ren, Y., Zheng, Y., Isaac, T., Bumeister, R., Ojima, I., et al. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm3003922 · Cited by 64

Using Small Molecules To Dissect Mechanisms of Microbial Pathogenesis

Puri, A. W., & Bogyo, M. S. (2009) · ACS Chemical Biology · doi:10.1021/cb9001409 · Cited by 64

Formation of glutathione conjugates of prostaglandin A1 in human red blood cells.

Cagen, L. M., Fales, H. M., & Pisano, J. J. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32982-4 · Cited by 62

Brostallicin, a novel anticancer agent whose activity is enhanced upon binding to glutathione.

Geroni, C., Marchini, S., Cozzi, P., Galliera, E., Ragg, E. M., Colombo, T., Battaglia, R., Howard, M., D’Incalci, M., & Broggini, M. (2002) · PubMed · Cited by 62

Tumor inhibitors. LVII. Reaction of endocyclic .alpha.,.beta.-unsaturated .gamma.-lactones with thiols

Kupchan, S. M., Giacobbe, T. J., Krull, I. S., Thomas, S. M., Eakin, M. A., & Fessler, D. C. (1970) · The Journal of Organic Chemistry · doi:10.1021/jo00835a078 · Cited by 61

Acylfulvenes, a new class of potent antitumor agents

McMorris, T. C., Kelner, M. J., Wang, W., Diaz, M. A., Estes, L. A., & Taetle, R. (1996) · Cellular and Molecular Life Sciences · doi:10.1007/bf01922420 · Cited by 61

The Chemistry and Biology of the Leptomycin Family

Kalesse, M., & Christmann, M. (2002) · Synthesis · doi:10.1055/s-2002-31946 · Cited by 61

The Role of Endogenous Catechol Quinones in the Initiation of Cancer and Neurodegenerative Diseases

Cavalieri, E. L., Rogan, E. G., & Chakravarti, D. (2004) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(04)82017-2 · Cited by 60

Abiotic Sulfhydryl Reactivity: A Predictor of Aquatic Toxicity for Carbonyl-Containing α,β-Unsaturated Compounds

Yarbrough, J. W., & Schultz, T. W. (2007) · Chemical Research in Toxicology · doi:10.1021/tx600344a · Cited by 60

Bicyclic Cyclohexenones as Inhibitors of NF-κB Signaling

Hexum, J. K., Tello‐Aburto, R., Struntz, N. B., Harned, A. M., & Harki, D. A. (2012) · ACS Medicinal Chemistry Letters · doi:10.1021/ml300034a · Cited by 59

2-(Quinazolin-4-ylamino)-[1,4]benzoquinones as Covalent-Binding, Irreversible Inhibitors of the Kinase Domain of Vascular Endothelial Growth Factor Receptor-2

Wissner, A., Floyd, M. B., Johnson, B. D., Fraser, H. L., Ingalls, C. L., Nittoli, T., Dushin, R. G., Discafani, C. M., Nilakantan, R., Marini, J., et al. (2005) · Journal of Medicinal Chemistry · doi:10.1021/jm050559f · Cited by 59

Read‐across to rank skin sensitization potential: subcategories for the Michael acceptor domain

Schultz, T. W., Rogers, K., & Aptula, A. O. (2009) · Contact Dermatitis · doi:10.1111/j.1600-0536.2008.01473.x · Cited by 59

Computational study of the covalent bonding of microcystins to cysteine residues – a reaction involved in the inhibition of the PPP family of protein phosphatases

Pereira, S. R., Vasconcelos, V. M., & Antunes, A. (2011) · FEBS Journal · doi:10.1111/j.1742-4658.2011.08454.x · Cited by 58

Lucidone Suppresses Hepatitis C Virus Replication by Nrf2-Mediated Heme Oxygenase-1 Induction

Chen, W., Wang, S., Chiu, C., Tseng, C.-K., Lin, C., Wang, H., & Lee, J. (2012) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.02053-12 · Cited by 58

Human Glutathione S-Transferase-Mediated Glutathione Conjugation of Curcumin and Efflux of These Conjugates in Caco-2 Cells

Usta, M., Wortelboer, H. M., Vervoort, J. J. M., Boersma, M. G., Rietjens, I. M. C. M., van BLADEREN, P. J., & Cnubben, N. H. P. (2007) · Chemical Research in Toxicology · doi:10.1021/tx7002245 · Cited by 58

Curcumin analog cytotoxicity against breast cancer cells: exploitation of a redox-dependent mechanism

Sun, A., Lu, Y., Hu, H., Shoji, M., Liotta, D. C., & Snyder, J. P. (2009) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2009.10.023 · Cited by 57

Simple synthesis of 1,3-cyclopentanedione derived probes for labeling sulfenic acid proteins

Qian, J. X., Klomsiri, C., Wright, M. W., King, S. B., Tsang, A. W., Poole, L. B., & Furdui, C. M. (2011) · Chemical Communications · doi:10.1039/c1cc12127h · Cited by 57

Click-based synthesis and proteomic profiling of lipstatin analogues

Ngai, M. H., Yang, P., Liu, K., Shen, Y., Wenk, M. R., Yao, S. Q., & Lear, M. J. (2010) · Chemical Communications · doi:10.1039/c0cc01276a · Cited by 55

Discovery of a Selective Irreversible BMX Inhibitor for Prostate Cancer

Liu, F., Zhang, X., Weisberg, E., Chen, S., Hur, W., Wu, H., Zhao, Z., Wang, W., Mao, M., Cai, C., et al. (2013) · ACS Chemical Biology · doi:10.1021/cb4000629 · Cited by 54

The Enterovirus Protease Inhibitor Rupintrivir Exerts Cross-Genotypic Anti-Norovirus Activity and Clears Cells from the Norovirus Replicon

Rocha‐Pereira, J., Nascimento, M. S. J., Ma, Q., Hilgenfeld, R., Neyts, J. H., & Jochmans, D. (2014) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.02546-13 · Cited by 54

Guaianolide Sesquiterpenoids: Pharmacology and Biosynthesis

Simonsen, H. T., Weitzel, C., & Christensen, S. B. (2013) · Springer eBooks · doi:10.1007/978-3-642-22144-6_134 · Cited by 53

The Clinical KRAS(G12C) Inhibitor AMG 510 Drives Anti-Tumour Immunity

Canon, J., Rex, K., Saiki, A. Y., Mohr, C., Cooke, K., Bagal, D., Gaida, K., Holt, T., Knutson, C. G., Koppada, N., et al. (2019) · Nature · doi:10.1038/s41586-019-1694-1 · Cited by 2,277

Curcumin: Biological, Pharmaceutical, Nutraceutical, and Analytical Aspects

Kotha, R. R., & Luthria, D. L. (2019) · Molecules · doi:10.3390/molecules24162930 · Cited by 960

The SARS-CoV-2 main protease as drug target

Ullrich, S., & Nitsche, C. (2020) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2020.127377 · Cited by 787

Emerging and Re-Emerging Warheads for Targeted Covalent Inhibitors: Applications in Medicinal Chemistry and Chemical Biology

Gehringer, M., & Laufer, S. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b01153 · Cited by 772

Put a ring on it: application of small aliphatic rings in medicinal chemistry

Bauer, M. R., Fruscia, P. D., Lucas, S. C. C., Michaelides, I. N., Nelson, J. E., Storer, R. I., & Whitehurst, B. C. (2021) · RSC Medicinal Chemistry · doi:10.1039/d0md00370k · Cited by 505

Progress in Michael Addition Reaction between Thiols and α,β-unsaturated Carbonyl Compounds

Dian-gang, B. (2007) · Journal of Anshan Normal University

Kinetics and Thermodynamics of Reversible Thiol Additions to Mono- and Diactivated Michael Acceptors: Implications for the Design of Drugs That Bind Covalently to Cysteines

Krenske, E. H., Petter, R. C., & Houk, K. N. (2016) · The Journal of Organic Chemistry · doi:10.1021/acs.joc.6b02188 · Cited by 152

The Tunable Functionality of α,β‐Unsaturated Carbonyl Compounds Enables Their Differential Application in Biological Systems

Amslinger, S. (2010) · ChemMedChem · doi:10.1002/cmdc.200900499 · Cited by 204

Reactions of Alpha Methylene Lactone Tumor Inhibitors with Model Biological Nucleophiles

Kupchan, S. M., Fessler, D. C., Eakin, M. A., & Giacobbe, T. J. (1970) · Science · doi:10.1126/science.168.3929.376 · Cited by 301

Reactivity assessment of chalcones by a kinetic thiol assay

Amslinger, S., Al‐Rifai, N., Winter, K., Wörmann, K., Scholz, R., Baumeister, P., & Wild, M. (2012) · Organic & Biomolecular Chemistry · doi:10.1039/c2ob27163j · Cited by 48