Rottlerin: an inappropriate and ineffective inhibitor of PKCδ

TSC2 Mediates Cellular Energy Response to Control Cell Growth and Survival

Inoki, K., Zhu, T., & Guan, K.-L. (2003) · Cell · doi:10.1016/s0092-8674(03)00929-2 · Cited by 3,914

Specificity and mechanism of action of some commonly used protein kinase inhibitors

DAVIES, S. P., REDDY, H., CAIVANO, M., & COHEN, P. (2000) · Biochemical Journal · doi:10.1042/bj3510095 · Cited by 3,132

Rottlerin, a Novel Protein Kinase Inhibitor

Gschwendt, M., Muller, H. J., Kielbassa, K., Zang, R., Kittstein, W., Rincke, G., & Marks, F. (1994) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1994.1199 · Cited by 841

Regulation of cell apoptosis by protein kinase c δ

Brodie, C., & Blumberg, P. M. (2003) · Apoptosis · doi:10.1023/a:1021640817208 · Cited by 421

Regulation of Phospholipid Scramblase Activity during Apoptosis and Cell Activation by Protein Kinase Cδ

Frasch, S. C., Henson, P. M., Kailey, J. M., Richter, D. A., Janes, M. S., Fadok, V. A., & Bratton, D. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003116200 · Cited by 234

6-Hydroxydopamine-induced Apoptosis Is Mediated via Extracellular Auto-oxidation and Caspase 3-dependent Activation of Protein Kinase Cδ

Hanrott, K., Gudmunsen, L., O’Neill, M. J., & Wonnacott, S. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511560200 · Cited by 230

Kinase Inhibitors: Not Just for Kinases Anymore

McGovern, S. L., & Shoichet, B. K. (2003) · Journal of Medicinal Chemistry · doi:10.1021/jm020427b · Cited by 230

Rottlerin Is a Mitochondrial Uncoupler That Decreases Cellular ATP Levels and Indirectly Blocks Protein Kinase Cδ Tyrosine Phosphorylation

Soltoff, S. P. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105073200 · Cited by 223

Caspase-3-Dependent Proteolytic Cleavage of Protein Kinase Cδ Is Essential for Oxidative Stress-Mediated Dopaminergic Cell Death after Exposure to Methylcyclopentadienyl Manganese Tricarbonyl

Anantharam, V., Kitazawa, M., Wagner, J., Kaul, S., & Kanthasamy, A. G. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-05-01738.2002 · Cited by 219

Novel Mechanism of Activation of NADPH Oxidase 5

Jagnandan, D., Church, J. E., Banfi, B., Stuehr, D. J., Marrero, M. B., & Fulton, D. J. R. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m608966200 · Cited by 210

Tyrosine Phosphorylation of Protein Kinase Cδ Is Essential for Its Apoptotic Effect in Response to Etoposide

Blass, M., Kronfeld, I., Kazimirsky, G., Blumberg, P. M., & Brodie, C. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.1.182-195.2002 · Cited by 197

Link between Mitochondria and NADPH Oxidase 1 Isozyme for the Sustained Production of Reactive Oxygen Species and Cell Death

Lee, S. B., Bae, I. H., Bae, Y. S., & Um, H.-D. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606702200 · Cited by 187

Lipopolysaccharide Induces Matrix Metalloproteinase-9 Expression via a Mitochondrial Reactive Oxygen Species-p38 Kinase-Activator Protein-1 Pathway in Raw 264.7 Cells

Woo, C.-H., Lim, J.-H., & Kim, J.-H. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.173.11.6973 · Cited by 175

Protein Kinase Cθ Cooperates with Calcineurin to Induce Fas Ligand Expression During Activation-Induced T Cell Death

Villalba, M., Kasibhatla, S., Genestier, L., Mahboubi, A., Green, D. R., & Altman, A. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.163.11.5813 · Cited by 131

Protein kinase ctheta cooperates with calcineurin to induce Fas ligand expression during activation-induced T cell death.

Villalba, M., Kasibhatla, S., Genestier, L., Mahboubi, A., Green, D. R., & Altman, A. (1999) · PubMed · Cited by 127

PKC-δ-dependent activation of oxidative stress in adipocytes of obese and insulin-resistant mice: role for NADPH oxidase

Talior, I., Tennenbaum, T., Kuroki, T., & Eldar-Finkelman, H. (2005) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00378.2004 · Cited by 120

ADAM10 Mediates Ectodomain Shedding of the Betacellulin Precursor Activated by p-Aminophenylmercuric Acetate and Extracellular Calcium Influx

Sanderson, M. P., Erickson, S. N., Gough, P. J., Garton, K. J., Wille, P. T., Raines, E. W., Dunbar, A. J., & Dempsey, P. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408804200 · Cited by 111

PKCδ regulates collagen-induced platelet aggregation through inhibition of VASP-mediated filopodia formation

Pula, G., Schuh, K., Nakayama, K., Nakayama, K., Walter, U., & Poole, A. W. (2006) · Blood · doi:10.1182/blood-2006-05-023739 · Cited by 110

Reactive Oxygen Species Regulate Caspase Activation in Tumor Necrosis Factor–Related Apoptosis-Inducing Ligand–Resistant Human Colon Carcinoma Cell Lines

Izeradjene, K., Douglas, L., Tillman, D. M., Delaney, A. B., & Houghton, J. A. (2005) · Cancer Research · doi:10.1158/0008-5472.can-04-2628 · Cited by 109

Coadministration of Sorafenib with Rottlerin Potently Inhibits Cell Proliferation and Migration in Human Malignant Glioma Cells

Jane, E. P., Premkumar, D. R., & Pollack, I. F. (2006) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.106.108621 · Cited by 104

Rottlerin sensitizes colon carcinoma cells to tumor necrosis factor-related apoptosis-inducing ligand-induced apoptosis via uncoupling of the mitochondria independent of protein kinase C.

Tillman, D. M., Izeradjene, K., Szücs, K. S., Douglas, L., & Houghton, J. A. (2003) · PubMed · Cited by 101

STAT1-Independent Cell Type-Specific Regulation of Antiviral APOBEC3G by IFN-α

Sarkis, P. T. N., Ying, S., Xu, R., & Yu, X.-F. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.7.4530 · Cited by 96

Mallotoxin Is a Novel Human Ether-a-go-go-Related Gene (hERG) Potassium Channel Activator

Zeng, H., Lozinskaya, I. M., Lin, Z., Willette, R. N., Brooks, D. P., & Xu, X. (2006) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.106.110593 · Cited by 76

Activation of the BK (SLO1) Potassium Channel by Mallotoxin

Zakharov, S. I., Morrow, J., Liu, G., Yang, L., & Marx, S. O. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505302200 · Cited by 68

Rottlerin, an inhibitor of protein kinase Cδ (PKCδ), inhibits astrocytic glutamate transport activity and reduces GLAST immunoreactivity by a mechanism that appears to be PKCδ‐independent

Susarla, B. T. S., & Robinson, M. B. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01886.x · Cited by 62

Modulation of PKCδ tyrosine phosphorylation and activity in salivary and PC-12 cells by Src kinases

Benes, C. H., & Soltoff, S. P. (2001) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.2001.280.6.c1498 · Cited by 62

Sphingosine-Induced Apoptosis in Rhabdomyosarcoma Cell Lines Is Dependent on Pre-Mitochondrial Bax Activation and Post-Mitochondrial Caspases

Phillips, D. C., Martin, S., Doyle, B. T., & Houghton, J. A. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-2374 · Cited by 49

Effects of rottlerin on silica-exacerbated systemic autoimmune disease in New Zealand mixed mice

Brown, J. M., Schwanke, C. M., Pershouse, M. A., Pfau, J. C., & Holian, A. (2005) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00078.2005 · Cited by 44

Rottlerin Inhibits Insulin-Stimulated Glucose Transport in 3T3-L1 Adipocytes by Uncoupling Mitochondrial Oxidative Phosphorylation

Kayali, A. G., Austin, D. A., & Webster, N. J. G. (2002) · Endocrinology · doi:10.1210/en.2002-220259 · Cited by 40

Rottlerin sensitizes glioma cells to TRAIL-induced apoptosis by inhibition of Cdc2 and the subsequent downregulation of survivin and XIAP

Kim, E. H., Kim, S. U., & Choi, K. S. (2004) · Oncogene · doi:10.1038/sj.onc.1208241 · Cited by 40

Mechanisms of apoptosis-induction by rottlerin: therapeutic implications for B-CLL

Ringshausen, I., Oelsner, M., Weick, K., Bogner, C., Peschel, C., & Decker, T. W. (2006) · Leukemia · doi:10.1038/sj.leu.2404113 · Cited by 39

Rottlerin-Independent Attenuation of Pervanadate-Induced Tyrosine Phosphorylation Events by Protein Kinase C-δ in Hemopoietic Cells

Leitges, M., Elis, W., Gimborn, K., & Huber, M. (2001) · Laboratory Investigation · doi:10.1038/labinvest.3780321 · Cited by 38

Rottlerin synergistically enhances imatinib-induced apoptosis of BCR/ABL-expressing cells through its mitochondrial uncoupling effect independent of protein kinase C-δ

Kurosu, T., Tsuji, K., Kida, A., Koyama, T., Yamamoto, M., & Miura, O. (2006) · Oncogene · doi:10.1038/sj.onc.1210117 · Cited by 35

PKCδ protects human breast tumor MCF‐7 cells against tumor necrosis factor‐related apoptosis‐inducing ligand‐mediated apoptosis

Zhang, J., Liu, N., Zhang, J., Liu, S., Liu, Y., & Zheng, D. (2005) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20535 · Cited by 30

Targeting the hypoxia inducible factor pathway with mitochondrial uncouplers

Thomas, R., & Kim, M. H. (2006) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-006-9295-3 · Cited by 19

Potentiation of Tumor Necrosis Factor-α-Induced Cell Death by Rottlerin through a Cytochrome-C-Independent Pathway

Basu, A., Johnson, D. E., & Woolard, M. D. (2002) · Experimental Cell Research · doi:10.1006/excr.2002.5587 · Cited by 17

Receptor Activator of Nuclear Factor-κB Is Induced by a Rottlerin-sensitive and p38 MAP Kinase-dependent Pathway during Monocyte Differentiation

Kang, H. S., Park, E. K., Kim, K., Park, J. Y., Choi, J., Shin, H., Jun, C., Kang, S., & Kim, S. (2004) · Molecules and Cells · doi:10.1016/s1016-8478(23)13064-0 · Cited by 14

Rottlerin inhibits multiple steps involved in insulin-induced glucose uptake in 3T3-L1 adipocytes

Bazuine, M., van der Zon, G. C. M., van de Ven, R., den Broek, P. J. A. V., & Maassen, J. A. (2004) · Biochemical Pharmacology · doi:10.1016/j.bcp.2004.02.032 · Cited by 12

TLR2- and TLR4-dependent activation of STAT1 serine phosphorylation in murine macrophages is protein kinase C-δ-independent

Shoenfelt, J. L., & Fenton, M. J. (2006) · Journal of Endotoxin Research · doi:10.1177/09680519060120040401 · Cited by 10

Activation of Protein Kinase C Isoforms and Its Impact on Diabetic Complications

Geraldes, P., & King, G. L. (2010) · Circulation Research · doi:10.1161/circresaha.110.217117 · Cited by 985

Structural Basis of Protein Kinase C Isoform Function

Steinberg, S. F. (2008) · Physiological Reviews · doi:10.1152/physrev.00034.2007 · Cited by 872

Silica, Silicosis, and Autoimmunity

Pollard, K. M. (2016) · Frontiers in Immunology · doi:10.3389/fimmu.2016.00097 · Cited by 431

Screen for Chemical Modulators of Autophagy Reveals Novel Therapeutic Inhibitors of mTORC1 Signaling

Balgi, A. D., Fonseca, B. D., Donohue, E., Tsang, T. C. F., Lajoie, P., Proud, C. G., Nabi, I. R., & Roberge, M. (2009) · PLoS ONE · doi:10.1371/journal.pone.0007124 · Cited by 344

Pitfalls of the MTT assay: Direct and off-target effects of inhibitors can result in over/underestimation of cell viability

Stepanenko, A. A., & Dmitrenko, V. V. (2015) · Gene · doi:10.1016/j.gene.2015.08.009 · Cited by 315