Protein kinases and phosphatases: The Yin and Yang of protein phosphorylation and signaling

Phosphorylated CREB binds specifically to the nuclear protein CBP

Chrivia, J. C., Kwok, R. P. S., Lamb, N., Hagiwara, M., Montminy, M. R., & Goodman, R. H. (1993) · Nature · doi:10.1038/365855a0 · Cited by 2,052

Nuclear protein CBP is a coactivator for the transcription factor CREB

Kwok, R. P. S., Lundblad, J. R., Chrivia, J. C., Richards, J. P., Bächinger, H. P., Brennan, R. G., Roberts, S. G. E., Green, M. R., & Goodman, R. H. (1994) · Nature · doi:10.1038/370223a0 · Cited by 1,443

MKP-1 (3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo.

Sun, H., Charles, C. H., Lau, L. F., & Tonks, N. K. (1993) · Cell · doi:10.1016/0092-8674(93)90383-2 · Cited by 1,156

Inactivation of p42 MAP kinase by protein phosphatase 2A and a protein tyrosine phosphatase, but not CL100, in various cell lines

Alessi, D. R., Gomez, N., Moorhead, G., Lewis, T., Keyse, S. M., & Cohen, P. (1995) · Current Biology · doi:10.1016/s0960-9822(95)00059-5 · Cited by 365

The Effects of Plant Flavonoids on Mammalian Cells:Implications for Inflammation, Heart Disease, and Cancer

Middleton, E., Kandaswami, C., & Theoharides, T. C. (2000) · Pharmacological Reviews · doi:10.1016/s0031-6997(24)01472-8 · Cited by 4,882

Signaling—2000 and Beyond

Hunter, T. (2000) · Cell · doi:10.1016/s0092-8674(00)81688-8 · Cited by 2,586

Dimerization of cell surface receptors in signal transduction

Heldin, C.-H. (1995) · Cell · doi:10.1016/0092-8674(95)90404-2 · Cited by 1,634

The molecular details of cytokine signaling via the JAK/STAT pathway

Morris, R., Kershaw, N. J., & Babon, J. J. (2018) · Protein Science · doi:10.1002/pro.3519 · Cited by 943

Phosphatase‐mediated crosstalk between MAPK signaling pathways in the regulation of cell survival

Junttila, M. R., Li, S., & Westermarck, J. (2008) · The FASEB Journal · doi:10.1096/fj.06-7859rev · Cited by 826

Invited review c-Fos as a transcription factor: a stressful (re)view from a functional map

Kovács, K. J. (1998) · Neurochemistry International · doi:10.1016/s0197-0186(98)00023-0 · Cited by 740

Dual-specificity phosphatases: critical regulators with diverse cellular targets

Patterson, K. I., Brummer, T., O'brien, P. M., & Daly, R. J. (2009) · Biochemical Journal · doi:10.1042/bj20082234 · Cited by 744

Protein Oxidation in Aging and Age‐Related Diseases

Stadtman, E. R. (2001) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2001.tb05632.x · Cited by 660

Blood-derived nurse-like cells protect chronic lymphocytic leukemia B cells from spontaneous apoptosis through stromal cell-derived factor-1.

Burger, J. A., Tsukada, N., Burger, M., Zvaifler, N. J., Dell'Aquila, M., & Kipps, T. J. (2000) · Blood · doi:10.1182/blood.v96.8.2655 · Cited by 607

The TGF-beta family mediator Smad1 is phosphorylated directly and activated functionally by the BMP receptor kinase

Kretzschmar, M., Liu, F., Hata, A., Doody, J., & Massagué, J. (1997) · Genes & Development · doi:10.1101/gad.11.8.984 · Cited by 574

Regulation of T Cell Receptor Signaling by Tyrosine Phosphatase SYP Association with CTLA-4

Marengère, L. E. M., Waterhouse, P., Duncan, G. S., Mittrücker, H.-W., Feng, G.-S., & Mak, T. W. (1996) · Science · doi:10.1126/science.272.5265.1170 · Cited by 551

Structure of the Protein Phosphatase 2A Holoenzyme

Xu, Y., Xing, Y., Chen, Y., Chao, Y., Lin, Z., Fan, E., Yu, J. W., Strack, S., Jeffrey, P. D., & Shi, Y. (2006) · Cell · doi:10.1016/j.cell.2006.11.033 · Cited by 450

Metabolic flux and the regulation of mammalian cell growth

Locasale, J. W., & Cantley, L. C. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.07.014 · Cited by 449

The structure of the protein phosphatase 2A PR65/A subunit reveals the conformation of its 15 tandemly repeated HEAT motifs

Groves, M. R., Hanlon, N., Turowski, P., Hemmings, B. A., & Barford, D. (1999) · Cell · doi:10.1016/s0092-8674(00)80963-0 · Cited by 442

Emerging paradigms of β-arrestin-dependent seven transmembrane receptor signaling

Shukla, A. K., Xiao, K., & Lefkowitz, R. J. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.06.003 · Cited by 418

Chapter 7 Protein Oxidation Processes in Aging Brain

Butterfield, D. A., & Stadtman, E. R. (1997) · Advances in cell aging and gerontology · doi:10.1016/s1566-3124(08)60057-7 · Cited by 390

STAT3β, a splice variant of transcription factor STAT3, is a dominant negative regulator of transcription

Caldenhoven, E., van Dijk, T. B., Solari, R., Armstrong, J., Raaijmakers, J. A. M., Lammers, J.-W. J., Koenderman, L., & de Groot, R. P. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.22.13221 · Cited by 373

Tau Post-translational Modifications: Dynamic Transformers of Tau Function, Degradation, and Aggregation

Alquezar, C., Arya, S., & Kao, A. W. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2020.595532 · Cited by 367

Structure of protein phosphatase 2A core enzyme bound to tumor-inducing toxins

Xing, Y., Xu, Y., Chen, Y., Jeffrey, P. D., Chao, Y., Lin, Z., Li, Z., Strack, S., Stock, J. B., & Shi, Y. (2006) · Cell · doi:10.1016/j.cell.2006.09.025 · Cited by 334

Comprehensive review of mechanisms of pathogenesis involved in Alzheimer’s disease and potential therapeutic strategies

Sharma, P., Srivastava, P., Seth, A., Tripathi, P. N., Banerjee, A. G., & Shrivastava, S. K. (2019) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.12.006 · Cited by 331

Leflunomide: an immunomodulatory drug for the treatment of rheumatoid arthritis and other autoimmune diseases

Herrmann, M. L., Schleyerbach, R., & Kirschbaum, B. J. (2000) · Immunopharmacology · doi:10.1016/s0162-3109(00)00191-0 · Cited by 273

The diverse and expanding role of mass spectrometry in structural and molecular biology

Lössl, P., van de Waterbeemd, M., & Heck, A. J. (2016) · The EMBO Journal · doi:10.15252/embj.201694818 · Cited by 222

Nitric Oxide and Oxidative Stress (H2O2) Control Mammalian Iron Metabolism by Different Pathways

Pantopoulos, K., Weiss, G., & Hentze, M. W. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.7.3781 · Cited by 195

Regulation of Phototropic Signaling in Arabidopsis via Phosphorylation State Changes in the Phototropin 1-interacting Protein NPH3

Pedmale, U. V., & Liscum, E. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702551200 · Cited by 169

Del1 Induces Integrin Signaling and Angiogenesis by Ligation of αVβ3

Penta, K., Varner, J. A., Liaw, L., Hidai, C., Schatzman, R., & Quertermous, T. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.16.11101 · Cited by 153

Bcl-xL Augmentation Potentially Reduces Ischemia/Reperfusion Induced Proximal and Distal Tubular Apoptosis and Autophagy

Chien, C.-T., Shyue, S.-K., & Lai, M.-K. (2007) · Transplantation · doi:10.1097/01.tp.0000287334.38933.e3 · Cited by 138

AURKA is one of the downstream targets of MAPK1/ERK2 in pancreatic cancer

Furukawa, T., Kanai, N., Shiwaku, H. O., Soga, N., Uehara, A., & Horii, A. (2006) · Oncogene · doi:10.1038/sj.onc.1209494 · Cited by 135

Inhibition of cytokines and JAK-STAT activation by distinct signaling pathways.

Sengupta, T. K., Schmitt, E. M., & Ivashkiv, L. B. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.18.9499 · Cited by 132

Exploring oxidative modifications of tyrosine: An update on mechanisms of formation, advances in analysis and biological consequences

Houée-Lévin, C., Bobrowski, K., Horakova, L., Karademir, B., Schöneich, C., Davies, M. J., & Spickett, C. M. (2015) · Free Radical Research · doi:10.3109/10715762.2015.1007968 · Cited by 126

Non-genomic mechanisms of protein phosphatase 2A (PP2A) regulation in cancer

Kauko, O., & Westermarck, J. (2018) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2018.01.005 · Cited by 111

Double-edged roles of protein tyrosine phosphatase SHP2 in cancer and its inhibitors in clinical trials

Song, Y., Zhao, M., Zhang, H., & Yu, B. (2022) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2021.107966 · Cited by 125

Phosphorylation of activation functions AF‐1 and AF‐2 of RARα and RARγ is indispensable for differentiation of F9 cells upon retinoic acid and cAMP treatment

Taneja, R., Rochette‐Egly, C., Plassat, J., Penna, L., Gaub, M., & Chambon, P. (1997) · The EMBO Journal · doi:10.1093/emboj/16.21.6452 · Cited by 113

Protein phosphatase 2A forms a molecular complex with Shc and regulates Shc tyrosine phosphorylation and downstream mitogenic signaling

Ugi, S., Imamura, T., Ricketts, W., & Olefsky, J. M. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.7.2375-2387.2002 · Cited by 95

Regulation of Interferon-α Responsiveness by the Duration of Janus Kinase Activity

Lee, C.-K., Bluyssen, H. A. R., & Levy, D. E. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.35.21872 · Cited by 87

Structure of the Ca2+-dependent PP2A heterotrimer and insights into Cdc6 dephosphorylation

Wlodarchak, N., Guo, F., Satyshur, K. A., Jiang, L., Jeffrey, P. D., Sun, T., Stanevich, V., Mumby, M. C., & Xing, Y. (2013) · Cell Research · doi:10.1038/cr.2013.77 · Cited by 72

Regulation of rat DOC-2 gene during castration-induced rat ventral prostate degeneration and its growth inhibitory function in human prostatic carcinoma cells

Tseng, C.-P., Ely, B. D., Li, Y., Pong, R.-C., & Hsieh, J.-T. (1998) · Endocrinology · doi:10.1210/endo.139.8.6159 · Cited by 74

Mass Spectrometry Based Immunopeptidomics Leads to Robust Predictions of Phosphorylated HLA Class I Ligands

Solleder, M., Guillaume, P., Racle, J., Michaux, J., Pak, H.-S., Müller, M., Coukos, G., Bassani-Sternberg, M., & Gfeller, D. (2020) · Molecular & Cellular Proteomics · doi:10.1074/mcp.tir119.001641 · Cited by 68

Effect of human papillomavirus type 16 oncogenes on MAP kinase activity

Gu, Z., & Matlashewski, G. (1995) · Journal of Virology · doi:10.1128/jvi.69.12.8051-8056.1995 · Cited by 62

Label-free quantitative phosphoproteomics with novel pairwise abundance normalization reveals synergistic RAS and CIP2A signaling

Kauko, O., Laajala, T. D., Jumppanen, M., Hintsanen, P., Suni, V., Haapaniemi, P., Corthals, G., Aittokallio, T., Westermarck, J., & Imanishi, S. Y. (2015) · Scientific Reports · doi:10.1038/srep13099 · Cited by 61

Mass spectrometric analysis of protein tyrosine nitration in aging and neurodegenerative diseases

Yeo, W., Kim, Y. J., Kabir, M. H., Kang, J. W., & Kim, K. P. (2015) · Mass Spectrometry Reviews · doi:10.1002/mas.21429 · Cited by 61

Prognostic Significance of Activated AKT Expression in Soft-Tissue Sarcoma

Tomita, Y., Morooka, T., Hoshida, Y., Zhang, B., Qiu, Y., Nakamichi, I., Hamada, K.-I., Ueda, T., Naka, N., Kudawara, I., et al. (2006) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-05-1732 · Cited by 59

Activation of c-Raf Kinase by Ultraviolet Light

Hoyos, B., Imam, A., Korichneva, I., Levi, E., Chua, R., & Hammerling, U. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110750200 · Cited by 55

Clinical protein science in translational medicine targeting malignant melanoma

Gil, J., Betancourt, L. H., Pla, I., Sanchez, A., Appelqvist, R., Miliotis, T., Kuras, M., Oskolas, H., Kim, Y., Horvath, Z., et al. (2019) · Cell Biology and Toxicology · doi:10.1007/s10565-019-09468-6 · Cited by 45

Molecular determinants for PP2A substrate specificity: Charged residues mediate dephosphorylation of tyrosine hydroxylase by the PP2A/B' regulatory subunit

Saraf, A., Oberg, E. A., & Strack, S. (2010) · Biochemistry · doi:10.1021/bi902160t · Cited by 45

PU.1 is a lineage-specific regulator of tyrosine phosphatase CD45

Anderson, K. L., Nelson, S. L., Perkin, H. B., Smith, K. A., Klemsz, M. J., & Torbett, B. E. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009133200 · Cited by 32

Corticotropin-releasing hormone stimulates SGK-1 kinase expression in cultured hippocampal neurons via CRH-R1

Sheng, H., Sun, T., Cong, B., He, P., Zhang, Y., Yan, J., Lu, C., & Ni, X. (2008) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90462.2008 · Cited by 21

Radiosensitization of Tumor Cells by Modulation of ATM Kinase

Choi, E. K., Ji, I. M., Lee, S. R., Kook, Y. H., Griffin, R. J., Lim, B. U., Kim, J.-S., Lee, D. S., Song, C. W., & Park, H. J. (2006) · International Journal of Radiation Biology · doi:10.1080/09553000600702346 · Cited by 19

Rapid alterations in cortical protein profiles underlie spontaneous sleep and wake bouts

Vazquez, J., Hall, S. C., Witkowska, H. E., & Greco, M. A. (2008) · Journal of Cellular Biochemistry · doi:10.1002/jcb.21970 · Cited by 18

Assessing the relation between protein phosphorylation, AlphaFold3 models, and conformational variability

Ramasamy, P., Zuallaert, J., Martens, L., & Vranken, W. F. (2026) · Protein Science · doi:10.1002/pro.70376 · Cited by 15

Sequence – dynamics – function relationships in protein tyrosine phosphatases

Crean, R. M., Corbella, M., Calixto, A. R., Hengge, A. C., & Kamerlin, S. C. L. (2024) · QRB Discovery · doi:10.1017/qrd.2024.3 · Cited by 12

Developmental and light regulation of tumor suppressor protein PP2A in the retina

Rajala, A., Wang, Y., Abcouwer, S. F., Gardner, T. W., & Rajala, R. V. S. (2018) · Oncotarget · doi:10.18632/oncotarget.23351 · Cited by 7