Structural mechanism of demethylation and inactivation of protein phosphatase 2A

[20] Processing of X-ray diffraction data collected in oscillation mode

Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475 · see citing works

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse‐Kunstleve, R. W., Jiang, J., Kuszewski, J. J., Nilges, M., Pannu, N., et al. (1998) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998003254 · Cited by 15,720 · see citing works

Improved methods for building protein models in electron density maps and the location of errors in these models

Jones, T. A., Zou, J.-Y., Cowan, S. W., & Kjeldgaard, M. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767390010224 · Cited by 12,650 · see citing works

Automated protein model building combined with iterative structure refinement.

Perrakis, A., Morris, R. J., & Lamzin, V. S. (1999) · Nature Structural Biology · doi:10.1038/8263 · Cited by 2,423 · see citing works

Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling

Janssens, V., & Goris, J. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3530417 · Cited by 1,890 · see citing works

Likelihood-enhanced fast translation functions

McCoy, A. J., Grosse‐Kunstleve, R. W., Storoni, L. C., & Read, R. J. (2005) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444905001617 · Cited by 1,641 · see citing works

Macromolecular TLS Refinement in REFMAC at Moderate Resolutions

Winn, M., Murshudov, G. N., & Papiz, M. Z. (2003) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(03)74014-2 · Cited by 804 · see citing works

Contributions of protein phosphatases PP1, PP2A, PP2B and PP5 to the regulation of tau phosphorylation

Liu, F., Grundke‐Iqbal, I., Iqbal, K., & Gong, C. (2005) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2005.04391.x · Cited by 759 · see citing works

Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme

Cho, U. S., & Xu, W. (2007) · Nature · doi:10.1038/nature05351 · Cited by 459 · see citing works

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 · see citing works

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 · see citing works

PP2A: the expected tumor suppressor

Janssens, V., Goris, J., & Van Hoof, C. (2005) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2004.12.004 · Cited by 426 · see citing works

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 · see citing works

Protein phosphatase 2A: a panoply of enzymes

Virshup, D. M. (2000) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(99)00074-5 · Cited by 330 · see citing works

Involvement of PP2A in viral and cellular transformation

Arroyo, J. D., & Hahn, W. C. (2005) · Oncogene · doi:10.1038/sj.onc.1209038 · Cited by 237 · see citing works

Carboxyl methylation regulates phosphoprotein phosphatase 2A by controlling the association of regulatory B subunits

Tolstykh, T., Lee, J., Vafai, S. B., & Stock, J. B. (2000) · The EMBO Journal · doi:10.1093/emboj/19.21.5682 · Cited by 233 · see citing works

Protein phosphatase 2A methyltransferase links homocysteine metabolism with tau and amyloid precursor protein regulation

Sontag, E., Nunbhakdi-Craig, V., Sontag, J.-M., Diaz-Arrastia, R., Ogris, E., Dayal, S., Lentz, S. R., Arning, E., & Bottiglieri, T. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.3316-06.2007 · Cited by 225 · see citing works

Protein phosphatase 2A: variety of forms and diversity of functions.

Lechward, K. A., Awotunde, O. S., Swiatek, W., & Muszyńska, G. (2001) · Acta Biochimica Polonica · doi:10.18388/abp.2001_3858 · Cited by 204 · see citing works

Downregulation of Protein Phosphatase 2A Carboxyl Methylation and Methyltransferase May Contribute to Alzheimer Disease Pathogenesis

Sontag, E., Hladik, C. L., Montgomery, L. G., Luangpirom, A., Mudrak, I., Ogris, E., & White, C. L. (2004) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/63.10.1080 · Cited by 191 · see citing works

A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A

Ogris, E., Du, X., Nelson, K. C., Mak, E. K., Yu, X. X., Lane, W. S., & Pallas, D. C. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.20.14382 · Cited by 191 · see citing works

Protein phosphatase 2A catalytic subunit is methyl-esterified at its carboxyl terminus by a novel methyltransferase.

Lee, J., & Stock, J. B. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)36497-x · Cited by 189 · see citing works

Role of serine/threonine protein phosphatase 2A in cancer

Schönthal, A. H. (2001) · Cancer Letters · doi:10.1016/s0304-3835(01)00561-4 · Cited by 186 · see citing works

Carboxyl methylation of the phosphoprotein phosphatase 2A catalytic subunit promotes its functional association with regulatory subunits in vivo

Wu, J., Tolstykh, T., Lee, J., Boyd, K., Stock, J. B., & Broach, J. R. (2000) · The EMBO Journal · doi:10.1093/emboj/19.21.5672 · Cited by 186 · see citing works

Selection of protein phosphatase 2A regulatory subunits is mediated by the C terminus of the catalytic Subunit

Longin, S., Zwaenepoel, K., Louis, J. V., Dilworth, S., Goris, J., & Janssens, V. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704059200 · Cited by 184 · see citing works

Methylated C-terminal leucine residue of PP2A catalytic subunit is important for binding of regulatory Bα subunit

BRYANT, J. C., Westphal, R. S., & Wadzinski, B. E. (1999) · Biochemical Journal · doi:10.1042/bj3390241 · Cited by 173 · see citing works

Methylation of the Protein Phosphatase 2A Catalytic Subunit Is Essential for Association of Bα Regulatory Subunit But Not SG2NA, Striatin, or Polyomavirus Middle Tumor Antigen

Yu, X. X., Du, X., Moreno, C. S., Green, R. E., Ogris, E., Feng, Q., Chou, L., McQuoid, M. J., & Pallas, D. C. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.1.185 · Cited by 160 · see citing works

The PP2A-Associated Protein α4 Is an Essential Inhibitor of Apoptosis

Kong, M., Fox, C. J., Mu, J., Solt, L., Xu, A., Cinalli, R. M., Birnbaum, M. J., Lindsten, T., & Thompson, C. B. (2004) · Science · doi:10.1126/science.1100537 · Cited by 149 · see citing works

Differential methylation and altered conformation of cytoplasmic and nuclear forms of protein phosphatase 2A during cell cycle progression.

Turowski, P., Fernandez, A., Favre, B., Lamb, N. J. C., & Hemmings, B. A. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.129.2.397 · Cited by 147 · see citing works

Purification of Porcine Brain Protein Phosphatase 2A Leucine Carboxyl Methyltransferase and Cloning of the Human Homologue,

BAERE, I. D., Derua, R., Janssens, V., Hoof, C. A. V., Waelkens, E., Merlevede, W. J., & Goris, J. (1999) · Biochemistry · doi:10.1021/bi991646a · Cited by 145 · see citing works

Molecular model of the A subunit of protein phosphatase 2A: interaction with other subunits and tumor antigens

Ruediger, R., Hentz, M., Fait, J., Mumby, M. C., & Walter, G. (1994) · Journal of Virology · doi:10.1128/jvi.68.1.123-129.1994 · Cited by 142 · see citing works

A specific protein carboxyl methylesterase that demethylates phosphoprotein phosphatase 2A in bovine brain.

Lee, J., Chen, Y., Tolstykh, T., & Stock, J. B. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.12.6043 · Cited by 138 · see citing works

Identification of Binding Sites on the Regulatory A Subunit of Protein Phosphatase 2A for the Catalytic C Subunit and for Tumor Antigens of Simian Virus 40 and Polyomavirus

Ruediger, R., Roeckel, D., Fait, J., Bergqvist, A., Magnusson, G., & Walter, G. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.11.4872 · Cited by 136 · see citing works

Protein phosphatase 2A subunit assembly: The catalytic subunit carboxy terminus is important for binding cellular B subunit but not polyomavirus middle tumor antigen

Ogris, E., Gibson, D. M., & Pallas, D. C. (1997) · Oncogene · doi:10.1038/sj.onc.1201259 · Cited by 134 · see citing works

Protein phosphatase 2A methylation: a link between elevated plasma homocysteine and Alzheimer's Disease

Vafai, S. B., & Stock, J. B. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02702-3 · Cited by 129 · see citing works

Carboxymethylation of the PP2A Catalytic Subunit in Saccharomyces cerevisiae Is Required for Efficient Interaction with the B-type Subunits Cdc55p and Rts1p

Wei, H., Ashby, D. G., Moreno, C. S., Ogris, E., Yeong, F. M., Corbett, A. H., & Pallas, D. C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008694200 · Cited by 128 · see citing works

Structural Basis of PP2A Inhibition by Small t Antigen

Cho, U., Morrone, S. R., Sablina, A. A., Arroyo, J. D., Hahn, W. C., & Xu, W. (2007) · PLoS Biology · doi:10.1371/journal.pbio.0050202 · Cited by 124 · see citing works

Protein phosphatase 2A is reversibly modified by methyl esterification at its C-terminal leucine residue in bovine brain.

Xie, H., & Clarke, S. G. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42124-7 · Cited by 123 · see citing works

A novel and essential mechanism determining specificity and activity of protein phosphatase 2A (PP2A) in vivoPreprint

Fellner, T., Lackner, D. H., Hombauer, H., Piribauer, P., Mudrak, I., Zaragoza, K., Juno, C., & Ogris, E. (2003) · Genes & Development · doi:10.1101/gad.259903 · Cited by 105 · see citing works

An inactive protein phosphatase 2A population is associated with methylesterase and can be re-activated by the phosphotyrosyl phosphatase activator

Longin, S., Jordens, J., MARTENS, E., Stevens, I., Janssens, V., Rondelez, E., BAERE, I. D., Derua, R., Waelkens, E., Goris, J., et al. (2004) · Biochemical Journal · doi:10.1042/bj20031643 · Cited by 101 · see citing works

Crystallographic structure analysis of lamprey hemoglobin from anomalous dispersion of synchrotron radiation

Hendrickson, W. A., Smith, J. L., Phizackerley, R. P., & Merritt, E. A. (1988) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340040202 · Cited by 93 · see citing works

Mutation of Tyr307 and Leu309 in the Protein Phosphatase 2A Catalytic Subunit Favors Association with the α4 Subunit Which Promotes Dephosphorylation of Elongation Factor-2

Chung, H., Nairn, A. C., Murata, K., & Brautigan, D. L. (1999) · Biochemistry · doi:10.1021/bi990902g · Cited by 90 · see citing works

Generation of Active Protein Phosphatase 2A Is Coupled to Holoenzyme Assembly

Hombauer, H., Weismann, D., Mudrak, I., Stanzel, C., Fellner, T., Lackner, D. H., & Ogris, E. (2007) · PLoS Biology · doi:10.1371/journal.pbio.0050155 · Cited by 88 · see citing works

Structural and biochemical insights into the regulation of protein phosphatase 2A by small t antigen of SV40

Chen, Y., Xu, Y., Bao, Q., Xing, Y., Li, Z., Lin, Z., Stock, J. B., Jeffrey, P. D., & Shi, Y. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1254 · Cited by 84 · see citing works

PP2A fulfills its promises as tumor suppressor

HOOF, C. V., & Goris, J. (2004) · Cancer Cell · doi:10.1016/s1535-6108(04)00027-3 · Cited by 76 · see citing works

Leucine carboxyl methyltransferase-1 is necessary for normal progression through mitosis in mammalian cells

Lee, J. A., & Pallas, D. C. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704861200 · Cited by 69 · see citing works

Methyl esterification of C-terminal leucine residues in cytosolic 36-kDa polypeptides of bovine brain. A novel eucaryotic protein carboxyl methylation reaction

Xie, H., & Clarke, S. G. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38660-0 · Cited by 64 · see citing works

Spatial control of protein phosphatase 2A (de)methylation

Longin, S., Zwaenepoel, K., Martens, E., Louis, J. V., Rondelez, E., Goris, J., & Janssens, V. (2007) · Experimental Cell Research · doi:10.1016/j.yexcr.2007.07.030 · Cited by 58 · see citing works

Carboxymethylation of nuclear protein serine/threonine phosphatase X

Kloeker, S., BRYANT, C. J., Strack, S., Colbran, R. J., & WADZINSKI, E. B. (1997) · Biochemical Journal · doi:10.1042/bj3270481 · Cited by 52 · see citing works

An Enzymatic Activity in Bovine Brain That Catalyzes the Reversal of the C-Terminal Methyl Esterification of Protein Phosphatase 2A

Xie, H., & Clarke, S. G. (1994) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1994.2383 · Cited by 36 · see citing works

Methylation of the C-terminal leucine residue of the PP2A catalytic subunit is unnecessary for the catalytic activity and the binding of regulatory subunit (PR55/B)

Ikehara, T., Ikehara, S., Imamura, S., Shinjo, F., & Yasumoto, T. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.01.085 · Cited by 33 · see citing works

A New Role for Protein Methylation: Switching Partners at the Phosphatase Ball

Mumby, M. C. (2001) · Science Signaling · doi:10.1126/stke.2001.79.pe1 · Cited by 30 · see citing works

PP2A as a mercenary for warring kinases in the egg

Yu, H. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0708582104 · Cited by 3 · see citing works

Serine/threonine phosphatases: mechanism through structure

Shi, Y. (2009) · Cell · doi:10.1016/j.cell.2009.10.006 · Cited by 1,488 · see citing works

From Promiscuity to Precision: Protein Phosphatases Get a Makeover

Virshup, D. M., & Shenolikar, S. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.02.015 · Cited by 643 · see citing works

The Metabolic Serine Hydrolases and Their Functions in Mammalian Physiology and Disease

Long, J. Z., & Cravatt, B. F. (2011) · Chemical Reviews · doi:10.1021/cr200075y · Cited by 422 · see citing works

PP2A as a master regulator of the cell cycle

Wlodarchak, N., & Xing, Y. (2016) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2016.1143913 · Cited by 366 · see citing works

The PP1 binding code: a molecular‐lego strategy that governs specificity

Heroes, E., Lesage, B., Görnemann, J., Beullens, M., Meervelt, L. V., & Bollen, M. (2012) · FEBS Journal · doi:10.1111/j.1742-4658.2012.08547.x · Cited by 318 · see citing works

All roads lead to <scp>PP</scp>2A: exploiting the therapeutic potential of this phosphatase

Sangodkar, J., Farrington, C. C., McClinch, K., Galsky, M. D., Kastrinsky, D. B., & Narla, G. (2016) · The FEBS Journal · doi:10.1111/febs.13573 · Cited by 312 · see citing works

Protein phosphatase 2A dysfunction in Alzheimer’s disease

Sontag, J.-M., & Sontag, E. (2014) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2014.00016 · Cited by 304 · see citing works

Structure of a Protein Phosphatase 2A Holoenzyme: Insights into B55-Mediated Tau Dephosphorylation

Xu, Y., Chen, Y., Zhang, P., Jeffrey, P. D., & Shi, Y. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.08.006 · Cited by 285 · see citing works

Sodium selenate mitigates tau pathology, neurodegeneration, and functional deficits in Alzheimer’s disease models

van Eersel, J., Ke, Y. D., Liu, X., Delerue, F., Kril, J. J., Götz, J., & Ittner, L. M. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1009038107 · Cited by 284 · see citing works

An integrated workflow for charting the human interaction proteome: insights into the PP2A system

Glatter, T., Wepf, A., Aebersold, R. H., & Gstaiger, M. (2009) · Molecular Systems Biology · doi:10.1038/msb.2008.75 · Cited by 259 · see citing works

Chemical probes and drug leads from advances in synthetic planning and methodology

Gerry, C. J., & Schreiber, S. L. (2018) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2018.53 · Cited by 228 · see citing works

Age-related changes in AMPK activation: Role for AMPK phosphatases and inhibitory phosphorylation by upstream signaling pathways

Salminen, A., Kaarniranta, K., & Kauppinen, A. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.04.003 · Cited by 206 · see citing works

Recent advances in activity-based probes (ABPs) and affinity-based probes (A f BPs) for profiling of enzymes

Fang, H., Peng, B., Ong, S. Y., Wu, Q., Li, L., & Yao, S. Q. (2021) · Chemical Science · doi:10.1039/d1sc01359a · Cited by 210 · see citing works

The biogenesis of active protein phosphatase 2A holoenzymes: a tightly regulated process creating phosphatase specificity

Sents, W., Ivanova, E., Lambrecht, C., Haesen, D., & Janssens, V. (2013) · The FEBS Journal · doi:10.1111/j.1742-4658.2012.08579.x · Cited by 204 · see citing works

Therapeutic targeting of PP2A

O’Connor, C. M., Perl, A. L., Léonard, D., Sangodkar, J., & Narla, G. (2017) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2017.10.008 · Cited by 181 · see citing works

Enhanced Phosphatase Activity Attenuates α-Synucleinopathy in a Mouse Model

Lee, K.-W., Chen, W. W., Junn, E., Im, J., Grosso, H., Sonsalla, P. K., Feng, X., Ray, N., Fernandez, J. R., Chao, Y., et al. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.6513-10.2011 · Cited by 184 · see citing works

α4 Is an Essential Regulator of PP2A Phosphatase Activity

Kong, M., Ditsworth, D., Lindsten, T., & Thompson, C. B. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.09.025 · Cited by 162 · see citing works

Quantitative interaction proteomics using mass spectrometry

Wepf, A., Glatter, T., Schmidt, A., Aebersold, R. H., & Gstaiger, M. (2009) · Nature Methods · doi:10.1038/nmeth.1302 · Cited by 151 · see citing works

The structural basis for tight control of PP2A methylation and function by LCMT-1

Stanevich, V., Jiang, L., Satyshur, K. A., Li, Y., Jeffrey, P. D., Li, Z., Menden, P., Semmelhack, M. F., & Xing, Y. (2011) · Molecular Cell · doi:10.1016/j.molcel.2010.12.030 · Cited by 142 · see citing works

S-Adenosyl Methionine and Transmethylation Pathways in Neuropsychiatric Diseases Throughout Life

Gao, J., Cahill, C. M., Huang, X., Roffman, J. L., Lamon‐Fava, S., D, M. F. M., Mischoulon, D., & Rogers, J. T. (2018) · Neurotherapeutics · doi:10.1007/s13311-017-0593-0 · Cited by 138 · see citing works

The metabolic advantage of tumor cells

Israël, M., & Schwartz, L. H. (2011) · Molecular Cancer · doi:10.1186/1476-4598-10-70 · Cited by 125 · see citing works

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

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

Phosphoprotein Phosphatase 2A: A Novel Druggable Target for Alzheimer’s Disease

Voronkov, M. V., Braithwaite, S. P., & Stock, J. B. (2011) · Future Medicinal Chemistry · doi:10.4155/fmc.11.47 · Cited by 121 · see citing works

Homocysteine-methionine cycle is a metabolic sensor system controlling methylation-regulated pathological signaling

Shen, W., Gao, C., Cueto, R., Liu, L., Fu, H., Shao, Y., Yang, W. Y., Fang, P., Choi, E. T., Wu, Q., et al. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101322 · Cited by 112 · see citing works

Academic cross-fertilization by public screening yields a remarkable class of protein phosphatase methylesterase-1 inhibitors

Bachovchin, D. A., Mohr, J. T., Speers, A. E., Wang, C., Berlin, J. M., Spicer, T., Fernández-Vega, V., Chase, P. S., Hodder, P., Schürer, S. C., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1015248108 · Cited by 108 · see citing works

Structural basis of PP2A activation by PTPA, an ATP-dependent activation chaperone

Guo, F., Stanevich, V., Wlodarchak, N., Sengupta, R., Jiang, L., Satyshur, K. A., & Xing, Y. (2014) · Cell Research · doi:10.1038/cr.2013.138 · Cited by 100 · see citing works

Untangling Tau and Iron: Exploring the Interaction Between Iron and Tau in Neurodegeneration

Rao, S. S., & Adlard, P. A. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00276 · Cited by 105 · see citing works

Proteomic Analysis of Hepatic Tissue of Zebrafish (Danio rerio) Experimentally Exposed to Chronic Microcystin-LR

Wang, M., Chan, L. L., Si, M., Hong, H., & Wang, D. (2009) · Toxicological Sciences · doi:10.1093/toxsci/kfp248 · Cited by 98 · see citing works

Chemical Proteomic Profiling of Human Methyltransferases

Horning, B. D., Suciu, R. M., Ghadiri, D. A., Ulanovskaya, O. A., Matthews, M. L., Lum, K. M., Backus, K. M., Brown, S. J., Rosen, H., & Cravatt, B. F. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b07830 · Cited by 97 · see citing works

Protein Phosphatase 2A in the Regulatory Network Underlying Biotic Stress Resistance in Plants

Durian, G., Rahikainen, M. M., Alegre, S., Brosché, M., & Kangasjärvi, S. (2016) · Frontiers in Plant Science · doi:10.3389/fpls.2016.00812 · Cited by 96 · see citing works

PME-1 Protects Extracellular Signal-Regulated Kinase Pathway Activity from Protein Phosphatase 2A–Mediated Inactivation in Human Malignant Glioma

Puustinen, P., Junttila, M. R., Vanhatupa, S., Sablina, A. A., Hector-Greene, M., Teittinen, K. J., Raheem, O., Ketola, K., Lin, S., Kast, J., et al. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-2760 · Cited by 95 · see citing works

PP2A holoenzymes, substrate specificity driving cellular functions and deregulation in cancer

(2019) · Advances in Cancer Research · doi:10.1016/bs.acr.2019.03.009 · Cited by 93 · see citing works

Protein phosphatases PP 2A, PP 4 and PP 6: mediators and regulators in development and responses to environmental cues

Lillo, C., Kataya, A. R. A., HEIDARI, B., Creighton, M. T., Nemie-Feyissa, D., Ginbot, Z., & Jonassen, E. M. (2014) · Plant Cell & Environment · doi:10.1111/pce.12364 · Cited by 84 · see citing works

Crystal structure of a PP2A B56-BubR1 complex and its implications for PP2A substrate recruitment and localization

Wang, J., Wang, Z., Yu, T., Yang, H., Virshup, D. M., Kops, G. J. P. L., Lee, S. H., Zhou, W., Li, X., Xu, W., et al. (2016) · Protein &amp; Cell · doi:10.1007/s13238-016-0283-4 · Cited by 80 · see citing works

Plant protein phosphatases: What do we know about their mechanism of action?

Bheri, M., Mahiwal, S., Sanyal, S. K., & Pandey, G. K. (2020) · FEBS Journal · doi:10.1111/febs.15454 · Cited by 78 · see citing works

Folate Deficiency Induces In Vitro and Mouse Brain Region-Specific Downregulation of Leucine Carboxyl Methyltransferase-1 and Protein Phosphatase 2A Bα Subunit Expression That Correlate with Enhanced Tau Phosphorylation

Sontag, J., Nunbhakdi‐Craig, V., Montgomery, L. G., Arning, E., Bottiglieri, T., & Sontag, E. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.2816-08.2008 · Cited by 77 · see citing works

Protein phosphatase 2A – structure, function and role in neurodevelopmental disorders

Sandal, P., Jong, C. J., Merrill, R. A., Song, J., & Strack, S. (2021) · Journal of Cell Science · doi:10.1242/jcs.248187 · Cited by 72 · see citing works

Antiphospholipid antibodies induce thrombosis by PP2A activation via apoER2-Dab2-SHC1 complex formation in endothelium

Sacharidou, A., Chambliss, K. L., Ulrich, V., Salmon, J. E., Shen, Y.-M. P., Herz, J., Hui, D. Y., Terada, L. S., Shaul, P. W., & Mineo, C. (2018) · Blood · doi:10.1182/blood-2017-11-814681 · Cited by 78 · see citing works

Phosphoproteome and drug-response effects mediated by the three protein phosphatase 2A inhibitor proteins CIP2A, SET, and PME-1

Kauko, O., Imanishi, S. Y., Kulesskiy, E., Yetukuri, L., Laajala, T. D., Sharma, M., Pavic, K., Aakula, A., Rupp, C., Jumppanen, M., et al. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.011265 · Cited by 65 · see citing works

Nitric oxide and protein phosphatase 2A provide novel therapeutic opportunities in ER-negative breast cancer

Switzer, C. H., Glynn, S. A., Ridnour, L. A., Cheng, R. Y.-S., Vitek, M. P., Ambs, S., & Wink, D. A. (2011) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2011.07.001 · Cited by 74 · see citing works

Taurine Antagonizes Macrophages M1 Polarization by Mitophagy-Glycolysis Switch Blockage via Dragging SAM-PP2Ac Transmethylation

Meng, L., Lu, C., Wu, B., Lan, C., Mo, L., Chen, C., Wang, X., Zhang, N., Li, L., Wang, Q., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.648913 · Cited by 75 · see citing works

Discovery and Optimization of Sulfonyl Acrylonitriles as Selective, Covalent Inhibitors of Protein Phosphatase Methylesterase-1

Bachovchin, D. A., Zuhl, A. M., Speers, A. E., Wolfe, M. R., Weerapana, E., Brown, S. J., Rosen, H., & Cravatt, B. F. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm200502u · Cited by 71 · see citing works

NNMT depletion contributes to liver cancer cell survival by enhancing autophagy under nutrient starvation

Shin, J. H., Park, C. W., Yoon, G., Hong, S. M., & Choi, K. Y. (2018) · Oncogenesis · doi:10.1038/s41389-018-0064-4 · Cited by 70 · see citing works

Activation of AMP-activated Protein Kinase Stimulates Na+,K+-ATPase Activity in Skeletal Muscle Cells

Benziane, B., Björnholm, M., Pirkmajer, S., Austin, R. L., Kotova, O., Viollet, B., Zierath, J. R., & Chibalin, A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.331926 · Cited by 66 · see citing works

NNMT contributes to high metastasis of triple negative breast cancer by enhancing PP2A/MEK/ERK/c-Jun/ABCA1 pathway mediated membrane fluidity

Wang, Y., Zhou, X., Lei, Y., Chu, Y., Yu, X., Tong, Q., Zhu, T., Yu, H., Fang, S., Li, G., et al. (2022) · Cancer Letters · doi:10.1016/j.canlet.2022.215884 · Cited by 67 · see citing works

Effects of manganese on tyrosine hydroxylase (TH) activity and TH-phosphorylation in a dopaminergic neural cell line

Zhang, D., Kanthasamy, A., Anantharam, V., & Kanthasamy, A. G. (2011) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2010.03.023 · Cited by 66 · see citing works

FICD activity and AMPylation remodelling modulate human neurogenesis

Kielkowski, P., Buchsbaum, I. Y., Kirsch, V. C., Bach, N. C., Drukker, M., Cappello, S., & Sieber, S. A. (2020) · Nature Communications · doi:10.1038/s41467-019-14235-6 · Cited by 65 · see citing works

Regulation of the phosphoprotein phosphatase 2A system and its modulation during oxidative stress: A potential therapeutic target?

Elgenaidi, I. S., & Spiers, P. (2019) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2019.02.011 · Cited by 65 · see citing works

Interferon-inducible cytoplasmic lncLrrc55-AS promotes antiviral innate responses by strengthening IRF3 phosphorylation

Zhou, Y., Li, M., Xue, Y., Li, Z., Wen, W., Liu, X., Ma, Y., Zhang, L., Shen, Z., & Cao, X. (2019) · Cell Research · doi:10.1038/s41422-019-0193-0 · Cited by 62 · see citing works

PME-1 Modulates Protein Phosphatase 2A Activity to Promote the Malignant Phenotype of Endometrial Cancer Cells

Wandzioch, E., Pusey, M., Werda, A., Bail, S., Bhaskar, A., Nestor, M., Yang, J., & Rice, L. M. (2014) · Cancer Research · doi:10.1158/0008-5472.can-13-3130 · Cited by 62 · see citing works

Potential Role of Epigenetic Mechanism in Manganese Induced Neurotoxicity

Tarale, P., Chakrabarti, T., Sivanesan, S., Naoghare, P. K., Bafana, A., & Krishnamurthi, K. (2016) · BioMed Research International · doi:10.1155/2016/2548792 · Cited by 61 · see citing works

PP2A methylation controls sensitivity and resistance to β-amyloid-induced cognitive and electrophysiological impairments

Nicholls, R. E., Sontag, J.-M., Zhang, H., Staniszewski, A., Yan, S., Kim, C. Y., Yim, M., Woodruff, C. M., Arning, E., Wasek, B., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1521018113 · Cited by 56 · see citing works

Regulation of protein phosphatase 2A methylation by LCMT1 and PME‐1 plays a critical role in differentiation of neuroblastoma cells

Sontag, J., Nunbhakdi‐Craig, V., Mitterhuber, M., Ogris, E., & Sontag, E. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.07049.x · Cited by 57 · see citing works

Biodegradation of polycyclic aromatic hydrocarbons (PAHs) by bacterial mixture

Xu, M., Wu, M., Zhang, Y., Zhang, H., Liu, W., Chen, G., Xiong, G., & Guo, L. (2021) · International Journal of Environmental Science and Technology · doi:10.1007/s13762-021-03284-4 · Cited by 57 · see citing works

Regulation of protein phosphatase 2A (PP2A) tumor suppressor function by PME-1

Kaur, A., & Westermarck, J. K. (2016) · Biochemical Society Transactions · doi:10.1042/bst20160161 · Cited by 53 · see citing works

Assembly and structure of protein phosphatase 2A

Shi, Y. (2009) · Science in China Series C Life Sciences · doi:10.1007/s11427-009-0018-3 · Cited by 55 · see citing works

Neuroprotective effects of donepezil against A β42‐induced neuronal toxicity are mediated through not only enhancing PP 2 A activity but also regulating GSK ‐3β and n AChR s activity

Noh, M., Koh, S. H., Kim, S., Maurice, T., Ku, S., & Kim, S. H. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12319 · Cited by 54 · see citing works

Redox inhibition of protein phosphatase PP2A: Potential implications in oncogenesis and its progression

Raman, D., & Pervaiz, S. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101105 · Cited by 54 · see citing works

Targeted therapies don't work for a reason; the neglected tumor suppressor phosphatase PP 2A strikes back

Westermarck, J. K. (2018) · FEBS Journal · doi:10.1111/febs.14617 · Cited by 49 · see citing works

Prolyl oligopeptidase inhibition activates autophagy via protein phosphatase 2A

Svarcbahs, R., Jäntti, M. H., Kilpeläinen, T. P., Julku, U. H., Urvas, L., Kivioja, S., Norrbacka, S., & Myöhänen, T. T. (2019) · Pharmacological Research · doi:10.1016/j.phrs.2019.104558 · Cited by 50 · see citing works

PP2A Inhibitor PME-1 Drives Kinase Inhibitor Resistance in Glioma Cells

Kaur, A., Denisova, O. V., Qiao, X., Jumppanen, M., Peuhu, E., Ahmed, S. U., Raheem, O., Haapasalo, H. K., Eriksson, J., Chalmers, A. J., et al. (2016) · Cancer Research · doi:10.1158/0008-5472.can-16-1134 · Cited by 47 · see citing works

Downregulation of protein phosphatase 2A by apolipoprotein E: Implications for Alzheimer's disease

Theendakara, V. P., Bredesen, D. E., & Rao, R. V. (2017) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2017.07.002 · Cited by 46 · see citing works

Dithiolethione compounds inhibit Akt signaling in human breast and lung cancer cells by increasing PP2A activity

Switzer, C., Ridnour, L. A., Cheng, R. Y. S., Sparatore, A., Soldato, P. D., Moody, T. W., Vitek, M. P., Roberts, D. D., & Wink, D. A. (2009) · Oncogene · doi:10.1038/onc.2009.244 · Cited by 46 · see citing works

Protein phosphatase 2A (PP2A): a key phosphatase in the progression of chronic obstructive pulmonary disease (COPD) to lung cancer

Nader, C. P., Cidem, A., Verrills, N. M., & Ammit, A. J. (2019) · Respiratory Research · doi:10.1186/s12931-019-1192-x · Cited by 40 · see citing works

Glycogen synthase kinase‐3β regulates leucine‐309 demethylation of protein phosphatase‐2A via PPMT1 and PME‐1

Yao, X., Li, X., Zhang, X., Yin, Y., Liu, B., Luo, D., Wang, Q., Wang, J., & Liu, G. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.06.018 · Cited by 37 · see citing works

Protein Phosphatase Methyl-Esterase PME-1 Protects Protein Phosphatase 2A from Ubiquitin/Proteasome Degradation

Yabe, R., Miura, A., Usui, T., Mudrak, I., Ogris, E., Ohama, T., & Sato, K. (2015) · PLoS ONE · doi:10.1371/journal.pone.0145226 · Cited by 37 · see citing works

Cornel Iridoid Glycoside Inhibits Tau Hyperphosphorylation via Regulating Cross-Talk Between GSK-3β and PP2A Signaling

Yang, C., Li, X., Gao, W., Wang, Q., Zhang, L., Li, Y., Li, L., & Zhang, L. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.00682 · Cited by 36 · see citing works

Biased holoenzyme assembly of protein phosphatase 2A (PP2A): From cancer to small molecules

Haanen, T. J., O’Connor, C. M., & Narla, G. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102656 · Cited by 36 · see citing works

PTPA variants and impaired PP2A activity in early-onset parkinsonism with intellectual disability

Fevga, C., Tesson, C., Mascaro, A. C., Courtin, T., van Coller, R., Sakka, S., Ferraro, F., Farhat, N., Bardien, S., Damak, M., et al. (2022) · Brain · doi:10.1093/brain/awac326 · Cited by 34 · see citing works

Structural Insights into a Novel Esterase from the East Pacific Rise and Its Improved Thermostability by a Semirational Design

Zhu, C., Chen, Y., Isupov, M. N., Littlechild, J. A., Sun, L., Liu, X., Wang, Q., Gong, H., Dong, P., Zhang, N., et al. (2021) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.0c06338 · Cited by 35 · see citing works

Protein phosphatase 2A (PP2A) is increased in old murine B cells and mediates p38 MAPK/tristetraprolin dephosphorylation and E47 mRNA instability

Frasca, D., Romero, M., Landin, A. M., Diaz, A., Riley, R. L., & Blomberg, B. B. (2010) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2010.02.002 · Cited by 35 · see citing works

PP2A: more than a reset switch to activate pRB proteins during the cell cycle and in response to signaling cues

Kurimchak, A., & Graña, X. (2014) · Cell Cycle · doi:10.4161/15384101.2014.985069 · Cited by 33 · see citing works

Beyond Amyloid

Lane, R. F., Shineman, D. W., Steele, J., Lee, L. H., & Fillit, H. M. (2012) · Advances in pharmacology · doi:10.1016/b978-0-12-394816-8.00007-6 · Cited by 33 · see citing works

Knockdown of microRNA-195 contributes to protein phosphatase-2A inactivation in rats with chronic brain hypoperfusion

Liu, C., Wang, Q., Zong, D., Pei, S., Yan, Y., Yan, M., Sun, L., Hao, Y.-Y., Mao, M., Xing, W., et al. (2016) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2016.05.010 · Cited by 32 · see citing works

5‐Aza‐2'‐deoxycytidine reactivates gene expression via degradation of pRb pocket proteins

Zheng, Z., Li, L., Liu, X., Wang, D., Tu, B., Wang, L., Wang, H., & Zhu, W. (2011) · The FASEB Journal · doi:10.1096/fj.11-190025 · Cited by 32 · see citing works

Ca 2+ -dependent demethylation of phosphatase PP2Ac promotes glucose deprivation–induced cell death independently of inhibiting glycolysis

Lee, H. Y., Itahana, Y., Schüchner, S., Fukuda, M., Je, H. S., Ogris, E., Virshup, D. M., & Itahana, K. (2018) · Science Signaling · doi:10.1126/scisignal.aam7893 · Cited by 31 · see citing works

Crystal Structure of a Novel Esterase Rv0045c from Mycobacterium tuberculosis

Zheng, X., Guo, J., Xu, L., Li, H., Zhang, D., Zhang, K., Sun, F., Wen, T., Liu, S., & Pang, H. (2011) · PLoS ONE · doi:10.1371/journal.pone.0020506 · Cited by 29 · see citing works

Cognitive Enhancers (Nootropics). Part 3: Drugs Interacting with Targets other than Receptors or Enzymes. Disease-modifying Drugs

Froestl, W., Pfeifer, A., & Muhs, A. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-121729 · Cited by 27 · see citing works

Regulation and role of the PP2A-B56 holoenzyme family in cancer

Peris, I., Romero-Murillo, S., Vicente, C., Narla, G., & Odero, M. D. (2023) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2023.188953 · Cited by 29 · see citing works

Regulation of PP2A, PP4, and PP6 holoenzyme assembly by carboxyl-terminal methylation

Lyons, S. P., Greiner, E. C., Cressey, L. E., Adamo, M. E., & Kettenbach, A. N. (2021) · Scientific Reports · doi:10.1038/s41598-021-02456-z · Cited by 27 · see citing works

Genetic amplification ofPPME1in gastric and lung cancer and its potential as a novel therapeutic target

Li, J., Han, S., Qian, Z., Su, X., Fan, S., Fu, J., Liu, Y., Yin, X., Gao, Z., Zhang, J., et al. (2013) · Cancer Biology & Therapy · doi:10.4161/cbt.27146 · Cited by 26 · see citing works

PP2A and Its Inhibitors in Helper T-Cell Differentiation and Autoimmunity

Khan, M. M., Ullah, U., Khan, M. H., & Lahesmaa, R. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2021.786857 · Cited by 25 · see citing works

F-box Protein FBXL16 Binds PP2A-B55α and Regulates Differentiation of Embryonic Stem Cells along the FLK1+ Lineage

Honarpour, N., Rose, C. M., Brumbaugh, J., Anderson, J., Graham, R. L. J., Sweredoski, M. J., Hess, S. Y., Coon, J. J., & Deshaies, R. J. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.031765 · Cited by 25 · see citing works

A stable association with PME ‐1 may be dispensable for PP 2A demethylation – implications for the detection of PP 2A methylation and immunoprecipitation

Yabe, R., Tsuji, S., Mochida, S., Ikehara, T., Usui, T., Ohama, T., & Sato, K. (2018) · FEBS Open Bio · doi:10.1002/2211-5463.12485 · Cited by 25 · see citing works

Mechanisms regulating phosphatase specificity and the removal of individual phosphorylation sites during mitotic exit

Rogers, S., McCloy, R. A., Watkins, D. N., & Burgess, A. (2016) · BioEssays · doi:10.1002/bies.201670905 · Cited by 24 · see citing works

PP2A Phosphatases Take a Giant Leap in the Post-Genomics Era

Bheri, M., & Pandey, G. K. (2019) · Current Genomics · doi:10.2174/1389202920666190517110605 · Cited by 24 · see citing works

Protein Phosphatase 2A Activation Via ApoER2 in Trophoblasts Drives Preeclampsia in a Mouse Model of the Antiphospholipid Syndrome

Chu, H., Sacharidou, A., Nguyen, A. L., Li, C., Chambliss, K. L., Salmon, J. E., Shen, Y.-M., Lo, J. Y., Leone, G. W., Herz, J., et al. (2021) · Circulation Research · doi:10.1161/circresaha.120.318941 · Cited by 23 · see citing works

Microcystin-LR inhibited hippocampal long-term potential via regulation of the glycogen synthase kinase-3β pathway

Wang, J., Lin, F., Cai, F., Yan, W., Zhou, Q., & Xie, L. (2013) · Chemosphere · doi:10.1016/j.chemosphere.2013.04.069 · Cited by 24 · see citing works

Methylation of protein phosphatase 2A—Influence of regulators and environmental stress factors

Creighton, M. T., Kołton, A., Kataya, A. R. A., Maple‐Grødem, J., Averkina, I. O., Heidari, B., & Lillo, C. (2017) · Plant Cell & Environment · doi:10.1111/pce.13038 · Cited by 23 · see citing works

Pleiotropy of PP2A Phosphatases in Cancer with a Focus on Glioblastoma IDH Wildtype

Kashani, E., & Vassella, E. (2022) · Cancers · doi:10.3390/cancers14215227 · Cited by 22 · see citing works

Phosphoinositide 3-Kinase γ Inhibits Cardiac GSK-3 Independently of Akt

Mohan, M. L., Jha, B. K., Gupta, M. K., Vasudevan, N. T., Martelli, E. E., Mosinski, J. D., & Prasad, S. V. N. (2013) · Science Signaling · doi:10.1126/scisignal.2003308 · Cited by 22 · see citing works

Crystal structure of the human Tip41 orthologue, TIPRL, reveals a novel fold and a binding site for the PP2Ac C-terminus

Scorsato, V., Lima, T. B., Righetto, G. L., Zanchin, N. I. T., Brandão-Neto, J., Sandy, J., Pereira, H. M., Ferrari, A., Gozzo, F. C., Smetana, J. H. C., et al. (2016) · Scientific Reports · doi:10.1038/srep30813 · Cited by 23 · see citing works

Understanding the regulatory landscape of protein phosphatase 2A (PP2A): Pharmacological modulators and potential therapeutics

Neale, D. B., Morris, J. C., Verrills, N. M., & Ammit, A. J. (2025) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2025.108834 · Cited by 24 · see citing works

Microcystin-LR and its health impacts: Chemistry, transmission routes, mechanisms of toxicity and target organs

Rajpoot, R., Rajput, S., & Koiri, R. K. (2025) · Toxicology Reports · doi:10.1016/j.toxrep.2025.101996 · Cited by 22 · see citing works

Cytoplasmic SET induces tau hyperphosphorylation through a decrease of methylated phosphatase 2A

Chasseigneaux, S., Clamagirand, C., Huguet, L., Gorisse-Hussonnois, L., Rose, C., & Allinquant, B. (2014) · BMC Neuroscience · doi:10.1186/1471-2202-15-82 · Cited by 22 · see citing works

Hyperphosphorylation of autoantigenic targets of paraproteins is due to inactivation of PP2A

Preuss, K., Pfreundschuh, M. G., Fadle, N., Regitz, E., Raudies, S., Murwaski, N., Ahlgrimm, M., Bittenbring, J. T., Klotz, M., Schäfer, K., et al. (2011) · Blood · doi:10.1182/blood-2011-04-351668 · Cited by 22 · see citing works

PP2A-B55 Holoenzyme Regulation and Cancer

Goguet-Rubio, P., Amin, P., Awal, S., Vigneron, S., Charrasse, S., Méchali, F., Labbé, J. C., Lorca, T., & Castro, A. (2020) · Biomolecules · doi:10.3390/biom10111586 · Cited by 21 · see citing works

Single‐residue posttranslational modification sites at the N‐terminus, C‐terminus or in‐between: To be or not to be exposed for enzyme access

Sirota, F. L., Maurer‐Stroh, S., Eisenhaber, B., & Eisenhaber, F. (2015) · PROTEOMICS · doi:10.1002/pmic.201400633 · Cited by 20 · see citing works

The unusual extended C-terminal helix of the peroxisomal α/β-hydrolase Lpx1 is involved in dimer contacts but dispensable for dimerization

Thoms, S., Hofhuis, J., Thöing, C., Gärtner, J., & Niemann, H. H. (2011) · Journal of Structural Biology · doi:10.1016/j.jsb.2011.06.008 · Cited by 21 · see citing works

Relevance Rank Platform (RRP) for Functional Filtering of High Content Protein–Protein Interaction Data*

Pokharel, Y. R., Saarela, J., Szwajda, A., Rupp, C., Rokka, A., Karna, S. K. L., Teittinen, K. J., Corthals, G. L., Kallioniemi, O., Wennerberg, K., et al. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m115.050773 · Cited by 21 · see citing works

11 Reversible methylation of protein phosphatase 2A

Longin, S., & Goris, J. (2006) · The Enzymes · doi:10.1016/s1874-6047(06)80013-2 · Cited by 8 · see citing works

A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A

Ogris, E., Du, X., Nelson, K. C., Mak, E. K., Yu, X. X., Lane, W. S., & Pallas, D. C. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.20.14382 · Cited by 191 · see citing works

Cryo-EM and cellular dissection uncover versatile PME-1 activities in PP2A holoenzyme demethylation and inhibitionPreprint

Xing, Y., Li, Y., Rowse, M., Wu, C.-G., Bravos, A. P., Ivarsson, Y., & Strack, S. (2021) · Research Square · doi:10.21203/rs.3.rs-372534/v1

Structural insights into tight control of PP2A methylation and function by LCMT‐1

Stanevich, V., Jiang, L., Satyshur, K. A., Li, Y., Jeffrey, P. D., Li, Z., Menden, P., Semmelhack, M. F., & Xing, Y. (2013) · The FASEB Journal · doi:10.1096/fasebj.27.1_supplement.1043.6

Structural investigation of human PP2A regulation by protein methylation

Tsai, M.-L. (2010) · UCL Discovery (University College London)