A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex linked to the cerebral cavernous malformation 3 (CCM3) protein

Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search.

Keller, A., Nesvizhskii, A., Kolker, E., & Aebersold, R. (2002) · Analytical Chemistry · doi:10.1021/ac025747h · Cited by 4,970 · see citing works

A statistical model for identifying proteins by tandem mass spectrometry.

Nesvizhskii, A., Keller, A., Kolker, E., & Aebersold, R. (2003) · Analytical Chemistry · doi:10.1021/ac0341261 · Cited by 4,902 · see citing works

Functional organization of the yeast proteome by systematic analysis of protein complexes

Gavin, A., Böesche, M., Krause, R., Grandi, P., Marzioch, M., Bauer, A., Schultz, J., Rick, J. M., Michon, A., Cruciat, C., et al. (2002) · Nature · doi:10.1038/415141a · Cited by 4,729 · see citing works

A comprehensive analysis of protein–protein interactions in Saccharomyces cerevisiae

Uetz, P., Giot, L., Cagney, G., Mansfield, T. A., Judson, R. S., Knight, J. R., Lockshon, D., Narayan, V., Srinivasan, M., Pochart, P., et al. (2000) · Nature · doi:10.1038/35001009 · Cited by 4,706 · see citing works

Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry

Ho, Y., Gruhler, A., Heilbut, A. M., Bader, G. D., Moore, L., Adams, S., Millar, A., Taylor, P. P., Bennett, K. L., Boutilier, K., et al. (2002) · Nature · doi:10.1038/415180a · Cited by 3,573 · see citing works

Global landscape of protein complexes in the yeast Saccharomyces cerevisiae

Krogan, N. J., Cagney, G., Yu, H., Zhong, G., Guo, X., Ignatchenko, A., Li, J., Pu, S., Datta, N., Tikuisis, A., et al. (2006) · Nature · doi:10.1038/nature04670 · Cited by 2,915 · see citing works

A generic protein purification method for protein complex characterization and proteome exploration

Rigaut, G., Shevchenko, A., Rutz, B., Wilm, M., Mann, M., & Séraphin, B. (1999) · Nature Biotechnology · doi:10.1038/13732 · Cited by 2,707 · see citing works

TANDEM: matching proteins with tandem mass spectra

Craig, R., & Beavis, R. C. (2004) · Bioinformatics · doi:10.1093/bioinformatics/bth092 · Cited by 2,553 · see citing works

Proteome survey reveals modularity of the yeast cell machinery

Gavin, A., Aloy, P., Grandi, P., Krause, R., Böesche, M., Marzioch, M., Rau, C., Jensen, L. J., Bastuck, S., Dümpelfeld, B., et al. (2006) · Nature · doi:10.1038/nature04532 · Cited by 2,544 · see citing works

A probability-based approach for high-throughput protein phosphorylation analysis and site localization

Beausoleil, S. A., Villén, J., Gerber, S. A., Rush, J., & Gygi, S. P. (2006) · Nature Biotechnology · doi:10.1038/nbt1240 · Cited by 1,577 · see citing works

Large‐scale mapping of human protein–protein interactions by mass spectrometry

Ewing, R. M., Chu, P. C., Elisma, F., Li, H., Taylor, P. P., Climie, S. C., McBroom, L. D. B., Robinson, M. D., O'Connor, L., Li, M. M., et al. (2007) · Molecular Systems Biology · doi:10.1038/msb4100134 · Cited by 985 · see citing works

A common open representation of mass spectrometry data and its application to proteomics research

Pedrioli, P. G. A., Eng, J. K., Hubley, R. M., Vogelzang, M., Deutsch, E. W., Raught, B., Pratt, B. S., Nilsson, E. J., Angeletti, R. H., Apweiler, R., et al. (2004) · Nature Biotechnology · doi:10.1038/nbt1031 · Cited by 782 · see citing works

Large-scale phosphorylation analysis of mouse liver

Villén, J., Beausoleil, S. A., Gerber, S. A., & Gygi, S. P. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0609836104 · Cited by 730 · see citing works

Analysis of protein complexes using mass spectrometry

Gingras, A., Gstaiger, M., Raught, B., & Aebersold, R. H. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2208 · Cited by 709 · see citing works

The BioGRID Interaction Database: 2008 update

Breitkreutz, B., Stark, C., Reguly, T., Boucher, L., Breitkreutz, A., Livstone, M. S., Oughtred, R., Lackner, D. H., Bähler, J., Wood, V., et al. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm1001 · Cited by 698 · see citing works

Protein serine/threonine phosphatases: structure, regulation, and functions in cell growth

Mumby, M. C., & Walter, G. (1993) · Physiological Reviews · doi:10.1152/physrev.1993.73.4.673 · Cited by 661 · 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

Mutations within the Programmed Cell Death 10 Gene Cause Cerebral Cavernous Malformations

Bergametti, F., Denier, C., Labauge, P. M., Arnoult, M., Boetto, S., Clanet, M., Coubes, P. A., Échenne, B., Ibrahim, R., Irthum, B., et al. (2004) · The American Journal of Human Genetics · doi:10.1086/426952 · Cited by 449 · 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

Genetics of cavernous angiomas

Labauge, P. M., Denier, C., Bergametti, F., & Tournier‐Lasserve, E. (2007) · The Lancet Neurology · doi:10.1016/s1474-4422(07)70053-4 · Cited by 384 · see citing works

Multilocus linkage identifies two new loci for a mendelian form of stroke, cerebral cavernous malformation, at 7p15-13 and 3q25.2-27

Craig, H. D., Günel, M., Cepeda, O. M., et al. (1998) · Human Molecular Genetics · doi:10.1093/hmg/7.12.1851 · Cited by 352 · see citing works

Phosphoproteomic Analysis of the Developing Mouse Brain

Ballif, B. A., Villén, J., Beausoleil, S. A., Schwartz, D., & Gygi, S. P. (2004) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m400085-mcp200 · Cited by 347 · 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

Identification of specific PP2A complexes involved in human cell transformation

Chen, W., Possemato, R., Campbell, K. T., Plattner, C. A., Pallas, D. C., & Hahn, W. C. (2004) · Cancer Cell · doi:10.1016/s1535-6108(04)00026-1 · Cited by 325 · see citing works

YSK1 is activated by the Golgi matrix protein GM130 and plays a role in cell migration through its substrate 14-3-3ζ

Preisinger, C., Short, B., de Corte, V., Bruyneel, E., Haas, A. H., Kopajtich, R., Gettemans, J., & Barr, F. (2004) · Nature reviews. Molecular cell biology · doi:10.1083/jcb.200310061 · Cited by 299 · see citing works

PP2A: Unveiling a Reluctant Tumor Suppressor

Mumby, M. (2007) · Cell · doi:10.1016/j.cell.2007.06.034 · Cited by 295 · see citing works

Regulation of Protein Phosphatase 2A by Direct Interaction with Casein Kinase 2α

Hèriché, J.-K., Lebrin, F., Rabilloud, T., Leroy, D., CHAMBAZ, E. M., & Goldberg, Y. (1997) · Science · doi:10.1126/science.276.5314.952 · Cited by 270 · see citing works

Alpha- and beta-forms of the 65-kDa subunit of protein phosphatase 2A have a similar 39 amino acid repeating structure

Hemmings, B. A., Adams-Pearson, C., Maurer, F., Mueller, P., Goris, J., Merlevede, W., Hofsteenge, J., & Stone, S. R. (1990) · Biochemistry · doi:10.1021/bi00465a002 · Cited by 243 · see citing works

A Signaling Complex of Ca 2+ -Calmodulin-Dependent Protein Kinase IV and Protein Phosphatase 2A

Westphal, R. S., Anderson, K. A., Means, A. R., & Wadzinski, B. E. (1998) · Science · doi:10.1126/science.280.5367.1258 · Cited by 233 · see citing works

Affinity purification‐mass spectrometry

Bauer, A., & Küster, B. (2003) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2003.03428.x · Cited by 232 · see citing works

Raf-1-associated Protein Phosphatase 2A as a Positive Regulator of Kinase Activation

Abraham, D., Podar, K., Pacher, M., Kubicek, M., Welzel, N., Hemmings, B. A., Dilworth, S. M., Mischak, H., Kölch, W., & Baccarini, M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003259200 · Cited by 219 · see citing works

Qualitative and Quantitative Analyses of Protein Phosphorylation in Naive and Stimulated Mouse Synaptosomal Preparations

Munton, R. P., Tweedie‐Cullen, R. Y., Livingstone-Zatchej, M., Weinandy, F., Waidelich, M., Longo, D., Gehrig, P., Potthast, F., Rutishauser, D., Gerrits, B., et al. (2006) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m600046-mcp200 · Cited by 215 · see citing works

B cell receptor-associated protein α4 displays rapamycin-sensitive binding directly to the catalytic subunit of protein phosphatase 2A

Murata, K., Wu, J., & Brautigan, D. L. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.20.10624 · Cited by 213 · see citing works

General framework for developing and evaluating database scoring algorithms using the TANDEM search engine

MacLean, B., Eng, J. K., Beavis, R. C., & McIntosh, M. W. (2006) · Bioinformatics · doi:10.1093/bioinformatics/btl379 · Cited by 210 · see citing works

Identification of Kinase-Phosphatase Signaling Modules Composed of p70 S6 Kinase-Protein Phosphatase 2A (PP2A) and p21-activated Kinase-PP2A

Westphal, R. S., Coffee, R. L., Marotta, A., Pelech, S., & Wadzinski, B. E. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.2.687 · Cited by 202 · see citing works

The t(6;8)(q27;p11) Translocation in a Stem Cell Myeloproliferative Disorder Fuses a Novel Gene, FOP, to Fibroblast Growth Factor Receptor 1

Popovici, C., Zhang, B., Gregoire, M., et al. (1999) · Blood · doi:10.1182/blood.v93.4.1381 · Cited by 199 · see citing works

Advances in protein complex analysis using mass spectrometry

Gingras, A., Aebersold, R. H., & Raught, B. (2004) · The Journal of Physiology · doi:10.1113/jphysiol.2004.080440 · Cited by 198 · see citing works

WD40 Repeat Proteins Striatin and S/G2 Nuclear Autoantigen Are Members of a Novel Family of Calmodulin-binding Proteins That Associate with Protein Phosphatase 2A

Moreno, C. S., Park, S., Nelson, K., Ashby, D., Hubalek, F., Lane, W. S., & Pallas, D. C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.8.5257 · Cited by 194 · see citing works

Quantitative Analysis of Synaptic Phosphorylation and Protein Expression

Trinidad, J. C., Thalhammer, A., Specht, C. G., Lynn, A. J., Baker, P. R., Schoepfer, R., & Burlingame, A. L. (2008) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m700170-mcp200 · Cited by 194 · see citing works

Cerebral cavernous malformation: new molecular and clinical insights

Revençu, N., & Vikkula, M. (2006) · Journal of Medical Genetics · doi:10.1136/jmg.2006.041079 · Cited by 189 · see citing works

Role for the PP2A/B56δ Phosphatase in Regulating 14-3-3 Release from Cdc25 to Control Mitosis

Margolis, S. S., Perry, J. A., Forester, C. M., Nutt, L. K., Guo, Y., Jardim, M. J., Thomenius, M. J., Freel, C. D., Darbandi, R., Ahn, J., et al. (2006) · Cell · doi:10.1016/j.cell.2006.10.035 · Cited by 187 · see citing works

A Novel, Evolutionarily Conserved Protein Phosphatase Complex Involved in Cisplatin Sensitivity

Gingras, A., Caballero, M., Zarske, M., Sanchez, A., Hazbun, T. R., Fields, S., Sonenberg, N., Hafen, E., Raught, B., & Aebersold, R. H. (2005) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m500231-mcp200 · Cited by 186 · see citing works

CCM3 interacts with CCM2 indicating common pathogenesis for cerebral cavernous malformations

Voß, K., Stahl, S., Schleider, E., Ullrich, S., Nickel, J., Mueller, T. D., & Felbor, U. (2007) · Neurogenetics · doi:10.1007/s10048-007-0098-9 · Cited by 176 · see citing works

α4 Associates with Protein Phosphatases 2A, 4, and 6

Chen, J., Peterson, R. T., & Schreiber, S. L. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.8792 · Cited by 175 · see citing works

Separation of PP2A core enzyme and holoenzyme with monoclonal antibodies against the regulatory A subunit: abundant expression of both forms in cells

Kremmer, E., Ohst, K., Kiefer, J., Brewis, N., & Walter, G. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.3.1692 · Cited by 175 · see citing works

Molecular cloning of cDNAs encoding two isoforms of the catalytic subunit of protein phosphatase 2A

Stone, S. R., Hofsteenge, J., & Hemmings, B. A. (1987) · Biochemistry · doi:10.1021/bi00397a003 · Cited by 168 · see citing works

Nucleoside Diphosphate Kinase, a Source of GTP, Is Required for Dynamin-Dependent Synaptic Vesicle Recycling

Krishnan, K. S., Rikhy, R., Rao, S., Shivalkar, M., Mosko, M., Narayanan, R., Etter, P. D., Estes, P. S., & Ramaswami, M. (2001) · Neuron · doi:10.1016/s0896-6273(01)00273-2 · Cited by 165 · see citing works

SIKE is an IKKε/TBK1‐associated suppressor of TLR3‐ and virus‐triggered IRF‐3 activation pathways

Huang, J., Liu, T., Xu, L., Chen, D., Zhai, Z., & Shu, H. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600863 · Cited by 155 · see citing works

PDCD10 Interacts with Ste20-related Kinase MST4 to Promote Cell Growth and Transformation via Modulation of the ERK Pathway

Ma, X., Zhao, H., Shan, J., Long, F., Chen, Y., Chen, Y., Zhang, Y., Xiao, H., & Ma, D. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-07-0608 · Cited by 154 · see citing works

Activation of a human Ste20‐like kinase by oxidant stress defines a novel stress response pathway.

Pombo, C. M., Bonventre, J. V., Molnar, A., Kyriakis, J. M., & Force, T. L. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00831.x · Cited by 149 · see citing works

Proteomic Identification of the Cerebral Cavernous Malformation Signaling Complex

Hilder, T. L., Malone, M. H., Bencharit, S., Colicelli, J., Haystead, T., Johnson, G. L., & Wu, C. C. (2007) · Journal of Proteome Research · doi:10.1021/pr0704276 · Cited by 147 · see citing works

A Complex of Two Centrosomal Proteins, CAP350 and FOP, Cooperates with EB1 in Microtubule Anchoring

Yan, X., Habedanck, R., & Nigg, E. A. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-08-0810 · Cited by 139 · see citing works

Protein phosphatase 2A: Who shall regulate the regulator?

Goldberg, Y. (1999) · Biochemical Pharmacology · doi:10.1016/s0006-2952(98)00245-7 · Cited by 138 · see citing works

GIPC Is Recruited by APPL to Peripheral TrkA Endosomes and Regulates TrkA Trafficking and Signaling

Varsano, T., Dong, M., Niesman, I. R., Gacula, H., Lou, X., Ma, T., Testa, J. R., Yates, J. R., & Farquhar, M. G. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00305-06 · Cited by 132 · see citing works

A novel calmodulin-binding protein, belonging to the WD-repeat family, is localized in dendrites of a subset of CNS neurons

Castets, F., Bartoli, M., Barnier, J. V., Baillat, G., Salin, P., Moqrich, A., Bourgeois, J. P., Denizot, F., Rougon, G., Calothy, G., et al. (1996) · The Journal of Cell Biology · doi:10.1083/jcb.134.4.1051 · Cited by 129 · see citing works

Zinedin, SG2NA, and Striatin Are Calmodulin-binding, WD Repeat Proteins Principally Expressed in the Brain

Castets, F., Rakitina, T. V., Gaillard, S., Moqrich, A., Mattéi, M., & Monneron, A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m909782199 · Cited by 127 · see citing works

A WD40 Repeat Protein Regulates Fungal Cell Differentiation and Can Be Replaced Functionally by the Mammalian Homologue Striatin

Pöggeler, S., & Kück, U. (2004) · Eukaryotic Cell · doi:10.1128/ec.3.1.232-240.2004 · Cited by 116 · see citing works

Affinity-purification mass spectrometry (AP-MS) of serine/threonine phosphatases

Chen, G. I., & Gingras, A.-C. (2007) · Methods · doi:10.1016/j.ymeth.2007.02.018 · Cited by 114 · cited 3× · see citing works

MST4, a new Ste20-related kinase that mediates cell growth and transformation via modulating ERK pathway

Lin, J.-L., Chen, H., Fang, H.-I., Robinson, D. R., Kung, H.-J., & Shih, H.-M. (2001) · Oncogene · doi:10.1038/sj.onc.1204818 · Cited by 113 · see citing works

The ham-2 Locus, Encoding a Putative Transmembrane Protein, Is Required for Hyphal Fusion in Neurospora crassa

Xiang, Q., Rasmussen, C. G., & Glass, N. L. (2002) · Genetics · doi:10.1093/genetics/160.1.169 · Cited by 110 · see citing works

Cloning and Characterization of a Human STE20-like Protein Kinase with Unusual Cofactor Requirements

Schinkmann, K. A., & Blenis, J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.45.28695 · Cited by 109 · see citing works

Identification of a novel gene, FGFR1OP2, fused to FGFR1 in 8p11 myeloproliferative syndrome

Grand, E., Grand, F., Chase, A., Ross, F., Corcoran, M., Oscier, D., & Cross, N. (2004) · Genes, Chromosomes and Cancer · doi:10.1002/gcc.20023 · Cited by 105 · see citing works

Far3 and Five Interacting Proteins Prevent Premature Recovery from Pheromone Arrest in the Budding Yeast Saccharomyces cerevisiae

Kemp, H. A., & Sprague, G. F. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.5.1750-1763.2003 · Cited by 105 · see citing works

The striatin family: A new signaling platform in dendritic spines

Benoist, M., Gaillard, S., & Castets, F. (2006) · Journal of Physiology-Paris · doi:10.1016/j.jphysparis.2005.12.006 · Cited by 104 · see citing works

Liprin-α proteins: scaffold molecules for synapse maturation

Spangler, S. A., & Hoogenraad, C. C. (2007) · Biochemical Society Transactions · doi:10.1042/bst0351278 · Cited by 104 · see citing works

Mutations in Apoptosis-related Gene, PDCD10, Cause Cerebral Cavernous Malformation 3

Güçlü, B., Ozturk, A. K., Pricola, K. L., et al. (2005) · Neurosurgery · doi:10.1227/01.neu.0000180811.56157.e1 · Cited by 96 · see citing works

A Mammalian Homolog of Yeast MOB1 Is Both a Member and a Putative Substrate of Striatin Family-Protein Phosphatase 2A Complexes

Moreno, C. S., Lane, W. S., & Pallas, D. C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102398200 · Cited by 95 · see citing works

A Developmentally Regulated, Neuron-specific Splice Variant of the Variable Subunit Bβ Targets Protein Phosphatase 2A to Mitochondria and Modulates Apoptosis

Dagda, R. K., Zaucha, J. A., Wadzinski, B. E., & Strack, S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302832200 · Cited by 92 · see citing works

Recent developments in the analysis of protein complexes1

Dziembowski, A., & Séraphin, B. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)01357-7 · Cited by 91 · see citing works

Control of mitotic exit by PP2A regulation of Cdc25C and Cdk1

Forester, C. M., Maddox, J., Louis, J. V., Goris, J., & Virshup, D. M. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709879104 · Cited by 91 · see citing works

Mapping protein–protein interactions by mass spectrometry

Vasilescu, J., & Figeys, D. (2006) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2006.06.008 · Cited by 81 · see citing works

PP4R4/KIAA1622 Forms a Novel Stable Cytosolic Complex with Phosphoprotein Phosphatase 4

Chen, G. I., Tisayakorn, S., Jørgensen, C., D'Ambrosio, L. M., Goudreault, M., & Gingras, A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803443200 · Cited by 80 · see citing works

Molecular Cloning and Characterization of Phocein, a Protein Found from the Golgi Complex to Dendritic Spines

Baillat, G., Moqrich, A., Castets, F., et al. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.3.663 · Cited by 78 · 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

Mass spectrometry‐based proteomic analysis of the epitope‐tag affinity purified protein complexes in eukaryotes

Chang, I. (2006) · PROTEOMICS · doi:10.1002/pmic.200600225 · Cited by 76 · see citing works

Mammalian NDR protein kinases: From regulation to a role in centrosome duplication

Hergovich, A., Cornils, H., & Hemmings, B. A. (2007) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2007.07.017 · Cited by 74 · see citing works

Genetics of cerebral cavernous malformations

Plummer, N. W., Zawistowski, J. S., & Marchuk, D. A. (2005) · Current Neurology and Neuroscience Reports · doi:10.1007/s11910-005-0063-7 · Cited by 73 · see citing works

Isolation and characterization of cortactin isoforms and a novel cortactin‐binding protein, CBP90

Ohoka, Y., & Takai, Y. (1998) · Genes to Cells · doi:10.1046/j.1365-2443.1998.00216.x · Cited by 72 · see citing works

Cloning and Characterization of MST4, a Novel Ste20-like Kinase

Qian, Z., Lin, C., Espinosa, R., Beau, M. M. L., & Rosner, M. R. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009323200 · Cited by 70 · see citing works

Interactions of Phocein with Nucleoside-Diphosphate Kinase, Eps15, and Dynamin I

Baillat, G., Gaillard, S., Castets, F., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108818200 · Cited by 65 · see citing works

Cloning of MASK, a Novel Member of the Mammalian Germinal Center Kinase III Subfamily, with Apoptosis-inducing Properties

Dan, I., Ong, S., Watanabe, N. M., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110882200 · Cited by 62 · see citing works

The GCK II and III subfamilies of the STE20 group kinases

Pombo, C. M. (2006) · Frontiers in bioscience · doi:10.2741/2107 · Cited by 50 · see citing works

Down-regulation of striatin, a neuronal calmodulin-binding protein, impairs rat locomotor activity

Bartoli, M., Ternaux, J., Forni, C., Portalier, P., Salin, P., Amalric, M., & Monneron, A. (1999) · Journal of Neurobiology · doi:10.1002/(sici)1097-4695(199908)40:2 · Cited by 48 · see citing works

A novel isoform of sarcolemmal membrane-associated protein (SLMAP) is a component of the microtubule organizing centre

Guzzo, R. M., Sevinc, S., Salih, M., et al. (2004) · Journal of Cell Science · doi:10.1242/jcs.01079 · Cited by 48 · see citing works

Identification of a Human Brain-specific Isoform of Mammalian STE20-like Kinase 3 That Is Regulated by cAMP-dependent Protein Kinase

Zhou, T.-H., Ling, K., Guo, J. Q., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.4.2513 · Cited by 45 · see citing works

FOP-FGFR1 tyrosine kinase, the product of a t(6;8) translocation, induces a fatal myeloproliferative disease in mice

Guasch, G., Delaval, B., Arnoulet, C., et al. (2003) · Blood · doi:10.1182/blood-2003-05-1690 · Cited by 44 · see citing works

Structure of the N-terminal Domain of the FOP (FGFR1OP) Protein and Implications for its Dimerization and Centrosomal Localization

Mikolajka, A., Yan, X., Popowicz, G. M., et al. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.03.070 · Cited by 40 · see citing works

Alternative Splicing, Expression, and Genomic Structure of the 3′ Region of the Gene Encoding the Sarcolemmal-associated Proteins (SLAPs) Defines a Novel Class of Coiled-coil Tail-anchored Membrane Proteins

Wielowieyski, P. A., Sevinc, S., Guzzo, R. M., Salih, M., Wigle, J. T., & Tuana, B. S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m007682200 · Cited by 38 · see citing works

Baculovirus expression, purification, and characterization of human protein phosphatase 2A catalytic subunits α and β

Ikehara, T., Shinjo, F., Ikehara, S., Imamura, S., & Yasumoto, T. (2005) · Protein Expression and Purification · doi:10.1016/j.pep.2005.06.002 · Cited by 37 · see citing works

Molecular Cloning, Expression, and Chromosomal Assignment of Sarcolemmal-associated Proteins

Wigle, J. T., Demchyshyn, L. L., Pratt, M. A. C., Staines, W. A., Salih, M., & Tuana, B. S. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.51.32384 · Cited by 35 · see citing works

YSK1, a novel mammalian protein kinase structurally related to Ste20 and SPS1, but is not involved in the known MAPK pathways

Osada, S., Izawa, M., Saito, R., Mizuno, K., Suzuki, A., Hirai, S.-I., & Ohno, S. (1997) · Oncogene · doi:10.1038/sj.onc.1201043 · Cited by 35 · see citing works

Regulated expression and temporal induction of the tail-anchored sarcolemmal-membrane-associated protein is critical for myoblast fusion

Guzzo, R. M., Wigle, J. T., Salih, M., et al. (2004) · Biochemical Journal · doi:10.1042/bj20031723 · Cited by 32 · see citing works

Powerful tools for the characterization of protein complexes

Bauer, A., & Küster, B. (2003) · Cited by 32 · see citing works

The Formation and Activity of PP2A Holoenzymes Do Not Depend on the Isoform of the Catalytic Subunit

Zhou, J., Pham, H. T., & Walter, G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211181200 · Cited by 29 · see citing works

Phocein: A potential actor in vesicular trafficking at Purkinje cell dendritic spines

Bailly, Y. J. R., & Castets, F. (2007) · The Cerebellum · doi:10.1080/14734220701225912 · Cited by 21 · see citing works

Liprin α1 interacts with PP2A B56γ

Arroyo, J. D., Lee, G. M., & Hahn, W. C. (2008) · Cell Cycle · doi:10.4161/cc.7.4.5390 · Cited by 19 · see citing works

The CRAPome: a contaminant repository for affinity purification–mass spectrometry data

Mellacheruvu, D., Wright, Z., Couzens, A. L., Lambert, J.-P., St-Denis, N. A., Li, T., Miteva, Y. V., Hauri, S., Sardiu, M. E., Low, T. Y., et al. (2013) · Nature Methods · doi:10.1038/nmeth.2557 · Cited by 1,686 · see citing works

The Hippo Signaling Pathway in Development and Disease

Zheng, Y., & Pan, D. (2019) · Developmental Cell · doi:10.1016/j.devcel.2019.06.003 · Cited by 867 · see citing works

A Genome-wide CRISPR Screen in Primary Immune Cells to Dissect Regulatory Networks

Parnas, O., Jovanovic, M., Eisenhaure, T. M., Herbst, R. H., Dixit, A., Ye, C. J., Przybylski, D., Platt, R. J., Tirosh, I., Sanjana, N. E., et al. (2015) · Cell · doi:10.1016/j.cell.2015.06.059 · Cited by 440 · see citing works

Affinity-purification coupled to mass spectrometry: basic principles and strategies

Dunham, W. H., Mullin, M., & Gingras, A. (2012) · PROTEOMICS · doi:10.1002/pmic.201100523 · Cited by 368 · see citing works

Quantitative analysis of fitness and genetic interactions in yeast on a genome scale

Baryshnikova, A., Costanzo, M., Kim, Y., Ding, H., Koh, J., Toufighi, K., Youn, J.-Y., Ou, J., San Luis, B.-J., Bandyopadhyay, S., et al. (2010) · Nature Methods · doi:10.1038/nmeth.1534 · Cited by 364 · see citing works

Protein Serine/Threonine Phosphatases: Keys to Unlocking Regulators and Substrates

Brautigan, D. L., & Shenolikar, S. (2018) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-062917-012332 · Cited by 191 · 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

Mapping of signaling networks through synthetic genetic interaction analysis by RNAi

Horn, T., Sandmann, T., Fischer, B., Axelsson, E., Huber, W., & Boutros, M. (2011) · Nature Methods · doi:10.1038/nmeth.1581 · Cited by 193 · see citing works

Cerebral cavernous malformations: from CCM genes to endothelial cell homeostasis

Fischer, A., Zalvide, J., Faurobert, E., Albiges-Rizo, C., & Tournier-Lasserve, E. (2013) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2013.02.004 · Cited by 199 · see citing works

The broken “Off” switch in cancer signaling: PP2A as a regulator of tumorigenesis, drug resistance, and immune surveillance

Ruvolo, P. P. (2016) · BBA Clinical · doi:10.1016/j.bbacli.2016.08.002 · Cited by 143 · see citing works

Structure, Regulation, and Pharmacological Modulation of PP2A Phosphatases

Lambrecht, C., Haesen, D., Sents, W., Ivanova, E., & Janssens, V. (2013) · Methods in Molecular Biology · doi:10.1007/978-1-62703-562-0_17 · Cited by 140 · see citing works

Identification of Protein Interactions Involved in Cellular Signaling

Westermarck, J., Ivaska, J., & Corthals, G. L. (2013) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r113.027771 · Cited by 143 · see citing works

Recurrent <i>PPP2R1A</i> Mutations in Uterine Cancer Act through a Dominant-Negative Mechanism to Promote Malignant Cell Growth

Haesen, D., Abbasi Asbagh, L., Derua, R., Hubert, A., Schrauwen, S., Hoorne, Y., Amant, F., Waelkens, E., Sablina, A., & Janssens, V. (2016) · Cancer Research · doi:10.1158/0008-5472.can-15-3342 · Cited by 124 · see citing works

B56δ-related protein phosphatase 2A dysfunction identified in patients with intellectual disability

Houge, G., Haesen, D., Vissers, L. E. L. M., Mehta, S., Parker, M. J., Wright, M., Vogt, J., McKee, S., Tolmie, J. L., Cordeiro, N., et al. (2015) · Journal of Clinical Investigation · doi:10.1172/jci79860 · Cited by 124 · see citing works

Cortactin-Binding Protein 2 Modulates the Mobility of Cortactin and Regulates Dendritic Spine Formation and Maintenance

Chen, Y.-K., & Hsueh, Y.-P. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.4405-11.2012 · Cited by 90 · 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

Mechanistic insight into GPCR-mediated activation of the microtubule-associated RhoA exchange factor GEF-H1

Meiri, D., Marshall, C. B., Mokady, D., LaRose, J., Mullin, M., Gingras, A.-C., Ikura, M., & Rottapel, R. (2014) · Nature Communications · doi:10.1038/ncomms5857 · Cited by 70 · see citing works

SAINT-MS1: protein-protein interaction scoring using label-free intensity data in affinity purification-mass spectrometry experiments

Choi, H., Glatter, T., Gstaiger, M., & Nesvizhskii, A. I. (2012) · Journal of Proteome Research · doi:10.1021/pr201185r · Cited by 68 · see citing works

Striatins contain a noncanonical coiled coil that binds protein phosphatase 2A A subunit to form a 2:2 heterotetrameric core of striatin-interacting phosphatase and kinase (STRIPAK) complex

Chen, C., Shi, Z., Zhang, W., Chen, M., He, F., Zhang, Z., Wang, Y., Feng, M., Wang, W., Zhao, Y., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.529297 · Cited by 47 · see citing works

B55α PP2A Holoenzymes Modulate the Phosphorylation Status of the Retinoblastoma-related Protein p107 and Its Activation

Jayadeva, G., Kurimchak, A., Garriga, J., Sotillo, E., Davis, A. J., Haines, D. S., Mumby, M., & Graña, X. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.162354 · Cited by 37 · see citing works

Beyond hairballs: The use of quantitative mass spectrometry data to understand protein–protein interactions

Gingras, A.-C., & Raught, B. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.03.065 · Cited by 34 · see citing works

Targeting PP2A in cancer: an underrated option

Sarais, F., Krempien, F., Koehn, C., Brewing, L., Classen, C. F., Walter, M., & Shokraie, O. (2025) · Journal of Experimental &amp; Clinical Cancer Research · doi:10.1186/s13046-025-03560-y · Cited by 8 · see citing works

Illuminating the dark protein-protein interactome

Tabar, M. S., Parsania, C., Chen, H., Su, X., Bailey, C. G., & Rasko, J. E. J. (2022) · Cell Reports Methods · doi:10.1016/j.crmeth.2022.100275 · Cited by 43 · see citing works

Regulating the regulator: Insights into the cardiac protein phosphatase 1 interactome

Chiang, D. Y.-E., Heck, A. J. R., Dobrev, D., et al. (2016) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2016.09.009 · Cited by 32 · see citing works

Docking Motif-Guided Mapping of the Interactome of Protein Phosphatase-1

Hendrickx, A., Beullens, M., Ceulemans, H., Abt, T. D., Eynde, A. V., Nicolaescu, E., Lesage, B., & Bollen, M. (2009) · Chemistry & Biology · doi:10.1016/j.chembiol.2009.02.012 · Cited by 314 · see citing works

Analysis of Coiled-Coil Interactions between Core Proteins of the Spindle Pole Body

Zizlsperger, N., Malashkevich, V. N., Pillay, S., & Keating, A. E. (2008) · Biochemistry · doi:10.1021/bi801378z · Cited by 21 · see citing works

Properties and Phosphorylation Sites of Baculovirus-expressed Nuclear Inhibitor of Protein Phosphatase-1 (NIPP-1)

Vulsteke, V., Beullens, M., Waelkens, E., et al. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.52.32972 · Cited by 52 · see citing works