Global, In Vivo, and Site-Specific Phosphorylation Dynamics in Signaling Networks

Mass spectrometry-based proteomics

Aebersold, R., & Mann, M. (2003) · Nature · doi:10.1038/nature01511 · Cited by 6,955

Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics

Ong, S.-E., Blagoev, B., Kratchmarova, I., Kristensen, D. B., Steen, H., Pandey, A., & Mann, M. (2002) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m200025-mcp200 · Cited by 5,574

AP-1 as a regulator of cell life and death

Shaulian, E., & Karin, M. (2002) · Nature Cell Biology · doi:10.1038/ncb0502-e131 · Cited by 2,961

The role of STATs in transcriptional control and their impact on cellular function

Bromberg, J., & Darnell, J. E. (2000) · Oncogene · doi:10.1038/sj.onc.1203476 · Cited by 1,201

Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips

Rappsilber, J., Mann, M., & Ishihama, Y. (2007) · Nature Protocols · doi:10.1038/nprot.2007.261 · Cited by 4,641

Lysine acetylation targets protein complexes and co-regulates major cellular functions

Choudhary, C., Kumar, C., Gnad, F., Nielsen, M. L., Rehman, M., Walther, T. C., Olsen, J. V., & Mann, M. (2009) · Science · doi:10.1126/science.1175371 · Cited by 4,040

PhosphoSitePlus, 2014: mutations, PTMs and recalibrations

Hornbeck, P. V., Zhang, B., Murray, B., Kornhauser, J. M., Latham, V., & Skrzypek, E. (2015) · Nucleic Acids Research · doi:10.1093/nar/gku1267 · Cited by 3,411

Global Survey of Phosphotyrosine Signaling Identifies Oncogenic Kinases in Lung Cancer

Rikova, K., Guo, A., Zeng, Q., Possemato, A., Yu, J., Haack, H., Nardone, J., Lee, K., Reeves, C., Li, Y., et al. (2007) · Cell · doi:10.1016/j.cell.2007.11.025 · Cited by 2,317

Mass-spectrometric exploration of proteome structure and function

Aebersold, R., & Mann, M. (2016) · Nature · doi:10.1038/nature19949 · Cited by 2,334

Epidermal Growth Factor Receptor Cell Proliferation Signaling Pathways

Wee, P., & Wang, Z. (2017) · Cancers · doi:10.3390/cancers9050052 · Cited by 2,027

A tissue-specific atlas of mouse protein phosphorylation and expression

Huttlin, E. L., Jedrychowski, M. P., Elias, J. E., Goswami, T., Rad, R., Beausoleil, S. A., Villén, J., Haas, W., Sowa, M. E., & Gygi, S. P. (2010) · Cell · doi:10.1016/j.cell.2010.12.001 · Cited by 1,778

A quantitative atlas of mitotic phosphorylation

Dephoure, N., Zhou, C., Villén, J., Beausoleil, S. A., Bakalarski, C. E., Elledge, S. J., & Gygi, S. P. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0805139105 · Cited by 1,608

The endoplasmic reticulum: structure, function and response to cellular signaling

Schwarz, D. S., & Blower, M. D. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2052-6 · Cited by 1,613

Protein Analysis by Shotgun/Bottom-up Proteomics

Zhang, Y., Fonslow, B. R., Shan, B., Baek, M.-C., & Yates, J. R. (2013) · Chemical Reviews · doi:10.1021/cr3003533 · Cited by 1,491

Mechanisms of specificity in protein phosphorylation

Ubersax, J. A., & Ferrell Jr, J. E. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2203 · Cited by 1,451

Serine/threonine phosphatases: mechanism through structure

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

mRNAs, proteins and the emerging principles of gene expression control

Buccitelli, C., & Selbach, M. (2020) · Nature Reviews Genetics · doi:10.1038/s41576-020-0258-4 · Cited by 1,243

PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity

Kane, L. A., Lazarou, M., Fogel, A. I., Li, Y., Yamano, K., Sarraf, S. A., Banerjee, S., & Youle, R. J. (2014) · Journal of Cell Biology · doi:10.1083/jcb.201402104 · Cited by 1,298

Proteomics by Mass Spectrometry: Approaches, Advances, and Applications

Yates, J. R., Ruse, C. I., & Nakorchevsky, A. (2009) · Annual Review of Biomedical Engineering · doi:10.1146/annurev-bioeng-061008-124934 · Cited by 1,078

Phosphoproteomics reveals that Parkinson's disease kinase LRRK2 regulates a subset of Rab GTPases

Steger, M., Tonelli, F., Ito, G., Davies, P., Trost, M., Vetter, M., Wachter, S., Lorentzen, E., Duddy, G., Wilson, S., et al. (2016) · eLife · doi:10.7554/elife.12813 · Cited by 1,042

ErbB receptors and signaling pathways in cancer

Hynes, N. E., & MacDonald, G. (2009) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2008.12.010 · Cited by 956

Functional and quantitative proteomics using SILAC

Mann, M. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2067 · Cited by 931

The emerging complexity of protein ubiquitination

Komander, D. (2009) · Biochemical Society Transactions · doi:10.1042/bst0370937 · Cited by 821

Quantitative mass spectrometry in proteomics: critical review update from 2007 to the present

Bantscheff, M., Lemeer, S., Savitski, M. M., & Kuster, B. (2012) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-012-6203-4 · Cited by 801

Phosphorylated TDP‐43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis

Hasegawa, M., Arai, T., Nonaka, T., Kametani, F., Yoshida, M., Hashizume, Y., Beach, T. G., Buratti, E., Baralle, F., Morita, M., et al. (2008) · Annals of Neurology · doi:10.1002/ana.21425 · Cited by 777

Quantitative, High-Resolution Proteomics for Data-Driven Systems Biology

Cox, J., & Mann, M. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061308-093216 · Cited by 685

SILAC mouse for quantitative proteomics uncovers kindlin-3 as an essential factor for red blood cell function

Krüger, M., Moser, M., Ussar, S., Thievessen, I., Luber, C. A., Forner, F., Schmidt, S., Zanivan, S., Fässler, R., & Mann, M. (2008) · Cell · doi:10.1016/j.cell.2008.05.033 · Cited by 680

Solution structure of the integral human membrane protein VDAC-1 in detergent micelles

Hiller, S., Garces, R. G., Malia, T. J., Orekhov, V. Y., Colombini, M., & Wagner, G. (2008) · Science · doi:10.1126/science.1161302 · Cited by 667

Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle

Daub, H., Olsen, J. V., Bairlein, M., Gnad, F., Oppermann, F. S., Körner, R., Greff, Z., Kéri, G., Stemmann, O., & Mann, M. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.07.007 · Cited by 594

Comparative proteomic phenotyping of cell lines and primary cells to assess preservation of cell type-specific functions

Pan, C., Kumar, C., Bohl, S., Klingmueller, U., & Mann, M. (2009) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m800258-mcp200 · Cited by 561

A comprehensive compilation of SUMO proteomics

Hendriks, I. A., & Vertegaal, A. C. O. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.81 · Cited by 514

Redox regulation of SIRT1 in inflammation and cellular senescence

Hwang, J.-W., Yao, H., Caito, S., Sundar, I. K., & Rahman, I. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.03.015 · Cited by 503

A Multidimensional Chromatography Technology for In-depth Phosphoproteome Analysis

Albuquerque, C. P., Smolka, M. B., Payne, S. H., Bafna, V., Eng, J., & Zhou, H. (2008) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m700468-mcp200 · Cited by 504

The functional landscape of the human phosphoproteome

Ochoa, D., Jarnuczak, A. F., Viéitez, C., Gehre, M., Soucheray, M., Mateus, A., Kleefeldt, A. A., Hill, A., Garcia-Alonso, L., Stein, F., et al. (2020) · Nature Biotechnology · doi:10.1038/s41587-019-0344-3 · Cited by 491

System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation

Rigbolt, K. T. G., Prokhorova, T. A., Akimov, V., Henningsen, J., Johansen, P. T., Kratchmarova, I., Kassem, M., Mann, M., Olsen, J. V., & Blagoev, B. (2011) · Science Signaling · doi:10.1126/scisignal.2001570 · Cited by 451

Regulating tumor suppressor genes: post-translational modifications

Chen, L., Liu, S., & Tao, Y. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-0196-9 · Cited by 449

Toward a comprehensive characterization of a human cancer cell phosphoproteome

Zhou, H., Di Palma, S., Preisinger, C., Peng, M., Polat, A. N., Heck, A. J. R., & Mohammed, S. (2013) · Journal of Proteome Research · doi:10.1021/pr300630k · Cited by 438

Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases

Smolka, M. B., Albuquerque, C. P., Chen, S.-H., & Zhou, H. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701622104 · Cited by 404

Modification‐specific proteomics: Strategies for characterization of post‐translational modifications using enrichment techniques

Zhao, Y., & Jensen, O. N. (2009) · PROTEOMICS · doi:10.1002/pmic.200900398 · Cited by 384

The Mediator complex and transcription regulation

Poss, Z. C., Ebmeier, C. C., & Taatjes, D. J. (2013) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2013.840259 · Cited by 364

Transmembrane proteins of the tight junctions at the blood–brain barrier: Structural and functional aspects

Haseloff, R. F., Dithmer, S., Winkler, L., Wolburg, H., & Blasig, I. E. (2015) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2014.11.004 · Cited by 353

Beige adipocyte maintenance is regulated by autophagy-induced mitochondrial clearance

Altshuler-Keylin, S., Shinoda, K., Hasegawa, Y., Ikeda, K., Hong, H., Kang, Q., Yang, Y., Perera, R. M., Debnath, J., & Kajimura, S. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.08.002 · Cited by 349

Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues

Lundby, A., Secher, A., Lage, K., Nordsborg, N. B., Dmytriyev, A., Lundby, C., & Olsen, J. V. (2012) · Nature Communications · doi:10.1038/ncomms1871 · Cited by 343

Phosphorylation in protein-protein binding: effect on stability and function

Nishi, H., Hashimoto, K., & Panchenko, A. R. (2011) · Structure · doi:10.1016/j.str.2011.09.021 · Cited by 322

Dynamics of the skeletal muscle secretome during myoblast differentiation

Henningsen, J., Rigbolt, K. T. G., Blagoev, B., Pedersen, B. K., & Kratchmarova, I. (2010) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m110.002113 · Cited by 303

PCNA: a silent housekeeper or a potential therapeutic target?

Wang, S.-C. (2014) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2014.02.004 · Cited by 285

Post-translational modifications of Hsp90 and their contributions to chaperone regulation

Mollapour, M., & Neckers, L. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.07.018 · Cited by 288

Trans-Omics: How To Reconstruct Biochemical Networks Across Multiple ‘Omic’ Layers

Yugi, K., Kubota, H., Hatano, A., & Kuroda, S. (2016) · Trends in Biotechnology · doi:10.1016/j.tibtech.2015.12.013 · Cited by 258

ERK1/2 Phosphorylate Raptor to Promote Ras-dependent Activation of mTOR Complex 1 (mTORC1)

Carriere, A., Romeo, Y., Acosta-Jaquez, H. A., Moreau, J., Bonneil, E., Thibault, P., Fingar, D. C., & Roux, P. P. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.159046 · Cited by 268

Ulk1-mediated phosphorylation of AMPK constitutes a negative regulatory feedback loop

Löffler, A. S., Alers, S., Dieterle, A. M., Keppeler, H., Franz-Wachtel, M., Kundu, M., Campbell, D. G., Wesselborg, S., Alessi, D. R., & Stork, B. (2011) · Autophagy · doi:10.4161/auto.7.7.15451 · Cited by 258

Proteome-wide Analysis of Lysine Acetylation Suggests its Broad Regulatory Scope in Saccharomyces cerevisiae

Henriksen, P., Wagner, S. A., Weinert, B. T., Sharma, S., Bačinskaja, G., Rehman, M., Juffer, A. H., Walther, T. C., Lisby, M., & Choudhary, C. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m112.017251 · Cited by 246

Mechanisms involved in the regulation of histone lysine demethylases

Lan, F., Nottke, A. C., & Shi, Y. (2008) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2008.03.004 · Cited by 241

A global view of protein expression in human cells, tissues, and organs

Pontén, F., Gry, M., Fagerberg, L., Lundberg, E., Asplund, A., Berglund, L., Oksvold, P., Björling, E., Hober, S., Kampf, C., et al. (2009) · Molecular Systems Biology · doi:10.1038/msb.2009.93 · Cited by 222

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

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

The physiology of the β‐amyloid precursor protein intracellular domain AICD

Pardossi‐Piquard, R., & Checler, F. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07475.x · Cited by 159

Mapping the Phosphoproteome of Influenza A and B Viruses by Mass Spectrometry

Hutchinson, E. C., Denham, E. M., Thomas, B., Trudgian, D. C., Hester, S. S., Ridlova, G., York, A., Turrell, L., & Fodor, E. (2012) · PLoS Pathogens · doi:10.1371/journal.ppat.1002993 · Cited by 151

Quantitative Proteomics by Metabolic Labeling of Model Organisms

Gouw, J. W., Krijgsveld, J., & Heck, A. J. R. (2010) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r900001-mcp200 · Cited by 151

Conformational Switching of the Molecular Chaperone Hsp90 via Regulated Phosphorylation

Soroka, J., Wandinger, S. K., Mäusbacher, N., Schreiber, T., Richter, K., Daub, H., & Buchner, J. (2012) · Molecular Cell · doi:10.1016/j.molcel.2011.12.031 · Cited by 139

Genetically encoding phosphotyrosine and its nonhydrolyzable analog in bacteria

Luo, X., Fu, G., Wang, R. E., Zhu, X., Zambaldo, C., Liu, R., Liu, T., Lyu, X., Du, J., Xuan, W., et al. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2405 · Cited by 134

Modulation of Phosphoprotein Activity by Phosphorylation Targeting Chimeras (PhosTACs)

Chen, P.-H., Hu, Z., An, E., Okeke, I., Zheng, S., Luo, X., Gong, A., Jaime-Figueroa, S., & Crews, C. M. (2021) · ACS Chemical Biology · doi:10.1021/acschembio.1c00693 · Cited by 130

WHEP Domains Direct Noncanonical Function of Glutamyl-Prolyl tRNA Synthetase in Translational Control of Gene Expression

Jia, J., Arif, A., Ray, P. S., & Fox, P. L. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.01.010 · Cited by 128

Eukaryotic DNA damage checkpoint activation in response to double-strand breaks

Finn, K., Lowndes, N. F., & Grenon, M. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-011-0875-3 · Cited by 127

Systems‐wide analysis of BCR signalosomes and downstream phosphorylation and ubiquitylation

Satpathy, S., Wagner, S. A., Beli, P., Gupta, R., Kristiansen, T. A., Malinova, D., Francavilla, C., Tolar, P., Bishop, G. A., Hostager, B. S., et al. (2015) · Molecular Systems Biology · doi:10.15252/msb.20145880 · Cited by 124

A post-translational modification code for transcription factors: sorting through a sea of signals

Benayoun, B. A., & Veitia, R. A. (2009) · Trends in Cell Biology · doi:10.1016/j.tcb.2009.02.003 · Cited by 121

Phosphosignature predicts dasatinib response in non-small cell lung cancer

Klammer, M., Kaminski, M., Zedler, A., Oppermann, F., Blencke, S., Marx, S., Müller, S., Tebbe, A., Godl, K., & Schaab, C. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.016410 · Cited by 118

A Phosphoproteomic Comparison of B-RAFV600E and MKK1/2 Inhibitors in Melanoma Cells*

Stuart, S. A., Houel, S., Lee, T., Wang, N., Old, W. M., & Ahn, N. G. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m114.047233 · Cited by 116

Emerin in health and disease

Koch, A. J., & Holaska, J. M. (2014) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2013.12.008 · Cited by 114

Global Dynamics of the Escherichia coli Proteome and Phosphoproteome During Growth in Minimal Medium

Soares, N. C., Spät, P., Krug, K., & Macek, B. (2013) · Journal of Proteome Research · doi:10.1021/pr3011843 · Cited by 113

Impact of phosphorylation on thermal stability of proteins

Potel, C. M., Kurzawa, N., Becher, I., Typas, A., Mateus, A., & Savitski, M. M. (2021) · Nature Methods · doi:10.1038/s41592-021-01177-5 · Cited by 103

Catch me if you can: Mass spectrometry‐based phosphoproteomics and quantification strategies

Eyrich, B., Sickmann, A., & Zahedi, R. P. (2011) · PROTEOMICS · doi:10.1002/pmic.201000489 · Cited by 104

Towards comprehensive and quantitative proteomics for diagnosis and therapy of human disease

Cifani, P., & Kentsis, A. (2017) · PROTEOMICS · doi:10.1002/pmic.201600079 · Cited by 101

INKA, an integrative data analysis pipeline for phosphoproteomic inference of active kinases

Beekhof, R., van Alphen, C., Henneman, A. A., Knol, J. C., Pham, T. V., Rolfs, F., Labots, M., Henneberry, E., Le Large, T. Y., de Haas, R. R., et al. (2019) · Molecular Systems Biology · doi:10.15252/msb.20188250 · Cited by 97

Label-free Quantitative Proteomics of Mouse Cerebrospinal Fluid Detects β-Site APP Cleaving Enzyme (BACE1) Protease Substrates In Vivo

Dislich, B., Wohlrab, F., Bachhuber, T., Müller, S. A., Kuhn, P.-H., Hogl, S., Meyer-Luehmann, M., & Lichtenthaler, S. F. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m114.041533 · Cited by 85

Fast and deep phosphoproteome analysis with the Orbitrap Astral mass spectrometer

(2024) · doi:10.1038/s41467-024-51274-0 · Cited by 83

Differential Reprogramming of Isogenic Colorectal Cancer Cells by Distinct Activating KRAS Mutations

Hammond, D. E., Mageean, C. J., Rusilowicz, E. V., Wickenden, J. A., Clague, M. J., & Prior, I. A. (2015) · Journal of Proteome Research · doi:10.1021/pr501191a · Cited by 81

Stimulus Design for Model Selection and Validation in Cell Signaling

Apgar, J. F., Toettcher, J. E., Endy, D., White, F. M., & Tidor, B. (2008) · PLoS Computational Biology · doi:10.1371/journal.pcbi.0040030 · Cited by 79

Phosphorylation acts positively and negatively to regulate MRTF-A subcellular localisation and activity

Panayiotou, R., Miralles, F., Pawlowski, R., Diring, J., Flynn, H. R., Skehel, M., & Treisman, R. (2016) · eLife · doi:10.7554/elife.15460 · Cited by 79

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

FIP200, a key signaling node to coordinately regulate various cellular processes

Gan, B., & Guan, J.-L. (2008) · Cellular Signalling · doi:10.1016/j.cellsig.2007.10.021 · Cited by 67

Casein kinase 2 phosphorylation of Hsp90 threonine 22 modulates chaperone function and drug sensitivity

Mollapour, M., Tsutsumi, S., Kim, Y. S., Trepel, J., & Neckers, L. (2011) · Oncotarget · doi:10.18632/oncotarget.272 · Cited by 66

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

Chemoproteomics Reveals Time-Dependent Binding of Histone Deacetylase Inhibitors to Endogenous Repressor Complexes

Becher, I., Dittmann, A., Savitski, M. M., Hopf, C., Drewes, G., & Bantscheff, M. (2014) · ACS Chemical Biology · doi:10.1021/cb500235n · Cited by 60

Quantitative analysis of the secretion of the MCP family of chemokines by muscle cells

Henningsen, J., Pedersen, B. K., & Kratchmarova, I. (2010) · Molecular BioSystems · doi:10.1039/c0mb00209g · Cited by 51

Machines vs. Ensembles: Effective MAPK Signaling through Heterogeneous Sets of Protein Complexes

Suderman, R., & Deeds, E. J. (2013) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1003278 · Cited by 52

Nuclear Phosphoproteomic Screen Uncovers ACLY as Mediator of IL-2-induced Proliferation of CD4+ T lymphocytes

Osinalde, N., Mitxelena, J., Sánchez-Quiles, V., Akimov, V., Aloria, K., Arizmendi, J. M., Zubiaga, A. M., Blagoev, B., & Kratchmarova, I. (2016) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m115.057158 · Cited by 48

Role of serine-threonine phosphoprotein phosphatases in smooth muscle contractility

Butler, T., Paul, J., Europe-Finner, N., Smith, R., & Chan, E.-C. (2013) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00161.2012 · Cited by 48

Quantitative Proteomics Reveals the Induction of Mitophagy in Tumor Necrosis Factor-α-activated (TNFα) Macrophages

Bell, C., English, L., Boulais, J., Chemali, M., Caron-Lizotte, O., Desjardins, M., & Thibault, P. (2013) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m112.025775 · Cited by 46

Recent insights into Histone Acetyltransferase-1: biological function and involvement in pathogenesis

Poziello, A., Nebbioso, A., Stunnenberg, H. G., Martens, J. H. A., Carafa, V., & Altucci, L. (2021) · Epigenetics · doi:10.1080/15592294.2020.1827723 · Cited by 44

Structural basis for interdomain communication in SHIP2 providing high phosphatase activity

Le Coq, J., Camacho-Artacho, M., Velázquez, J. V., Santiveri, C. M., Gallego, L. H., Campos-Olivas, R., Dölker, N., & Lietha, D. (2017) · eLife · doi:10.7554/elife.26640 · Cited by 42

PTMScout, a Web Resource for Analysis of High Throughput Post-translational Proteomics Studies

Naegle, K. M., Gymrek, M., Joughin, B. A., Wagner, J. P., Welsch, R. E., Yaffe, M. B., Lauffenburger, D. A., & White, F. M. (2010) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m110.001206 · Cited by 41

CD74-dependent deregulation of the tumor suppressor Scribble in human epithelial and breast cancer cells

Metodieva, G., Nogueira-de-Souza, N. C., Greenwood, C., Al-Janabi, K., Leng, L., Bucala, R., & Metodiev, M. V. (2013) · Neoplasia · doi:10.1593/neo.13464 · Cited by 40

The Molecular Mechanism of Eukaryotic Elongation Factor 2 Kinase Activation

Tavares, C. D. J., Ferguson, S. B., Giles, D. H., Wang, Q., Wellmann, R. M., O'Brien, J. P., Warthaka, M., Brodbelt, J. S., Ren, P., & Dalby, K. N. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.577148 · Cited by 38

Phosphorylation of the p68 subunit of Pol δ acts as a molecular switch to regulate its interaction with PCNA

Rahmeh, A. A., Zhou, Y., Xie, B., Li, H., Lee, E. Y. C., & Lee, M. Y. W. T. (2012) · Biochemistry · doi:10.1021/bi201638e · Cited by 33

Quantitative proteomics for the analysis of spatio-temporal protein dynamics during autophagy

Zimmermann, A. C., Zarei, M., Eiselein, S., & Dengjel, J. (2010) · Autophagy · doi:10.4161/auto.6.8.12786 · Cited by 28

The C-terminal region of the human p23 chaperone modulates its structure and function

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