Quantitative Proteomic Analysis of Histone Modifications

Mapping Sites of O-GlcNAc Modification Using Affinity Tags for Serine and Threonine Post-translational Modifications

Wells, L., Vosseller, K., Cole, R. N., Cronshaw, J. M., Matunis, M. J., & Hart, G. W. (2002) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m200048-mcp200 · Cited by 420

Overlapping but Distinct Patterns of Histone Acetylation by the Human Coactivators p300 and PCAF within Nucleosomal Substrates

Schiltz, R. L., Mizzen, C. A., Vassilev, A., Cook, R. G., Allis, C. D., & Nakatani, Y. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.3.1189 · Cited by 415

Citrullination regulates pluripotency and histone H1 binding to chromatin

Christophorou, M. A., Castelo-Branco, G., Halley-Stott, R. P., Oliveira, C. S., Loos, R., Radzisheuskaya, A., Mowen, K. A., Bertone, P., Silva, J. C. R., Zernicka-Goetz, M., et al. (2014) · Nature · doi:10.1038/nature12942 · Cited by 412

Large-scale database searching using tandem mass spectra: Looking up the answer in the back of the book

Sadygov, R. G., Cociorva, D., & Yates, J. R. (2004) · Nature Methods · doi:10.1038/nmeth725 · Cited by 408

Epigenetics and cardiovascular disease

Ordovás, J. M., & Smith, C. E. (2010) · Nature Reviews Cardiology · doi:10.1038/nrcardio.2010.104 · Cited by 402

Ischemia in tumors induces early and sustained phosphorylation changes in stress kinase pathways but does not affect global protein levels

Mertins, P., Yang, F., Liu, T., Mani, D. R., Petyuk, V. A., Gillette, M. A., Clauser, K. R., Qiao, J. W., Gritsenko, M. A., Moore, R. J., et al. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.036392 · Cited by 400

Performance Characteristics of Electron Transfer Dissociation Mass Spectrometry

Good, D. M., Wirtala, M., McAlister, G. C., & Coon, J. J. (2007) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m700073-mcp200 · Cited by 396

Signaling Network Model of Chromatin

Schreiber, S. L., & Bernstein, B. E. (2002) · Cell · doi:10.1016/s0092-8674(02)01196-0 · Cited by 393

Metabolic Labeling of Mammalian Organisms with Stable Isotopes for Quantitative Proteomic Analysis

Wu, C. C., MacCoss, M. J., Howell, K. E., Matthews, D. E., & Yates, J. R. (2004) · Analytical Chemistry · doi:10.1021/ac049208j · Cited by 386

Proteomic analysis of S-nitrosylation and denitrosylation by resin-assisted capture

Forrester, M. T., Thompson, J. W., Foster, M. W., Nogueira, L., Moseley, M. A., & Stamler, J. S. (2009) · Nature Biotechnology · doi:10.1038/nbt.1545 · Cited by 385

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

Probability-Based Validation of Protein Identifications Using a Modified SEQUEST Algorithm

MacCoss, M. J., Wu, C. C., & Yates, J. R. (2002) · Analytical Chemistry · doi:10.1021/ac025826t · Cited by 377

Jmjd2b antagonizes H3K9 trimethylation at pericentric heterochromatin in mammalian cells

Fodor, B. D., Kubicek, S., Yonezawa, M., O’Sullivan, R. J., Sengupta, R., Perez-Burgos, L., Opravil, S., Mechtler, K., Schotta, G., & Jenuwein, T. (2006) · Genes & Development · doi:10.1101/gad.388206 · Cited by 374

β- N -acetylglucosamine (O-GlcNAc) is part of the histone code

Sakabe, K., Wang, Z., & Hart, G. W. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1009023107 · Cited by 373

Signaling Kinase AMPK Activates Stress-Promoted Transcription via Histone H2B Phosphorylation

Bungard, D., Fuerth, B. J., Zeng, P.-Y., Faubert, B., Maas, N. L., Viollet, B., Carling, D., Thompson, C. B., Jones, R. G., & Berger, S. L. (2010) · Science · doi:10.1126/science.1191241 · Cited by 372

Quantitative Phosphoproteomic Analysis of T Cell Receptor Signaling Reveals System-Wide Modulation of Protein-Protein Interactions

Mayya, V., Lundgren, D. H., Hwang, S.-I., Rezaul, K., Wu, L., Eng, J. K., Rodionov, V., & Han, D. K. (2009) · Science Signaling · doi:10.1126/scisignal.2000007 · Cited by 372

Localization of Labile Posttranslational Modifications by Electron Capture Dissociation: The Case of γ-Carboxyglutamic Acid

Kelleher, N. L., Zubarev, R. A., Bush, K., Furie, B., Furie, B. C., McLafferty, F. W., & Walsh, C. T. (1999) · Analytical Chemistry · doi:10.1021/ac990684x · Cited by 368

Myc-binding-site recognition in the human genome is determined by chromatin context

Guccione, E., Martinato, F., Finocchiaro, G., Luzi, L., Tizzoni, L., Dall' Olio, V., Zardo, G., Nervi, C., Bernard, L., & Amati, B. (2006) · Nature Cell Biology · doi:10.1038/ncb1434 · Cited by 366

Cathepsin L Proteolytically Processes Histone H3 During Mouse Embryonic Stem Cell Differentiation

Duncan, E. M., Muratore-Schroeder, T. L., Cook, R. G., Garcia, B. A., Shabanowitz, J., Hunt, D. F., & Allis, C. D. (2008) · Cell · doi:10.1016/j.cell.2008.09.055 · Cited by 364

OPERating ON Chromatin, a Colorful Language where Context Matters

Gardner, K. E., Allis, C. D., & Strahl, B. D. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.01.040 · Cited by 361

Electron-capture dissociation tandem mass spectrometry

Zubarev, R. A. (2004) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2003.12.002 · Cited by 360

Unimod: Protein modifications for mass spectrometry

Creasy, D. M., & Cottrell, J. S. (2004) · PROTEOMICS · doi:10.1002/pmic.200300744 · Cited by 354

Hdac3 is essential for the maintenance of chromatin structure and genome stability

Bhaskara, S., Knutson, S. K., Jiang, G., Chandrasekharan, M. B., Wilson, A. J., Zheng, S., Yenamandra, A., Locke, K., Yuan, J.-L., Bonine-Summers, A. R., et al. (2010) · Cancer Cell · doi:10.1016/j.ccr.2010.10.022 · Cited by 353

Recognition of a Mononucleosomal Histone Modification Pattern by BPTF via Multivalent Interactions

Ruthenburg, A. J., Li, H., Milne, T. A., Dewell, S., McGinty, R. K., Yuen, M., Ueberheide, B., Dou, Y., Muir, T. W., Patel, D. J., et al. (2011) · Cell · doi:10.1016/j.cell.2011.03.053 · Cited by 352

Site-specific characterization of the Asp- and Glu-ADP-ribosylated proteome

Zhang, Y., Wang, J., Ding, M., & Yu, Y. (2013) · Nature Methods · doi:10.1038/nmeth.2603 · Cited by 352

Partitioning of Histone H3-H4 Tetramers During DNA Replication–Dependent Chromatin Assembly

Xu, M., Long, C., Chen, X., Huang, C., Chen, S., & Zhu, B. (2010) · Science · doi:10.1126/science.1178994 · Cited by 351

Every amino acid matters: essential contributions of histone variants to mammalian development and disease

Maze, I., Noh, K.-M., Soshnev, A. A., & Allis, C. D. (2014) · Nature Reviews Genetics · doi:10.1038/nrg3673 · Cited by 349

Novel Linear Quadrupole Ion Trap/FT Mass Spectrometer: Performance Characterization and Use in the Comparative Analysis of Histone H3 Post-translational Modifications

Syka, J. E. P., Marto, J. A., Bai, D. L., Horning, S., Senko, M. W., Schwartz, J. C., Ueberheide, B., Garcia, B., Busby, S., Muratore, T., et al. (2004) · Journal of Proteome Research · doi:10.1021/pr0499794 · Cited by 348

The BAH domain of ORC1 links H4K20me2 to DNA replication licensing and Meier–Gorlin syndrome

Kuo, A. J., Song, J., Cheung, P., Ishibe-Murakami, S., Yamazoe, S., Chen, J. K., Patel, D. J., & Gozani, O. (2012) · Nature · doi:10.1038/nature10956 · Cited by 348

Screen for DNA‐damage‐responsive histone modifications identifies H3K9Ac and H3K56Ac in human cells

Tjeertes, J. V., Miller, K. M., & Jackson, S. P. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.119 · Cited by 347

Symmetric dimethylation of H3R2 is a newly identified histone mark that supports euchromatin maintenance

Migliori, V., Müller, J., Phalke, S., Low, D., Bezzi, M., Mok, W. C., Sahu, S. K., Gunaratne, J., Capasso, P., Bassi, C., et al. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2209 · Cited by 345

Hydrophilic Interaction Chromatography Reduces the Complexity of the Phosphoproteome and Improves Global Phosphopeptide Isolation and Detection

McNulty, D. E., & Annan, R. S. (2008) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m700543-mcp200 · Cited by 345

O-Linked N-Acetylglucosamine Proteomics of Postsynaptic Density Preparations Using Lectin Weak Affinity Chromatography and Mass Spectrometry

Vosseller, K., Trinidad, J. C., Chalkley, R. J., Specht, C. G., Thalhammer, A., Lynn, A. J., Snedecor, J. O., Guan, S., Medzihradszky, K. F., Maltby, D. A., et al. (2006) · Molecular & Cellular Proteomics · doi:10.1074/mcp.t500040-mcp200 · Cited by 345

Histone sumoylation is a negative regulator in Saccharomyces cerevisiae and shows dynamic interplay with positive-acting histone modifications

Nathan, D., Ingvarsdottir, K., Sterner, D. E., Bylebyl, G. R., Dokmanovic, M., Dorsey, J. A., Whelan, K. A., Krsmanovic, M., Lane, W. S., Meluh, P. B., et al. (2006) · Genes & Development · doi:10.1101/gad.1404206 · Cited by 344

An evaluation, comparison, and accurate benchmarking of several publicly available MS/MS search algorithms: Sensitivity and specificity analysis

Kapp, E. A., Schütz, F., Connolly, L. M., Chakel, J. A., Meza, J. E., Miller, C. A., Fenyo, D., Eng, J. K., Adkins, J. N., Omenn, G. S., et al. (2005) · PROTEOMICS · doi:10.1002/pmic.200500126 · Cited by 344

Methylation of Histone H3 by Coactivator-Associated Arginine Methyltransferase 1

Schurter, B. T., Koh, S. S., Chen, D., Bunick, G. J., Harp, J. M., Hanson, B. L., Henschen-Edman, A., Mackay, D. R., Stallcup, M. R., & Aswad, D. W. (2001) · Biochemistry · doi:10.1021/bi002631b · Cited by 342

Chemical reporters for biological discovery

Grammel, M., & Hang, H. C. (2013) · Nature Chemical Biology · doi:10.1038/nchembio.1296 · Cited by 342

Probing the dynamics of O-GlcNAc glycosylation in the brain using quantitative proteomics

Khidekel, N., Ficarro, S. B., Clark, P. M., Bryan, M. C., Swaney, D. L., Rexach, J. E., Sun, Y. E., Coon, J. J., Peters, E. C., & Hsieh-Wilson, L. C. (2007) · Nature Chemical Biology · doi:10.1038/nchembio881 · Cited by 339

Extremely long-lived nuclear pore proteins in the rat brain

Savas, J. N., Toyama, B. H., Xu, T., Yates, J. R., & Hetzer, M. W. (2012) · Science · doi:10.1126/science.1217421 · Cited by 335

Diverse polyubiquitin interaction properties of ubiquitin-associated domains

Raasi, S., Varadan, R., Fushman, D., & Pickart, C. M. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb962 · Cited by 335

Expression Patterns and Post-translational Modifications Associated with Mammalian Histone H3 Variants

Hake, S. B., Garcia, B. A., Duncan, E. M., Kauer, M., Dellaire, G., Shabanowitz, J., Bazett-Jones, D. P., Allis, C. D., & Hunt, D. F. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m509266200 · Cited by 333

Refined Preparation and Use of Anti-diglycine Remnant (K-ε-GG) Antibody Enables Routine Quantification of 10,000s of Ubiquitination Sites in Single Proteomics Experiments

Udeshi, N. D., Svinkina, T., Mertins, P., Kuhn, E., Mani, D. R., Qiao, J. W., & Carr, S. A. (2013) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o112.027094 · Cited by 333

GlcNAcylation of histone H2B facilitates its monoubiquitination

Fujiki, R., Hashiba, W., Sekine, H., Yokoyama, A., Chikanishi, T., Ito, S., Imai, Y., Kim, J., He, H. H., Igarashi, K., et al. (2011) · Nature · doi:10.1038/nature10656 · Cited by 330

Extending Top-Down Mass Spectrometry to Proteins with Masses Greater Than 200 Kilodaltons

Han, X., Jin, M., Breuker, K., & McLafferty, F. W. (2006) · Science · doi:10.1126/science.1128868 · Cited by 328

Cross-talk between GlcNAcylation and phosphorylation: Site-specific phosphorylation dynamics in response to globally elevated O -GlcNAc

Wang, Z., Gucek, M., & Hart, G. W. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0806216105 · Cited by 328

A tagging-via-substrate technology for detection and proteomics of farnesylated proteins

Kho, Y., Kim, S. C., Jiang, C., Barma, D., Kwon, S. W., Cheng, J., Jaunbergs, J., Weinbaum, C., Tamanoi, F., Falck, J., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0403413101 · Cited by 327

Mass Spectral Analysis in Proteomics

Yates, J. R. (2004) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.33.111502.082538 · Cited by 326

Proline Isomerization of Histone H3 Regulates Lysine Methylation and Gene Expression

Nelson, C. J., Santos-Rosa, H., & Kouzarides, T. (2006) · Cell · doi:10.1016/j.cell.2006.07.026 · Cited by 319

Structural Mechanism of the Bromodomain of the Coactivator CBP in p53 Transcriptional Activation

Mujtaba, S., He, Y., Zeng, L., Yan, S., Plotnikova, O., Sachchidanand, Sanchez, R., Zeleznik-Le, N. J., Ronai, Z., & Zhou, M.-M. (2004) · Molecular Cell · doi:10.1016/s1097-2765(03)00528-8 · Cited by 319

Quantifying protein interaction dynamics by SWATH mass spectrometry: application to the 14-3-3 system

Collins, B. C., Gillet, L. C., Rosenberger, G., Röst, H. L., Vichalkovski, A., Gstaiger, M., & Aebersold, R. (2013) · Nature Methods · doi:10.1038/nmeth.2703 · Cited by 314

Organismal Differences in Post-translational Modifications in Histones H3 and H4

Garcia, B. A., Hake, S. B., Diaz, R. L., Kauer, M., Morris, S. A., Recht, J., Shabanowitz, J., Mishra, N., Strahl, B. D., Allis, C. D., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m607900200 · Cited by 313

Readout of Epigenetic Modifications

Patel, D. J., & Wang, Z. (2013) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-072711-165700 · Cited by 313

Crosstalk between CARM1 Methylation and CBP Acetylation on Histone H3

Daujat, S., Bauer, U.-M., Shah, V., Turner, B., Berger, S., & Kouzarides, T. (2002) · Current Biology · doi:10.1016/s0960-9822(02)01387-8 · Cited by 313

High Throughput Characterization of Combinatorial Histone Codes

Young, N. L., DiMaggio, P. A., Plazas-Mayorca, M. D., Baliban, R. C., Floudas, C. A., & Garcia, B. A. (2009) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m900238-mcp200 · Cited by 312

Chemical Studies of Histone Acetylation

Gershey, E. L., Vidali, G., & Allfrey, V. G. (1968) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)91985-x · Cited by 306

PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation

Hyllus, D., Stein, C., Schnabel, K., Schiltz, E., Imhof, A., Dou, Y., Hsieh, J., & Bauer, U.-M. (2007) · Genes & Development · doi:10.1101/gad.447007 · Cited by 306

Phosphorylation of histone H3T6 by PKCβI controls demethylation at histone H3K4

Metzger, E., Imhof, A., Patel, D., Kahl, P., Hoffmeyer, K., Friedrichs, N., Müller, J. M., Greschik, H., Kirfel, J., Ji, S., et al. (2010) · Nature · doi:10.1038/nature08839 · Cited by 304

Isolation and Characterization of Suv39h2, a Second Histone H3 Methyltransferase Gene That Displays Testis-Specific Expression

O'Carroll, D., Scherthan, H., Peters, A. H. F. M., Opravil, S., Haynes, A. R., Laible, G., Rea, S., Schmid, M., Lebersorger, A., Jerratsch, M., et al. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.24.9423-9433.2000 · Cited by 304

Tandem mass spectrometry identifies many mouse brain O -GlcNAcylated proteins including EGF domain-specific O -GlcNAc transferase targets

Alfaro, J. F., Gong, C.-X., Monroe, M. E., Aldrich, J. T., Clauss, T. R. W., Purvine, S. O., Wang, Z., Camp, D. G., Shabanowitz, J., Stanley, P., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1200425109 · Cited by 300

Exploring the O -GlcNAc proteome: Direct identification of O -GlcNAc-modified proteins from the brain

Khidekel, N., Ficarro, S. B., Peters, E. C., & Hsieh-Wilson, L. C. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0403471101 · Cited by 299

Disruptor of Telomeric Silencing-1 Is a Chromatin-specific Histone H3 Methyltransferase

Lacoste, N., Utley, R. T., Hunter, J. M., Poirier, G. G., & Côté, J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200366200 · Cited by 298

Large-scale identification of ubiquitination sites by mass spectrometry

Udeshi, N. D., Mertins, P., Svinkina, T., & Carr, S. A. (2013) · Nature Protocols · doi:10.1038/nprot.2013.120 · Cited by 296

Histone variants: dynamic punctuation in transcription

Weber, C. M., & Henikoff, S. (2014) · Genes & Development · doi:10.1101/gad.238873.114 · Cited by 296

Enrichment of phosphorylated proteins and peptides from complex mixtures using metal oxide/hydroxide affinity chromatography (MOAC)

Wolschin, F., Wienkoop, S., & Weckwerth, W. (2005) · PROTEOMICS · doi:10.1002/pmic.200402049 · Cited by 296

Certain and Progressive Methylation of Histone H4 at Lysine 20 during the Cell Cycle

Pesavento, J. J., Yang, H., Kelleher, N. L., & Mizzen, C. A. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01517-07 · Cited by 289

Western Blots versus Selected Reaction Monitoring Assays: Time to Turn the Tables?

Aebersold, R., Burlingame, A. L., & Bradshaw, R. A. (2013) · Molecular & Cellular Proteomics · doi:10.1074/mcp.e113.031658 · Cited by 288

Solid-phase extraction of N-linked glycopeptides

Tian, Y., Zhou, Y., Elliott, S., Aebersold, R., & Zhang, H. (2007) · Nature Protocols · doi:10.1038/nprot.2007.42 · Cited by 286

Identification of Lysine Succinylation Substrates and the Succinylation Regulatory Enzyme CobB in Escherichia coli

Colak, G., Xie, Z., Zhu, A. Y., Dai, L., Lu, Z., Zhang, Y., Wan, X., Chen, Y., Cha, Y. H., Lin, H., et al. (2013) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.031567 · Cited by 278

Global chromatin profiling reveals NSD2 mutations in pediatric acute lymphoblastic leukemia

Jaffe, J. D., Wang, Y., Chan, H. M., Zhang, J., Huether, R., Kryukov, G. V., Bhang, H.-E. C., Taylor, J. E., Hu, M., Englund, N. P., et al. (2013) · Nature Genetics · doi:10.1038/ng.2777 · Cited by 277

A large-scale method to measure absolute protein phosphorylation stoichiometries

Wu, R., Haas, W., Dephoure, N., Huttlin, E. L., Zhai, B., Sowa, M. E., & Gygi, S. P. (2011) · Nature Methods · doi:10.1038/nmeth.1636 · Cited by 276

Acetylation dynamics and stoichiometry in Saccharomyces cerevisiae

Weinert, B. T., Iesmantavicius, V., Moustafa, T., Schölz, C., Wagner, S. A., Magnes, C., Zechner, R., & Choudhary, C. (2014) · Molecular Systems Biology · doi:10.1002/msb.134766 · Cited by 275

Proteome-Wide Mapping of the Drosophila Acetylome Demonstrates a High Degree of Conservation of Lysine Acetylation

Weinert, B. T., Wagner, S. A., Horn, H., Henriksen, P., Liu, W. R., Olsen, J. V., Jensen, L. J., & Choudhary, C. (2011) · Science Signaling · doi:10.1126/scisignal.2001902 · Cited by 275

Identification of novel histone post-translational modifications by peptide mass fingerprinting

Zhang, L., Eugeni, E. E., Parthun, M. R., & Freitas, M. A. (2003) · Chromosoma · doi:10.1007/s00412-003-0244-6 · Cited by 274

ATRX ADD domain links an atypical histone methylation recognition mechanism to human mental-retardation syndrome

Iwase, S., Xiang, B., Ghosh, S., Ren, T., Lewis, P. W., Cochrane, J. C., Allis, C. D., Picketts, D. J., Patel, D. J., Li, H., et al. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2062 · Cited by 271

Regulation of Transcription through Acetylation of H3K122 on the Lateral Surface of the Histone Octamer

Tropberger, P., Pott, S., Keller, C., Kamieniarz-Gdula, K., Caron, M., Richter, F., Li, G., Mittler, G., Liu, E. T., Bühler, M., et al. (2013) · Cell · doi:10.1016/j.cell.2013.01.032 · Cited by 270

Confident Phosphorylation Site Localization Using the Mascot Delta Score

Savitski, M. M., Lemeer, S., Boesche, M., Lang, M., Mathieson, T., Bantscheff, M., & Kuster, B. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m110.003830 · Cited by 265

PARP1 ADP-ribosylates lysine residues of the core histone tails

Messner, S., Altmeyer, M., Zhao, H., Pozivil, A., Roschitzki, B., Gehrig, P., Rutishauser, D., Huang, D., Caflisch, A., & Hottiger, M. O. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq463 · Cited by 264

Enrichment and Site Mapping of O-Linked N-Acetylglucosamine by a Combination of Chemical/Enzymatic Tagging, Photochemical Cleavage, and Electron Transfer Dissociation Mass Spectrometry

Wang, Z., Udeshi, N. D., O'Malley, M., Shabanowitz, J., Hunt, D. F., & Hart, G. W. (2010) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m900268-mcp200 · Cited by 261

In Vivo Residue-specific Histone Methylation Dynamics

Zee, B. M., Levin, R. S., Xu, B., LeRoy, G., Wingreen, N. S., & Garcia, B. A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.063784 · Cited by 260

Proteomic and phosphoproteomic comparison of human ES and iPS cells

Phanstiel, D. H., Brumbaugh, J., Wenger, C. D., Tian, S., Probasco, M. D., Bailey, D. J., Swaney, D. L., Tervo, M. A., Bolin, J. M., Ruotti, V., et al. (2011) · Nature Methods · doi:10.1038/nmeth.1699 · Cited by 259

Ion Coalescence of Neutron Encoded TMT 10-Plex Reporter Ions

Werner, T., Sweetman, G., Savitski, M. F., Mathieson, T., Bantscheff, M., & Savitski, M. M. (2014) · Analytical Chemistry · doi:10.1021/ac500140s · Cited by 258

Chromatin dynamics: Interplay between remodeling enzymes and histone modifications

Swygert, S. G., & Peterson, C. L. (2014) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2014.02.013 · Cited by 256

Eight-channel iTRAQ Enables Comparison of the Activity of Six Leukemogenic Tyrosine Kinases

Pierce, A., Unwin, R. D., Evans, C. A., Griffiths, S., Carney, L., Zhang, L., Jaworska, E., Lee, C.-F., Blinco, D., Okoniewski, M. J., et al. (2008) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m700251-mcp200 · Cited by 255

Gene bookmarking accelerates the kinetics of post-mitotic transcriptional re-activation

Zhao, R., Nakamura, T., Fu, Y., Lazar, Z., & Spector, D. L. (2011) · Nature Cell Biology · doi:10.1038/ncb2341 · Cited by 253

Fast liquid chromatography: The domination of core?shell and very fine particles

Fekete, S., Olh, E., & Fekete, J. (2012) · Journal of Chromatography A · doi:10.1016/j.chroma.2011.09.050 · Cited by 251

Histone H4 acetylation distinguishes coding regions of the human genome from heterochromatin in a differentiation-dependent but transcription-independent manner.

O'Neill, L. P., & Turner, B. M. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb00066.x · Cited by 249

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

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