Quantitative Proteomic Analysis of Histone Modifications

Histone H3 Lysine 56 Methylation Regulates DNA Replication through Its Interaction with PCNA

Yu, Y., Song, C., Zhang, Q., DiMaggio, P. A., Garcia, B. A., York, A. G., Carey, M., & Grunstein, M. R. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.01.019 · Cited by 130

Automated de novo protein sequencing of monoclonal antibodies

Bandeira, N., Pham, V. C., Pevzner, P. A., Arnott, D. P., & Lill, J. R. (2008) · Nature Biotechnology · doi:10.1038/nbt1208-1336 · Cited by 130

Protein Interactions, Post-translational Modifications and Topologies in Human Cells

Chavez, J. D., Weisbrod, C. R., Zheng, C., Eng, J. K., & Bruce, J. E. (2013) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m112.024497 · Cited by 128

Comparative Analysis of Cleavable Azobenzene-Based Affinity Tags for Bioorthogonal Chemical Proteomics

Yang, Y., Grammel, M., Raghavan, A. S., Charron, G., & Hang, H. C. (2010) · Chemistry & Biology · doi:10.1016/j.chembiol.2010.09.012 · Cited by 126

β-N-Acetylglucosamine (O-GlcNAc) Is a Novel Regulator of Mitosis-specific Phosphorylations on Histone H3

Fong, J. J., Nguyen, B. L., Bridger, R., Medrano, E. E., Wells, L., Pan, S., & Sifers, R. N. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.315804 · Cited by 126

Structural Insight into the Zinc Finger CW Domain as a Histone Modification Reader

He, F., Umehara, T., Saito, K., Harada, T., Watanabe, S., Yabuki, T., Kigawa, T., Takahashi, M., Kuwasako, K., Tsuda, K., et al. (2010) · Structure · doi:10.1016/j.str.2010.06.012 · Cited by 126

Quantitative Dynamics of the Link between Cellular Metabolism and Histone Acetylation

Evertts, A. G., Zee, B. M., DiMaggio, P. A., Gonzales-Cope, M., Coller, H. A., & Garcia, B. A. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.428318 · Cited by 125

Chromatin as an expansive canvas for chemical biology

Fierz, B., & Muir, T. W. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.938 · Cited by 125

Site‐Specific Incorporation of ε‐N‐Crotonyllysine into Histones

Kim, C. H., Kang, M., Kim, H. J., Chatterjee, A., & Schultz, P. G. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201203349 · Cited by 125

Measurement of acetylation turnover at distinct lysines in human histones identifies long-lived acetylation sites

Zheng, Y., Thomas, P. M., & Kelleher, N. L. (2013) · Nature Communications · doi:10.1038/ncomms3203 · Cited by 124

Breaking the histone code with quantitative mass spectrometry

Britton, L.-M. P., Gonzales-Cope, M., Zee, B. M., & Garcia, B. A. (2011) · Expert Review of Proteomics · doi:10.1586/epr.11.47 · Cited by 124

An N α-Acetyltransferase Responsible for Acetylation of the N-terminal Residues of Histones H4 and H2A

Song, O.-K., Wang, I. X., Waterborg, J. H., & Sternglanz, R. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c300355200 · Cited by 124

RECENT ADVANCES IN QUANTITATIVE NEUROPROTEOMICS

Craft, G., Chen, A., & Nairn, A. (2013) · Methods · doi:10.1016/j.ymeth.2013.04.008 · Cited by 124

Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation

Still, A. J., Floyd, B. J., Hebert, A. S., Bingman, C. A., Carson, J. J., Gunderson, D. R., Dolan, B. K., Grimsrud, P. A., Dittenhafer-Reed, K. E., Stapleton, D. S., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.483396 · Cited by 123

Identification of Protein Modifications Using MS/MS de Novo Sequencing and the OpenSea Alignment Algorithm

Searle, B. C., Dasari, S., Wilmarth, P. A., Turner, M., Reddy, A. P., David, L. L., & Nagalla, S. R. (2005) · Journal of Proteome Research · doi:10.1021/pr049781j · Cited by 123

Extending the Scope of NMR Spectroscopy with Microcoil Probes

Schroeder, F. C., & Gronquist, M. R. (2006) · Angewandte Chemie International Edition · doi:10.1002/anie.200601789 · Cited by 120

Modification Site Localization Scoring Integrated into a Search Engine

Baker, P. R., Trinidad, J. C., & Chalkley, R. J. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.008078 · Cited by 120

The enhancement of histone H4 and H2A serine 1 phosphorylation during mitosis and S-phase is evolutionarily conserved

Barber, C. M., Turner, F. B., Wang, Y., Hagstrom, K., Taverna, S. D., Mollah, S., Ueberheide, B. M., Meyer, B. J., Hunt, D. F., Cheung, P., et al. (2004) · Chromosoma · doi:10.1007/s00412-004-0281-9 · Cited by 119

Histone H2B Phosphorylation in Mammalian Apoptotic Cells

Ajiro, K. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.1.439 · Cited by 119

NeuCode Labels for Relative Protein Quantification

Merrill, A. E., Hebert, A. S., MacGilvray, M. E., Rose, C. M., Bailey, D. J., Bradley, J. C., Wood, W. W., Masri, M. E., Westphall, M. S., Gasch, A. P., et al. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m114.040287 · Cited by 119

A Combination of H2A.Z and H4 Acetylation Recruits Brd2 to Chromatin during Transcriptional Activation

Draker, R., Ng, M. K., Sarcinella, E., Ignatchenko, V., Kislinger, T., & Cheung, P. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1003047 · Cited by 118

The Human N-Alpha-Acetyltransferase 40 (hNaa40p/hNatD) Is Conserved from Yeast and N-Terminally Acetylates Histones H2A and H4

Hole, K., Damme, P. V., Dalva, M., Aksnes, H., Glomnes, N., Varhaug, J. E., Lillehaug, J. R., Gevaert, K., & Arnesen, T. (2011) · PLoS ONE · doi:10.1371/journal.pone.0024713 · Cited by 117

Modification Site Localization Scoring: Strategies and Performance

Chalkley, R. J., & Clauser, K. R. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r111.015305 · Cited by 116

Proteome-wide prediction of acetylation substrates

Basu, A. B., Rose, K. L., Zhang, J., Beavis, R. C., Ueberheide, B. M., Garcia, B. A., Chait, B. T., Zhao, Y., Hunt, D. F., Segal, E., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0906801106 · Cited by 116

Combining affinity purification by ADP-ribose-binding macro domains with mass spectrometry to define the mammalian ADP-ribosyl proteome

Dani, N., Stilla, A., Marchegiani, A., Tamburro, A., Till, S., Ladurner, A. G., Corda, D., & Girolamo, M. D. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900066106 · Cited by 114

Construction of a hybrid quadrupole/fourier transform ion cyclotron resonance mass spectrometer for versatile MS/MS above 10 kDa

Patrie, S. M., Charlebois, J. P., Whipple, D., Kelleher, N. L., Hendrickson, C. L., Quinn, J. P., Marshall, A. G., & Mukhopadhyay, B. (2004) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2004.04.031 · Cited by 114

Generation of acetyllysine antibodies and affinity enrichment of acetylated peptides

Guan, K., Yu, W., Lin, Y., Xiong, Y., & Zhao, S. (2010) · Nature Protocols · doi:10.1038/nprot.2010.117 · Cited by 113

Design, Implementation and Multisite Evaluation of a System Suitability Protocol for the Quantitative Assessment of Instrument Performance in Liquid Chromatography-Multiple Reaction Monitoring-MS (LC-MRM-MS)

Abbatiello, S. E., Mani, D. R., Schilling, B., MacLean, B., Zimmerman, L. J., Feng, X., Cusack, M. P., Sedransk, N., Hall, S. C., Addona, T. A., et al. (2013) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m112.027078 · Cited by 113

Gene-Specific Characterization of Human Histone H2B by Electron Capture Dissociation

Siuti, N., Roth, M. J., Mizzen, C. A., Kelleher, N. L., & Pesavento, J. J. (2006) · Journal of Proteome Research · doi:10.1021/pr050268v · Cited by 112

Phosphorylation of Histone H3 Thr-45 Is Linked to Apoptosis

Hurd, P. J., Bannister, A. J., Halls, K., Dawson, M. A., Vermeulen, M., Olsen, J. V., Ismail, H. M., Somers, J., Mann, M., Owen‐Hughes, T., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.005421 · Cited by 112

The significance, development and progress of high-throughput combinatorial histone code analysis

Young, N. L., DiMaggio, P. A., & Garcia, B. A. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0475-7 · Cited by 111

Structures of protein domains that create or recognize histone modifications

Bottomley, M. J. (2004) · EMBO Reports · doi:10.1038/sj.embor.7400146 · Cited by 110

Exploiting the kernel trick to correlate fragment ions for peptide identification via tandem mass spectrometry

Fu, Y., Yang, Q., Sun, R.-X., Li, D., Zeng, R., Ling, C. X., & Gao, W. (2004) · Bioinformatics · doi:10.1093/bioinformatics/bth186 · Cited by 110

Deimination of Histone H2A and H4 at Arginine 3 in HL-60 Granulocytes

Hagiwara, T., Hidaka, Y., & Yamada, M. (2005) · Biochemistry · doi:10.1021/bi047505c · Cited by 108

The CW domain, a new histone recognition module in chromatin proteins

Hoppmann, V., Thorstensen, T., Kristiansen, P. E., Veiseth, S. V., Rahman, M. A., Finne, K., Aalen, R. B., & Aasland, R. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.108 · Cited by 108

Histone H1 variant-specific lysine methylation by G9a/KMT1C and Glp1/KMT1D

Weiss, T., Hergeth, S., Zeißler, U., Izzo, A., Tropberger, P., Zee, B. M., Dundr, M., Garcia, B. A., Daujat, S., & Schneider, R. (2010) · Epigenetics & Chromatin · doi:10.1186/1756-8935-3-7 · Cited by 107

Histone H1 phosphorylation is associated with transcription by RNA polymerases I and II

Zheng, Y., John, S., Pesavento, J. J., Schultz-Norton, J. R., Schiltz, R. L., Baek, S., Nardulli, A. M., Hager, G. L., Kelleher, N. L., & Mizzen, C. A. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201001148 · Cited by 107

Quantitative Proteomic Analysis Using Isobaric Protein Tags Enables Rapid Comparison of Changes in Transcript and Protein Levels in Transformed Cells

Unwin, R. D., Pierce, A., Watson, R. B., Sternberg, D., & Whetton, A. D. (2005) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m400193-mcp200 · Cited by 106

Mitotic phosphorylation of histone H3 at threonine 3

Polioudaki, H., Markaki, Y., Kourmouli, N., Dialynas, G. K., Theodoropoulos, P. A., Singh, P. B., & Georgatos, S. D. (2004) · FEBS Letters · doi:10.1016/s0014-5793(04)00060-2 · Cited by 105

Methylation of H2AR29 is a novel repressive PRMT6 target

Waldmann, T., Izzo, A., Kamieniarz-Gdula, K., Richter, F. M., Vogler, C., Sarg, B., Lindner, H. H., Young, N. L., Mittler, G., Garcia, B. A., et al. (2011) · Epigenetics & Chromatin · doi:10.1186/1756-8935-4-11 · Cited by 105

Characterization of Global Yeast Quantitative Proteome Data Generated from the Wild-Type and Glucose Repression Saccharomyces cerevisiae Strains: The Comparison of Two Quantitative Methods

Usaite, R., Wohlschlegel, J. A., Venable, J. D., Park, S. K., Nielsen, J., Lisbeth Olsson, A., & Yates, J. R. (2008) · Journal of Proteome Research · doi:10.1021/pr700580m · Cited by 105

Popitam: Towards new heuristic strategies to improve protein identification from tandem mass spectrometry data

Hernandez, P., Gras, R., Frey, J., & Appel, R. D. (2003) · PROTEOMICS · doi:10.1002/pmic.200300402 · Cited by 105

Applying Label-Free Quantitation to Top Down Proteomics

Ntai, I., Kim, K., Fellers, R. T., Skinner, O. S., Smith, A. D., Early, B. P., Savaryn, J. P., LeDuc, R. D., Thomas, P. M., & Kelleher, N. L. (2014) · Analytical Chemistry · doi:10.1021/ac500395k · Cited by 104

Phosphorylation of H3S10 Blocks the Access of H3K9 by Specific Antibodies and Histone Methyltransferase

Duan, Q., Chen, H., Costa, M., & Dai, W. H. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803312200 · Cited by 103

PTMap—A sequence alignment software for unrestricted, accurate, and full-spectrum identification of post-translational modification sites

Chen, Y., Chen, W., Cobb, M. H., & Zhao, Y. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0811739106 · Cited by 102

Analysis of Intact Protein Isoforms by Mass Spectrometry

Tipton, J. D., Tran, J. C., Catherman, A. D., Ahlf, D. R., Durbin, K. R., & Kelleher, N. L. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.r111.239442 · Cited by 102

TiO2-Based Phosphoproteomic Analysis of the Plasma Membrane and the Effects of Phosphatase Inhibitor Treatment

Thingholm, T. E., Larsen, M. R., Ingrell, C. R., Kassem, M. S., & Jensen, O. N. (2008) · Journal of Proteome Research · doi:10.1021/pr800099y · Cited by 99

A dual role of linker histone H1.4 Lys 34 acetylation in transcriptional activationPreprint

Kamieniarz, K., Izzo, A., Dundr, M., Tropberger, P., Ozretic, L., Kirfel, J., Scheer, E., Tropel, P., Wiśniewski, J. R., Tora, L., et al. (2012) · Genes & Development · doi:10.1101/gad.182014.111 · Cited by 99

De Novo Sequencing Methods in Proteomics

Hughes, C., Ma, B., & Lajoie, G. (2009) · Methods in molecular biology · doi:10.1007/978-1-60761-444-9_8 · Cited by 97

P-Mod: An Algorithm and Software To Map Modifications To Peptide Sequences Using Tandem MS Data

Hansen, B. T., Davey, S. W., Ham, A. L., & Liebler, D. C. (2005) · Journal of Proteome Research · doi:10.1021/pr0498234 · Cited by 97

Human Naa50p (Nat5/San) Displays Both Protein Nα- and Nϵ-Acetyltransferase Activity

Evjenth, R., Hole, K., Karlsen, O. A., Ziegler, M., Arnesen, T., & Lillehaug, J. R. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.001347 · Cited by 97

Quantitative Phosphoproteomic Analysis of the Tumor Necrosis Factor Pathway

Cantin, G. T., Venable, J. D., Cociorva, D., & Yates, J. R. (2005) · Journal of Proteome Research · doi:10.1021/pr050270m · Cited by 96

Apoptosis-associated acetylation on histone H2B is an epitope for lupus autoantibodies

van Bavel, C. C., Dieker, J., Muller, S., et al. (2009) · Molecular Immunology · doi:10.1016/j.molimm.2009.08.009 · Cited by 95

Top-down quantitation and characterization of SILAC-labeled proteins

Waanders, L. F., Hanke, S., & Mann, M. (2007) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2007.09.001 · Cited by 95

Online Nanoflow Multidimensional Fractionation for High Efficiency Phosphopeptide Analysis

Ficarro, S. B., Zhang, Y., Carrasco-Alfonso, M. J., Garg, B. K., Adelmant, G., Webber, J. T., Luckey, C. J., & Marto, J. A. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o111.011064 · Cited by 95

Identifying differences in protein expression levels by spectral counting and feature selection

Carvalho, P. C., Hewel, J. A., Barbosa, V. C., & Yates, J. R. (2008) · Genetics and Molecular Research · doi:10.4238/vol7-2gmr426 · Cited by 94

Chemical Approaches for Studying Histone Modifications

Chatterjee, C., & Muir, T. W. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.r109.080291 · Cited by 92

SLoMo: Automated Site Localization of Modifications from ETD/ECD Mass Spectra

Bailey, C. M., Sweet, S. M. M., Cunningham, D. L., Zeller, M., Heath, J. K., & Cooper, H. J. (2009) · Journal of Proteome Research · doi:10.1021/pr800917p · Cited by 91

Phosphoproteomic Analysis of Human Brain by Calcium Phosphate Precipitation and Mass Spectrometry

Xia, Q., Cheng, D., Duong, D. M., Gearing, M., Lah, J. J., Levey, A. I., & Peng, J. (2008) · Journal of Proteome Research · doi:10.1021/pr8000496 · Cited by 90

Histone modifications in Trypanosoma brucei

Mandava, V., Fernandez, J., Deng, H., Janzen, C. J., Hake, S. B., & Cross, G. (2007) · Molecular and Biochemical Parasitology · doi:10.1016/j.molbiopara.2007.07.005 · Cited by 89

Highly selective and rapid enrichment of phosphorylated peptides using gallium oxide‐coated magnetic microspheres for MALDI‐TOF‐MS and nano‐LC‐ESI‐MS/MS/MS analysis

Li, Y., Lin, H., Deng, C., Yang, P., & Zhang, X. (2007) · PROTEOMICS · doi:10.1002/pmic.200700454 · Cited by 89

A Comparative Study of Electrostatic Repulsion-Hydrophilic Interaction Chromatography (ERLIC) versus SCX-IMAC-Based Methods for Phosphopeptide Isolation/Enrichment

Gan, C. S., Guo, T., Zhang, H., Lim, S. K., & Sze, S. K. (2008) · Journal of Proteome Research · doi:10.1021/pr800473j · Cited by 89

Quantitative analysis of intact apolipoproteins in human HDL by top-down differential mass spectrometry

Mazur, M. T., Cardasis, H. L., Spellman, D. S., Liaw, A., Yates, N. A., & Hendrickson, R. C. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0910776107 · Cited by 87

Middle‐down hybrid chromatography/tandem mass spectrometry workflow for characterization of combinatorial post‐translational modifications in histones

Sidoli, S., Schwämmle, V., Ruminowicz, C., Hansen, T. A., Wu, X., Helin, K., & Jensen, O. N. (2014) · PROTEOMICS · doi:10.1002/pmic.201400084 · Cited by 87

A Universal Chemical Enrichment Method for Mapping the Yeast N-glycoproteome by Mass Spectrometry (MS)

Chen, W., Smeekens, J. M., & Wu, R. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.036251 · Cited by 87

Global Assessment of Combinatorial Post-translational Modification of Core Histones in Yeast Using Contemporary Mass Spectrometry

Jiang, L., Smith, J. N., Anderson, S. L., Ma, P., Mizzen, C. A., & Kelleher, N. L. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704194200 · Cited by 87

Histone Deacetylase Inhibitors Globally Enhance H3/H4 Tail Acetylation Without Affecting H3 Lysine 56 Acetylation

Drogaris, P., Villeneuve, V., Pomiès, C., Lee, E. H., Bourdeau, V., Bonneil, É., Ferbeyre, G., Verreault, A., & Thibault, P. (2012) · Scientific Reports · doi:10.1038/srep00220 · Cited by 87

Role of hMOF-Dependent Histone H4 Lysine 16 Acetylation in the Maintenance of TMS1/ASC Gene Activity

Kapoor-Vazirani, P., Kagey, J. D., Powell, D. R., & Vertino, P. M. (2008) · Cancer Research · doi:10.1158/0008-5472.can-08-0141 · Cited by 87

Building and Searching Tandem Mass Spectral Libraries for Peptide Identification

Lam, H. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r111.008565 · Cited by 87

PhosphoScore: An Open-Source Phosphorylation Site Assignment Tool for MSn Data

Ruttenberg, B. E., Pisitkun, T., Knepper, M. A., & Hoffert, J. D. (2008) · Journal of Proteome Research · doi:10.1021/pr800169k · Cited by 87

The Bromodomain of Gcn5 Regulates Site Specificity of Lysine Acetylation on Histone H3

Cieniewicz, A. M., Moreland, L. E., Ringel, A. E., Mackintosh, S. G., Raman, A., Gilbert, T. M., Wolberger, C., Tackett, A. J., & Taverna, S. D. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m114.038174 · Cited by 85

Proteogenomic characterization and mapping of nucleosomes decoded by Brd and HP1 proteins

LeRoy, G., Chepelev, I., DiMaggio, P. A., Blanco, M. A., Zee, B. M., Zhao, K., & Garcia, B. A. (2012) · Genome Biology · doi:10.1186/gb-2012-13-8-r68 · Cited by 84

Exploring the binding profiles of ConA, boronic acid and WGA by MALDI-TOF/TOF MS and magnetic particles☆

Sparbier, K., WENZEL, T., & Kostrzewa, M. (2006) · Journal of Chromatography B · doi:10.1016/j.jchromb.2006.06.028 · Cited by 84

Structure of polyubiquitinated histone H2A

Nickel, B. E., & Davie, J. (1989) · Biochemistry · doi:10.1021/bi00429a007 · Cited by 83

Open source libraries and frameworks for mass spectrometry based proteomics: A developer's perspective

Pérez‐Riverol, Y., Wang, R., Hermjakob, H., Müller, M., Vesada, V., & Vizcaíno, J. A. (2013) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2013.02.032 · Cited by 83

The methylproteome and the intracellular methylation network

Erce, M. A., Pang, C. N. I., Hart‐Smith, G., & Wilkins, M. R. (2012) · PROTEOMICS · doi:10.1002/pmic.201100397 · Cited by 83

Proteomic Analysis of Arginine Methylation Sites in Human Cells Reveals Dynamic Regulation During Transcriptional Arrest

Sylvestersen, K. B., Horn, H., Jungmichel, S., Jensen, L. J., & Nielsen, M. L. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o113.032748 · Cited by 83

Heritable chromatin structure: Mapping “memory” in histones H3 and H4

Smith, C. M., Haimberger, Z. W., Johnson, C. O., Wolf, A. J., Gafken, P. R., Zhang, Z., Parthun, M. R., & Gottschling, D. E. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.182424999 · Cited by 82

Mapping Post-translational Modifications of the Histone Variant MacroH2A1 Using Tandem Mass Spectrometry

Feixia Chu, C., Nusinow, D. A., Chalkley, R. J., Plath, K., Panning, B., & Burlingame, A. L. (2005) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m500285-mcp200 · Cited by 82

Structure and function of the BAH domain in chromatin biology

Yang, N., & Xu, R.-M. (2012) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2012.742035 · Cited by 82

Origins and Formation of Histone Methylation across the Human Cell Cycle

Zee, B. M., Britton, L.-M. P., Wolle, D. G., Haberman, D. M., & Garcia, B. A. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.06673-11 · Cited by 81

Enrichment and analysis of phosphopeptides under different experimental conditions using titanium dioxide affinity chromatography and mass spectrometry

Aryal, U. K., & Ross, A. R. S. (2009) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.4377 · Cited by 81

Molecular Insights into the Recognition of N-Terminal Histone Modifications by the BRPF1 Bromodomain

Poplawski, A., Hu, K., Lee, W., Natesan, S., Peng, D., Carlson, S., Shi, X., Baláž, Š., Markley, J. L., & Glass, K. C. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.12.007 · Cited by 81

H3K56me3 Is a Novel, Conserved Heterochromatic Mark That Largely but Not Completely Overlaps with H3K9me3 in Both Regulation and Localization

Jack, A. P. M., Bussemer, S., Hahn, M., Pünzeler, S., Snyder, M., Wells, M. B., Csankovszki, G., Solovei, I. V., Schotta, G., & Hake, S. B. (2013) · PLoS ONE · doi:10.1371/journal.pone.0051765 · Cited by 81

Selective Detection of Membrane Proteins Without Antibodies

Arnott, D. P., Kishiyama, A., Luis, E., Ludlum, S. G., Marsters, J. C., & Stults, J. T. (2002) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m100027-mcp200 · Cited by 81

SILAC-based proteomic analysis to dissect the “histone modification signature” of human breast cancer cells

Cuomo, A., Moretti, S., Minucci, S., & Bonaldi, T. (2010) · Amino Acids · doi:10.1007/s00726-010-0668-2 · Cited by 80

Improving Protein and Proteome Coverage through Data-Independent Multiplexed Peptide Fragmentation

Blackburn, K., Mbeunkui, F., Mitra, S. K., Mentzel, T., & Goshe, M. B. (2010) · Journal of Proteome Research · doi:10.1021/pr100144z · Cited by 79

EGFR Modulates DNA Synthesis and Repair through Tyr Phosphorylation of Histone H4

Chou, R., Wang, Y., Hsieh, Y., Li, L., Xia, W., Chang, W., Chang, L., Cheng, C.-C., Lai, C., Hsu, J. L., et al. (2014) · Developmental Cell · doi:10.1016/j.devcel.2014.06.008 · Cited by 78

Quantitative Assessment of Chromatin Immunoprecipitation Grade Antibodies Directed against Histone Modifications Reveals Patterns of Co-occurring Marks on Histone Protein Molecules

Peach, S. E., Rudomin, E. L., Udeshi, N. D., Carr, S. A., & Jaffe, J. D. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.015941 · Cited by 78

Tandem Mass Tag Protein Labeling for Top-Down Identification and Quantification

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Large Scale Analysis of Co-existing Post-translational Modifications in Histone Tails Reveals Global Fine Structure of Cross-talk

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