Uncovering post-translational modification-associated protein–protein interactions

Histone Recognition and Large-Scale Structural Analysis of the Human Bromodomain Family

Filippakopoulos, P., Picaud, S., Mangos, M., Keates, T., Lambert, J., Baršytė-Lovejoy, D., Felletár, I., Volkmer, R., Müller, S., Pawson, T. J., et al. (2012) · Cell · doi:10.1016/j.cell.2012.02.013 · Cited by 1,759

Protein Posttranslational Modifications: The Chemistry of Proteome Diversifications

Walsh, C. T., Garneau‐Tsodikova, S., & Gatto, G. J. J. (2005) · Angewandte Chemie International Edition · doi:10.1002/anie.200501023 · Cited by 1,654

ERK1/2-dependent phosphorylation and nuclear translocation of PKM2 promotes the Warburg effect

Yang, W., Zheng, Y., Xia, Y., Ji, H., Chen, X., Guo, F., Lyssiotis, C. A., Aldape, K., Cantley, L. C., & Lu, Z. (2012) · Nature Cell Biology · doi:10.1038/ncb2629 · Cited by 926

Post-translational modifications in signal integration

Deribe, Y. L., Pawson, T., & Dikic, I. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1842 · Cited by 876

Quantitative interaction proteomics and genome-wide profiling of epigenetic histone marks and their readers

Vermeulen, M., Eberl, H. C., Matarese, F., Marks, H., Denissov, S., Butter, F., Lee, K. K., Olsen, J. V., Hyman, A. A., Stunnenberg, H. G., et al. (2010) · Cell · doi:10.1016/j.cell.2010.08.020 · Cited by 806

Phosphorylation of OPTN by TBK1 enhances its binding to Ub chains and promotes selective autophagy of damaged mitochondria

Richter, B., Sliter, D. A., Herhaus, L., Stolz, A., Wang, C., Beli, P., Zaffagnini, G., Wild, P., Martens, S., Wagner, S. A., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1523926113 · Cited by 755

Expanding and reprogramming the genetic code

Chin, J. W. (2017) · Nature · doi:10.1038/nature24031 · Cited by 740

Systematic Discovery of In Vivo Phosphorylation Networks

Linding, R., Jensen, L. J., Ostheimer, G. J., van Vugt, M. A. T. M., Jørgensen, C., Miron, I. M., Diella, F., Colwill, K., Taylor, L., Elder, K., et al. (2007) · Cell · doi:10.1016/j.cell.2007.05.052 · Cited by 739

Reading protein modifications with interaction domains

Seet, B. T., Đikić, I., Zhou, M., & Pawson, T. J. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1960 · Cited by 665

Native Chemical Ligation and Extended Methods: Mechanisms, Catalysis, Scope, and Limitations

Agouridas, V., Mahdi, O. E., Diemer, V., Cargoët, M., Monbaliu, J. M., & Melnyk, O. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00712 · Cited by 656

Integrated proteomic analysis of post-translational modifications by serial enrichment

Mertins, P., Qiao, J., Patel, J., Udeshi, N. D., Clauser, K. R., Mani, D. R., Burgess, M. W., Gillette, M. A., Jaffe, J. D., & Carr, S. A. (2013) · Nature Methods · doi:10.1038/nmeth.2518 · Cited by 619

Status of Large-scale Analysis of Post-translational Modifications by Mass Spectrometry

Olsen, J. V., & Mann, M. (2013) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o113.034181 · Cited by 607

Genetically encoding Nε-acetyllysine in recombinant proteins

Neumann, H., Peak‐Chew, S., & Chin, J. W. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.73 · Cited by 593

Transient Protein-Protein Interactions: Structural, Functional, and Network Properties

Perkins, J. R., Diboun, I., Dessailly, B. H., Lees, J., & Orengo, C. A. (2010) · Structure · doi:10.1016/j.str.2010.08.007 · Cited by 547

Computed structures of core eukaryotic protein complexes

Humphreys, I. R., Pei, J., Baek, M., Krishnakumar, A., Anishchenko, I., Ovchinnikov, S., Zhang, J., Ness, T. J., Banjade, S., Bagde, S. R., et al. (2021) · Science · doi:10.1126/science.abm4805 · Cited by 542

The Site-Specific Installation of Methyl-Lysine Analogs into Recombinant Histones

Simon, M. D., Feixia Chu, C., Racki, L. R., de la Cruz, C. C., Burlingame, A. L., Panning, B., Narlikar, G. J., & Shokat, K. M. (2007) · Cell · doi:10.1016/j.cell.2006.12.041 · Cited by 476

TRIM24 links a non-canonical histone signature to breast cancer

Tsai, W.-W., Wang, Z., Yiu, T. T., Akdemir, K. C., Xia, W., Winter, S., Tsai, C., Shi, X., Schwarzer, D., Plunkett, W. K., et al. (2010) · Nature · doi:10.1038/nature09542 · Cited by 453

Molecular Coupling of Histone Crotonylation and Active Transcription by AF9 YEATS Domain

Li, Y., Sabari, B. R., Panchenko, T., Wen, H., Zhao, D., Guan, H., Wan, L., Huang, H., Tang, Z., Zhao, Y., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.03.028 · Cited by 384

Expanding the Genetic Code of Escherichia coli with Phosphoserine

Park, H.-S., Hohn, M. J., Umehara, T., Guo, L., Osborne, E. M., Benner, J. S., Noren, C. J., Rinehart, J., & Söll, D. G. (2011) · Science · doi:10.1126/science.1207203 · Cited by 377

A “Tag-and-Modify” Approach to Site-Selective Protein Modification

Chalker, J. M., Bernardes, G. J. L., & Davis, B. G. (2011) · Accounts of Chemical Research · doi:10.1021/ar200056q · Cited by 354

Playing with the Molecules of Life

Young, D. D., & Schultz, P. G. (2018) · ACS Chemical Biology · doi:10.1021/acschembio.7b00974 · Cited by 346

Readout of Epigenetic Modifications

Patel, D. J., & Wang, Z. (2013) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-072711-165700 · Cited by 324

DNA binding of in vitro activated Stat1 alpha, Stat1 beta and truncated Stat1: interaction between NH2‐terminal domains stabilizes binding of two dimers to tandem DNA sites.

Vinkemeier, U., Cohen, S. L., Moarefi, I., Chait, B. T., Kuriyan, J., & Darnell, J. E. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00946.x · Cited by 308

Is there a code embedded in proteins that is based on post-translational modifications?

Sims, R. J., & Reinberg, D. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2502 · Cited by 289

Transient protein-protein interactions

Acuner, S. E., Engin, H. B., Gürsoy, A., & Keskin, Ö. (2011) · Protein Engineering Design and Selection · doi:10.1093/protein/gzr025 · Cited by 275

Deciphering protein post-translational modifications using chemical biology tools

Conibear, A. C. (2020) · Nature Reviews Chemistry · doi:10.1038/s41570-020-00223-8 · Cited by 252

Chemoenzymatic Semisynthesis of Proteins

Thompson, R. E., & Muir, T. W. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00450 · Cited by 245

Efficient genetic encoding of phosphoserine and its nonhydrolyzable analog

Rogerson, D. T., Sachdeva, A., Wang, K., Haq, T., Kazlauskaite, A., Hancock, S. M., Huguenin‐Dezot, N., Muqit, M. M. K., Fry, A. M., Bayliss, R. W., et al. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1823 · Cited by 231

Selective recognition of histone crotonylation by double PHD fingers of MOZ and DPF2

Xiong, X., Panchenko, T., Yang, S., Zhao, S., Yan, P., Zhang, W., Xie, W., Li, Y., Zhao, Y., Allis, C. D., et al. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2218 · Cited by 198

In rose, transcription factor PTM balances growth and drought survival via PIP2;1 aquaporin

Zhang, S., Ming, F., Chen, W., Zhou, X., Lu, J., Wang, Y., Li, Y., Jiang, C., Gan, S., Ma, N., et al. (2019) · Nature Plants · doi:10.1038/s41477-019-0376-1 · Cited by 179

Glutamine Triggers Acetylation-Dependent Degradation of Glutamine Synthetase via the Thalidomide Receptor Cereblon

Van Nguyen, T., Lee, J. E., Sweredoski, M. J., Yang, S.-J., Jeon, S.-J., Harrison, J. S., Yim, J.-H., Lee, S. G., Handa, H., Kuhlman, B., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.02.032 · Cited by 177

Synthesis of modified proteins via functionalization of dehydroalanine

Daďová, J., Galan, S. R. G., & Davis, B. G. (2018) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2018.05.022 · Cited by 173

Glutarylation of Histone H4 Lysine 91 Regulates Chromatin Dynamics

Bao, X., Liu, Z., Zhang, W., Gladysz, K., Fung, Y. M. E., Tian, G., Xiong, Y., Wong, J. W. H., Yuen, K. W. Y., & Li, X. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.08.018 · Cited by 171

Biosynthesis and genetic encoding of phosphothreonine through parallel selection and deep sequencing

Zhang, M. S., Brunner, S. F., Huguenin‐Dezot, N., Liang, A. D., Schmied, W. H., Rogerson, D. T., & Chin, J. W. (2017) · Nature Methods · doi:10.1038/nmeth.4302 · Cited by 160

Recombinant expression of selectively sulfated proteins in Escherichia coli

Liu, C. C., & Schultz, P. G. (2006) · Nature Biotechnology · doi:10.1038/nbt1254 · Cited by 157

Site-specific ubiquitylation and SUMOylation using genetic-code expansion and sortase

Fottner, M., Brunner, A., Bittl, V., Horn‐Ghetko, D., Jussupow, A., Kaila, V. R. I., Bremm, A., & Lang, K. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0227-4 · 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

Quantitative Chemical Proteomics Approach To Identify Post-translational Modification-Mediated Protein–Protein Interactions

Li, X., Foley, E. A., Molloy, K. R., Li, Y., Chait, B. T., & Kapoor, T. M. (2012) · Journal of the American Chemical Society · doi:10.1021/ja210528v · Cited by 128

Engineering a Proximity-Directed O-GlcNAc Transferase for Selective Protein O-GlcNAcylation in Cells

Ramirez, D. H., Aonbangkhen, C., Wu, H., Naftaly, J. A., Tang, S., O’Meara, T. R., & Woo, C. M. (2020) · ACS Chemical Biology · doi:10.1021/acschembio.0c00074 · Cited by 128

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

Genetically Encoding Protein Oxidative Damage

Neumann, H., Hazen, J. L., Weinstein, J. R., Mehl, R. A., & Chin, J. W. (2008) · Journal of the American Chemical Society · doi:10.1021/ja710100d · Cited by 122

Site-Specific Introduction of an Acetyl-Lysine Mimic into Peptides and Proteins by Cysteine Alkylation

Huang, R., Holbert, M. A., Tarrant, M. K., Curtet, S., Colquhoun, D. R., Rabbitts, B. M., Dancy, B. C. R., Hwang, Y., Tang, Y., Meeth, K. M., et al. (2010) · Journal of the American Chemical Society · doi:10.1021/ja103954u · Cited by 116

Site-specific incorporation of phosphotyrosine using an expanded genetic code

Hoppmann, C., Wong, A., Yang, B., Li, S., Hunter, T., Shokat, K. M., & Wang, L. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2406 · Cited by 112

A Genetically Encoded Metabolically Stable Analogue of Phosphotyrosine in Escherichia coli

Xie, J., Supeková, Ľ., & Schultz, P. G. (2007) · ACS Chemical Biology · doi:10.1021/cb700083w · Cited by 102

Photo-lysine captures proteins that bind lysine post-translational modifications

Yang, T., Li, X., Bao, X., Fung, Y. M. E., & Li, X. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1990 · Cited by 97

Protein Glycoengineering Enabled by the Versatile Synthesis of Aminooxy Glycans and the Genetically Encoded Aldehyde Tag

Hudak, J. E., Yu, H. H., & Bertozzi, C. R. (2011) · Journal of the American Chemical Society · doi:10.1021/ja206023e · Cited by 93

Genetically encoded protein sulfation in mammalian cells

Italia, J. S., Peeler, J. C., Hillenbrand, C. M., Latour, C., Weerapana, E., & Chatterjee, A. (2020) · Nature Chemical Biology · doi:10.1038/s41589-020-0493-1 · Cited by 91

Ubiquitin utilizes an acidic surface patch to alter chromatin structure

Debelouchina, G. T., Gerecht, K., & Muir, T. W. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2235 · Cited by 86

Identification of the YEATS domain of GAS41 as a pH-dependent reader of histone succinylation

Wang, Y., Jin, J., Chung, M. W. H., Feng, L., Sun, H., & Hao, Q. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1717664115 · Cited by 86

SIRT1 modulates cell cycle progression by regulating CHK2 acetylation−phosphorylation

Zhang, W., Feng, Y., Guo, Q., Guo, W., Xu, H., Li, X., Yi, F., Guan, Y., Geng, N., Wang, P., et al. (2019) · Cell Death and Differentiation · doi:10.1038/s41418-019-0369-7 · Cited by 86

Developing diazirine-based chemical probes to identify histone modification ‘readers’ and ‘erasers’

Yang, T., Liu, Z., & Li, X. (2014) · Chemical Science · doi:10.1039/c4sc02328e · Cited by 80

A modular toolbox to generate complex polymeric ubiquitin architectures using orthogonal sortase enzymes

Fottner, M., Weyh, M., Gaussmann, S., Schwarz, D., Sattler, M., & Lang, K. (2021) · Nature Communications · doi:10.1038/s41467-021-26812-9 · Cited by 73

Genetic recoding to dissect the roles of site-specific protein O-GlcNAcylation

Gorelik, A., Bartual, S. G., Borodkin, V. S., Varghese, J., Ferenbach, A. T., & van Aalten, D. M. F. (2019) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0325-8 · Cited by 69

Arginine Citrullination at the C-Terminal Domain Controls RNA Polymerase II Transcription

Sharma, P., Lioutas, A., Fernández‐Fuentes, N., Quilez, J., Carbonell‐Caballero, J., Wright, R. H. G., Vona, C. D., Dily, F. L., Schüller, R., Eick, D., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.10.016 · Cited by 66

Genetically Encoded Photoaffinity Histone Marks

Xie, X., Li, X., Lin, J., Lin, J., Zhang, G., Zhao, J., Bao, X., Zhu, R., Song, H., Li, X., et al. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b01431 · Cited by 65

Genetic Incorporation of ε-N-2-Hydroxyisobutyryl-lysine into Recombinant Histones

Xiao, H., Xuan, W., Shao, S., Liu, T., & Schultz, P. G. (2015) · ACS Chemical Biology · doi:10.1021/cb501055h · Cited by 64

Integrative Chemical Biology Approaches for Identification and Characterization of “Erasers” for Fatty‐Acid‐Acylated Lysine Residues within Proteins

Liu, Z., Yang, T., Li, X., Peng, T., Hang, H. C., & Li, X. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201408763 · Cited by 63

Capturing Post-Translational Modification-Triggered Protein–Protein Interactions Using Dual Noncanonical Amino Acid Mutagenesis

Zheng, Y., Gilgenast, M. J., Hauc, S. C., & Chatterjee, A. (2018) · ACS Chemical Biology · doi:10.1021/acschembio.8b00021 · Cited by 63

Semisynthesis of site-specifically succinylated histone reveals that succinylation regulates nucleosome unwrapping rate and DNA accessibility

Jing, Y., Ding, D., Tian, G., Kwan, K. C. J., Liu, Z., Ishibashi, T., & Li, X. D. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa663 · Cited by 62

Histone peptide microarray screen of chromo and Tudor domains defines new histone lysine methylation interactions

Shanle, E. K., Shinsky, S. A., Bridgers, J. B., Bae, N., Sagum, C. A., Krajewski, K., Rothbart, S. B., Bedford, M. T., & Strahl, B. D. (2017) · Epigenetics & Chromatin · doi:10.1186/s13072-017-0117-5 · Cited by 61

Site-specific incorporation of citrulline into proteins in mammalian cells

Mondal, S., Wang, S., Zheng, Y., Sen, S., Chatterjee, A., & Thompson, P. R. (2021) · Nature Communications · doi:10.1038/s41467-020-20279-w · Cited by 59

Sirtuins 1 and 2 Are Universal Histone Deacetylases

Hsu, W. W., Wu, B., & Liu, W. R. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.5b00886 · Cited by 56

Chemical Synthesis of Atomically Tailored SUMO E2 Conjugating Enzymes for the Formation of Covalently Linked SUMO–E2–E3 Ligase Ternary Complexes

Zhang, Y., Hirota, T., Kuwata, K., Oishi, S., Gramani, S. G., & Bode, J. W. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.9b06820 · Cited by 55

Chemical Probes Reveal Sirt2’s New Function as a Robust “Eraser” of Lysine Lipoylation

Xie, Y., Chen, L., Wang, R. Y., Wang, J., Li, J., Xu, W., Li, Y., Yao, S. Q., Zhang, L. N., Hao, Q., et al. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.9b06913 · Cited by 55

A computational method for the analysis and prediction of protein:phosphopeptide‐binding sites

Joughin, B. A., Tidor, B., & Yaffe, M. B. (2004) · Protein Science · doi:10.1110/ps.04964705 · Cited by 46

Proteomic Identification of Protein Tyrosine Phosphatase and Substrate Interactions in Living Mammalian Cells by Genetic Encoding of Irreversible Enzyme Inhibitors

Tang, H., Dai, Z., Qin, X., Cai, W., Hu, L., Huang, Y., Cao, W., Yang, F., Wang, C., & Liu, T. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b06922 · Cited by 46

The Methods Employed in Mass Spectrometric Analysis of Posttranslational Modifications (PTMs) and Protein–Protein Interactions (PPIs)

Yakubu, R., Nieves, E., & Weiss, L. M. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-15950-4_10 · Cited by 46

A tri-functional amino acid enables mapping of binding sites for posttranslational-modification-mediated protein-protein interactions

Lin, J., Bao, X., & Li, X. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.04.001 · Cited by 46

Wnt5a induces ROR1 to associate with 14-3-3ζ for enhanced chemotaxis and proliferation of chronic lymphocytic leukemia cells

Yu, J., Chen, L., Chen, Y., Hasan, M. K., Ghia, E. M., Zhang, L., Wu, R., Rassenti, L. Z., Widhopf, G. F., Shen, Z., et al. (2017) · Leukemia · doi:10.1038/leu.2017.132 · Cited by 43

Encoding human serine phosphopeptides in bacteria for proteome-wide identification of phosphorylation-dependent interactions

Barber, K. W., Muir, P., Szeligowski, R. V., Rogulina, S., Gerstein, M., Sampson, J. R., Isaacs, F. J., & Rinehart, J. (2018) · Nature Biotechnology · doi:10.1038/nbt.4150 · Cited by 43

Examining post‐translational modification‐mediated protein–protein interactions using a chemical proteomics approach

Li, X., Foley, E. A., Kawashima, S. A., Molloy, K. R., Li, Y., Chait, B. T., & Kapoor, T. M. (2012) · Protein Science · doi:10.1002/pro.2210 · Cited by 42

CpOGA D298N in complex with hOGA-derived S-GlcNAc peptide

Aalten, D. V., Bartual, S. G., & Gorelik, A. (2019) · Worldwide Protein Data Bank · doi:10.2210/pdb6rhe/pdb · Cited by 34

Targeted and Interactome Proteomics Revealed the Role of PHD2 in Regulating BRD4 Proline Hydroxylation

Erber, L. N., Luo, A., & Chen, Y. (2019) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra119.001535 · Cited by 31

Site-specific azide-acetyllysine photochemistry on epigenetic readers for interactome profiling

Sudhamalla, B., Dey, D., Breski, M., Nguyen, T. T. M., & Islam, K. (2017) · Chemical Science · doi:10.1039/c7sc00284j · Cited by 28

Crosstalk of Phosphorylation and Arginine Methylation in Disordered SRGG Repeats of Saccharomyces cerevisiae Fibrillarin and Its Association with Nucleolar Localization

Smith, D.-L., Erce, M. A., Lai, Y.-W., Tomasetig, F., Hart‐Smith, G., Hamey, J. J., & Wilkins, M. R. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.11.006 · Cited by 27

Identification of SUMO Binding Proteins Enriched after Covalent Photo-Cross-Linking

Brüninghoff, K., Aust, A., Taupitz, K. F., Wulff, S., Dörner, W., & Mootz, H. D. (2020) · ACS Chemical Biology · doi:10.1021/acschembio.0c00609 · Cited by 27

Citrullination of HP1γ chromodomain affects association with chromatin

Wiese, M., Bannister, A. J., Basu, S., Boucher, W., Wohlfahrt, K., Christophorou, M. A., Nielsen, M. L., Klenerman, D., Laue, E. D., & Kouzarides, T. (2019) · Epigenetics & Chromatin · doi:10.1186/s13072-019-0265-x · Cited by 23

Chemical proteomics approaches to examine novel histone posttranslational modifications

Li, X., & Li, X. D. (2014) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2014.10.015 · Cited by 21

Peptide-based approaches to identify and characterize proteins that recognize histone post-translational modifications

Lin, J., & Li, X. (2018) · Chinese Chemical Letters · doi:10.1016/j.cclet.2018.05.017 · Cited by 18

A Universal Peptide Matrix Interactomics Approach to Disclose Motif-Dependent Protein Binding

Ramberger, E., Suarez-Artiles, L., Pérez-Hernández, D., Haji, M., Popp, O., Reimer, U., Leutz, A., Dittmar, G., & Mertins, P. (2021) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2021.100135 · Cited by 18

Phosphorylation Modulates the Coregulatory Protein Exchange of the Nuclear Receptor Pregnane X Receptor

Cui, W., Shen, X., Agbas, E., Tompkins, B., Cameron-Carter, H. A., & Staudinger, J. L. (2020) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.119.264762 · Cited by 17

p50 mono-ubiquitination and interaction with BARD1 regulates cell cycle progression and maintains genome stability

Wu, L., Crawley, C. D., Garofalo, A., Nichols, J. W., Campbell, P.-A., Khramtsova, G. F., Olopade, O. I., Weichselbaum, R. R., & Yamini, B. (2020) · Nature Communications · doi:10.1038/s41467-020-18838-2 · Cited by 17

Glucocorticoid receptor Thr524 phosphorylation by MINK1 induces interactions with 14-3-3 protein regulators

Munier, C. C., Maria, L. D., Edman, K., Gunnarsson, A., Longo, M., MacKintosh, C., Patel, S., Snijder, A., Wissler, L., Brunsveld, L., et al. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100551 · Cited by 16

Integrative Chemical Biology Approaches for Identification and Characterization of “Erasers” for Fatty‐Acid‐Acylated Lysine Residues within Proteins

Liu, Z., Yang, T., Li, X., Peng, T., Hang, H. C., & Li, X. (2014) · Angewandte Chemie · doi:10.1002/ange.201408763 · Cited by 12

Peptide array–based interactomics

Pérez-Hernández, D., & Dittmar, G. (2021) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-021-03367-8 · Cited by 9

Engineering an acetyllysine reader with a photocrosslinking amino acid for interactome profiling

Roy, A., Barman, S., Padhan, J., & Sudhamalla, B. (2021) · Chemical Communications · doi:10.1039/d1cc04611j · Cited by 8

An Integrated Approach for Combinatorial Readout of Dual Histone Modifications by Epigenetic Tandem Domains

Chen, P., Zhuo, Y., Tian, S., Zhang, T., Zhai, G., Fan, E., Ma, Z., Zhang, Y., & Zhang, K. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.9b05394 · Cited by 4

Protein posttranslational modifications in health and diseases: Functions, regulatory mechanisms, and therapeutic implications

Zhong, Q., Xiao, X., Qiu, Y., Xu, Z., Chen, C., Chong, B., Zhao, X., Hai, S., Li, S., An, Z., et al. (2023) · MedComm · doi:10.1002/mco2.261 · Cited by 442

Post-translational modifications in drug resistance

Miao, C., Huang, Y., Zhang, C., Wang, X., Wang, B., Zhou, X., Song, Y., Wu, P., Chen, Z., & Feng, Y. (2024) · Drug Resistance Updates · doi:10.1016/j.drup.2024.101173 · Cited by 75

Post-Translational Modifications of cGAS-STING: A Critical Switch for Immune Regulation

Yu, Y., Liu, J., Liu, C., Liu, R., Liu, L., Yu, Z., Zhuang, J., & Sun, C. (2022) · Cells · doi:10.3390/cells11193043 · Cited by 59

Glycolysis, a driving force of rheumatoid arthritis

Gan, P., Wu, H., Zhu, Y., Shu, Y., & Wei, Y. (2024) · International Immunopharmacology · doi:10.1016/j.intimp.2024.111913 · Cited by 57

Aberrant methylmalonylation underlies methylmalonic acidemia and is attenuated by an engineered sirtuin

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