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 1,719 · see citing works

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 1,609 · see citing works

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 910 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 735 · see citing works

Expanding and reprogramming the genetic code

Chin, J. W. (2017) · Nature · doi:10.1038/nature24031 · Cited by 730 · see citing works

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 662 · see citing works

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 653 · see citing works

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 · see citing works

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 · see citing works

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 586 · see citing works

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 · see citing works

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

Perkins, J. R., Diboun, I., Dessailly, B. H., Lees, J. G., & Orengo, C. A. (2010) · Structure · doi:10.1016/j.str.2010.08.007 · Cited by 522 · see citing works

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 475 · see citing works

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 435 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Playing with the Molecules of Life

Young, D. D., & Schultz, P. G. (2018) · ACS Chemical Biology · doi:10.1021/acschembio.7b00974 · Cited by 348 · see citing works

Readout of Epigenetic Modifications

Patel, D. J., & Wang, Z. (2013) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-072711-165700 · Cited by 315 · see citing works

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 · see citing works

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 · see citing works

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 265 · see citing works

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 247 · see citing works

Chemoenzymatic Semisynthesis of Proteins

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

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 233 · see citing works

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 192 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 164 · see citing works

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 158 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 85 · see citing works

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 82 · see citing works

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 79 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 64 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 57 · see citing works

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 · see citing works

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 · see citing works

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 54 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 45 · see citing works

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 · see citing works

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 · see citing works

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 42 · see citing works

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 · see citing works

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 29 · see citing works

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 · see citing works

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 · see citing works

Crosstalk of phosphorylation and arginine methylation in disordered SRGG repeats of S. cerevisiae fibrillarin and its association with nucleolar localisation.

Smith, D.-L., Erce, M. A., Lai, Y.-W., Tomasetig, F., Hart-Smith, G., Hamey, J. J., & Wilkins, M. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.11.006 · Cited by 24 · see citing works

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 22 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Peptide array–based interactomics

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

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 · see citing works

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 · see citing works

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 · see citing works

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 72 · see citing works

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 58 · see citing works

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 · see citing works

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

Head, P. E., Myung, S., Chen, Y., Schneller, J. L., Wang, C., Duncan, N., Hoffman, P., Chang, D., Gebremariam, A., Gucek, M., et al. (2022) · Science Translational Medicine · doi:10.1126/scitranslmed.abn4772 · Cited by 52 · see citing works

PTMint database of experimentally verified PTM regulation on protein–protein interaction

Hong, X., Li, N., Lv, J., Zhang, Y., Li, J., Zhang, J., & Chen, H. (2022) · Bioinformatics · doi:10.1093/bioinformatics/btac823 · Cited by 33 · see citing works

Genetically encoded crosslinkers to address protein–protein interactions

Aydin, Y., & Coin, I. (2023) · Protein Science · doi:10.1002/pro.4637 · Cited by 32 · see citing works

Post‐translational modifications of proteins in cardiovascular diseases examined by proteomic approaches

Stastna, M. (2024) · The FEBS Journal · doi:10.1111/febs.17108 · Cited by 28 · see citing works

MG53 alleviates hypoxia/reoxygenation-induced cardiomyocyte injury by succinylation and ubiquitination modification

Wang, Y., Zhou, H., Wu, J., & Ye, S. (2023) · Clinical and Experimental Hypertension · doi:10.1080/10641963.2023.2271196 · Cited by 27 · see citing works

Ubiquitination and deubiquitination: Implications for the pathogenesis and treatment of osteoarthritis

Su, S.-B., Tian, R.-J., Jiao, Y., Zheng, S., Liang, S., Liu, T., Tian, Z., Cao, X., Xing, Y., Ma, C., et al. (2024) · Journal of Orthopaedic Translation · doi:10.1016/j.jot.2024.09.011 · Cited by 29 · see citing works

Strategies to Expand the Genetic Code of Mammalian Cells

Osgood, A. O., Huang, Z., Szalay, K. H., & Chatterjee, A. (2025) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00730 · Cited by 25 · see citing works

SENP3-mediated deSUMOylation of c-Jun facilitates microglia-induced neuroinflammation after cerebral ischemia and reperfusion injury

Xia, Q., Mao, M., Zhan, G., Luo, Z., Zhao, Y., & Li, X. (2023) · iScience · doi:10.1016/j.isci.2023.106953 · Cited by 22 · see citing works

Lysine N-methyltransferase SETD7 promotes bladder cancer progression and immune escape via STAT3/PD-L1 cascade

Lv, J., Wu, Q., Li, K., Bai, K., Yu, H., Zhuang, J., Sun, H., Yang, H., Yang, X. F., & Lü, Q. (2023) · International Journal of Biological Sciences · doi:10.7150/ijbs.87182 · Cited by 22 · see citing works

PTMs of PD-1/PD-L1 and PROTACs application for improving cancer immunotherapy

Ren, X., Wang, L., Liu, L., & Liu, J. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1392546 · Cited by 21 · see citing works

PRMT5 Facilitates Infectious Bursal Disease Virus Replication through Arginine Methylation of VP1

Hu, X., Chen, Z., Wu, X., Fu, Q., Chen, Z., Huang, Y., & Wu, H. (2023) · Journal of Virology · doi:10.1128/jvi.01637-22 · Cited by 21 · see citing works

Acetylation: a new target for protein degradation in cancer

Crawford, C. E. W., & Burslem, G. M. (2025) · Trends in Cancer · doi:10.1016/j.trecan.2025.01.013 · Cited by 20 · see citing works

‘Intelligent’ proteins

Tripathi, T., Uversky, V. N., & Giuliani, A. (2025) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-025-05770-1 · Cited by 20 · see citing works

Cross-talk between BCKDK-mediated phosphorylation and STUB1-dependent ubiquitination degradation of BCAT1 promotes GBM progression

Wang, W., Li, Y., Tang, L., Shi, Y., Li, W., Zou, L., Zhang, L., Cheng, Y., Zheng, Y., Zhu, F., et al. (2024) · Cancer Letters · doi:10.1016/j.canlet.2024.216849 · Cited by 18 · see citing works

Decoding the functional impact of the cancer genome through protein–protein interactions

Fu, H., Mo, X., & Ivanov, A. A. (2025) · Nature reviews. Cancer · doi:10.1038/s41568-024-00784-6 · Cited by 21 · see citing works

Posttranslational Modification in Bone Homeostasis and Osteoporosis

Lin, Y., Jiang, S., Yao, Y., Li, H., Jin, H., Yang, G., Ji, B., & Li, Y. (2025) · MedComm · doi:10.1002/mco2.70159 · Cited by 18 · see citing works

Deciphering the functional landscape of phosphosites with deep neural network

Liang, Z. T., Liu, T., Li, Q., Zhang, G., Zhang, B., Du, X.-K., Liu, J., Chen, Z., Ding, H., Hu, G., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.113048 · Cited by 19 · see citing works

Role of lysine lactylation in neoplastic and inflammatory pulmonary diseases (Review)

Wang, S.-S., Zheng, H., Zhao, J.-P., & Xie, J.-G. (2025) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2025.5512 · Cited by 15 · see citing works

Mild therapeutic hypothermia upregulates the O-GlcNAcylation level of COX10 to alleviate mitochondrial damage induced by myocardial ischemia–reperfusion injury

Deng, W., Chen, Y., Zhang, J., Ling, J., Xu, Z., Zhu, Z., Tang, X., Liu, X., Zhang, D., Zhu, H., et al. (2024) · Journal of Translational Medicine · doi:10.1186/s12967-024-05264-x · Cited by 15 · see citing works

Integrated mass spectrometry strategy for functional protein complex discovery and structural characterization

Liu, Z., Chen, X., Yang, S., Tian, R., & Wang, F. (2023) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2023.102305 · Cited by 15 · see citing works

Nuclear factor-Y transcription factors in crops: Biological roles, regulation, and breeding applications

Wu, H., Hou, X., & Zhang, C. (2025) · Plant Communications · doi:10.1016/j.xplc.2025.101530 · Cited by 14 · see citing works

USP5-Mediated PD-L1 deubiquitination regulates immunotherapy efficacy in melanoma

Xie, J., Zhang, P., Liu, Y., Wu, D., Ou, X., Wang, M., Yan, W., Liu, J.-L., Tang, J., Ni, T., et al. (2025) · Journal of Translational Medicine · doi:10.1186/s12967-025-06812-9 · Cited by 13 · see citing works

New Strategies for Probing the Biological Functions of Protein Post-translational Modifications in Mammalian Cells with Genetic Code Expansion

Ding, W., Zhao, H., Chen, Y., & Lin, S. (2023) · Accounts of Chemical Research · doi:10.1021/acs.accounts.3c00460 · Cited by 13 · see citing works

The Role and Mechanism of Protein Post‑Translational Modification in Rheumatoid Arthritis

Wen, J., Liu, J., Wan, L., & Wang, F. (2025) · Journal of Inflammation Research · doi:10.2147/jir.s528487 · Cited by 13 · see citing works

Dapagliflozin suppressed gastric cancer growth via regulating OTUD5 mediated YAP1 deubiquitination

Ren, K., Wang, X., Ma, R., Chen, H., Min, T., Ma, Y., Xie, X., Wang, W., Deng, X., Zhou, Z., et al. (2024) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2024.177002 · Cited by 12 · see citing works

Pupylation-Based Proximity-Tagging of FERONIA-Interacting Proteins in Arabidopsis

Lin, Z., Liu, D., Xu, Y., Wang, M., Yu, Y., Diener, A. C., & Liu, K.-H. (2024) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2024.100828 · Cited by 11 · see citing works

Oxyberberine Inhibits Hepatic Gluconeogenesis via AMPK ‐Mediated Suppression of FoxO1 and CRTC2 Signaling Axes

Wu, F., Lu, F., Dong, H., Hu, M., Xu, L., & Wang, D. (2024) · Phytotherapy Research · doi:10.1002/ptr.8381 · Cited by 10 · see citing works

Emerging approaches to investigating functional protein dynamics in modular redox enzymes: Nitric oxide synthase as a model system

Jiang, T., Thielges, M. C., & Feng, C. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.108282 · Cited by 11 · see citing works

Coumarins at the Crossroads of Drug Development: Enzyme Modulation for Clinical Advances

Mustafa, Y. F. (2025) · Indian Journal of Clinical Biochemistry · doi:10.1007/s12291-025-01331-2 · Cited by 10 · see citing works

Lactylation: the regulatory code of cellular life activity and a barometer of diseases

Xu, X., Wu, X., Jin, D., Ji, J., Wu, T., Huang, M., Zhao, J., Shi, Z., Zhou, L., He, X., et al. (2025) · Cellular Oncology · doi:10.1007/s13402-025-01083-4 · Cited by 9 · see citing works

Large-Scale Identification of Lysine Crotonylation Reveals Its Potential Role in Oral Squamous Cell Carcinoma

Yin, X., Hongbo, Z., Wei, Z., Wang, Y., Han, S., Zhou, M., Xu, W., & Han, W. (2023) · Cancer Management and Research · doi:10.2147/cmar.s424422 · Cited by 9 · see citing works

An Overview of the Deubiquitinase USP53: A Promising Diagnostic Marker and Therapeutic Target

Xia, G., Guo, Y., Zhang, J., Han, M., Meng, X., & Lv, J. (2024) · Current Protein and Peptide Science · doi:10.2174/0113892037292440240518194922 · Cited by 8 · see citing works

Epigenetic modifications involving ncRNAs in digestive system cancers: focus on histone modification

Yin, X., Li, J., Zhao, J., Zheng, W., Zhang, A., & Ma, J. (2024) · Clinical Epigenetics · doi:10.1186/s13148-024-01773-0 · Cited by 8 · see citing works

Mass Spectrometry‐Based Proteomics Technologies to Define Endogenous Protein‐Protein Interactions and Their Applications to Cancer and Viral Infectious Diseases

Yu, C., Adavikolanu, R., Kaake, R. M., & Huang, L. (2025) · Mass Spectrometry Reviews · doi:10.1002/mas.21926 · Cited by 8 · see citing works

Neutrophil-derived heparin-binding protein increases endothelial permeability in acute lung injury by promoting TRIM21 and the ubiquitination of P65

Zhang, J., Cao, Y., Shu, W., Dong, S., Sun, Y., & Ma, X. (2025) · Cell Biology and Toxicology · doi:10.1007/s10565-025-10005-x · Cited by 8 · see citing works

Protein Post‐Translational Modification‐Mediated Control of Type I Interferon Cascade Signaling

Chen, X., Cheng, Q., Gong, F., & Zheng, H. (2025) · Medicine Bulletin · doi:10.1002/mdb2.70000 · Cited by 9 · see citing works

Biocompatible ligand balancing in transition metal coordination enables benign in-cell protein arylation

Fu, X., Liu, W., Demyanenko, Y., Kamel, W., Ravi, R. T., Ruscica, V., Noerenberg, M., Yin, X., Jiang, Y., Fan, C.-H., et al. (2026) · Nature Chemistry · doi:10.1038/s41557-025-02017-1 · Cited by 8 · see citing works

The acetylation of pknH is linked to the ethambutol resistance of Mycobacterium tuberculosis

Sun, Q., Zou, Y., Feng, Q., Gong, Z., Song, M., Li, M., & Chen, Z. (2023) · Archives of Microbiology · doi:10.1007/s00203-023-03676-9 · Cited by 8 · see citing works

Engineering unnatural cells with a 21st amino acid as a living epigenetic sensor

Hu, Y., Wang, Y., Cheng, L., Wang, C., Liu, Y., Wang, Y., Chen, Y., Yang, S., Guo, Y., Jiang, S. J., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-64448-1 · Cited by 8 · see citing works

Post‐translational Modifications in Proteins: Prediction Methods, Biological Functions, and Diseases

Zhang, S., li, J., Chen, M., & Huang, H. (2026) · MedComm · doi:10.1002/mco2.70729 · Cited by 7 · see citing works

Proteomic Comparison of Acute Myeloid Leukemia Cells and Normal CD34+ Bone Marrow Cells: Studies of Leukemia Cell Differentiation and Regulation of Iron Metabolism/Ferroptosis

Selheim, F., Aasebø, E., Reikvam, H., Bruserud, Ø., & Hernandez-Valladares, M. (2025) · Proteomes · doi:10.3390/proteomes13010011 · Cited by 7 · see citing works

Allostery in Biomolecular Condensates

Nussinov, R., Regev, C., & Jang, H. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169446 · Cited by 6 · see citing works

Post-translational modifications regulating microglial inflammation in central nervous system disorders: a review

Wang, X., Yang, M., Wang, Y., & Zhu, F. (2025) · Inflammation Research · doi:10.1007/s00011-025-02123-3 · Cited by 6 · see citing works

Exploring and expanding the chemical multiverse of peptides

López‐López, E., Sánchez-Castañeda, J. P., Martínez-Cortés, M. S., de la Fuente‐Núñez, C., & Medina‐Franco, J. L. (2025) · Chemical Science · doi:10.1039/d5sc04465k · Cited by 6 · see citing works

IQGAP1 Is a Phosphotyrosine-Regulated Scaffold for SH2-Containing Proteins

Thines, L., Li, Z., & Sacks, D. B. (2023) · Cells · doi:10.3390/cells12030483 · Cited by 6 · see citing works

Monitoring Functional Posttranslational Modifications Using a Data‐Driven Proteome Informatic Pipeline

Nickchi, P., Vadadokhau, U., Mirzaie, M., Baumann, M., Saei, A. A., & Jafari, M. (2025) · PROTEOMICS · doi:10.1002/pmic.202400238 · Cited by 6 · see citing works

FAM50A drives breast cancer brain metastasis through interaction with C9ORF78 to enhance ʟ-asparagine production

Chen, W., Qin, Y., Qiao, L., Liu, X., Gao, C., Li, T., Luo, Y., Li, D., Yan, H., Han, L., et al. (2025) · Science Advances · doi:10.1126/sciadv.adt3075 · Cited by 5 · see citing works

ALDH2 in autophagy and cell death: molecular mechanisms and implications for diseases

Duan, Y., Shan, Z.-C., Pang, J., & Chen, Y. (2025) · Military Medical Research · doi:10.1186/s40779-025-00646-8 · Cited by 6 · see citing works

Interplay between NRF2 post-translational modifications and protein-protein interactions: Perspectives from emerging structural and functional evidence

Ozleyen, A., Kulabas, S. S., Novak, M. J., Cichoń, M., Heras, C. M. D. L., Honda, T., Doveston, R. G., Dinkova‐Kostova, A. T., Grochot‐Przeczek, A., & Tumer, T. B. (2026) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2026.110847 · Cited by 5 · see citing works

PPM1G Inhibits Epithelial–Mesenchymal Transition in Cholangiocarcinoma by Catalyzing TET1 Dephosphorylation for Destabilization to Impair Its Targeted Demethylation of the CLDN3 Promoter

Liu, W., Kuai, Y., Wang, D., Chen, J., Xiong, F., Wu, G., Wang, Q., Huang, W., Qi, Y., Wang, B., et al. (2024) · Advanced Science · doi:10.1002/advs.202407323 · Cited by 5 · see citing works

“Intrinsic disorder-protein modification-LLPS-tumor” regulatory axis: From regulatory mechanisms to precision medicine

Cheng, Z., Cheng, Z., Zhang, Y., & Zhang, S. (2024) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2024.189242 · Cited by 5 · see citing works

Ubiquitin-dependent proteasomal degradation of small hepatitis B virus surface antigen mediated by TRIM21 and antagonized by OTUD4

Wu, S., Chen, Z., Zhang, Z., Xu, J., Li, H., Lin, M.-X., Xie, W., Chen, Y., Lin, X., & Lin, X. (2025) · Journal of Virology · doi:10.1128/jvi.02309-24 · Cited by 5 · see citing works

Dynamic Proximity Tagging in Living Plant Cells with Pupylation-Based Interaction Tagging

Ye, R., Lin, Z., Liu, K.-H., Sheen, J., & Chen, S. (2023) · Methods in molecular biology · doi:10.1007/978-1-0716-3327-4_14 · Cited by 5 · see citing works

In silico Analysis of Human Endothelial Cell-specific Molecule 1 and Interleukin-6 Genetic Variants Involved in Coronary Artery Disease

Kulkarni, V., Shetty, S., Bhandary, R. R., & Mary, Y. (2024) · Biomedical and Biotechnology Research Journal (BBRJ) · doi:10.4103/bbrj.bbrj_258_24 · Cited by 5 · see citing works

Reading and Writing the Ubiquitin Code Using Genetic Code Expansion

Patel, R. S., Pannala, N. M., & Das, C. (2024) · ChemBioChem · doi:10.1002/cbic.202400190 · Cited by 5 · see citing works

Metabolic control of glycosylation forms for establishing glycan-dependent protein interaction networks

Liu, X., Yi, L., Lin, Z., Chen, S., Wang, S., Sheng, Y., Lebrilla, C. B., Garcia, B. A., & Xie, Y. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2422936122 · Cited by 4 · see citing works

2-Bromopalmitate inhibits malignant behaviors of HPSCC cells by hindering the membrane location of Ras protein

Wang, C., Cui, Z.-Y., Chang, H., Wu, C.-Z., Yu, Z., Wang, X., Liu, Y., Li, C., Du, X.-G., & Li, J. (2023) · Experimental Biology and Medicine · doi:10.1177/15353702231220671 · Cited by 4 · see citing works

Insight into the Interaction Mechanism of Pseudorabies Virus Infection

Chen, X., & Yu, Z. (2024) · Biology · doi:10.3390/biology13121013 · Cited by 4 · see citing works

Global Profiling of Lactylation Proteomics and Specific Lactylated Site Validation in Rheumatoid Arthritis Patients

Hu, J., Jin, Z., Gao, Y., Liu, Q., Yu, Y., Kong, R., Zhao, D., & Gao, J. (2025) · Journal of Proteome Research · doi:10.1021/acs.jproteome.4c00680 · Cited by 4 · see citing works

Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell

He, J., Lai, T., Zhou, Z., Yang, H., Zheng, L., Liu, Z., Li, N., He, Y., Zeng, S., Munai, E., et al. (2025) · Scientific Reports · doi:10.1038/s41598-025-09937-5 · Cited by 4 · see citing works

MILKSHAKE Western blot and Sundae ELISA: We all scream for better antibody validation

Mendez, Q. M., Driscoll, H. A., Mirando, G. R., Acca, F. E., Chapados, C. D., Jones, K. S., Weiner, M. P., Li, X., & Ferguson, M. R. (2023) · Journal of Immunological Methods · doi:10.1016/j.jim.2023.113540 · Cited by 4 · see citing works

Protein SUMOylation and Its Functional Role in Nuclear Receptor Control

Wild, N., Kaiser, C. S., Wunderlich, G., Liebau, E., & Wrenger, C. (2024) · Receptors · doi:10.3390/receptors3030020 · Cited by 4 · see citing works

Mapping and visualization of global research progress on deubiquitinases in ovarian cancer: a bibliometric analysis

Qiu, F., Li, Y., Zhou, L., Wu, Y., Wu, Y., Fan, Z., Wang, Y., Qin, D., & Li, C. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1445037 · Cited by 6 · see citing works

Targeting BRD4 in cancer therapy: From inhibitors and degraders to novel combination strategies and resistance mechanisms

Wang, X., Meng, R.-J., Cao, W.-J., Cheng, L., Zhang, J., & Chen, S. (2025) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2025.118473 · Cited by 3 · see citing works

Deacetylated PCBP1 licenses PARP1 activity for DNA damage repair

Shu, Y., Zhang, J., Zhou, L., Feng, T., Chen, F., Tang, H., Li, M., Qian, J., Qin, M., Wang, Z., et al. (2026) · Molecular Cell · doi:10.1016/j.molcel.2026.05.008 · Cited by 3 · see citing works

Ribosomal Translation and Display Selection of Cyclic Glycopeptides through Genetic Reprogramming

Johansen‐Leete, J., Zhong, Y., Cui, B., Sebold, B. C., Kambanis, L., Shepperson, C. E., Lehmann, C., Mak, K. H. T., Tang, A. H., Burchfield, J. G., et al. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.5c22682 · Cited by 3 · see citing works

Mechanisms and Research Methods of Protein Modification in Virus Entry

Xiao, Y., Gao, M., Mo, X., Lang, J., Wang, Z., Ma, Z., Meng, Y., Tang, B.-L., Liu, D., & He, H. (2025) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-025-05333-x · Cited by 3 · see citing works

An Automated Workflow to Address Proteome Complexity and the Large Search Space Problem in Proteomics and HLA-I Immunopeptidomics

Horokhovskyi, Y., Roetschke, H. P., Cormican, J. A., Pašen, M., Garazhian, S., Mishto, M., & Liepe, J. (2025) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2025.101039 · Cited by 3 · see citing works

Multiplex mapping of protein–protein interaction interfaces

He, J., Zou, L.-N., Pareek, V., & Benkovic, S. J. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2425774122 · Cited by 3 · see citing works

Molecular Interactions between a Flavonoid and Lysozyme: A Spectroscopic, Thermodynamic, and Computational Study

Mandal, J. (2023) · ChemistrySelect · doi:10.1002/slct.202301651 · Cited by 3 · see citing works

E3 ubiquitin-ligase RNF138 may regulate p53 protein expression to regulate the self-renewal and tumorigenicity of glioma stem cells

Chao, Q., Li, X., & Huang, Y. (2023) · Journal of Cancer Research and Therapeutics · doi:10.4103/jcrt.jcrt_733_23 · Cited by 3 · see citing works

Lipopolysaccharide Regulates the Macrophage RNA-Binding Proteome

Rathore, D., Marino, M. J., Issara-Amphorn, J., Yoon, S. H., Manes, N. P., & Nita‐Lazar, A. (2024) · Journal of Proteome Research · doi:10.1021/acs.jproteome.3c00838 · Cited by 3 · see citing works

Progress in enrichment methods for protein N-phosphorylation

JIANG, B., Bo, G. A. O., Wei, S.-X., Liang, Z., Zhang, L., & Zhang, Y. (2024) · Chinese Journal of Chromatography · doi:10.3724/sp.j.1123.2024.04029 · Cited by 3 · see citing works

HBFormer: a single-stream framework based on hybrid attention mechanism for identification of human-virus protein–protein interactions

Zhang, L., Wang, S., Wang, Y., & Zhao, T. (2024) · Bioinformatics · doi:10.1093/bioinformatics/btae724 · Cited by 3 · see citing works

Bacterial two-hybrid systems evolved: innovations for protein-protein interaction research

Richardson, R. M., & Pascal, S. M. (2025) · Journal of Bacteriology · doi:10.1128/jb.00129-25 · Cited by 3 · see citing works

Enzymatic post-translational modifications of proteins in chronic kidney disease: mechanisms, regulation, and clinical significance

Wei, M., Lin, J., Zeng, Y. A., Wang, X., Wen, J., Wang, J., Zou, W., Tu, K., Liu, M., & Li, J. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1678812 · Cited by 2 · see citing works

Mapping Context-Aware Phosphosite Regulation of Protein–Protein Interactions Using Deep Learning and Pan-Cancer Proteomics

Cai, M., Xiao, Y., Zheng, J., Shi, J., Wu, J., Kong, X., & Liang, Z. T. (2025) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.5c01504 · Cited by 2 · see citing works

Towards the targeted activation of silent biosynthetic gene clusters by chemical elicitors

Zhou, Z., Guan, Y.-T., Li, Z., Wu, X., Xin, J.-X., Wang, H., & Wei, B. (2026) · Biotechnology Advances · doi:10.1016/j.biotechadv.2026.108870 · Cited by 2 · see citing works

The Role of Protein Post-Translational Modifications in the Pathogenesis of Nephrolithiasis: Mechanistic Insights and Translational Potential

Wan, W., Wang, B., Yang, J., Xun, Y., & Yu, X. (2026) · Cells · doi:10.3390/cells15060554 · Cited by 2 · see citing works

Targeting the ODC1-YBX1 axis reverses gastric cancer chemoresistance via transcriptional control of SLC7A11-mediated ferroptosis

Li, R., Baral, S., Zhao, F., Zhang, C., Zhou, J., Li, B., Cheng, Y., Fang, D., Xu, Z., Fu, Y., et al. (2026) · Cell Death Discovery · doi:10.1038/s41420-026-03067-1 · Cited by 2 · see citing works

From mechanisms to therapies: exploiting epigenetic and post-translational modifications of mitochondrial quality control in diabetic kidney disease

Zhao, D.-M., Yan, Z., Yu, Y., Zhang, Y., & Luan, Z.-Q. (2026) · Frontiers in Endocrinology · doi:10.3389/fendo.2026.1821507 · Cited by 2 · see citing works

Proteomic analysis of global protein acetylation in response to WSSV infection in a crustacean Cherax quadricarinatus

Liu, L.-K., Yang, L.-L., Jiang, Q., Wu, W.-L., & Liu, H. (2024) · Aquaculture · doi:10.1016/j.aquaculture.2024.741754 · Cited by 2 · see citing works

Post-translational modifications of RGS protein family: Pivotal switches in cellular signaling transduction and diseases

Song, Y., An, Z., Wang, J., Xu, Q., Li, J., & Tang, C. (2025) · Pharmacological Research · doi:10.1016/j.phrs.2025.107801 · Cited by 2 · see citing works

Global Profiling of Protein β-hydroxybutyrylome in Porcine Liver

Fan, S., Guan, J., Tian, F., Ye, H., Wang, Q., Lv, L., Liu, Y., Zheng, X., Yin, Z., & Zhang, X. (2025) · Biology · doi:10.3390/biology14091183 · Cited by 2 · see citing works

In situ insertion of one or two types of hydroxy-rich noncanonical amino acids into one protein

Fan, X., Liu, Y., & Chen, Z. (2025) · Process Biochemistry · doi:10.1016/j.procbio.2025.04.022 · Cited by 1 · see citing works

New trends and hotspots in sepsis-related protein post-translational modification: a bibliometric and visual analysis

Song, L., Ma, J., Jiang, W., Liu, K., Wang, J., Lin, H., Yu, J., & Zheng, R. (2025) · Frontiers in Medicine · doi:10.3389/fmed.2025.1606786 · Cited by 1 · see citing works

Emerging Insights into Protein Post-Translational Modifications in Chlamydia-Host Interactions

Luo, X., Wang, X., Hu, C., Liu, Z., Lu, C., Chen, S., Bai, Q., Zeng, X., & Chen, L. (2025) · American Journal Of Pathology · doi:10.1016/j.ajpath.2025.06.011 · Cited by 1 · see citing works

Post-translational modification gene signatures implicate FBXW7 in immune and vascular dysregulation of Moyamoya disease

Yu, X., Wang, Z., Zhou, Z., Liu, Y., He, S., & Zhao, Y. (2025) · Frontiers in Genetics · doi:10.3389/fgene.2025.1723233 · Cited by 1 · see citing works

Post-translational modifications of proteins: dynamic regulatory network and therapeutic targets of tumor immune escape in pan-cancer

Yan, Q., Zhai, Q., Yu, S., & Zhang, W. (2025) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/10408363.2025.2598380 · Cited by 1 · see citing works

Pancancer Analyses of KISS1 as a Potential Biomarker for Tumor Metastasis and Immunotherapy and Therapeutic Target for Breast Cancer

Wu, C., Jiang, H., Xu, W., Li, B., Zhang, H., Zhang, L., Li, Z., & Xiao, J. (2026) · International Journal of Genomics · doi:10.1155/ijog/5902518 · Cited by 1 · see citing works

Regulation of Keratin Chemical Modifications: Potential Molecular Mechanisms in Proliferative Diseases

Ma, X., Jiang, X., Song, M., Bai, B., Hou, X., & Wu, Q. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27020972 · Cited by 1 · see citing works

Decoding lactylation heterogeneity in glioblastoma: machine learning identifies G6PC3 as a prognostic target

Liu, Y., Deng, H., Song, P., Qiu, Q., Bu, J., & Zhang, M. (2026) · BMC Cancer · doi:10.1186/s12885-026-16225-6 · Cited by 1 · see citing works

Pharmacological ZO-1 agonist treatment attenuates ammonia nitrogen stress-induced mucosal inflammation and intestinal barrier failure in Leiocassis longirostris

Liu, S., Feng, Y., Mou, C., Zhang, L., Duan, Y., Huang, Z., Zhao, H., Zhou, J. T., Du, J., Li, Q., et al. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1842403 · Cited by 1 · see citing works

Metabolic Fuel, Molecular Code: How Cancer Rewires Metabolite-Driven Post-Translational Modifications to Shape Tumor Fate

Wang, Y., Li, C., Liu, B., & Chen, X. (2026) · Cancer Bioscience · doi:10.1016/j.cbs.2026.100005 · Cited by 1 · see citing works

Electrochemical Biosensing Strategies for Oral Health: From Engineered Interfaces to Advanced Transistor Architectures

Jiang, X., Zheng, J., Ma, H., Yu, J., Zhou, R., Fu, W., Yan, H., Liang, Z., Wu, G., Wang, X., et al. (2026) · Advanced Healthcare Materials · doi:10.1002/adhm.71448 · Cited by 1 · see citing works

Tight junction protein LSR is a host defense factor against SARS-CoV-2 infection in the small intestine

An, Y., Wang, C., Wang, Z., Kong, F., Liu, H., Jiang, M., Liu, T., Zhang, S., Du, K., Yin, L., et al. (2024) · The EMBO Journal · doi:10.1038/s44318-024-00281-4 · Cited by 1 · see citing works

Studying post-translational modifications with protein interaction networks

Woodsmith, J., & Stelzl, U. (2013) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2013.11.009 · Cited by 54 · see citing works

Mining impact of protein modifications on protein-protein interactions from literature

Siu, A. Y., Arighi, C. N., Nchoutmboube, J., Tudor, C. O., Vijay‐Shanker, K., & Wu, C. H. (2009) · IEEE International Conference on Bioinformatics and Biomedicine Workshops (BIBMW) · doi:10.1109/bibmw.2009.5332069

Importance of protein post-translational modifications in finding partners

Zhu, W., Hou, T., & XiaoPeng, L. U. (2017) · Chinese Science Bulletin (Chinese Version) · doi:10.1360/n972016-00833

PTM-Psi: A Python package to facilitate the computational investigation of post-translational modification on protein structures and their impacts on dynamics and functions

Cheung, M. S., Mejı́a-Rodrı́guez, D., Kim, H. S., Sadler, N., Li, X., Bohutskyi, P., Valiev, M., & Qian, W. (2024) · Biophysical Journal · doi:10.1016/j.bpj.2023.11.2147 · Cited by 2 · see citing works

The role of post-translational modifications in the context of protein interaction networks

Duan, G., & Walther, D. (2013) · doi:10.13140/2.1.4832.0965