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

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

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

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

Genetically encoded crosslinkers to address protein–protein interactions

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

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

Št́astná, M. (2024) · FEBS Journal · doi:10.1111/febs.17108 · Cited by 32

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

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

Su, S., Tian, R., 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 27

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 26

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

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

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 23

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

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

‘Intelligent’ proteins

Tripathi, T., Uversky, V. N., & Giuliani, A. (2025) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-025-05770-1 · Cited by 21

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

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 22

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

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

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

Wang, S., Zheng, H., Zhao, J., & Xie, J. (2025) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2025.5512 · Cited by 18

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

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

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

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 15

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

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

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 13

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

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 11

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

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

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

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

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

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 9

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 10

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

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

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

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

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

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 9

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

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

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

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 11

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

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

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 6

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

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

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

“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

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

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

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

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

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

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

Insight into the Interaction Mechanism of Pseudorabies Virus Infection

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

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

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

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

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

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

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 4

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 4

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

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 5

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 2

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

Yan, Q., Qingqing, Z., Yu, S., & Zhang, W. (2025) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/10408363.2025.2598380 · Cited by 2

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

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

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

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

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

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

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

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 55

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

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