Critical roles of non-histone protein lysine methylation in human tumorigenesis

Epigenetic Regulations of GABAergic Neurotransmission: Relevance for Neurological Disorders and Epigenetic Therapy

Shrestha, S., & Offer, S. M. (2016) · Medical Epigenetics · doi:10.1159/000444713 · Cited by 8,951

Mutational landscape and significance across 12 major cancer types

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Histone demethylation mediated by the nuclear amine oxidase homolog LSD1

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VEGF receptor signalling ? in control of vascular function

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Regulation of chromatin structure by site-specific histone H3 methyltransferases

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The mutational landscape of lethal castration-resistant prostate cancer

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HSP90 and the chaperoning of cancer

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Histone demethylation by a family of JmjC domain-containing proteins

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EZH2 inhibition as a therapeutic strategy for lymphoma with EZH2-activating mutations

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The HSP70 chaperone machinery: J proteins as drivers of functional specificity

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Roles of Lysine Methylation in Glucose and Lipid Metabolism: Functions, Regulatory Mechanisms, and Therapeutic Implications

Wang, Z., & Liu, H. (2024) · Biomolecules · doi:10.3390/biom14070862 · Cited by 14

Tailoring a novel colorectal cancer stem cell-targeted therapy by inhibiting the SMYD3/c-MYC axis

Signorile, M. L., Nicola, E. D., Forte, G., Sanese, P., Fasano, C., Disciglio, V., Marco, K. D., Latrofa, M., Cecco, L. D., Ficorilli, M., et al. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02290-z · Cited by 15

An Information Entropy-Based Approach for Computationally Identifying Histone Lysine Butyrylation

Huang, G., Zheng, Y., Wu, Y., Han, G., & Yu, Z. (2020) · Frontiers in Genetics · doi:10.3389/fgene.2019.01325 · Cited by 14

Design Two Novel Tetrahydroquinoline Derivatives against Anticancer Target LSD1 with 3D-QSAR Model and Molecular Simulation

Xu, Y., Fan, B., Gao, Y., Chen, Y., Han, D., Lu, J., Liu, T., Gao, Q., Zhang, J. Z. H., & Wang, M. (2022) · Molecules · doi:10.3390/molecules27238358 · Cited by 14

Critical roles of protein methyltransferases and demethylases in the regulation of embryonic stem cell fate

Vougiouklakis, T., Nakamura, Y., & Saloura, V. (2017) · Epigenetics · doi:10.1080/15592294.2017.1391430 · Cited by 14

Prevalence of Enhancer of Zeste Homolog 2 in Patients with Resected Small Cell Lung Cancer

Toyokawa, G., Takada, K., Tagawa, T., Kinoshita, F., Kozuma, Y., Matsubara, T., Haratake, N., Takamori, S., Akamine, T., Hirai, F., et al. (2018) · Anticancer Research · doi:10.21873/anticanres.12649 · Cited by 14

Epigenetic Mechanisms Underlying COVID-19 Pathogenesis

Kaneko, S., Takasawa, K., Asada, K., Shinkai, N., Bolatkan, A., Yamada, M., Takahashi, S., Machino, H., Kobayashi, K., Komatsu, M., et al. (2021) · Biomedicines · doi:10.3390/biomedicines9091142 · Cited by 13

Discovery of tetrahydrofuranyl spirooxindole-based SMYD3 inhibitors against gastric cancer via inducing lethal autophagy

Zhu, H.-P., Chai, J., Qin, R., Leng, H., Wen, X., Peng, C. M., He, G., & Han, B. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.115009 · Cited by 13

Conformational Dynamics of Lysine Methyltransferase Smyd2. Insights into the Different Substrate Crevice Characteristics of Smyd2 and Smyd3

Chandramouli, B., & Chillemi, G. (2016) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.6b00652 · Cited by 13

RNA-seq based transcriptome analysis of EHMT2 functions in breast cancer

Kim, K., Ryu, T. Y., Ryu, J., Han, T.-S., Jung, C., Son, M., Kim, D., & Cho, H. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.01.128 · Cited by 13

Polycomb Paralog Chromodomain Inhibitors Active against Both CBX6 and CBX8**

Milosevich, N., Wilson, C. R., Brown, T. M., Alpsoy, A., Wang, S., Connelly, K. E., Sinclair, K. A. D., Ponio, F., Hof, R., Dykhuizen, E. C., et al. (2021) · ChemMedChem · doi:10.1002/cmdc.202100262 · Cited by 13

Histone demethylase LSD1 deficiency and biological sex: impact on blood pressure and aldosterone production

Huang, Y., Ting, P. Y., Yao, T. M., Homma, T., Brooks, D. L. P., Rangel, I. K., Adler, G. K., Romero, J. R., Williams, J. S., Pojoga, L. H., et al. (2018) · Journal of Endocrinology · doi:10.1530/joe-18-0247 · Cited by 13

NSD2 methylates AROS to promote SIRT1 activation and regulates fatty acid metabolism-mediated cancer radiotherapy

Li, X., Song, D., Chen, Y., Huang, C., Liu, A., Wu, Q., She, X., Li, K., Wan, K., Yu, C., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.113126 · Cited by 12

A Chemoselective Enrichment Strategy for In‐Depth Coverage of the Methyllysine Proteome

Yan, L., Zheng, M., Fan, M., Yao, R., Zou, K., Feng, S., & Wu, M. (2024) · Angewandte Chemie International Edition · doi:10.1002/anie.202408564 · Cited by 13

U/G SNP rs111904020 in 3′UTR of STAT3 regulated by miR-214 promotes hepatocellular carcinoma development in Chinese population

Fan, Y., Qian, X., & Zhang, C. (2016) · Tumor Biology · doi:10.1007/s13277-016-5352-z · Cited by 12

Genomics and advances towards precision medicine for head and neck squamous cell carcinoma

Waes, C. V., & Musbahi, O. (2017) · Laryngoscope Investigative Otolaryngology · doi:10.1002/lio2.86 · Cited by 12

Structural basis for antigen recognition by methylated lysine–specific antibodies

Ishii, M., Nakakido, M., Caaveiro, J. M. M., Kuroda, D., Okumura, C. J., Maruyama, T., Entzminger, K. C., & Tsumoto, K. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.015996 · Cited by 12

Novel inhibitors design through structural investigations and simulation studies for human PKMTs (SMYD2) involved in cancer

Yadav, A. K., & Singh, T. R. (2021) · Molecular Simulation · doi:10.1080/08927022.2021.1957882 · Cited by 12

The Organelle-Specific Regulations and Epigenetic Regulators in Ferroptosis

Zhang, Y., Li, M., Guo, Y., Liu, S., & Tao, Y. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.905501 · Cited by 12

The Prognostic Impact of Jumonji Domain-containing 2B in Patients with Resected Lung Adenocarcinoma

Toyokawa, G., Taguchi, K., Edagawa, M., Shimamatsu, S., Toyozawa, R., Nosaki, K., Hirai, F., Yamaguchi, M., Shimokawa, M., Seto, T., et al. (2016) · Anticancer Research · doi:10.21873/anticanres.11046 · Cited by 12

Outer Membrane Protein OmpB Methylation May Mediate Bacterial Virulence

Yang, D. C. H., Abeykoon, A. H., Choi, B.-E., Ching, W., & Chock, P. B. (2017) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2017.09.005 · Cited by 12

MLysPRED: graph-based multi-view clustering and multi-dimensional normal distribution resampling techniques to predict multiple lysine sites

Zuo, Y., Hong, Y., Zeng, X., Zhang, Q., & Liu, X. (2022) · Briefings in Bioinformatics · doi:10.1093/bib/bbac277 · Cited by 11

Lysine Methylation-Dependent Proteolysis by the Malignant Brain Tumor (MBT) Domain Proteins

Sun, H., & Zhang, H. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25042248 · Cited by 11

Methylation of ESCRT-III components regulates the timing of cytokinetic abscission

Richard, A., Berthelet, J., Judith, D., Advedissian, T., Espadas, J., Jannot, G., Amo, A., Loew, D., Lombard, B., Casanova, A. G., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-47717-3 · Cited by 11

Lysine methylation modifications in tumor immunomodulation and immunotherapy: regulatory mechanisms and perspectives

Luo, Y., Lu, J., Lei, Z., Zhu, H., Rao, D., Wang, T., Fu, C., Zhang, Z., Xia, L., & Huang, W. (2024) · Biomarker Research · doi:10.1186/s40364-024-00621-w · Cited by 12

SMYD3 drives cell cycle and epithelial-mesenchymal transition pathways through dual gene transcriptional repression and activation in HPV-negative head and neck cancer

Murali, M., Saeed, A., Kim, S., Burkitt, K., Cheng, H., Moshiri, A., Akhtar, J., Tsai, D., Luff, M. K., Karim, B. O., et al. (2025) · Scientific Reports · doi:10.1038/s41598-024-83396-2 · Cited by 11

Elevated Metabolic Activity on 18F-FDG PET/CT Is Associated with the Expression of EZH2 in Non-small Cell Lung Cancer

Toyokawa, G., Takada, K., Okamoto, T., Kozuma, Y., Matsubara, T., Haratake, N., Akamine, T., Takamori, S., Katsura, M., Shoji, F., et al. (2017) · Anticancer Research · doi:10.21873/anticanres.11461 · Cited by 11

Unveiling epidithiodiketopiperazine as a non-histone arginine methyltransferase inhibitor by chemical protein methylome analyses

Sohtome, Y., Shimazu, T., Barjau, J., Fujishiro, S., Akakabe, M., Terayama, N., Dodo, K., Ito, A., Yoshida, M., Shinkai, Y., et al. (2018) · Chemical Communications · doi:10.1039/c8cc03907k · Cited by 11

Insights into novel emerging epigenetic drugs in myeloid malignancies

Chandhok, N. S., & Prébet, T. (2019) · Therapeutic Advances in Hematology · doi:10.1177/2040620719866081 · Cited by 11

Loss of histone H4 lysine 20 trimethylation in osteosarcoma is associated with aberrant expression ofhistone methyltransferase SUV420H2

Piao, L., Yuan, X., Wang, L., Xu, X., Zhuang, M., Li, J., Kong, R., & Liu, Z. (2020) · Oncology Letters · doi:10.3892/ol.2020.11887 · Cited by 11

A transcriptome-wide association study of uterine fibroids to identify potential genetic markers and toxic chemicals

Kim, G., Jang, G., Song, J., Kim, D., Lee, S., Joo, J. W. J., & Jang, W. (2022) · PLoS ONE · doi:10.1371/journal.pone.0274879 · Cited by 11

Probing the interaction of the p53 C-terminal domain to the histone demethylase LSD1

Speranzini, V., Ciossani, G., Marabelli, C., & Mattevi, A. (2017) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2017.07.021 · Cited by 11

Development of Chaetocin and S ‐Adenosylmethionine Analogues as Tools for Studying Protein Methylation

Sohtome, Y., & Sodeoka, M. (2018) · The Chemical Record · doi:10.1002/tcr.201800118 · Cited by 11

The Updating of Biological Functions of Methyltransferase SETDB1 and Its Relevance in Lung Cancer and Mesothelioma

Li, Y., Sun, B., Xu, L., Chen, L., & Ou, W. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22147416 · Cited by 11

A Genetically Encoded Allysine for the Synthesis of Proteins with Site‐Specific Lysine Dimethylation

Wang, Z. A., Zeng, Y., Kurra, Y., Wang, X., Tharp, J. M., Vatansever, E. C., Hsu, W. W., Dai, S. Y., Fang, X., & Liu, W. R. (2016) · Angewandte Chemie · doi:10.1002/ange.201609452 · Cited by 11

Histone methyltransferase SUV39H2 serves oncogenic roles in osteosarcoma

Piao, L., Yuan, X., Zhuang, M., Qiu, X., Xu, X., Kong, R., & Liu, Z. (2018) · Oncology Reports · doi:10.3892/or.2018.6843 · Cited by 11

Fine-tuning AKT kinase activity through direct lysine methylation

Guo, J., & Wei, W. (2019) · Cell Cycle · doi:10.1080/15384101.2019.1609832 · Cited by 12

SETD6 mediates selective interaction and genomic occupancy of BRD4 and MITF in melanoma cells

Biton, T. E., Feldman, M., Davidy, T., Moskovitz, N. T., Levin, L., Sevilla-Sánchez, D., Goding, C. R., Bernstein, E., & Levy, D. (2025) · NAR Cancer · doi:10.1093/narcan/zcaf023 · Cited by 10

Metabolic labeling based methylome profiling enables functional dissection of histidine methylation in C3H1 zinc fingers

Wang, K., Zhang, L., Zhang, S., Liu, Y., Mao, J., Liu, Z., Xu, L., Li, K., Wang, J., Ma, Y., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-51979-2 · Cited by 10

Identification of potential target genes associated with the reversion of androgen-dependent skeletal muscle atrophy

Coelho, P. D. O., Guarnier, F. A., Figueiredo, L. B., Zaramela, L. S., Pacini, E. S. A., Godinho, R. O., & Gomes, M. D. (2019) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2019.01.009 · Cited by 10

Aberrant JmjC domain-containing protein 8 (JMJD8) expression promotes activation of AKT and tumor epithelial–mesenchymal transition

Yao, S., Wang, X., Guo, Z. G., & Wang, J. (2020) · Oncogene · doi:10.1038/s41388-020-01446-1 · Cited by 10

Mechanism of the Conformational Change of the Protein Methyltransferase SMYD3: A Molecular Dynamics Simulation Study

Sun, J., Li, Z., & Yang, N. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22137185 · Cited by 10

Proteome-wide identification of non-histone lysine methylation in tomato during fruit ripening

Xiao, L., Liang, H., Jiang, G., Ding, X., Liu, X., Sun, J., Jiang, Y., Song, L., & Duan, X. (2022) · Journal of Advanced Research · doi:10.1016/j.jare.2022.02.013 · Cited by 10

Hippo signaling and histone methylation control cardiomyocyte cell cycle re-entry through distinct transcriptional pathways

Zhang, Z., Freeman, M. D., Zhang, Y., El‐Nachef, D., Davenport, G., Williams, A. L., & MacLellan, W. R. (2023) · PLoS ONE · doi:10.1371/journal.pone.0281610 · Cited by 10

Divergent Synthesis of Styryl–Cinnamate Hybrid Analogues Inspired by the Natural Product Salvianolic Acid F as a Premise To Investigate Their Anticancer Activity and Its Metabolomic Profiling

Shard, A., Rawat, K., Sinha, A. K., Padwad, Y. S., & Kumar, D. (2016) · European Journal of Organic Chemistry · doi:10.1002/ejoc.201601104 · Cited by 10

Overexpression of SET and MYND domain-containing protein 2 (SMYD2) is associated with poor prognosis in pediatric B lineage acute lymphoblastic leukemia

Zhang, P., Ruan, J., Weng, W., & Tang, Y. (2019) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.1080/10428194.2019.1675875 · Cited by 10

The role of SET domain containing lysine methyltransferase 7 in tumorigenesis and development

Yang, S., Wang, X., Bai, J., & Duan, B. (2022) · Cell Cycle · doi:10.1080/15384101.2022.2122257 · Cited by 9

DMSO‐Related Effects on Ligand‐Binding Properties of Lysine Methyltransferases G9a and SETD8

Feoli, A., Sarno, G., Castellano, S., & Sbardella, G. (2024) · ChemBioChem · doi:10.1002/cbic.202300809 · Cited by 9

Versatile and efficient chromatin pull-down methodology based on DNA triple helix formation

Isogawa, A., Fuchs, R. P., & 藤井, 慎. (2018) · Scientific Reports · doi:10.1038/s41598-018-24417-9 · Cited by 9

Characterization of Squamous Cell Lung Cancers from Appalachian Kentucky

Liu, J., Murali, T., Yu, T., Liu, C., Sivakumaran, T. A., Moseley, H., Zhulin, I. B., Weiss, H. L., Durbin, E. B., Ellingson, S. R., et al. (2018) · Cancer Epidemiology Biomarkers & Prevention · doi:10.1158/1055-9965.epi-17-0984 · Cited by 9

Methylation deficiency of chromatin proteins is a non-mutational and epigenetic-like trait in evolved lines of the archaeon Sulfolobus solfataricus

Johnson, T. B., Payne, S., Grove, R. A., McCarthy, S., Oeltjen, E., Mach, C., Adamec, J., Wilson, M. A., Cott, K. E. V., & Blum, P. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.006469 · Cited by 9

Conformational Selection in Ligand Recognition by the First Tudor Domain of PHF20L1

Lv, M., Gao, J., Li, M., Ma, R., Li, F., Liu, Y., Liu, M., Zhang, J., Yao, X., Wu, J., et al. (2020) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.0c02039 · Cited by 9

Synthesis and structure–activity relationship studies of LLY-507 analogues as SMYD2 inhibitors

Zhang, B., Liao, L., Wu, F., Zhang, F., Sun, Z., Chen, H., & Luo, C. (2020) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2020.127598 · Cited by 9

Investigation of H2 AX methylation by the SUV 39H2 protein lysine methyltransferase

Schuhmacher, M. K., Kudithipudi, S., & Jeltsch, A. (2016) · FEBS Letters · doi:10.1002/1873-3468.12216 · Cited by 10

The Role of Chromatin-Associated Proteins in Cancer

Helin, K., & Minucci, S. (2016) · Annual Review of Cancer Biology · doi:10.1146/annurev-cancerbio-050216-034422 · Cited by 9

SMYD2 Inhibition Downregulates TMPRSS2 and Decreases SARS-CoV-2 Infection in Human Intestinal and Airway Epithelial Cells

Yu, Y., Herrmann, A., Thonn, V., Cordsmeier, A., Neurath, M. F., Ensser, A., & Becker, C. (2022) · Cells · doi:10.3390/cells11081262 · Cited by 9

Inhibition of protein arginine methyltransferase 6 activates interferon signaling and induces the apoptosis of endometrial cancer cells via histone modification

Inoue, F., Sone, K., Kumegawa, K., Hachijo, R., Suzuki, E., Tanimoto, S., Tsuboyama, N., Kato, K., Toyohara, Y., Takahashi, Y., et al. (2024) · International Journal of Oncology · doi:10.3892/ijo.2024.5620 · Cited by 8

Binding Methylarginines and Methyllysines as Free Amino Acids: A Comparative Study of Multiple Host Classes**

Warmerdam, Z., Kamba, B. E., Le, M., Schrader, T. H., Isaacs, L., Bayer, P., & Hof, F. A. (2021) · ChemBioChem · doi:10.1002/cbic.202100502 · Cited by 8

Histone methyltransferase SUV420H1 / KMT5B contributes to poor prognosis in hepatocellular carcinoma

Kato, H., Hayami, S., Ueno, M., Suzaki, N., Nakamura, M., Yoshimura, T., Miyamoto, A., Shigekawa, Y., Okada, K., Miyazawa, M., et al. (2023) · Cancer Science · doi:10.1111/cas.16038 · Cited by 7

To Erase or Not to Erase: Non-Canonical Catalytic Functions and Non-Catalytic Functions of Members of Histone Lysine Demethylase Families

Nisio, E. D., Manzini, V., Licursi, V., & Negri, R. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25136900 · Cited by 7

Methyltransferases in cancer drug resistance: Unlocking the potential of targeting SMYD3 to sensitize cancer cells

Sanese, P., Fasano, C., Signorile, M. L., Marco, K. D., Forte, G., Disciglio, V., Grossi, V., & Simone, C. (2024) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2024.189203 · Cited by 8

Therapeutic targeting potential of the protein lysine and arginine methyltransferases to reverse cancer chemoresistance

Micallef, I., Fenech, K., & Baron, B. (2024) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2024.1455415 · Cited by 7

Computational approach for assessing the involvement of SMYD2 protein in human cancers using TCGA data

Yadav, A. K., & Singh, T. R. (2023) · Journal of Genetic Engineering and Biotechnology · doi:10.1186/s43141-023-00594-7 · Cited by 7

Phenotypic characterization of SETD3 knockout Drosophila

Tiebe, M., Lutz, M., Levy, D., & Teleman, A. A. (2018) · PLoS ONE · doi:10.1371/journal.pone.0201609 · Cited by 7

Lysine methylation regulates nervous system diseases

Wang, Z., & Liu, H. (2019) · Neuropeptides · doi:10.1016/j.npep.2019.04.004 · Cited by 7

Protein arginine methyltransferases as regulators of cellular stress

Zaccarelli‐Magalhães, J., Citadin, C. T., Langman, J., Smith, D. J., Matuguma, L. H., Lin, H. W., & Udo, M. S. B. (2024) · Experimental Neurology · doi:10.1016/j.expneurol.2024.115060 · Cited by 6

Insights into The Function and Regulation of Jumonji C Lysine Demethylases as Hypoxic Responsive Enzymes

Chopra, A., Adhikary, H., Willmore, W. G., & Biggar, K. K. (2019) · Current Protein and Peptide Science · doi:10.2174/1389203721666191231104225 · Cited by 7

Structure-function conservation between the methyltransferases SETD3 and SETD6

Admoni-Elisha, L., Abaev-Schneiderman, E., Cohn, O., Shapira, G., Shomron, N., Feldman, M., & Levy, D. (2022) · Biochimie · doi:10.1016/j.biochi.2022.05.003 · Cited by 6

Epigenetic Mechanisms in Head and Neck Cancer

Osorio, J. C., & Castillo, A. (2016) · InTech eBooks · doi:10.5772/61135 · Cited by 7

Identification and functional characterization of lysine methyltransferases of Entamoeba histolytica

Borbolla‐Vázquez, J., Orozco, E., Medina‐Gómez, C., Martínez‐Higuera, A., Javier‐Reyna, R., Chávez, B., Betanzos, A., & Rodríguez, M. A. (2016) · Molecular Microbiology · doi:10.1111/mmi.13394 · Cited by 6

Clinical Perspective of Posttranslational Modifications

Kawa, I. A., Masood, A., Amin, S., Mustafa, M. F., & Rashid, F. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-811913-6.00002-3 · Cited by 7

The post translational modification of key regulators of ATR signaling in DNA replication

Chen, Y., & Yuan, J. (2021) · Genome Instability & Disease · doi:10.1007/s42764-021-00036-z · Cited by 6

Distribution bias analysis of germline and somatic single-nucleotide variations that impact protein functional site and neighboring amino acids

Pan, Y., Yan, C., Hu, Y., Fan, Y., Pan, Q., Wan, Q., Torcivia-Rodriguez, J., & Mazumder, R. (2017) · Scientific Reports · doi:10.1038/srep42169 · Cited by 6

The molecular genetics of adrenal cushing

Vaduva, P., & Bertherat, J. Y. (2024) · HORMONES · doi:10.1007/s42000-024-00608-0 · Cited by 5

Regulation of autophagy and cellular signaling through non-histone protein methylation

Bao, Y., Ma, Y., Huang, W., Bai, Y., Gao, S., Xiu, L., Xie, Y., Wan, X., Shan, S., Chen, C., et al. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.139057 · Cited by 5

New insights into methionine’s role in maintaining intestinal stem cell regeneration via autophagy regulation

Lv, Y., Feng, Y., Lu, J., Zhang, S., Wei, Y., & Gao, C. (2025) · Animal nutrition · doi:10.1016/j.aninu.2025.04.008 · Cited by 5

Posttranslational modifications in Helicobacter pylori-associated gastric pathogenesis: Bridging inflammation and carcinogenesis

Li, W., Liu, T., Wu, T., Cai, T., Wang, F. W., & Zhang, M. (2025) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2025.189492 · Cited by 5

An antibody‐free enrichment approach enabled by reductive glutaraldehydation for monomethyllysine proteome analysis

Li, Z., Wang, Q., Wang, K., Zhang, W., & Ye, M. (2022) · PROTEOMICS · doi:10.1002/pmic.202100378 · Cited by 5

Site-Selective Modification of Secondary Amine Moieties on Native Peptides, Proteins, and Natural Products with Ynones

Gao, F., Chang, M., Xiang, M., Xu, H., Gnawali, G. R., Dong, Y., Lopez, B., & Wang, W. (2023) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.3c00246 · Cited by 5

Proteome-Wide Identification of Non-histone Lysine Methylation during Grape Berry Ripening

Pei, M., Liu, H., Wei, T., & Guo, D. (2023) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.3c03144 · Cited by 6

Lysine Demethylases

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The activity of a yeast Family 16 methyltransferase, Efm2, is affected by a conserved tryptophan and its N‐terminal region

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