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Global Proteome Analyses of Lysine Acetylation and Succinylation Reveal the Widespread Involvement of both Modification in Metabolism in the Embryo of Germinating Rice Seed
Abstract
Regulation of rice seed germination has been shown to mainly occur at post-transcriptional levels, of which the changes on proteome status is a major one. Lysine acetylation and succinylation are two prevalent protein post-translational modifications (PTMs) involved in multiple biological processes, especially for metabolism regulation. To investigate the potential mechanism controlling metabolism regulation in rice seed germination, we performed the lysine acetylation and succinylation analyses simultaneously. Using high-accuracy nano-LC-MS/MS in combination with the enrichment of lysine acetylated or succinylated peptides from digested embryonic proteins of 24 h after imbibition (HAI) rice seed, a total of 699 acetylated sites from 389 proteins and 665 succinylated sites from 261 proteins were identified. Among these modified lysine sites, 133 sites on 78 proteins were commonly modified by two PTMs. The overlapped PTM sites were more likely to be in polar acidic/basic amino acid regions and exposed on the protein surface. Both of the acetylated and succinylated proteins cover nearly all aspects of cellular functions. Ribosome complex and glycolysis/gluconeogenesis-related proteins were significantly enriched in both acetylated and succinylated protein profiles through KEGG enrichment and protein-protein interaction network analyses. The acetyl-CoA and succinyl-CoA metabolism-related enzymes were found to be extensively modified by both modifications, implying the functional interaction between the two PTMs. This study provides a rich resource to examine the modulation of the two PTMs on the metabolism pathway and other biological processes in germinating rice seed.
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Citations
Cites
Lysine acetylation targets protein complexes and co-regulates major cellular functions
Choudhary, C., Kumar, C., Gnad, F., Nielsen, M. L., Rehman, M., Walther, T. C., Olsen, J. V., & Mann, M. (2009) · Science · doi:10.1126/science.1175371 · Cited by 4,040
ACETYLATION AND METHYLATION OF HISTONES AND THEIR POSSIBLE ROLE IN THE REGULATION OF RNA SYNTHESIS
Allfrey, V. G., Faulkner, R. D., & Mirsky, A. E. (1964) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.51.5.786 · Cited by 2,788
Tan, M., Luo, H., Lee, S., Jin, F., Yang, J. S., Montellier, E., Buchou, T., Cheng, Z., Rousseaux, S., Rajagopal, N., et al. (2011) · Cell · doi:10.1016/j.cell.2011.08.008 · Cited by 1,902
Self-citationSirt5 Is a NAD-Dependent Protein Lysine Demalonylase and Desuccinylase
Du, J., Zhou, Y., Su, X., Yu, J. J., Khan, S., Jiang, H., Kim, J., Woo, J., Kim, J. H., Choi, B. H., et al. (2011) · Science · doi:10.1126/science.1207861 · Cited by 1,429
Multivalent engagement of chromatin modifications by linked binding modules
Ruthenburg, A. J., Li, H., Patel, D. J., & Allis, C. D. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2298 · Cited by 1,039
Identification of lysine succinylation as a new post-translational modification
Zhang, Z., Tan, M., Xie, Z., Dai, L., Chen, Y., & Zhao, Y. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.495 · Cited by 1,027
SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways
Park, J., Chen, Y., Tishkoff, D. X., Peng, C., Tan, M., Dai, L., Xie, Z., Zhang, Y., Zwaans, B. M. M., Skinner, M. E., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.06.001 · Cited by 1,000
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
Pandey, R. (2002) · Nucleic Acids Research · doi:10.1093/nar/gkf660 · Cited by 783
Weinert, B. T., Scholz, C. W., Wagner, S., Iešmantavičius, V., Su, D., Daniel, J. A., & Choudhary, C. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.07.024 · Cited by 774
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Ryan, D. G., Murphy, M. P., Frezza, C., Prag, H. A., Chouchani, E. T., O’Neill, L. A., & Mills, E. L. (2018) · Nature Metabolism · doi:10.1038/s42255-018-0014-7 · Cited by 398
Succinylation Links Metabolism to Protein Functions
Yang, Y., & Gibson, G. E. (2019) · Neurochemical Research · doi:10.1007/s11064-019-02780-x · Cited by 231
Peroxiredoxins and Redox Signaling in Plants
Liebthal, M. F., Maynard, D., & Dietz, K. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7164 · Cited by 216
Lysine acetylome profiling uncovers novel histone deacetylase substrate proteins in Arabidopsis
Hartl, M., Füßl, M., Boersema, P. J., Jost, J. O., Kramer, K., Bakirbas, A., Sindlinger, J., Plöchinger, M., Leister, D., Uhrig, R. G., et al. (2017) · Molecular Systems Biology · doi:10.15252/msb.20177819 · Cited by 162
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Willems, P., Horne, A., van Parys, T., Goormachtig, S., Smet, I. D., Botzki, A., Breusegem, F. V., & Gevaert, K. (2019) · The Plant Journal · doi:10.1111/tpj.14345 · Cited by 98
Oxidative stress‐triggered interactions between the succinyl‐ and acetyl‐proteomes of rice leaves
Zhou, H., Finkemeier, I., Guan, W., Tossounian, M., Wei, B., Young, D., Huang, J., Messens, J., Yang, X., Zhu, J., et al. (2017) · Plant Cell & Environment · doi:10.1111/pce.13100 · Cited by 125
Mitochondrial Energy Signaling and Its Role in the Low-Oxygen Stress Response of Plants
Wagner, S., Aken, O. V., Elsässer, M., & Schwarzländer, M. (2018) · PLANT PHYSIOLOGY · doi:10.1104/pp.17.01387 · Cited by 99
Sun, H., Liu, X., Li, F., Li, W., Zhang, J., Xiao, Z., Shen, L., Li, Y., Wang, F., & Yang, J. (2017) · Scientific Reports · doi:10.1038/s41598-017-03369-6 · Cited by 96
Fu, Y., Yu, J., Li, F., & Ge, S. (2022) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-022-02338-w · Cited by 104
Liu, S., Xue, C., Fang, Y., Chen, G., Peng, X., Zhou, Y., Chen, C., Liu, G., Gu, M., Wang, K., et al. (2018) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra118.000640 · Cited by 88
Impact of Post-Translational Modifications of Crop Proteins under Abiotic Stress
Hashiguchi, A., & Komatsu, S. (2016) · Proteomes · doi:10.3390/proteomes4040042 · Cited by 87
Histone deacetylases control lysine acetylation of ribosomal proteins in rice
Xu, Q., Liu, Q., Chen, Z., Yue, Y., Liu, Y., Zhao, Y. J., & Zhou, D. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab244 · Cited by 89
Lysine acetylation in mitochondria: From inventory to function
Hosp, F., Lassowskat, I., Santoro, V., Vleesschauwer, D. D., Fliegner, D., Redestig, H., Mann, M., Christian, S., Hannah, M. A., & Finkemeier, I. (2016) · Mitochondrion · doi:10.1016/j.mito.2016.07.012 · Cited by 89
Zhen, S., Deng, X., Wang, J., Zhu, G., Cao, H., Yuan, L., & Yan, Y. (2016) · Scientific Reports · doi:10.1038/srep31576 · Cited by 83
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Ren, S., Yang, M., Yue, Y., Ge, F., Li, Y., Guo, X., Zhang, J., Zhang, F., Nie, X., & Wang, S. (2018) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra117.000393 · Cited by 80
Zhao, G., Zhen, J., Liu, X., Guo, J. J., Li, D., Xie, J., & Xie, L. (2022) · Genes & Diseases · doi:10.1016/j.gendis.2022.03.009 · Cited by 68
Global analysis of protein lysine succinylation profiles in common wheat
Zhang, Y., Wang, G., Song, L., Mu, P., Wang, S., Liang, W., & Lin, Q. F. (2017) · BMC Genomics · doi:10.1186/s12864-017-3698-2 · Cited by 67
Tao, Q.-Q., Liu, L., Wang, P., Long, Q.-S., Zhao, Y., Jin, L., Xu, W.-M., Chen, Y., Li, Z., & Yang, S. (2019) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.9b02734 · Cited by 66
Proteome-wide Analysis of Lysine 2-hydroxyisobutyrylation in Developing Rice (Oryza sativa) Seeds
Meng, X., Xing, S., Perez, L. M., Peng, X., Zhao, Q., Redoña, E. D., Wang, C., & Peng, Z. (2017) · Scientific Reports · doi:10.1038/s41598-017-17756-6 · Cited by 66
Plant proteomic research for improvement of food crops under stresses: a review
Mustafa, G., & Komatsu, S. (2021) · Molecular Omics · doi:10.1039/d1mo00151e · Cited by 63
Xu, Y., Shen, C., Ma, J., Chen, W., Mao, J., Zhou, Y., & Chen, L. (2017) · Scientific Reports · doi:10.1038/s41598-017-02128-x · Cited by 56
Song, Y., Wang, J., Cheng, Z., Gao, P., Sun, J., Chen, X., Chen, C., Wang, Y., & Wang, Z. (2017) · Scientific Reports · doi:10.1038/srep42053 · Cited by 53
Self-citationAdvances in proteome-wide analysis of plant lysine acetylation
Xia, L., Kong, X., Song, H., Han, Q., & Zhang, S. (2021) · Plant Communications · doi:10.1016/j.xplc.2021.100266 · Cited by 55
Global Proteome Analysis Links Lysine Acetylation to Diverse Functions in Oryza Sativa
Xue, C., Liu, S., Chen, C., Zhu, J., Yang, X., Zhou, Y., Guo, R., Liu, X., & Gong, Z. (2017) · PROTEOMICS · doi:10.1002/pmic.201700036 · Cited by 52
ROS-stimulated protein lysine acetylation is required for crown root development in rice
Xu, Q., Wang, Y., Chen, Z., Yue, Y., Huang, H., Wu, B., Liu, Y., Zhou, D., & Zhao, Y. J. (2022) · Journal of Advanced Research · doi:10.1016/j.jare.2022.07.010 · Cited by 49
Systematic analysis of the lysine acetylome in Fusarium graminearum
Zhou, S., Yang, Q., Yin, C., Liu, L., & Liang, W. (2016) · BMC Genomics · doi:10.1186/s12864-016-3361-3 · Cited by 48
Large-Scale Assessment of Bioinformatics Tools for Lysine Succinylation Sites
Hasan, M. M., Khatun, M. S., & Kurata, H. (2019) · Cells · doi:10.3390/cells8020095 · Cited by 46
Meng, X., Mujahid, H., Zhang, Y., Peng, X., Redoña, E. D., Wang, C., & Peng, Z. (2019) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra119.001426 · Cited by 46
He, D., Li, M., Damaris, R. N., Bu, C., Xue, J., & Yang, P. (2019) · The Plant Journal · doi:10.1111/tpj.14593 · Cited by 46
Self-citationPan, R., He, D., Xu, L., Zhou, M., Li, C., Wu, C. L., Xu, Y., & Zhang, W. (2019) · BMC Genomics · doi:10.1186/s12864-018-5405-3 · Cited by 45
Self-citationZhang, N., Gao, R., Yang, J., Zhu, Y., Zhang, Z., Xu, X., Wang, J., Liu, X., Li, Z., Li, Z., et al. (2018) · PROTEOMICS · doi:10.1002/pmic.201800001 · Cited by 44
Meng, X., Lv, Y., Mujahid, H., Edelmann, M. J., Zhao, H. Q., Peng, X., & Peng, Z. (2017) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2017.12.001 · Cited by 44
Feng, S., Jiao, K., Guo, H., Jiang, M., Hao, J., Wang, H., & Shen, C. (2017) · BMC Genomics · doi:10.1186/s12864-017-3978-x · Cited by 44
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Liu, S., Yu, F., Yang, Z., Wang, T., Xiong, H., Chang, C., Yu, W., & Li, N. (2018) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra117.000530 · Cited by 41
Long, Q.-S., Liu, L., Zhao, Y., Wang, P., Chen, B., Li, Z., & Yang, S. (2019) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.9b03419 · Cited by 43
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Cerrato, A., Aita, S. E., Capriotti, A. L., Cavaliere, C., Montone, C. M., Laganà, A., & Piovesana, S. (2020) · Talanta · doi:10.1016/j.talanta.2020.121262 · Cited by 42
Mujahid, H., Meng, X., Xing, S., Peng, X., Wang, C., & Peng, Z. (2017) · Journal of Proteomics · doi:10.1016/j.jprot.2017.08.021 · Cited by 41
Xu, Y., Chen, W., Ma, C.-L., Shen, S.-Y., Zhou, Y., Zhou, L., & Chen, L. (2017) · Frontiers in Plant Science · doi:10.3389/fpls.2017.02104 · Cited by 41
Ren, S., Yang, M., Li, Y., Zhang, F., Chen, Z., Zhang, J., Yang, G., Yue, Y., Li, S., Ge, F., et al. (2016) · Scientific Reports · doi:10.1038/srep34078 · Cited by 40
Zhu, G., Yan, X., Zhu, D. Z., Deng, X., Wu, J., Xia, J. L., & Yan, Y. (2018) · Journal of Proteomics · doi:10.1016/j.jprot.2018.06.019 · Cited by 40
Balparda, M., Elsässer, M., Badia, M. B., Giese, J., Bovdilova, A., Hüdig, M., Reinmuth, L., Eirich, J., Schwarzländer, M., Finkemeier, I., et al. (2021) · The Plant Journal · doi:10.1111/tpj.15556 · Cited by 38
Li, X., Ye, J., Ma, H., & Lu, P. (2018) · The Plant Journal · doi:10.1111/tpj.13766 · Cited by 39
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Николаевна, С. Г., Gorbach, D., Lukasheva, E., Mavropolo-Stolyarenko, G., Bilova, T. E., Soboleva, A., Tsarev, A. A., Romanovskaya, E. V., Podolskaya, E. P., Zhukov, V. A., et al. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21239162 · Cited by 41
Systematic Analysis of the Lysine Succinylome in Candida albicans
Zheng, H., He, Y., Zhou, X., Qian, G., Lv, G., Shen, Y., Liu, J., Li, D., Li, X., & Liu, W. (2016) · Journal of Proteome Research · doi:10.1021/acs.jproteome.6b00578 · Cited by 36
Ubiquitinome Profiling Reveals the Landscape of Ubiquitination Regulation in Rice Young Panicles
Zhu, L., Cheng, H., Peng, G., Wang, S., Zhang, Z., Ni, E., Fu, X., Zhuang, C., Liu, Z., & Zhou, H. L. (2020) · Genomics Proteomics & Bioinformatics · doi:10.1016/j.gpb.2019.01.005 · Cited by 34
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Yu, F., Li, M., He, D., & Yang, P. (2021) · Frontiers in Plant Science · doi:10.3389/fpls.2021.642979 · Cited by 34
Self-citationTappiban, P., Ying, Y., Xu, F., & Bao, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22115901 · Cited by 36
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Jin, X., Li, X., da Silva, J. A. T., & Liu, X. (2024) · Journal of Integrative Plant Biology · doi:10.1111/jipb.13756 · Cited by 34
Zhang, Z., Zeng, Y., Hou, J., & Li, L. (2024) · Planta · doi:10.1007/s00425-024-04518-8 · Cited by 33
Fan, S., Zhang, D., Lei, C., Chen, H., Xing, L., Ma, J., Zhao, C., & Han, M. (2016) · Journal of Proteome Research · doi:10.1021/acs.jproteome.6b00357 · Cited by 32
Xu, X., Liang, R., Li, D., ChengYao, J., & Lin, S. (2020) · Journal of Functional Foods · doi:10.1016/j.jff.2020.103909 · Cited by 32
Xu, X., Liu, T., Yang, J., Chen, L., Liu, B., Wei, C., Wang, L., & Jin, Q. (2017) · BMC Genomics · doi:10.1186/s12864-017-3977-y · Cited by 32
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Ma, Y., Yang, M., Lin, X., Liu, X., Huang, H., & Ge, F. (2017) · Journal of Proteome Research · doi:10.1021/acs.jproteome.7b00017 · Cited by 31
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Lassowskat, I., Hartl, M., Hosp, F., Boersema, P. J., Mann, M., & Finkemeier, I. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-7225-8_5 · Cited by 31
Zhang, H., Li, P., Ren, S., Cheng, Z., Zhao, G., & Zhao, W. (2019) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra118.001298 · Cited by 29
Self-citationGlobal analysis of lysine succinylation in patchouli plant leaves
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Xue, C., Qiao, Z., Chen, X., Cao, P., Liu, K., Liu, S., Lu, Y., & Gong, Z. (2020) · Rice · doi:10.1186/s12284-020-00389-1 · Cited by 30
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Li, W., Xiong, Y., Lai, L. B., Zhang, K., Li, Z., Kang, H., Dai, L., Gopalan, V., Wang, G., & Liu, W. (2021) · Plant Biotechnology Journal · doi:10.1111/pbi.13612 · Cited by 28
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Proteomic analysis of lysine succinylation of the human pathogen Histoplasma capsulatum
Xie, L., Li, J., Deng, W., Yu, Z., Fang, W., Chen, M., Liao, W., Xie, J., & Pan, W. (2017) · Journal of Proteomics · doi:10.1016/j.jprot.2016.12.020 · Cited by 28
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Guo, W., Han, L., Li, X., Wang, H., Mu, P., Qi, L., Liu, Q., & Zhang, Y. (2020) · Scientific Reports · doi:10.1038/s41598-020-70230-8 · Cited by 25
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Ren, Z., Qi, D., Pugh, N., Li, K., Wen, B., Zhou, R., Xu, S., Liu, S., & Jones, A. R. (2018) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra118.000832 · Cited by 24
Sano, N., Takebayashi, Y., To, A., Mhiri, C., Rajjou, L., Nakagami, H., & Kanekatsu, M. (2019) · Plant and Cell Physiology · doi:10.1093/pcp/pcz152 · Cited by 27
Yang, C., Shen, S., Zhan, C., Li, Y., Zhang, R., Lv, Y., Yang, Z., Zhou, J., Shi, Y., Liu, X., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-51145-8 · Cited by 22
Protein acetylation as a mechanism for Kandelia candel’s adaption to daily flooding
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Cao, S., Chen, Z., Yue, L., Jiang, H., Ma, R.-Y., & Dong, L. (2022) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2022.783739 · Cited by 22
Zeng, F., Pang, H., Chen, Y., Zheng, H., Li, W., Ramanathan, S., Hoare, R., Monaghan, S. J., Lin, X., & Jian, J. (2021) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2020.626574 · Cited by 22
Protein Modification in Plants in Response to Abiotic Stress
Qazi, H. A., Jan, N., Ramazan, S., & John, R. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-811913-6.00008-4 · Cited by 22
Global analysis of lysine acetylation in soybean leaves
Li, G., Zheng, B., Zhao, W., Ren, T., Zhang, X., Ning, T., & Liu, P. (2021) · Scientific Reports · doi:10.1038/s41598-021-97338-9 · Cited by 19
Liu, X., Yang, M., Wang, Y., Chen, Z., Zhang, J., Lin, X., Ge, F., & Zhao, J. (2018) · Plant and Cell Physiology · doi:10.1093/pcp/pcy080 · Cited by 20
Systematic Identification and Analysis of Lysine Succinylation in Strawberry Stigmata
Fang, X., Xin, Y., Sheng, Z., Liu, H., Jiang, A., Wang, F., Yang, J., Xi, X., Zha, Q., Zhang, L., et al. (2018) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.8b02708 · Cited by 20
Yuan, B., Liu, T., Cheng, Y., Gao, S., Li, L., Cai, L., Yang, J., Chen, J., & Zhong, K. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.672559 · Cited by 19
Luo, W., He, M., Luo, Q., & Li, Y. (2023) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2022.1066822 · Cited by 20
Wang, J., Li, L., Chai, R., Zhang, Z., Qiu, H., Mao, X., Hao, Z., Wang, Y., & Sun, G. (2019) · Scientific Reports · doi:10.1038/s41598-018-36852-9 · Cited by 18
Mapping the N-linked glycosites of rice (Oryza sativa L.) germinating embryos
Ying, J., Zhao, J., Hou, Y., Wang, Y., Qiu, J., Li, Z., Tong, X., Shi, Z., Zhu, J., & Zhang, J. (2017) · PLoS ONE · doi:10.1371/journal.pone.0173853 · Cited by 18
Protein post-translational modification in plants: regulation and beyond
Li, Z., Qin, L., Wang, D., Cui, T., Liang, Y., Zang, S., Sun, T., Zhao, W., Wu, Q., & Que, Y. (2025) · Horticultural Plant Journal · doi:10.1016/j.hpj.2025.02.003 · Cited by 16
Dong, Y., & Chen, C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031173 · Cited by 16
YAAM: Yeast Amino Acid Modifications Database
Ledesma, L., Sandoval, E., Cruz-Martínez, U., Escalante, A. M., Mejía, S., Moreno‐Alvarez, P., Ávila, E., García, E., Coello, G., & Torres‐Quiroz, F. (2017) · Database · doi:10.1093/database/bax099 · Cited by 16
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Wang, Y., Yang, M., Ge, F., Jiang, B., Hu, R., Zhou, X., Yang, Y., & Liu, M. (2022) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2022.100490 · Cited by 14
Singh, P. K., Gao, W., Liao, P., Li, Y., Xu, F., Ma, X., Long, L., & Song, C. (2020) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2020.02.031 · Cited by 16
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He, D., Damaris, R. N., Li, M., Khan, I., & Yang, P. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21217909 · Cited by 17
Self-citationProteomics in relation to abiotic stress tolerance in plants
Gautam, A., Pandey, P., & Pandey, A. K. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-818204-8.00023-0 · Cited by 15
Mao, M., Xue, Y., He, Y., Zhou, X., Rafique, F., Hu, H., Liu, J., Feng, L., Yang, W., Li, X., et al. (2020) · BMC Genomics · doi:10.1186/s12864-020-6750-6 · Cited by 14
Wu, J. T., Meng, X., Jiang, W., Wang, Z., Zhang, J., Meng, F., Yao, X., Ye, M., Yao, L., Wang, L., et al. (2022) · Frontiers in Plant Science · doi:10.3389/fpls.2022.822374 · Cited by 14
Chen, J., Li, F., Liu, Y., Shen, W., Du, X., He, L., Meng, Z., Ma, X.-L., & Wang, Y. (2017) · Journal of Proteomics · doi:10.1016/j.jprot.2017.12.019 · Cited by 14
Tan, L., Yang, Y., Shang, W., Hu, Z., Peng, H., Li, S., Hu, X., & Rao, X. (2022) · Microbiology Spectrum · doi:10.1128/spectrum.03481-22 · Cited by 13
Wang, Z.-X., Hu, R.-S., Zhou, C., He, J.-J., Elsheikha, H. M., & Zhu, X. (2019) · Microorganisms · doi:10.3390/microorganisms7110510 · Cited by 12
Sharma, N., Madan, B., Khan, M. S., Sandhu, K. S., & Raghuram, N. (2023) · Frontiers in Plant Science · doi:10.3389/fpls.2023.1135675 · Cited by 11
Global Analysis of Lysine Lactylation of Germinated Seeds in Wheat
Zhu, J., Guo, W., & Lan, Y. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242216195 · Cited by 10
Crotonylation versus acetylation in petunia corollas with reduced acetyl‐CoA due to PaACL silencing
Yang, W., Li, X., Jiang, G., Yu, L., Li, H., Yu, S., Zhao, H., & Liu, J. (2022) · Physiologia Plantarum · doi:10.1111/ppl.13794 · Cited by 10
Liao, X., Zhang, X., Li, X., Tian, Y., Qing, Y., Wang, Y., Tang, S., Luo, X., Zhang, F., Zhang, L., et al. (2023) · PLANT PHYSIOLOGY · doi:10.1093/plphys/kiad285 · Cited by 11
He, D., Damaris, R. N., Fu, J., Tu, J., Fu, T., Chen, X. X., Yi, B., & Yang, P. (2016) · Frontiers in Plant Science · doi:10.3389/fpls.2016.00988 · Cited by 10
Self-citationHe, D., Cai, M., Liu, M., & Yang, P. (2022) · Journal of Proteomics · doi:10.1016/j.jprot.2022.104736 · Cited by 9
Self-citationDing, Y., Liu, Y., Yang, K., Zhao, Y., Wen, C., Yang, Y., & Zhang, W. (2024) · Genes · doi:10.3390/genes15040499 · Cited by 7
Ouyang, L., You, W., Poetsch, A., & Wei, L. (2024) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.4c05869 · Cited by 7
Metadata
- Authors
- He, D., Wang, Q., Li, M., Damaris, R. N., Yi, X., Cheng, Z., & Yang, P.
- Affiliations
- Chinese Academy of Sciences (CN)
- Jingjie PTM Biolabs (Hangzhou) Co. Ltd., Hangzhou 310018, China
- Corresponding author
- Yang, Pingfang
- Venue
- Journal of Proteome Research
- Publisher
- American Chemical Society (ACS)
- Published
- 2016-01-28
- Volume
- 15
- Issue
- 3
- Pages
- 879-890
- ISSN
- 1535-3893 (ISSN-L)
- 1535-3907
- OpenAlex
- W2235305215
- Cited by
- 124
- References
- 58
- Citations by year
- 2026: 2 · 2025: 6 · 2024: 7 · 2023: 4 · 2022: 17 · 2021: 14 · 2020: 12 · 2019: 18 · 2018: 12 · 2017: 22 · 2016: 9
- FWCI
- 23.81
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Proteome Research (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Natural Science Foundation of China (31101213, 31271805)
- Chinese Academy of Sciences
- Central People's Government of the People's Republic of China (SAJC201324)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Seed Germination and Physiology
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Molecular Biology Research
- Keywords
- lysine acetylation, lysine succinylation, post-translational modification, rice seed germination, seed embryo, metabolic regulation, acetyl-CoA metabolism, glycolysis/gluconeogenesis
- MeSH terms
- Acetylation, Amino Acid Sequence, Lysine, Plant Proteins, Protein Processing, Post-Translational, Oryza, Seeds, Germination, Succinic Acid, Proteome, Amino Acid Motifs, Seedlings, Metabolic Networks and Pathways, Protein Interaction Maps, Gene Ontology
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