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

Hallmarks of Cancer: The Next Generation

Hanahan, D., & Weinberg, R. A. (2011) · Cell · doi:10.1016/j.cell.2011.02.013 · Cited by 66,590 · see citing works

The Hallmarks of Aging

López-Otín, C., Blasco, M. A., Partridge, L., Serrano, M., & Kroemer, G. (2013) · Cell · doi:10.1016/j.cell.2013.05.039 · Cited by 14,982 · see citing works

Sarcopenia: revised European consensus on definition and diagnosis

Cruz-Jentoft, A. J., Bahat, G., Bauer, J., Boirie, Y., Bruyère, O., Cederholm, T., Cooper, C., Landi, F., Rolland, Y., Sayer, A. A., et al. (2019) · Age and Ageing · doi:10.1093/ageing/afy169 · Cited by 13,818 · see citing works

Sorafenib in advanced hepatocellular carcinoma

Llovet, J. M., Ricci, S., Mazzaferro, V., Hilgard, P., Gane, E., Blanc, J.-F., de Oliveira, A. C., Santoro, A., Raoul, J.-L., Forner, A., et al. (2008) · New England Journal of Medicine · doi:10.1056/nejmoa0708857 · Cited by 13,097 · see citing works

UniProt: a worldwide hub of protein knowledge

The UniProt Consortium (2019) · Nucleic Acids Research · doi:10.1093/nar/gky1049 · Cited by 7,698 · see citing works

From Dietary Fiber to Host Physiology: Short-Chain Fatty Acids as Key Bacterial Metabolites

Koh, A., De Vadder, F., Kovatcheva-Datchary, P., & Bäckhed, F. (2016) · Cell · doi:10.1016/j.cell.2016.05.041 · Cited by 7,070 · see citing works

A New Era of Systemic Therapy for Hepatocellular Carcinoma with Regorafenib and Lenvatinib

Kudo, M. (2017) · Liver Cancer · doi:10.1159/000462153 · Cited by 5,974 · see citing works

Erlotinib versus standard chemotherapy as first-line treatment for European patients with advanced EGFR mutation-positive non-small-cell lung cancer (EURTAC): a multicentre, open-label, randomised phase 3 trial

Rosell, R., Carcereny, E., Gervais, R., Vergnenegre, A., Massuti, B., Felip, E., Palmero, R., Garcia-Gomez, R., Pallares, C., Sanchez, J. M., et al. (2012) · The Lancet Oncology · doi:10.1016/s1470-2045(11)70393-x · Cited by 5,489 · see citing works

Reactive oxygen species (ROS) as pleiotropic physiological signalling agents

Sies, H., & Jones, D. P. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0230-3 · Cited by 5,335 · see citing works

The role of short-chain fatty acids in the interplay between diet, gut microbiota, and host energy metabolism

den Besten, G., van Eunen, K., Groen, A. K., Venema, K., Reijngoud, D.-J., & Bakker, B. M. (2013) · Journal of Lipid Research · doi:10.1194/jlr.r036012 · Cited by 5,048 · see citing works

Targeting Hypoxia-Inducible Factors for the Treatment of Anemia in Chronic Kidney Disease Patients

Locatelli, F., Fishbane, S. N., Block, G. A., & Macdougall, I. C. (2017) · American Journal of Nephrology · doi:10.1159/000455166 · Cited by 4,834 · see citing works

Metabolic regulation of gene expression by histone lactylation

Zhang, D., Tang, Z., Huang, H., Zhou, G., Cui, C., Weng, Y., Liu, W., Kim, S., Lee, S., Perez-Neut, M., et al. (2019) · Nature · doi:10.1038/s41586-019-1678-1 · Cited by 4,371 · see citing works

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 · see citing works

The ubiquitin code

Komander, D., & Rape, M. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060310-170328 · Cited by 3,679 · see citing works

Neutrophil extracellular traps in immunity and disease

Papayannopoulos, V. (2017) · Nature reviews. Immunology · doi:10.1038/nri.2017.105 · Cited by 3,428 · see citing works

Everolimus for Advanced Pancreatic Neuroendocrine Tumors

Yao, J. C., Shah, M. H., Ito, T., Lombard‐Bohas, C., Wolin, E. M., Cutsem, E. V., Hobday, T. J., Okusaka, T., Capdevila, J., de Vries, E. G. E., et al. (2011) · New England Journal of Medicine · doi:10.1056/nejmoa1009290 · Cited by 2,879 · see citing works

Cellular senescence: from physiology to pathology

Muñoz-Espín, D., & Serrano, M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3823 · Cited by 2,818 · see citing works

Endoplasmic reticulum stress and the inflammatory basis of metabolic disease

Hotamisligil, G. S. (2010) · Cell · doi:10.1016/j.cell.2010.02.034 · Cited by 2,802 · see citing works

Glycosylation in Cellular Mechanisms of Health and Disease

Ohtsubo, K., & Marth, J. D. (2006) · Cell · doi:10.1016/j.cell.2006.08.019 · Cited by 2,765 · see citing works

2. Classification and Diagnosis of Diabetes: Standards of Medical Care in Diabetes—2019

(2018) · Diabetes Care · doi:10.2337/dc19-s002 · Cited by 2,738 · see citing works

Fibroblast growth factor signalling: from development to cancer

Turner, N., & Grose, R. (2010) · Nature Reviews. Cancer · doi:10.1038/nrc2780 · Cited by 2,689 · see citing works

Oxidative Stress in Cancer

Hayes, J. D., Dinkova-Kostova, A. T., & Tew, K. D. (2020) · Cancer Cell · doi:10.1016/j.ccell.2020.06.001 · Cited by 2,654 · see citing works

Biological roles of glycans

Varki, A. (2017) · Glycobiology · doi:10.1093/glycob/cww086 · Cited by 2,635 · see citing works

Hallmarks of Cellular Senescence

Hernandez-Segura, A., Nehme, J., & Demaria, M. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.02.001 · Cited by 2,605 · see citing works

The many roles of histone deacetylases in development and physiology: implications for disease and therapy

Haberland, M., Montgomery, R. L., & Olson, E. N. (2008) · Nature Reviews Genetics · doi:10.1038/nrg2485 · Cited by 2,541 · see citing works

Pazopanib in Locally Advanced or Metastatic Renal Cell Carcinoma: Results of a Randomized Phase III Trial

Sternberg, C. N., Davis, I. D., Mardiak, J., Szczylik, C. A., Lee, E., Wagstaff, J., Barrios, C. H., Salman, P., Gladkov, O. A., Kavina, A., et al. (2010) · Journal of Clinical Oncology · doi:10.1200/jco.2009.23.9764 · Cited by 2,470 · see citing works

Signaling to NF-κB by Toll-like receptors

Kawai, T., & Akira, S. (2007) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2007.09.002 · Cited by 2,395 · see citing works

LinkedOmics: analyzing multi-omics data within and across 32 cancer types

Vasaikar, S. V., Straub, P., Wang, J., & Zhang, B. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx1090 · Cited by 2,324 · see citing works

Histone methylation: a dynamic mark in health, disease and inheritance

Greer, E. L., & Shi, Y. (2012) · Nature Reviews Genetics · doi:10.1038/nrg3173 · Cited by 2,241 · see citing works

Trapping of PARP1 and PARP2 by Clinical PARP Inhibitors

Murai, J., Huang, S.-Y. N., Das, B. B., Renaud, A., Zhang, Y., Doroshow, J. H., Ji, J. J., Takeda, S., & Pommier, Y. G. (2012) · Cancer Research · doi:10.1158/0008-5472.can-12-2753 · Cited by 2,217 · see citing works

Histone demethylation by a family of JmjC domain-containing proteins

Tsukada, Y.-I., Fang, J., Erdjument‐Bromage, H., Warren, M., Borchers, C. H., Tempst, P., & Zhang, Y. (2005) · Nature · doi:10.1038/nature04433 · Cited by 2,171 · see citing works

Glycosylation in health and disease

Reily, C., Stewart, T. J., Renfrow, M. B., & Novak, J. (2019) · Nature Reviews Nephrology · doi:10.1038/s41581-019-0129-4 · Cited by 2,075 · see citing works

Ubiquitin modifications

Swatek, K. N., & Komander, D. (2016) · Cell Research · doi:10.1038/cr.2016.39 · Cited by 2,070 · see citing works

The diverse functions of histone lysine methylation

Martin, C., & Zhang, Y. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1761 · Cited by 2,066 · see citing works

Amyloid Precursor Protein Processing and Alzheimer's Disease

O'Brien, R. J., & Wong, P. C. (2011) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-061010-113613 · Cited by 2,061 · see citing works

Phosphorylation of innate immune adaptor proteins MAVS, STING, and TRIF induces IRF3 activation

Liu, S., Cai, X., Wu, J., Cong, Q., Chen, X., Li, T., Du, F., Ren, J., Wu, Y.-T., Grishin, N. V., et al. (2015) · Science · doi:10.1126/science.aaa2630 · Cited by 1,927 · see citing works

Loss of acetylation at Lys16 and trimethylation at Lys20 of histone H4 is a common hallmark of human cancer

Fraga, M. F., Ballestar, E., Villar‐Garea, A., Boix-Chornet, M., Espada, J., Schotta, G., Bonaldi, T., Haydon, C. E., Ropero, S., Petrie, K. R., et al. (2005) · Nature Genetics · doi:10.1038/ng1531 · Cited by 1,926 · see citing works

Regulation of cellular metabolism by protein lysine acetylation

Zhao, S., Xu, W., Jiang, W., Yu, W., Lin, Y., Zhang, T., Yao, J., Zhou, L., Zeng, Y., Li, H., et al. (2010) · Science · doi:10.1126/science.1179689 · Cited by 1,910 · see citing works

Identification of 67 Histone Marks and Histone Lysine Crotonylation as a New Type of Histone Modification

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 · see citing works

Protein Tyrosine Phosphatases in the Human Genome

Alonso, A., Sasin, J., Bottini, N., Friedberg, I., Friedberg, I., Osterman, A., Godzik, A., Hunter, T., Dixon, J., & Mustelin, T. (2004) · Cell · doi:10.1016/j.cell.2004.05.018 · Cited by 1,886 · see citing works

Lack of Fucose on Human IgG1 N-Linked Oligosaccharide Improves Binding to Human FcγRIII and Antibody-dependent Cellular Toxicity

Shields, R. L., Lai, J., Keck, R., O'Connell, L. Y., Hong, K., Meng, Y. G., Weikert, S. H. A., & Presta, L. G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202069200 · Cited by 1,835 · see citing works

Protein Arginine Methylation in Mammals: Who, What, and Why

Bedford, M. T., & Clarke, S. G. (2009) · Molecular Cell · doi:10.1016/j.molcel.2008.12.013 · Cited by 1,810 · see citing works

Entrectinib in Patients with Advanced or Metastatic NTRK Fusion-Positive Solid Tumours: Integrated Analysis of Three Phase 1-2 Trials

Doebele, R. C., Drilon, A., Paz-Ares, L., Siena, S., Shaw, A. T., Farago, A. F., Blakely, C. M., Seto, T., Cho, B. C., Tosi, D., et al. (2020) · The Lancet Oncology · doi:10.1016/s1470-2045(19)30691-6 · Cited by 1,790 · see citing works

CBP/p300 in cell growth, transformation, and development

Goodman, R. H., & Smolik, S. (2000) · Genes & Development · doi:10.1101/gad.14.13.1553 · Cited by 1,778 · see citing works

Requirement of NAD and <i>SIR2</i> for Life-Span Extension by Calorie Restriction in <i>Saccharomyces cerevisiae</i>

Lin, S.-J., Defossez, P.-A., & Guarente, L. (2000) · Science · doi:10.1126/science.289.5487.2126 · Cited by 1,775 · see citing works

Ulcerative colitis

Kobayashi, T., Siegmund, B., Berre, C. L., Wei, S. C., Ferrante, M., Shen, B., Bernstein, C. N., Danese, S., Peyrin‐Biroulet, L., & Hibi∥, T. (2020) · Nature Reviews Disease Primers · doi:10.1038/s41572-020-0205-x · Cited by 1,744 · see citing works

Vertebrate protein glycosylation: diversity, synthesis and function

Moremen, K. W., Tiemeyer, M., & Nairn, A. V. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3383 · Cited by 1,681 · 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

The Adaptor Protein MITA Links Virus-Sensing Receptors to IRF3 Transcription Factor Activation

Zhong, B., Yang, Y., Li, S., Wang, Y., Li, Y., Diao, F., Lei, C., He, X., Zhang, L., Tien, P., et al. (2008) · Immunity · doi:10.1016/j.immuni.2008.09.003 · Cited by 1,513 · see citing works

PAD4 is essential for antibacterial innate immunity mediated by neutrophil extracellular traps

Li, P., Li, M., Lindberg, M. R., Kennett, M. J., Xiong, N., & Wang, Y. (2010) · Journal of Experimental Medicine · doi:10.1084/jem.20100239 · Cited by 1,495 · see citing works

Serine/threonine phosphatases: mechanism through structure

Shi, Y. (2009) · Cell · doi:10.1016/j.cell.2009.10.006 · Cited by 1,488 · see citing works

Mechanisms of specificity in protein phosphorylation

Ubersax, J. A., & Ferrell Jr, J. E. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2203 · Cited by 1,451 · see citing works

Sirt5 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 · see citing works

Mucin dynamics and enteric pathogens

McGuckin, M. A., Lindén, S. K., Sutton, P., & Florin, T. H. (2011) · Nature Reviews Microbiology · doi:10.1038/nrmicro2538 · Cited by 1,428 · see citing works

Precision mapping of the human O‐GalNAc glycoproteome through SimpleCell technology

Steentoft, C., Vakhrushev, S. Y., Joshi, H. J., Kong, Y., Vester-Christensen, M. B., Schjoldager, K. T.-B. G., Lavrsen, K., Dabelsteen, S., Pedersen, N. B., Marcos-Silva, L., et al. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.79 · Cited by 1,410 · see citing works

Ubiquitination in disease pathogenesis and treatment

Popovic, D., Vucic, D., & Đikić, I. (2014) · Nature Medicine · doi:10.1038/nm.3739 · Cited by 1,405 · see citing works

Unravelling mechanisms of p53-mediated tumour suppression

Bieging-Rolett, K. T., Mello, S. S., & Attardi, L. D. (2014) · Nature reviews. Cancer · doi:10.1038/nrc3711 · Cited by 1,389 · see citing works

Immune checkpoint signaling and cancer immunotherapy

He, X., & Xu, C. (2020) · Cell Research · doi:10.1038/s41422-020-0343-4 · Cited by 1,384 · see citing works

The multifaceted functions of neutrophils

Mayadas, T. N., Cullere, X., & Lowell, C. A. (2014) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathol-020712-164023 · Cited by 1,356 · see citing works

The crucial role of protein phosphorylation in cell signaling and its use as targeted therapy (Review)

Ardito, F., Giuliani, M., PERRONE, D., Troiano, G., & Muzio, L. L. (2017) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2017.3036 · Cited by 1,349 · see citing works

The growing landscape of lysine acetylation links metabolism and cell signalling

Choudhary, C., Weinert, B. T., Nishida, Y., Verdin, E., & Mann, M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3841 · Cited by 1,324 · see citing works

Global view of human protein glycosylation pathways and functions

Schjoldager, K. T.-B. G., Narimatsu, Y., Joshi, H. J., & Clausen, H. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-00294-x · Cited by 1,322 · see citing works

Fuel Metabolism in Starvation

Cahill, G. F. (2006) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.26.061505.111258 · Cited by 1,318 · see citing works

The cancer metabolic reprogramming and immune response

Xia, L., Oyang, L., Lin, J., Tan, S., Han, Y., Wu, N., Yi, P., Tang, L., Pan, Q., Rao, S., et al. (2021) · Molecular Cancer · doi:10.1186/s12943-021-01316-8 · Cited by 1,312 · see citing works

Calorie restriction reduces oxidative stress by SIRT3-mediated SOD2 activation

Qiu, X., Brown, K., Hirschey, M. D., Verdin, E., & Chen, D. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.11.015 · Cited by 1,310 · see citing works

Cysteine-Mediated Redox Signaling: Chemistry, Biology, and Tools for Discovery

Paulsen, C. E., & Carroll, K. S. (2013) · Chemical Reviews · doi:10.1021/cr300163e · Cited by 1,282 · see citing works

Kinase-targeted cancer therapies: progress, challenges and future directions

Bhullar, K. S., Orrego-Lagarón, N., McGowan, E. M., Parmar, I., Jha, A., Hubbard, B. P., & Rupasinghe, H. P. V. (2018) · Molecular Cancer · doi:10.1186/s12943-018-0804-2 · Cited by 1,260 · see citing works

VEGF targets the tumour cell

Goel, H. L., & Mercurio, A. M. (2013) · Nature reviews. Cancer · doi:10.1038/nrc3627 · Cited by 1,258 · see citing works

Writing, erasing and reading histone lysine methylations

Hyun, K., Jeon, J., Park, K., & Kim, J. (2017) · Experimental &amp; Molecular Medicine · doi:10.1038/emm.2017.11 · Cited by 1,250 · see citing works

Functions and mechanisms of non-histone protein acetylation

Narita, T., Weinert, B. T., & Choudhary, C. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0081-3 · Cited by 1,232 · see citing works

New insights into the molecular and cellular functions of poly(ADP-ribose) and PARPs

Gibson, B. A., & Kraus, W. L. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3376 · Cited by 1,226 · see citing works

Proteasome-Independent Functions of Ubiquitin in Endocytosis and Signaling

Mukhopadhyay, D., & Riezman, H. (2007) · Science · doi:10.1126/science.1127085 · Cited by 1,221 · see citing works

Cabozantinib in Progressive Medullary Thyroid Cancer

Elisei, R., Schlumberger, M. J., Müller, S. P., Schöffski, P., Brose, M. S., Shah, M. H., Licitra, L., Jarzab, B., Medvedev, V., Kreissl, M. C., et al. (2013) · Journal of Clinical Oncology · doi:10.1200/jco.2012.48.4659 · Cited by 1,217 · see citing works

Programmed cell death 1 forms negative costimulatory microclusters that directly inhibit T cell receptor signaling by recruiting phosphatase SHP2

Yokosuka, T., Takamatsu, M., Kobayashi-Imanishi, W., Hashimoto-Tane, A., Azuma, M., & Saito, T. (2012) · Journal of Experimental Medicine · doi:10.1084/jem.20112741 · Cited by 1,161 · see citing works

Structure of the DDB1–CRBN E3 ubiquitin ligase in complex with thalidomide

Fischer, E. S., Böhm, K., Lydeard, J. R., Yang, H., Stadler, M. B., Cavadini, S., Nagel, J., Serluca, F., Acker, V., Lingaraju, G. M., et al. (2014) · Nature · doi:10.1038/nature13527 · Cited by 1,141 · see citing works

Metabolic regulation of gene expression through histone acylations

Sabari, B. R., Zhang, D., Allis, C. D., & Zhao, Y. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.140 · Cited by 1,134 · see citing works

Targeting the cancer epigenome for therapy

Jones, P. A., Issa, J. J., & Baylin, S. B. (2016) · Nature Reviews Genetics · doi:10.1038/nrg.2016.93 · Cited by 1,132 · see citing works

Histone post-translational modifications - cause and consequence of genome function

Millán-Zambrano, G., Burton, A., Bannister, A. J., & Schneider, R. (2022) · Nature Reviews Genetics · doi:10.1038/s41576-022-00468-7 · Cited by 1,116 · see citing works

Siglec-mediated regulation of immune cell function in disease

Macauley, M. S., Crocker, P. R., & Paulson, J. C. (2014) · Nature reviews. Immunology · doi:10.1038/nri3737 · Cited by 1,104 · see citing works

Sumoylation: A Regulatory Protein Modification in Health and Disease

Flotho, A., & Melchior, F. (2013) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061909-093311 · Cited by 1,101 · see citing works

Integrated Proteogenomic Characterization of HBV-Related Hepatocellular Carcinoma

Gao, Q., Zhu, H., Dong, L., Shi, W., Chen, R., Song, Z., Huang, C., Li, J., Dong, X., Zhou, Y., et al. (2019) · Cell · doi:10.1016/j.cell.2019.08.052 · Cited by 1,096 · see citing works

Proteolysis-Targeting Chimeras as Therapeutics and Tools for Biological Discovery

Burslem, G. M., & Crews, C. M. (2020) · Cell · doi:10.1016/j.cell.2019.11.031 · Cited by 1,079 · see citing works

Mechanisms of receptor tyrosine kinase activation in cancer

Du, Z., & Lovly, C. M. (2018) · Molecular Cancer · doi:10.1186/s12943-018-0782-4 · Cited by 1,066 · see citing works

Tuning gene expression to changing environments: from rapid responses to evolutionary adaptation

López-Maury, L., Marguerat, S., & Bähler, J. (2008) · Nature Reviews Genetics · doi:10.1038/nrg2398 · Cited by 1,061 · see citing works

The increasing complexity of the ubiquitin code

Yau, R., & Rape, M. (2016) · Nature Cell Biology · doi:10.1038/ncb3358 · Cited by 1,054 · see citing works

SUMO-1 Modification of IκBα Inhibits NF-κB Activation

Desterro, J. M. P., Rodríguez, M. S., & Hay, R. T. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80133-1 · Cited by 1,048 · see citing works

Mechanisms of Deubiquitinase Specificity and Regulation

Mevissen, T. E. T., & Komander, D. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-044916 · Cited by 1,035 · see citing works

Encorafenib plus binimetinib versus vemurafenib or encorafenib in patients with BRAF-mutant melanoma (COLUMBUS): a multicentre, open-label, randomised phase 3 trial

Dummer, R., Ascierto, P. A., Gogas, H. J., Arance, A. M., Mandalà, M., Liszkay, G., Garbe, C., Schadendorf, D., Krajsová, I., Gutzmer, R., et al. (2018) · The Lancet Oncology · doi:10.1016/s1470-2045(18)30142-6 · Cited by 1,034 · see citing works

Free Fatty Acid Receptors in Health and Disease

Kimura, I., Ichimura, A., Ohue‐Kitano, R., & Igarashi, M. (2019) · Physiological Reviews · doi:10.1152/physrev.00041.2018 · Cited by 1,032 · see citing works

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 · see citing works

Cyclin D–CDK4 kinase destabilizes PD-L1 via cullin 3–SPOP to control cancer immune surveillance

Zhang, J., Bu, X., Wang, H., Zhu, Y., Geng, Y., Nihira, N. T., Tan, Y., Ci, Y., Wu, F., Dai, X., et al. (2018) · Nature · doi:10.1038/nature25015 · Cited by 1,013 · see citing works

Human PAD4 Regulates Histone Arginine Methylation Levels via Demethylimination

Wang, Y., Wysocka, J., Sayegh, J., Lee, Y., Perlin, J. R., Leonelli, L., Sonbuchner, L. S., McDonald, C. H., Cook, R. G., Dou, Y., et al. (2004) · Science · doi:10.1126/science.1101400 · Cited by 1,013 · see citing works

Post-translational modifications in the context of therapeutic proteins

Walsh, G., & Jefferis, R. (2006) · Nature Biotechnology · doi:10.1038/nbt1252 · Cited by 1,007 · see citing works

Mode of action of nintedanib in the treatment of idiopathic pulmonary fibrosis

Wollin, L., Wex, E., Pautsch, A., Schnapp, G., Hostettler, K. E., Stowasser, S., & Kolb, M. (2015) · European Respiratory Journal · doi:10.1183/09031936.00174914 · Cited by 1,005 · see citing works

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 · see citing works

Obesity, inflammation, and atherosclerosis

Rocha, V. Z., & Libby, P. (2009) · Nature Reviews Cardiology · doi:10.1038/nrcardio.2009.55 · Cited by 994 · see citing works

PAD, a growing family of citrullinating enzymes: genes, features and involvement in disease

Vossenaar, E. R., Zendman, A. J. W., VENROOIJ, W. J. V., & Pruijn, G. J. M. (2003) · BioEssays · doi:10.1002/bies.10357 · Cited by 986 · see citing works

Modulation of cellular processes by histone and non-histone protein acetylation

Shvedunova, M., & Akhtar, A. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00441-y · Cited by 975 · see citing works

ATP-dependent reduction of cysteine–sulphinic acid by S. cerevisiae sulphiredoxin

Biteau, B., Labarre, J., & Tolédano, M. B. (2003) · Nature · doi:10.1038/nature02075 · Cited by 970 · see citing works

Alzheimer’s disease: risk factors and potentially protective measures

Silva, M. V. F., Loures, C. D. M. G., Alves, L. C. V., de Souza, L. C., Borges, K. B. G., & Ferriani, M. D. G. C. (2019) · Journal of Biomedical Science · doi:10.1186/s12929-019-0524-y · Cited by 962 · see citing works

Histone lactylation drives oncogenesis by facilitating m6A reader protein YTHDF2 expression in ocular melanoma

Yu, J., Chai, P., Xie, M., Ge, S., Ruan, J., Fan, X., & Jia, R. (2021) · Genome biology · doi:10.1186/s13059-021-02308-z · Cited by 955 · see citing works

Inactivating mutations of acetyltransferase genes in B-cell lymphoma

Pasqualucci, L., Dominguez-Sola, D., Chiarenza, A., Fabbri, G., Grunn, A., Trifonov, V., Kasper, L. H., Lerach, S., Tang, H., Ma, J., et al. (2011) · Nature · doi:10.1038/nature09730 · Cited by 949 · see citing works

Acetylation of Tau Inhibits Its Degradation and Contributes to Tauopathy

Min, S.-W., Cho, S.-H., Zhou, Y., Schroeder, S., Haroutunian, V., Seeley, W. W., Huang, E. J., Shen, Y., Masliah, E., Mukherjee, C., et al. (2010) · Neuron · doi:10.1016/j.neuron.2010.08.044 · Cited by 949 · see citing works

Enhancement of proteasome activity by a small-molecule inhibitor of USP14

Lee, B., Lee, M. J., Park, S., Oh, D., Elsasser, S., Chen, P., Gartner, C. A., Dimova, N. V., Hanna, J. W., Gygi, S. P., et al. (2010) · Nature · doi:10.1038/nature09299 · Cited by 943 · see citing works

Linear ubiquitination prevents inflammation and regulates immune signalling

Gerlach, B., Cordier, S. M., Schmukle, A. C., Emmerich, C. H., Rieser, E., Haas, T. L., Webb, A. I., Rickard, J. A., Anderton, H., Wong, W. W.-L., et al. (2011) · Nature · doi:10.1038/nature09816 · Cited by 940 · see citing works

Precision Mapping of an In Vivo N-Glycoproteome Reveals Rigid Topological and Sequence Constraints

Zielinska, D. F., Gnad, F., Wiśniewski, J. R., & Mann, M. (2010) · Cell · doi:10.1016/j.cell.2010.04.012 · Cited by 895 · see citing works

Integrated Proteogenomic Characterization of HBV-Related Hepatocellular Carcinoma.

Gao, Q., Zhu, H.-W., Dong, L.-Q., Shi, W.-W., Chen, R., Song, Z.-J., Huang, C., Li, J., Dong, X., Zhou, Y.-T., et al. (2019) · Cell · doi:10.1016/j.cell.2019.10.038 · Cited by 895 · see citing works

Classification of small molecule protein kinase inhibitors based upon the structures of their drug-enzyme complexes

Roskoski, R. (2016) · Pharmacological Research · doi:10.1016/j.phrs.2015.10.021 · Cited by 886 · see citing works

Everolimus for angiomyolipoma associated with tuberous sclerosis complex or sporadic lymphangioleiomyomatosis (EXIST-2): a multicentre, randomised, double-blind, placebo-controlled trial

Bissler, J. J., Kingswood, J. C., Radzikowska, E., Zonnenberg, B. A., Frost, M., Белоусова, Е. Д., Sauter, M., Nonomura, N., Brakemeier, S., de Vries, P. J., et al. (2013) · The Lancet · doi:10.1016/s0140-6736(12)61767-x · Cited by 880 · see citing works

Brain-Specific Phosphorylation of MeCP2 Regulates Activity-Dependent Bdnf Transcription, Dendritic Growth, and Spine Maturation

Zhou, Z., Hong, E. J., Cohen, S., Zhao, W.-N., Ho, H.-Y. H., Schmidt, L., Chen, W. G., Lin, Y., Savner, E., Griffith, E. C., et al. (2006) · Neuron · doi:10.1016/j.neuron.2006.09.037 · Cited by 877 · see citing works

50 years of protein acetylation: from gene regulation to epigenetics, metabolism and beyond

Verdin, E. M., & Ott, M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3931 · Cited by 876 · see citing works

Control of mucin-type O-glycosylation: A classification of the polypeptide GalNAc-transferase gene family

Bennett, E. P., Mandel, U., Clausen, H., Gerken, T. A., Fritz, T. A., & Tabak, L. A. (2012) · Glycobiology · doi:10.1093/glycob/cwr182 · Cited by 876 · see citing works

Positive feedback regulation of microglial glucose metabolism by histone H4 lysine 12 lactylation in Alzheimer’s disease

Pan, R.-Y., He, L., Zhang, J., Liu, X., Liao, Y., Gao, J., Liao, Y., Yan, Y., Li, Q., Zhou, X., et al. (2022) · Cell Metabolism · doi:10.1016/j.cmet.2022.02.013 · Cited by 862 · see citing works

An epigenetic blockade of cognitive functions in the neurodegenerating brain

Gräff, J., Rei, D., Guan, J.-S., Wang, W.-Y., Seo, J., Hennig, K. M., Nieland, T. J. F., Fass, D. M., Kao, P. F., Kahn, M., et al. (2012) · Nature · doi:10.1038/nature10849 · Cited by 853 · see citing works

Lysine glutarylation is a protein posttranslational modification regulated by SIRT5

Tan, M., Peng, C., Anderson, K. A., Chhoy, P., Xie, Z., Dai, L., Park, J., Chen, Y., Huang, H., Zhang, Y., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.03.014 · Cited by 844 · see citing works

Class I histone deacetylases (HDAC1–3) are histone lysine delactylases

Moreno-Yruela, C., Zhang, D., Wei, W., Bæk, M., Liu, W., Gao, J., Danková, D., Nielsen, A. L., Bolding, J. E., Yang, L., et al. (2022) · Science Advances · doi:10.1126/sciadv.abi6696 · Cited by 841 · see citing works

Systemic Lupus Erythematosus

Kiriakidou, M., & Ching, C. L. (2020) · Annals of Internal Medicine · doi:10.7326/aitc202006020 · Cited by 838 · see citing works

MUC1: a multifaceted oncoprotein with a key role in cancer progression

Nath, S., & Mukherjee, P. (2014) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2014.02.007 · Cited by 837 · see citing works

Glycosylation as a strategy to improve antibody-based therapeutics

Jefferis, R. (2009) · Nature Reviews Drug Discovery · doi:10.1038/nrd2804 · Cited by 829 · see citing works

Histone Methyltransferases Direct Different Degrees of Methylation to Define Distinct Chromatin Domains

Rice, J. C., Briggs, S. D., Ueberheide, B. M., Barber, C. M., Shabanowitz, J., Hunt, D. F., Shinkai, Y., & Allis, C. D. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00479-9 · Cited by 828 · see citing works

Proteogenomic Characterization Reveals Therapeutic Vulnerabilities in Lung Adenocarcinoma

Gillette, M. A., Satpathy, S., Cao, S., Dhanasekaran, S. M., Vasaikar, S. V., Krug, K., Petralia, F., Li, Y., Liang, W.-W., Reva, B., et al. (2020) · Cell · doi:10.1016/j.cell.2020.06.013 · Cited by 820 · see citing works

Proteogenomic Analysis of Human Colon Cancer Reveals New Therapeutic Opportunities

Vasaikar, S., Huang, C., Wang, X., Petyuk, V. A., Savage, S. R., Wen, B., Dou, Y., Zhang, Y., Shi, Z., Arshad, O. A., et al. (2019) · Cell · doi:10.1016/j.cell.2019.03.030 · Cited by 799 · see citing works

The world of protein acetylation

Drazic, A., Myklebust, L. M., Ree, R., & Arnesen, T. (2016) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2016.06.007 · Cited by 798 · see citing works

Stat3 Dimerization Regulated by Reversible Acetylation of a Single Lysine Residue

Yuan, Z.-L., Guan, Y.-J., Chatterjee, D., & Chin, Y. E. (2005) · Science · doi:10.1126/science.1105166 · Cited by 790 · see citing works

Post-translational modifications in proteins: resources, tools and prediction methods

Ramazi, S., & Zahiri, J. (2021) · Database · doi:10.1093/database/baab012 · Cited by 787 · see citing works

The SET-domain protein superfamily: protein lysine methyltransferases.

Dillon, S. C., Zhang, X. Y., Trievel, R. C., & Cheng, X. (2005) · Genome biology · doi:10.1186/gb-2005-6-8-227 · Cited by 784 · see citing works

Tyrosine Phosphorylation Inhibits PKM2 to Promote the Warburg Effect and Tumor Growth

Hitosugi, T., Kang, S., Vander Heiden, M. G., Chung, T.-W., Elf, S., Lythgoe, K., Dong, S., Lonial, S., Wang, X., Chen, G. Z., et al. (2009) · Science Signaling · doi:10.1126/scisignal.2000431 · Cited by 784 · see citing works

O-GlcNAcylation regulates phosphorylation of tau: A mechanism involved in Alzheimer's disease

Liu, F., Iqbal, K., Grundke-Iqbal, I., Hart, G. W., & Gong, C.-X. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400348101 · Cited by 775 · see citing works

Sumo, ubiquitin's mysterious cousin

Müller, S. P., Hoege, C., Pyrowolakis, G., & Jentsch, S. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35056591 · Cited by 765 · see citing works

Lysine propionylation and butyrylation are novel post-translational modifications in histones

Chen, Y., Sprung, R., Tang, Y., Ball, H., Sangras, B., Kim, S. C., Falck, J. R., Peng, J., Gu, W., & Zhao, Y. (2007) · Molecular &amp; Cellular Proteomics · doi:10.1074/mcp.m700021-mcp200 · Cited by 764 · see citing works

Role of Glycosylation in Development

Haltiwanger, R. S., & Lowe, J. B. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.074043 · Cited by 757 · see citing works

Ubiquitin-Binding Proteins: Decoders of Ubiquitin-Mediated Cellular Functions

Husnjak, K., & Đikić, I. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-051810-094654 · Cited by 755 · see citing works

The first identification of lysine malonylation substrates and its regulatory enzyme

Peng, C., Lu, Z., Xie, Z., Cheng, Z., Chen, Y., Tan, M., Luo, H., Zhang, Y., He, W., Yang, K., et al. (2011) · Molecular &amp; Cellular Proteomics · doi:10.1074/mcp.m111.012658 · Cited by 751 · see citing works

JMJD6 Is a Histone Arginine Demethylase

Chang, B., Chen, Y., Zhao, Y., & Bruick, R. K. (2007) · Science · doi:10.1126/science.1145801 · Cited by 746 · see citing works

Metabolic Regulation of Gene Expression by Histone Lysine β-Hydroxybutyrylation

Xie, Z., Zhang, D., Chung, D., Tang, Z., Huang, H., Dai, L., Qi, S., Li, J., Colak, G., Chen, Y., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.03.036 · Cited by 744 · see citing works

SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells

Hamamoto, R., Furukawa, Y., Morita, M., Iimura, Y., Pittella-Silva, F., Li, M., Yagyu, R., & Nakamura, Y. (2004) · Nature Cell Biology · doi:10.1038/ncb1151 · Cited by 738 · see citing works

Activation of STING requires palmitoylation at the Golgi

Mukai, K., Konno, H., Akiba, T., Uemura, T., Waguri, S., Kobayashi, T., Barber, G. N., Arai, H., & Taguchi, T. (2016) · Nature Communications · doi:10.1038/ncomms11932 · Cited by 733 · see citing works

How to diagnose rheumatoid arthritis early: A prediction model for persistent (erosive) arthritis

VISSER, H. K. A., le Cessie, S., Vos, K., Breedveld, F. C., & Hazes, J. M. W. (2002) · Arthritis & Rheumatism · doi:10.1002/art.10117 · Cited by 730 · see citing works

Integrated Proteogenomic Characterization of Clear Cell Renal Cell Carcinoma

Clark, D. J., Dhanasekaran, S. M., Petralia, F., Pan, J., Song, X., Hu, Y., da Veiga Leprevost, F., Reva, B., Lih, T.-S. M., Chang, H.-Y., et al. (2019) · Cell · doi:10.1016/j.cell.2019.10.007 · Cited by 730 · see citing works

Lactate as a fulcrum of metabolism

Brooks, G. A. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101454 · Cited by 724 · see citing works

SIRT5 Regulates the Mitochondrial Lysine Succinylome and Metabolic Networks

Rardin, M. J., He, W., Nishida, Y., Newman, J. C., Carrico, C., Danielson, S. R., Guo, A., Gut, P., Sahu, A. K., Li, B., et al. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.11.013 · Cited by 711 · see citing works

Protein carbamylation links inflammation, smoking, uremia and atherogenesis

Wang, Z., Nicholls, S. J., Rodríguez, E. R., Kummu, O., Hörkkö, S., Barnard, J., Reynolds, W. F., Topol, E. J., DiDonato, J. A., & Hazen, S. L. (2007) · Nature Medicine · doi:10.1038/nm1637 · Cited by 706 · see citing works

Structural insights into the catalysis and regulation of E3 ubiquitin ligases

Buetow, L., & Huang, D. T. C. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.91 · Cited by 688 · see citing works

The prolyl isomerase PIN1: a pivotal new twist in phosphorylation signalling and disease

Lu, K. P., & Zhou, X. Z. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2261 · Cited by 682 · see citing works

Metabolites as regulators of insulin sensitivity and metabolism

Yang, Q., Vijayakumar, A., & Kahn, B. B. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0044-8 · Cited by 681 · see citing works

Histone acetylation: molecular mnemonics on the chromatin

Gräff, J., & Tsai, L.-H. (2013) · Nature Reviews Neuroscience · doi:10.1038/nrn3427 · Cited by 680 · see citing works

Cyclic Dinucleotides Trigger ULK1 (ATG1) Phosphorylation of STING to Prevent Sustained Innate Immune Signaling

Konno, H., Konno, K., & Barber, G. N. (2013) · Cell · doi:10.1016/j.cell.2013.09.049 · Cited by 676 · see citing works

Proteogenomic and metabolomic characterization of human glioblastoma

Wang, L.-B., Karpova, A., Gritsenko, M. A., Kyle, J. E., Cao, S., Li, Y., Rykunov, D., Colaprico, A., Rothstein, J. H., Hong, R., et al. (2021) · Cancer Cell · doi:10.1016/j.ccell.2021.01.006 · Cited by 661 · see citing works

Intracellular Crotonyl-CoA Stimulates Transcription through p300-Catalyzed Histone Crotonylation

Sabari, B. R., Tang, Z., Huang, H., Yong-Gonzalez, V., Molina, H., Kong, H. E., Dai, L., Shimada, M., Cross, J. R., Zhao, Y., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.02.029 · Cited by 659 · see citing works

The regulation, functions and clinical relevance of arginine methylation

Guccione, E., & Richard, S. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0155-x · Cited by 642 · see citing works

USP10 Regulates p53 Localization and Stability by Deubiquitinating p53

Yuan, J., Luo, K., Zhang, L., Cheville, J. C., & Lou, Z. (2010) · Cell · doi:10.1016/j.cell.2009.12.032 · Cited by 637 · see citing works

Post-Translational Modification Control of Innate Immunity

Liu, J., Qian, C., & Cao, X. (2016) · Immunity · doi:10.1016/j.immuni.2016.06.020 · Cited by 632 · see citing works

Acalabrutinib with or without obinutuzumab versus chlorambucil and obinutuzumab for treatment-naive chronic lymphocytic leukaemia (ELEVATE-TN): a randomised, controlled, phase 3 trial

Sharman, J. P., Egyed, M., Jurczak, W. J., Skarbnik, A. P. Z., Pagel, J. M., Flinn, I. W., Kamdar, M. K., Munir, T., Walewska, R. J., Corbett, G., et al. (2020) · The Lancet · doi:10.1016/s0140-6736(20)30262-2 · Cited by 632 · see citing works

Increased dosage of mammalian Sir2 in pancreatic β cells enhances glucose-stimulated insulin secretion in mice

Moynihan, K. A., Grimm, A. A., Plueger, M. M., Bernal‐Mizrachi, E., Ford, E. L., CRAS-MÉNEUR, C. M. H., Permutt, M. A., & Imai, S. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.07.001 · Cited by 630 · see citing works

Caloric Restriction Mimetics against Age-Associated Disease: Targets, Mechanisms, and Therapeutic Potential

Madeo, F., Carmona-Gutierrez, D., Hofer, S. J., & Kroemer, G. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.01.018 · Cited by 630 · see citing works

CREBBP mutations in relapsed acute lymphoblastic leukaemia

Mullighan, C. G., Zhang, J., Kasper, L. H., Lerach, S., Payne-Turner, D., Phillips, L. A., Heatley, S. L., Holmfeldt, L., Collins-Underwood, J. R., Ma, J., et al. (2011) · Nature · doi:10.1038/nature09727 · Cited by 628 · see citing works

Protein neddylation: beyond cullin–RING ligases

Enchev, R. I., Schulman, B. A., & Peter, M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3919 · Cited by 622 · see citing works

Tau fragmentation, aggregation and clearance: the dual role of lysosomal processing

Wang, Y., Martinez-Vicente, M., Krüger, U., Kaushik, S., Wong, E., Mandelkow, E.-M., Cuervo, A. M., & Mandelkow, E. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp367 · Cited by 617 · see citing works

Causes and Consequences of Increased Glucose Metabolism of Cancers

Gillies, R. J., Robey, I., & Gatenby, R. A. (2008) · Journal of Nuclear Medicine · doi:10.2967/jnumed.107.047258 · Cited by 617 · see citing works

Integrative Proteomic Characterization of Human Lung Adenocarcinoma

Xu, J., Zhang, C., Wang, X., Zhai, L., Ma, Y., Mao, Y., Qian, K., Sun, C., Liu, Z., Jiang, S., et al. (2020) · Cell · doi:10.1016/j.cell.2020.05.043 · Cited by 612 · see citing works

Plasma phosphorylated tau 217 and phosphorylated tau 181 as biomarkers in Alzheimer's disease and frontotemporal lobar degeneration: a retrospective diagnostic performance study

Thijssen, E. H., La Joie, R., Strom, A., Fonseca, C., Iaccarino, L., Wolf, A., Spina, S., Allen, I. E., Cobigo, Y., Heuer, H., et al. (2021) · The Lancet Neurology · doi:10.1016/s1474-4422(21)00214-3 · Cited by 607 · see citing works

Acetylation Targets the M2 Isoform of Pyruvate Kinase for Degradation through Chaperone-Mediated Autophagy and Promotes Tumor Growth

Lv, L., Dong, L., Zhao, D., Lin, R., Chu, Y., Zhang, H., Zha, Z., Liu, Y., Li, Z., Xu, Y., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.04.025 · Cited by 605 · see citing works

Autoantibodies recognizing carbamylated proteins are present in sera of patients with rheumatoid arthritis and predict joint damage

Shi, J., Knevel, R., Suwannalai, P., van der Linden, M. P. M., Janssen, G. M. C., van Veelen, P. A., Levarht, N. E. W., Mil, A. H. M. V. D. H., Cerami, A., Huizinga, T. W. J., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1114465108 · Cited by 595 · see citing works

Virus glycosylation: role in virulence and immune interactions

Vigerust, D. J., & Shepherd, V. L. (2007) · Trends in Microbiology · doi:10.1016/j.tim.2007.03.003 · Cited by 593 · see citing works

Neratinib after trastuzumab-based adjuvant therapy in HER2-positive breast cancer (ExteNET): 5-year analysis of a randomised, double-blind, placebo-controlled, phase 3 trial

Martín, M., Holmes, F. A., Ejlertsen, B., Delaloge, S., Moy, B., Iwata, H., von Minckwitz, G., Chia, S., Mansi, J., Barrios, C. H., et al. (2017) · The Lancet Oncology · doi:10.1016/s1470-2045(17)30717-9 · Cited by 587 · see citing works

Targeted protein degradation: elements of PROTAC design

Paiva, S.-L., & Crews, C. M. (2019) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2019.02.022 · Cited by 586 · see citing works

E2 enzymes: more than just middle men

Stewart, M. D., Ritterhoff, T., Klevit, R. E., & Brzović, P. S. (2016) · Cell Research · doi:10.1038/cr.2016.35 · Cited by 585 · see citing works

Proteogenomic characterization of pancreatic ductal adenocarcinoma

Cao, L., Huang, C., Cui Zhou, D., Hu, Y., Lih, T. M., Savage, S. R., Krug, K., Clark, D. J., Schnaubelt, M., Chen, L., et al. (2021) · Cell · doi:10.1016/j.cell.2021.08.023 · Cited by 578 · see citing works

H3K79 methylation profiles define murine and human MLL-AF4 leukemias

Krivtsov, A., Feng, Z.-H., Lemieux, M., Faber, J., Vempati, S., Sinha, A., Xia, X.-B., Jesneck, J., Bracken, A., Silverman, L., et al. (2008) · Cancer Cell · doi:10.1016/j.ccr.2008.10.001 · Cited by 573 · see citing works

Stem cell metabolism in tissue development and aging

Shyh‐Chang, N., Daley, G. Q., & Cantley, L. C. (2013) · Development · doi:10.1242/dev.091777 · Cited by 573 · see citing works

Inhibiting PD-L1 palmitoylation enhances T-cell immune responses against tumours

Yao, H., Lan, J., Li, C., Shi, H., Brosseau, J., Wang, H., Lu, H., Fang, C., Zhang, Y., Liang, L., et al. (2019) · Nature Biomedical Engineering · doi:10.1038/s41551-019-0375-6 · Cited by 572 · see citing works

Tumour suppressor SIRT3 deacetylates and activates manganese superoxide dismutase to scavenge ROS

Chen, Y., Zhang, J., Lin, Y., Lei, Q., Guan, K., Zhao, S., & Xiong, Y. (2011) · The EMBO Reports · doi:10.1038/embor.2011.65 · Cited by 572 · see citing works

KAT2A coupled with the α-KGDH complex acts as a histone H3 succinyltransferase

Wang, Y., Guo, Y. R., Liu, K., Yin, Z., Liu, R., Xia, Y., Tan, L., Yang, P., Lee, J.-H., Li, X.-J., et al. (2017) · Nature · doi:10.1038/nature25003 · Cited by 567 · see citing works

Ubiquitin-like protein conjugation and the ubiquitin–proteasome system as drug targets

Bedford, L., Lowe, J., Dick, L. R., Mayer, R. J., & Brownell, J. E. (2011) · Nature Reviews Drug Discovery · doi:10.1038/nrd3321 · Cited by 563 · see citing works

Frameshift Mutants of β Amyloid Precursor Protein and Ubiquitin-B in Alzheimer's and Down Patients

van Leeuwen, F. W., de Kleijn, D. P. V., van den Hurk, H., Neubauer, A., Sonnemans, M. A. F., Sluijs, J. A., Köycü, S., Ramdjielal, R. D. J., Salehi, A., Martens, G. J. M., et al. (1998) · Science · doi:10.1126/science.279.5348.242 · Cited by 561 · see citing works

Regulating the regulator: post-translational modification of RAS

Ahearn, I. M., Haigis, K. M., Bar‐Sagi, D., & Philips, M. R. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3255 · Cited by 560 · see citing works

Reversing the Inactivation of Peroxiredoxins Caused by Cysteine Sulfinic Acid Formation

Woo, H. A., Chae, H. Z., Hwang, S. C., Yang, K., Kang, S. W., Kim, K., & Rhee, S. G. (2003) · Science · doi:10.1126/science.1080273 · Cited by 558 · see citing works

Ubiquitin chain diversity at a glance

Akutsu, M., Đikić, I., & Bremm, A. (2016) · Journal of Cell Science · doi:10.1242/jcs.183954 · Cited by 555 · see citing works

Protein Phosphorylation: A Major Switch Mechanism for Metabolic Regulation

Humphrey, S. J., James, D. E., & Mann, M. (2015) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2015.09.013 · Cited by 554 · see citing works

Proteogenomic Landscape of Breast Cancer Tumorigenesis and Targeted Therapy

Krug, K., Jaehnig, E. J., Satpathy, S., Blumenberg, L. M., Karpova, A. Y., Anurag, M., Miles, G., Mertins, P., Geffen, Y., Tang, L. C., et al. (2020) · Cell · doi:10.1016/j.cell.2020.10.036 · Cited by 532 · see citing works

Post-translational modifications of intermediate filament proteins: mechanisms and functions

Snider, N. T., & Omary, M. B. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3753 · Cited by 528 · see citing works

Signal-dependent activation of the MEF2 transcription factor by dissociation from histone deacetylases

Lu, J., McKinsey, T. A., Nicol, R. L., & Olson, E. N. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.080064097 · Cited by 518 · see citing works

Roles of F-box proteins in cancer

Wang, Z. P., Liu, P., Inuzuka, H., & Wei, W. (2014) · Nature reviews. Cancer · doi:10.1038/nrc3700 · Cited by 516 · see citing works

Ibrutinib and Venetoclax for First-Line Treatment of CLL

Jain, N., Keating, M. J., Thompson, P. A., Ferrajoli, A., Burger, J. A., Borthakur, G. M., Takahashi, K., Estrov, Z. E., Fowler, N. H., Kadia, T. M., et al. (2019) · New England Journal of Medicine · doi:10.1056/nejmoa1900574 · Cited by 512 · see citing works

Global Impairment of the Ubiquitin-Proteasome System by Nuclear or Cytoplasmic Protein Aggregates Precedes Inclusion Body Formation

Bennett, E. J., Bence, N., Rajadas, J., & Kopito, R. R. (2005) · Molecular Cell · doi:10.1016/j.molcel.2004.12.021 · Cited by 509 · see citing works

Anti-angiogenic tyrosine kinase inhibitors: what is their mechanism of action?

Gotink, K. J., & Verheul, H. M. W. (2009) · Angiogenesis · doi:10.1007/s10456-009-9160-6 · Cited by 506 · see citing works

Citrullination: A posttranslational modification in health and disease

György, B., Tóth, E., Tarcsa, E., Falus, A., & Buzás, E. I. (2006) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2006.03.008 · Cited by 503 · see citing works

Protein Lipidation: Occurrence, Mechanisms, Biological Functions, and Enabling Technologies

Jiang, H., Zhang, X., Chen, X., Aramsangtienchai, P., Tong, Z., & Lin, H. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00750 · Cited by 501 · see citing works

Targeting Proteins for Destruction by the Ubiquitin System: Implications for Human Pathobiology

Schwartz, A. L., & Ciechanover, A. J. (2008) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.051208.165340 · Cited by 491 · see citing works

Uncovering global SUMOylation signaling networks in a site-specific manner

Hendriks, I. A., D’Souza, R. C. J., Yang, B., Vries, M. V., Mann, M., & Vertegaal, A. C. O. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2890 · Cited by 488 · see citing works

The repertoire of glycan determinants in the human glycome

Cummings, R. D. (2009) · Molecular BioSystems · doi:10.1039/b907931a · Cited by 487 · see citing works

Exploitation of glycosylation in enveloped virus pathobiology

Watanabe, Y., Bowden, T. A., Wilson, I. A., & Crispin, M. (2019) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2019.05.012 · Cited by 485 · see citing works

SIRT5 regulates both cytosolic and mitochondrial protein malonylation with glycolysis as a major target

Nishida, Y., Rardin, M. J., Carrico, C., He, W., Sahu, A. K., Gut, P., Najjar, R., Fitch, M., Hellerstein, M., Gibson, B. W., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.05.022 · Cited by 481 · see citing works

Non-histone protein methylation as a regulator of cellular signalling and function

Biggar, K. K., & Li, S. S.-C. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3915 · Cited by 479 · see citing works

Targeting Alterations in the RAF–MEK Pathway

Yaeger, R. D., & Corcoran, R. B. (2019) · Cancer Discovery · doi:10.1158/2159-8290.cd-18-1321 · Cited by 474 · see citing works

The tumour glyco-code as a novel immune checkpoint for immunotherapy

RodrÍguez, E., Schetters, S. T. T., & van Kooyk, Y. (2018) · Nature Reviews Immunology · doi:10.1038/nri.2018.3 · Cited by 473 · see citing works

The ageing epigenome and its rejuvenation

Zhang, W., Qu, J. T., Liu, G., & Belmonte, J. C. I. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0204-5 · Cited by 472 · see citing works

Autoimmunity to specific citrullinated proteins gives the first clues to the etiology of rheumatoid arthritis

Wegner, N., Lundberg, K., Kinloch, A., Fisher, B. A., Malmström, V., Feldmann, M., & Venables, P. J. (2009) · Immunological Reviews · doi:10.1111/j.0105-2896.2009.00850.x · Cited by 470 · see citing works

SUMOylation and De-SUMOylation: Wrestling with Life's Processes

Yeh, E. T. H. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800050200 · Cited by 469 · see citing works

Targeting epigenetic and posttranslational modifications regulating ferroptosis for the treatment of diseases

Wang, Y., Hu, J., Wu, S., Fleishman, J. S., Li, Y., Xu, Y.-S., Zou, W., Wang, J., Feng, Y., Chen, J., et al. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01720-0 · Cited by 218 · see citing works

Real-time detection of 20 amino acids and discrimination of pathologically relevant peptides with functionalized nanopore

Zhang, M., Tang, C., Wang, Z., Chen, S., Zhang, D., Li, K., Sun, K., Zhao, C., Wang, Y., Xu, M., et al. (2024) · Nature Methods · doi:10.1038/s41592-024-02208-7 · Cited by 140 · see citing works

Altered glycosylation in cancer: molecular functions and therapeutic potential

Xu, X., Peng, Q., Jiang, X., Tan, S., Yang, W., Han, Y., Oyang, L., Lin, J., Shen, M., Wang, J., et al. (2024) · 癌症：英文版 · doi:10.1002/cac2.12610 · Cited by 131 · see citing works

From Omics to Multi-Omics: A Review of Advantages and Tradeoffs

Hayes, C. N., Nakahara, H., Ono, A., Tsuge, M., & Oka, S. (2024) · Genes · doi:10.3390/genes15121551 · Cited by 119 · see citing works

Biochemistry and regulation of histone lysine l-lactylation

Sheng, X., Lin, H.-N., Cole, P. A., & Zhao, Y. (2025) · Nature reviews. Molecular cell biology · doi:10.1038/s41580-025-00876-7 · Cited by 105 · see citing works

The logic of protein post‐translational modifications (PTMs): Chemistry, mechanisms and evolution of protein regulation through covalent attachments

Suskiewicz, M. (2024) · Bioessays · doi:10.1002/bies.202300178 · Cited by 84 · see citing works

Calcium (Ca2+) signaling in plants: A plant stress perspective

Naz, M., Afzal, M. R., Raza, M. A., Pandey, S., Qi, S., Dai, Z., & Du, D. (2024) · South African Journal of Botany · doi:10.1016/j.sajb.2024.04.047 · Cited by 73 · see citing works

PTM-Mamba: a PTM-aware protein language model with bidirectional gated Mamba blocks

Peng, F. Z., Wang, C.-T., Chen, T., Schussheim, B., Vincoff, S., & Chatterjee, P. (2025) · Nature Methods · doi:10.1038/s41592-025-02656-9 · Cited by 32 · see citing works

Endoplasmic reticulum stress as a driver and therapeutic target for kidney disease

Byun, J. H., Lebeau, P. F., Trink, J., Uppal, N., Lanktree, M. B., Krepinsky, J. C., & Austin, R. C. (2025) · Nature Reviews Nephrology · doi:10.1038/s41581-025-00938-1 · Cited by 67 · see citing works

O‐GlcNAcylation: cellular physiology and therapeutic target for human diseases

Ye, L., Ding, W., Xiao, D., Jia, Y., Zhao, Z., Ao, X., & Wang, J. (2023) · MedComm · doi:10.1002/mco2.456 · Cited by 51 · see citing works

Irinotecan alleviates chemoresistance to anthracyclines through the inhibition of AARS1-mediated BLM lactylation and homologous recombination repair

Li, X., Zhang, C., Mei, Y., Zhong, W., Fan, W. Q., Liu, L., Feng, Z., Bai, X., Liu, C., Xiao, M., et al. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02302-y · Cited by 46 · see citing works

Current Technologies Unraveling the Significance of Post-Translational Modifications (PTMs) as Crucial Players in Neurodegeneration

Zafar, S., Fatima, S. I., Schmitz, M., & Zerr, I. (2024) · Biomolecules · doi:10.3390/biom14010118 · Cited by 42 · see citing works

Age-, sex- and proximal–distal-resolved multi-omics identifies regulators of intestinal aging in non-human primates

Wang, X., Luo, Y., He, S., Lu, Y., Gong, Y., Gao, L. P., Mao, S., Liu, X., Jiang, N., Pu, Q., et al. (2024) · Nature Aging · doi:10.1038/s43587-024-00572-9 · Cited by 42 · see citing works

Post-translational modifications of cancer immune checkpoints: mechanisms and therapeutic strategies

Jia, H., Jiang, L., Shen, X., Ye, H., Li, X., Zhang, L., Hu, Y., Song, D., Jia, H., & Wang, Z. (2025) · Molecular Cancer · doi:10.1186/s12943-025-02397-5 · Cited by 48 · see citing works

Acetylation in pathogenesis: Revealing emerging mechanisms and therapeutic prospects

Jiang, N., Li, W., Jiang, S., Xie, M., & Liu, R. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115519 · Cited by 38 · see citing works

Post-translational acylation of proteins in cardiac hypertrophy

Liu, Y., Yang, Q., & He, G. (2025) · Nature Reviews Cardiology · doi:10.1038/s41569-025-01150-1 · Cited by 38 · see citing works

Molecular Mediators of Metabolic Reprogramming in Cancer: Mechanisms, Regulatory Networks, and Therapeutic Strategies

Ahuja, S., & Zaheer, S. (2025) · Immunology · doi:10.1111/imm.70045 · Cited by 39 · see citing works

The Role of Autophagy as a Trigger of Post-Translational Modifications of Proteins and Extracellular Vesicles in the Pathogenesis of Rheumatoid Arthritis

Riitano, G., Recalchi, S., Capozzi, A., Manganelli, V., Misasi, R., Garofalo, T., Sorice, M., & Longo, A. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241612764 · Cited by 29 · see citing works

Regulation of HNRNP family by post-translational modifications in cancer

Li, B., Wen, M., Gao, F., Wang, Y., Wei, G., & Duan, Y. (2024) · Cell Death Discovery · doi:10.1038/s41420-024-02198-7 · Cited by 28 · see citing works

Oxidative Cysteine Post Translational Modifications Drive the Redox Code Underlying Neurodegeneration and Amyotrophic Lateral Sclerosis

Percio, A., Cicchinelli, M., Masci, D., Summo, M., Urbani, A., & Greco, V. (2024) · Antioxidants · doi:10.3390/antiox13080883 · Cited by 24 · see citing works

Palmitoylation regulates myelination by modulating the ZDHHC3-Cadm4 axis in the central nervous system

Chang, Y., Zhu, J., Li, X., Deng, Y., Lai, B., Ma, Y., Tong, J., Liu, H., Li, J., Yang, C., et al. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01971-5 · Cited by 24 · see citing works

Protein Oxidative Modifications in Neurodegenerative Diseases: From Advances in Detection and Modelling to Their Use as Disease Biomarkers

Anjo, S. I., He, Z., Hussain, Z., Farooq, A., McIntyre, A., Laughton, C. A., Carvalho, A. N., & Finelli, M. J. (2024) · Antioxidants · doi:10.3390/antiox13060681 · Cited by 23 · see citing works

A Versatile Method for Site-Specific Chemical Installation of Aromatic Posttranslational Modification Analogs into Proteins

Lin, X., Mandal, S., Nithun, R. V., Rajasekhar, K., Bouri, B., Lashuel, H. A., & Jbara, M. (2024) · Journal of the American Chemical Society · doi:10.1021/jacs.4c08416 · Cited by 22 · see citing works

Structural and Functional Insights into Dishevelled-Mediated Wnt Signaling

Wang, L., Zhu, R., Wen, Z., Fan, H., Norwood-Jackson, T., Jathan, D., & Lee, H. (2024) · Cells · doi:10.3390/cells13221870 · Cited by 23 · see citing works

Clinical glycoproteomics: methods and diseases

Wang, Y., Lei, K., Zhao, L., & Zhang, Y. (2024) · MedComm · doi:10.1002/mco2.760 · Cited by 21 · see citing works

Arginine methyltransferase PRMT1 promotes ferroptosis through EGR1/GLS2 axis in sepsis-related acute lung injury

Li, M., Hu, L., Ke, Q., Zhao, L., Ruan, C., Lu, H., & Liu, X. (2025) · Communications Biology · doi:10.1038/s42003-025-07531-z · Cited by 21 · see citing works

Leveraging AI to explore structural contexts of post-translational modifications in drug binding

Medvedev, K. E., Schaeffer, R. D., & Grishin, N. V. (2025) · Journal of Cheminformatics · doi:10.1186/s13321-025-01019-y · Cited by 21 · see citing works

Protein modification in neurodegenerative diseases

Ramazi, S., Dadzadi, M., Darvazi, M., Seddigh, N., & Allahverdi, A. (2024) · MedComm · doi:10.1002/mco2.674 · Cited by 24 · see citing works

Low-input redoxomics facilitates global identification of metabolic regulators of oxidative stress in the gut

Xiao, X., Hu, M., Gao, L. P., Yuan, H., Chong, B., Liu, Y., Zhang, R., Gong, Y., Du, D., Zhang, Y., et al. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02094-7 · Cited by 20 · see citing works

Pan-cancer analysis of CTNNB1 with potential as a therapeutic target for human tumorigenesis

AmeliMojarad, M., AmeliMojarad, M., Cui, X., & Shariati, P. (2023) · Informatics in Medicine Unlocked · doi:10.1016/j.imu.2023.101331 · 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 19 · see citing works

The mechanism of AKT activation in cancer

Meng, F., Li, H., Wang, Y., Zheng, Z., & Chen, Y. (2025) · Cell investigation. · doi:10.1016/j.clnves.2025.100046 · Cited by 19 · see citing works

Unlocking the secrets of the immunopeptidome: MHC molecules, ncRNA peptides, and vesicles in immune response

Balakrishnan, A., Winiarek, G., Hołówka, O., Godlewski, J. A., & Bronisz, A. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1540431 · Cited by 19 · see citing works

scMINER: a mutual information-based framework for clustering and hidden driver inference from single-cell transcriptomics data

Pan, Q., Ding, L., Hladyshau, S., Yao, X., Zhou, J., Yan, L., Dhungana, Y., Shi, H., Qian, C., Dong, X., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-59620-6 · Cited by 18 · see citing works

USP36 promotes tumorigenesis and tamoxifen resistance in breast cancer by deubiquitinating and stabilizing ERα

Zhuang, T., Zhang, S., Liu, D., Li, Z., Li, X., Li, J., Yang, P., Zhang, C., Cui, J., Fu, M., et al. (2024) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-024-03160-2 · Cited by 17 · see citing works

Subcellular Proteomic Mapping of Lysine Lactylation

Bao, Q., Wan, N., He, Z., Cao, J., Yuan, W., Hao, H., & Ye, H. (2024) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.4c00366 · Cited by 19 · see citing works

Recapitulating the potential contribution of protein S-palmitoylation in cancer

Chaturvedi, S., & Sonawane, A. (2024) · Cancer and Metastasis Reviews · doi:10.1007/s10555-024-10217-3 · Cited by 17 · see citing works

Rethinking Parkinson's: The role of proteostasis networks and autophagy in disease progression

Sharma, A., Mannan, A., & Singh, T. G. (2025) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2025.104023 · Cited by 17 · see citing works

Computation strategies and clinical applications in neoantigen discovery towards precision cancer immunotherapy

Wang, Z., Gu, Y., Sun, X., & Huang, H. (2025) · Biomarker Research · doi:10.1186/s40364-025-00808-9 · Cited by 17 · see citing works

PTMs as molecular encoders: reprogramming chaperones into epichaperomes for network control in disease

Chu, F., Sharma, S., Ginsberg, S. D., & Chiosis, G. (2025) · TIBS -Trends in Biochemical Sciences. Regular ed · doi:10.1016/j.tibs.2025.07.006 · Cited by 21 · see citing works

Chemical Proteomic Profiling of Protein Dopaminylation in Colorectal Cancer Cells

Zhang, N., Gao, S., Peng, H., Wu, J., Li, H., Gibson, C., Wu, S., Zhu, J., & Zheng, Q. (2024) · Journal of Proteome Research · doi:10.1021/acs.jproteome.4c00379 · Cited by 17 · see citing works

Dual role of exosomal circCMTM3 derived from GSCs in impeding degradation and promoting phosphorylation of STAT5A to facilitate vasculogenic mimicry formation in glioblastoma

Wang, C., Liu, Y., Zuo, Z., Cui, D., Xu, Y., Li, L., & Jiang, Y. (2024) · Theranostics · doi:10.7150/thno.97057 · Cited by 17 · see citing works

The role of oxidative post-translational modifications in type 1 diabetes pathogenesis

Alhamar, G., Vinci, C., Franzese, V., Tramontana, F., Goux, N. L., Ludvigsson, J., Nissim, A., & Strollo, R. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1537405 · Cited by 16 · see citing works

Obesity and type 2 diabetes mellitus: insights from skeletal muscle extracellular matrix remodeling

Wu, L., & Coletta, D. K. (2025) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00154.2024 · Cited by 17 · see citing works

Key Considerations on CITE‐Seq for Single‐Cell Multiomics

Song, H.-W., Martin, J., Shi, X., & Tyznik, A. J. (2025) · PROTEOMICS · doi:10.1002/pmic.202400011 · Cited by 18 · see citing works

Exploring the landscape of post-translational modification in drug discovery

Cao, Y., Yu, T., Zhu, Z., Zhang, Y., Sun, S., Li, N., Gu, C., & Yang, Y. (2024) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2024.108749 · Cited by 15 · see citing works

Roles of Post-Translational Modifications of Transcription Factors Involved in Breast Cancer Hypoxia

Seymour, L., Nuru, N., Johnson, K. R., Villalpando-Gutierrez, J. M., Njoku, V. T., Darie, C. C., & Neagu, A.-N. (2025) · Molecules · doi:10.3390/molecules30030645 · Cited by 15 · see citing works

An outlier approach: advancing diagnosis of neurological diseases through integrating proteomics into multi-omics guided exome reanalysis

Chui, M. M. C., Kwong, A. K., Leung, H. Y. C., Pang, C., Scheller, I. F., Wong, S. S.-N., Fung, C., Yépez, V. A., Gagneur, J., Mak, C. C. Y., et al. (2025) · npj Genomic Medicine · doi:10.1038/s41525-025-00493-5 · Cited by 15 · see citing works

Paricalcitol attenuates oxidative stress and inflammatory response in the liver of NAFLD rats by regulating FOXO3a and NFκB acetylation

Malladi, N., Lahamge, D., Somwanshi, B. S., Tiwari, V., Deshmukh, K., Balani, J. K., Chakraborty, S., Alam, J., & Banerjee, S. K. (2024) · Cellular Signalling · doi:10.1016/j.cellsig.2024.111299 · Cited by 15 · see citing works

Insights on post-translational modifications in fatty liver and fibrosis progression

Raju, C. N., & Sankaranarayanan, K. (2025) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2025.167659 · Cited by 15 · see citing works

Integrative Omics Uncovers Low Tumorous Magnesium Content as A Driver Factor of Colorectal Cancer

Zhang, R., Hu, M., Liu, Y., Li, W., Xu, Z., He, S., Lu, Y., Gong, Y., Wang, X., Hai, S., et al. (2024) · Genomics Proteomics & Bioinformatics · doi:10.1093/gpbjnl/qzae053 · Cited by 14 · see citing works

Binding of α-synuclein to ACO2 promotes progressive mitochondrial dysfunction in Parkinson's disease models

Jiao, J., Gao, G., Zhu, J., Wang, C., Liu, L., & Yang, H. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103399 · Cited by 14 · see citing works

Potential of lactylation as a therapeutic target in cancer treatment (Review)

Zhu, Z., Zheng, X., Zhao, P., Chen, C., Xu, G., & Ke, X. (2025) · Molecular Medicine Reports · doi:10.3892/mmr.2025.13456 · Cited by 14 · see citing works

Nanobody-thioesterase chimeras to specifically target protein palmitoylation

Kuo, C.-W. S., Gök, Ç., Fulton, H., Dickson-Murray, E., Adu, S., Gallen, E., Mary, S., Robertson, A. D., Jordan, F., Dunning, E., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-56716-x · Cited by 14 · see citing works

Acetylation profiling by Iseq-Kac reveals insights into HSC aging and lineage decision

Gong, Y., Zhan, H., Wei, N., Liu, M., Liu, Y., Guan, P., Xie, Y., Deng, Y., Pu, Q., Lou, X., et al. (2025) · Nature Chemical Biology · doi:10.1038/s41589-025-01916-1 · Cited by 13 · see citing works

Novel insights into lncRNAs as key regulators of post-translational modifications in cancer: mechanisms and therapeutic potential

Han, Y., Li, S., Oyang, L., Cui, S., Zhang, W., Yang, W., Peng, M., Tan, S., Xia, L., Lin, J., et al. (2025) · Cellular Oncology · doi:10.1007/s13402-025-01086-1 · Cited by 14 · see citing works

Translating Senotherapeutic Interventions into the Clinic with Emerging Proteomic Technologies

Dey, A. K., Banarjee, R., Boroumand, M., Rutherford, D. V., Strassheim, Q., Nyunt, T., Olinger, B., & Basisty, N. (2023) · Biology · doi:10.3390/biology12101301 · Cited by 12 · see citing works

Unraveling the Peroxidase Activity in Peroxiredoxins: A Comprehensive Review of Mechanisms, Functions, and Biological Significance

Qausain, S., & Basheeruddin, M. (2024) · Cureus · doi:10.7759/cureus.66117 · Cited by 13 · see citing works

Regulation of autophagy by protein lipidation

Shao, Y., Hu, J., Li, H., & Lu, K. (2024) · Advanced Biotechnology · doi:10.1007/s44307-024-00040-w · Cited by 13 · see citing works

Extracellular microvesicles from patients with Rheumatoid arthritis promote dendritic cell activation in vitro

Buttari, B., Recalchi, S., Riitano, G., Capozzi, A., Ucci, F. M., Manganelli, V., Fratini, F., Profumo, E., Garofalo, T., Alessandri, C., et al. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1532114 · Cited by 13 · see citing works

The role of novel protein acylations in cancer

Cao, D., Sun, W., Li, X., Jian, L., Zhou, X., Bode, A. M., & Luo, X. (2024) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2024.176841 · Cited by 14 · see citing works

Bio-Pathological Functions of Posttranslational Modifications of Histological Biomarkers in Breast Cancer

Neagu, A.-N., Josan, C.-L., Jayaweera, T. M., Morrissiey, H., Johnson, K. R., & Darie, C. C. (2024) · Molecules · doi:10.3390/molecules29174156 · Cited by 12 · see citing works

The Role of E3 Ubiquitin Ligase Gene FBK in Ubiquitination Modification of Protein and Its Potential Function in Plant Growth, Development, Secondary Metabolism, and Stress Response

Wu, Y., Zhang, Y., Ni, W., Li, Q., Zhou, M., & Li, Z. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26020821 · Cited by 12 · see citing works

Aging and diet alter the protein ubiquitylation landscape in the mouse brain

Marino, A., Fraia, D. D., Panfilova, D., Sahu, A. K., Minetti, A., Omrani, O., Cirri, E., & Ori, A. (2025) · Nature Communications · doi:10.1038/s41467-025-60542-6 · Cited by 17 · see citing works

A coarse-grained model for simulations of phosphorylated disordered proteins

Rauh, A. S., Hedemark, G. S., Tesei, G., & Lindorff‐Larsen, K. (2025) · Biophysical Journal · doi:10.1016/j.bpj.2025.07.001 · Cited by 12 · see citing works

Protein post-translational modifications in serine synthetic pathway: functions and molecular mechanisms

Shu, M., Liu, Y., & Wang, J. (2025) · Cell Communication and Signaling · doi:10.1186/s12964-025-02327-4 · Cited by 12 · see citing works

Threonine Phosphorylation and the Yin and Yang of STAT1: Phosphorylation-Dependent Spectrum of STAT1 Functionality in Inflammatory Contexts

Elbrashy, M. M., Metwally, H., Sakakibara, S., & Kishimoto, T. (2024) · Cells · doi:10.3390/cells13181531 · Cited by 11 · see citing works

Epigenetic regulation and post-translational modifications of ferroptosis-related factors in cardiovascular diseases

Jing, C., Wu, Y., Zhang, Y., Zhu, Z., Zhang, Y., Liu, Z., & Sun, D. (2025) · Clinical Epigenetics · doi:10.1186/s13148-024-01809-5 · Cited by 11 · see citing works

AXL Tyrosine Kinases: A Growing Isoform Family That Promotes Cancer Pathogenesis

Gjerstad, M. E., Aehnlich, P., Gélébart, P., & McCormack, E. (2025) · Cancer Research · doi:10.1158/0008-5472.can-24-3841 · Cited by 12 · see citing works

Exosomal miR-196a-5p Secreted by Bone Marrow Mesenchymal Stem Cells Inhibits Ferroptosis and Promotes Drug Resistance of Acute Myeloid Leukemia

Fan, B., Wang, L., Hu, T., Zheng, L., & Wang, J. (2025) · Antioxidants and Redox Signaling · doi:10.1089/ars.2024.0882 · Cited by 11 · see citing works

Theranostic Nanoparticles in Prostate Cancer: Disrupting Hypoxia‐Induced Glycolysis by Targeting Hypoxia‐Inducible Factor‐1 Alpha and Downstream Metabolites

Uti, D. E., Omang, W. A., Alum, E. U., Bawa, I., Ugwu, O. P.-C., Idowu, A. O., Atangwho, I. J., & Egbung, G. E. (2026) · Cancer Medicine · doi:10.1002/cam4.71519 · Cited by 10 · see citing works

Overview of the Zinc Functional Interactome Through Health Hallmarks and Medical Conditions

Pavić, M., Micek, V., Breljak, D., Vrhovac, I., Madunić, J., & Ljubojević, M. (2026) · Nutrients · doi:10.3390/nu18020336 · Cited by 10 · see citing works

Advances in the Understanding of Akt Signaling in Cancers and the Potential of Inhibiting Akt-Driven Tumors Using Small Molecule Inhibitors: An Overview

Aswathanarayan, J. B., Naaz, R., Doreswamy, S. H., Karnik, M., Kumar, S. M. N., Sreenivasan, A., Sharma, A. K., & Madhunapantula, S. V. (2026) · Cancers · doi:10.3390/cancers18040578 · Cited by 11 · see citing works

Pharmacologically inducing anoikis offers novel therapeutic opportunities in hepatocellular carcinoma

Wang, Y., Fleishman, J. S., Wang, J., Chen, J., Zhao, L., & Ding, M. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.116878 · Cited by 10 · see citing works

Site-Specific Histidine Aza-Michael Addition in Proteins Enabled by a Ferritin-Based Metalloenzyme

Tsou, J.-C., Tsou, C.-M., Wang, C.-H., Ko, A.-L. A., Wang, Y. H., Liang, H.-J., Sun, J., Huang, K.-F., Ko, T., Lin, S., et al. (2024) · Journal of the American Chemical Society · doi:10.1021/jacs.4c14446 · Cited by 10 · see citing works

Efficient purification of exosomes and subpopulations in fresh bovine milk via fine isolation of free-flow isoelectric focusing in large scale

Khan, M. I., Chen, K., Zhang, L., Saud, S., Zhang, Q., Xiao, H., Mu, Z., & Cao, C. (2025) · Chemical Engineering Journal · doi:10.1016/j.cej.2025.160850 · Cited by 10 · see citing works

Effects of obesity‐associated plasma markers on adipose stem cell function and epigenetic regulation

Bispo, A. F. S., Simão, J. D. J., Moraes, M., Abel, A. B. M., Plata, V. T. G., Telles, M. M., Santana, A. V., Volpe, P., Armelin‐Correa, L., & Alonso‐Vale, M. I. C. (2025) · Obesity · doi:10.1002/oby.24321 · Cited by 10 · see citing works

Posttranslational Regulation of Mammalian Sulfur Amino Acid Metabolism

Pajares, M. A. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26062488 · Cited by 9 · see citing works

Decoding Glycosylation in Neurodegenerative Diseases: Mechanistic Insights and Therapeutic Opportunities

Yu, H., Chen, X., Yang, Y., Gu, M., Ren, K., & Wei, Z. (2025) · The FASEB Journal · doi:10.1096/fj.202502809r · Cited by 9 · see citing works

Analysis of Structural Changes in the Protein near the Phosphorylation Site

Nikolsky, K. S., Kulikova, L. I., Petrovskiy, D. V., Rudnev, V. R., Malsagova, K. A., & Kaysheva, A. L. (2023) · Biomolecules · doi:10.3390/biom13111564 · Cited by 9 · see citing works

Regulatory-Associated Protein of mTOR-Mediated Signaling: A Nexus Between Tumorigenesis and Disease

Chouhan, S., Kumar, A., Piprode, V., Dasgupta, A., Singh, S., & Khalique, A. (2024) · Targets · doi:10.3390/targets2040020 · Cited by 9 · see citing works

Interplay of Metal Ions and Posttranslational Modifications in Proteins

Peana, M., Frączyk, T., & Zoroddu, M. A. (2024) · European Journal of Inorganic Chemistry · doi:10.1002/ejic.202400175 · 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

Computational studies on the functional and structural impact of pathogenic mutations in enzymes

Dissanayake, U. C., Roy, A., Maghsoud, Y., Polara, S., Debnath, T., & Cisneros, G. A. (2025) · Protein Science · doi:10.1002/pro.70081 · Cited by 8 · see citing works

Post-translational modifications: Bridging viral infections and inflammatory bowel disease

Xiao, J., Han, Y., Liu, K., Wang, X., Li, S., Yi, J., & Liu, X. (2025) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2025.101417 · Cited by 8 · see citing works

The actionable transcriptome: a framework for incorporating RNA sequencing into precision oncology

Johnson, A., Shen, Y., Zheng, X., Su, F., Zeng, J., Uzunparmak, B., Breuer, E.-K. Y., Holla, V. R., Kahle, M., Kim, S.-H., et al. (2026) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-025-01110-1 · Cited by 9 · see citing works

Oxidative Stress as a Regulatory Checkpoint in the Production of Antiphospholipid Autoantibodies: The Protective Role of NRF2 Pathway

Sorice, M., Profumo, E., Capozzi, A., Recalchi, S., Riitano, G., Veroli, B. D., Saso, L., & Buttari, B. (2023) · Biomolecules · doi:10.3390/biom13081221 · Cited by 10 · see citing works

GSK3β and UCHL3 govern RIPK4 homeostasis via deubiquitination to enhance tumor metastasis in ovarian cancer

Shan, W., Peng, W., Chen, Y., Wang, Y., Yu, Q., Tian, Y., Dou, Y., Tu, J., Huang, X., Li, X., et al. (2024) · Oncogene · doi:10.1038/s41388-024-03040-1 · Cited by 8 · see citing works

PhosBERT: A self-supervised learning model for identifying phosphorylation sites in SARS-CoV-2-infected human cells

Li, Y., Gao, R., Liu, S., Zhang, H., Lv, H., & Lai, H. (2024) · Methods · doi:10.1016/j.ymeth.2024.08.004 · Cited by 8 · see citing works

USP24 is an ISG15 cross-reactive deubiquitinase that mediates IFN-I production by de-ISGylating the RNA helicase MOV10Preprint

Mukhopadhyay, R., Draganov, S. D., Akkermans, J. J. L. L., Kikkert, M., Knobeloch, K., Fritz, G., Guzmán, M. G., Zúñiga, S., Kim, R. Q., Kessler, B. M., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.09.06.611391 · Cited by 8 · see citing works

Acetylation, ADP-ribosylation and methylation of malate dehydrogenase

Kuhn, M. L., Rakus, J. F., & Quénet, D. (2024) · Essays in Biochemistry · doi:10.1042/ebc20230080 · Cited by 7 · see citing works

Global Profiling of Protein Phosphorylation, Acetylation, and β-Hydroxybutyrylation in Nannochloropsis oceanica

Ouyang, L., You, W., Poetsch, A., & Wei, L. (2024) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.4c05869 · Cited by 7 · see citing works

Shrimp allergen extract immunotherapy induces prolonged immune tolerance in a gastro-food allergy mouse model

Marhaeny, H. D., Rohmah, L., Pratama, Y. A., Kasatu, S. M., Miatmoko, A., Addimaysqi, R., van den Bogaart, G., Ho, F. Y., Taher, M., & Khotib, J. (2024) · PLoS ONE · doi:10.1371/journal.pone.0315312 · Cited by 7 · see citing works

Programmable protein stabilization with language model-derived peptide guides

Hong, L., Ye, T., Wang, T. Z., Srijay, D., Liu, H., Zhao, L., Watson, R., Vincoff, S., Chen, T., Kholina, K., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-58872-6 · Cited by 7 · see citing works

Single-Cell Analysis of Posttranslational Modifications Identifies Immunosuppressive Macrophage Subtypes in the HBV-Positive Hepatocellular Carcinoma Microenvironment

Zhao, H., Ren, R., Zhang, X., Zhan, M., Cui, J., Zhang, J., Liu, X., Wu, L., Chen, Y., Zhou, Y. J., et al. (2025) · Cancer Immunology Research · doi:10.1158/2326-6066.cir-24-1298 · Cited by 7 · see citing works

Bioluminescence-based assays for quantifying endogenous protein interactions in live cells

Niles, A. L., Dibble, M., Machleidt, T., Martino, K., Swiatnicki, M., Vu, E. H., & Schwinn, M. K. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110454 · Cited by 7 · see citing works

Emerging Roles of Post-Translational Modifications in Metabolic Homeostasis and Type 2 Diabetes

Kim, Y. K., & Kim, H. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262311552 · Cited by 7 · see citing works

High-throughput chemical proteomics workflow for profiling protein citrullination dynamics

González, R. M., Laposchan, S., Riedel, E., Fürst, A., O'Sullivan, N., Gabriel, W., Wilhelm, M., Knolle, P. A., Médard, G., Küster, B., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-69490-1 · Cited by 7 · see citing works

Kinase signaling in liver disease via clinical-trial-on-a-PamChip: A distinctive methodology for drug mechanisms and personalized medicine

Kipp, Z. A., Bates, E. A., Martinez, G. J., Lee, W., Pauss, S. N., & Hinds, T. D. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.111379 · Cited by 7 · see citing works

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 7 · see citing works

Protein Modification

Liu, D. (2024) · CRC Press eBooks · doi:10.1201/9781003055211-30 · Cited by 2 · see citing works

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 6 · see citing works

Small Changes Huge Impact: The Role of Protein Posttranslational Modifications in Cellular Homeostasis and Disease

Karve, T. M., & Cheema, A. K. (2011) · Journal of Amino Acids · doi:10.4061/2011/207691 · Cited by 364 · see citing works

Posttranslational Modifications: Key Players in Health and Disease

Nita‐Lazar, A. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-821618-7.00067-5 · Cited by 2 · see citing works

Posttranslational Modifications of Proteins and Their Role in Biological Processes and Associated Diseases

Tak, I.-U.-R., Ali, F., Dar, J. S., Magray, A. R., Ganai, B. A., & Chishti, M. Z. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-811913-6.00001-1 · Cited by 34 · see citing works