1 P.R. Gajjala, D. Fliser, T. Speer, et al.Emerging role of post-translational modifications in chronic kidney disease and cardiovascular disease Nephrol Dial Transplant, 30 (11) (2015), pp. 1814-1824

2 J. Liu, L. Zhong, R. GuoThe role of posttranslational modification and mitochondrial quality control in cardiovascular diseases Oxid Med Cell Longev, 2021 (2021), Article 6635836

3 R. Bischoff, H. SchlüterAmino acids: chemistry, functionality and selected non-enzymatic post-translational modifications J Proteonomics, 75 (8) (2012), pp. 2275-2296

4 M.M. MüllerPost-translational modifications of protein backbones: unique functions, mechanisms, and challenges Biochemistry, 57 (2) (2018), pp. 177-185

5 C. D'Hondt, J. Iyyathurai, M. Vinken, et al.Regulation of connexin- and pannexin-based channels by post-translational modifications Biol Cell, 105 (9) (2013), pp. 373-398

6 K.K. Han, A. MartinagePost-translational chemical modifications of proteins—III. Current developments in analytical procedures of identification and quantitation of post-translational chemically modified amino acid(s) and its derivatives Int J Biochem, 25 (7) (1993), pp. 957-970

7 Y. Chen, Y. WangMapping histone modification-dependent protein interactions with chemical proteomics Trends Biochem Sci, 47 (3) (2022), pp. 189-193

8 L. Cai, F. Hu, W. Fu, et al.Ginsenoside Rg2 ameliorates brain injury after intracerebral hemorrhage in a rat model of preeclampsia Reprod Sci, 28 (12) (2021), pp. 3431-3439

9 Z. Wu, J. Connolly, K.K. BiggarBeyond histones - the expanding roles of protein lysine methylation FEBS J, 284 (17) (2017), pp. 2732-2744

10 J. Liu, C. Qian, X. CaoPost-translational modification control of innate immunity Immunity, 45 (1) (2016), pp. 15-30

11 G. Jiang, C. Li, M. Lu, et al.Protein lysine crotonylation: past, present, perspective Cell Death Dis, 12 (7) (2021), p. 703

12 Y. Liu, M. Li, M. Fan, et al.Chromodomain Y-like protein-mediated histone crotonylation regulates stress-induced depressive behaviors Biol Psychiatr, 85 (8) (2019), pp. 635-649

13 Z. Wang, Y. Zhao, N. Xu, et al.NEAT1 regulates neuroglial cell mediating Aβ clearance via the epigenetic regulation of endocytosis-related genes expression Cell Mol Life Sci, 76 (15) (2019), pp. 3005-3018

14 Y. Zhao, M. Yang, S. Wang, et al.An overview of epigenetic methylation in pancreatic cancer progression Front Oncol, 12 (2022), Article 854773

15 J.J. Zhang, Y. Zhu, Y. Zhu, et al.Association of increased DNA methyltransferase expression with carcinogenesis and poor prognosis in pancreatic ductal adenocarcinoma Clin Transl Oncol, 14 (2) (2012), pp. 116-124

16 N. Zhang, H. Jiang, K. Zhang, et al.OGT as potential novel target: structure, function and inhibitors Chem Biol Interact, 357 (2022), Article 109886

17 W. Wang, T. Okajima, H. TakeuchiSignificant roles of Notch O-glycosylation in cancer Molecules, 27 (6) (2022), p. 1783

18 A.K. Jansson, L.X. Chan, D.R. Lubans, et al.Effect of resistance training on HbA1c in adults with type 2 diabetes mellitus and the moderating effect of changes in muscular strength: a systematic review and meta-analysis BMJ Open Diabetes Res Care, 10 (2) (2022), Article e002595

19 A.L. Rebelo, M.T. Chevalier, L. Russo, et al.Role and therapeutic implications of protein glycosylation in neuroinflammation Trends Mol Med, 28 (4) (2022), pp. 270-289

20 F. Kobeissy, A. Kobaisi, W. Peng, et al.Glycomic and glycoproteomic techniques in neurodegenerative disorders and neurotrauma: towards personalized markers Cells, 11 (3) (2022), p. 581

21 P.A. Contreras-de la Rosa, C. Aragón-Rodríguez, J.A. Ceja-López, et al.Lysine crotonylation: a challenging new player in the epigenetic regulation of plants J Proteonomics, 255 (2022), Article 104488

22 K. Boulias, E.L. GreerMeans, mechanisms and consequences of adenine methylation in DNA Nat Rev Genet, 23 (7) (2022), pp. 411-428

23 Y. Chen, Y. Song, J. Liu, et al.Ubiquitination of receptorsomes, frontline of plant immunity Int J Mol Sci, 23 (6) (2022), p. 2937

24 H. Qi, J. Yang, J. Yu, et al.Glucose-responsive nanogels efficiently maintain the stability and activity of therapeutic enzymes Nanotechnol Rev, 11 (1) (2022), pp. 1511-1524

25 E. Arc, M. Galland, G. Cueff, et al.Reboot the system thanks to protein post-translational modifications and proteome diversity: how quiescent seeds restart their metabolism to prepare seedling establishment Proteomics, 11 (9) (2011), pp. 1606-1618

26 B.R. Sabari, D. Zhang, C.D. Allis, et al.Metabolic regulation of gene expression through histone acylations Nat Rev Mol Cell Biol, 18 (2) (2017), pp. 90-101

27 Y. Shi, Y. Li, K. Yang, et al.Antimicrobial peptide BCp12 inhibits Staphylococcus aureus growth by altering lysine malonylation levels in the arginine synthesis pathway J Agric Food Chem, 70 (1) (2022), pp. 403-414

28 M. Xu, X. Tian, T. Ku, et al.Global identification and systematic analysis of lysine malonylation in maize (Zea mays L.) Front Plant Sci, 12 (2021), Article 728338

29 J.N. Peoples, N. Ghazal, D.M. Duong, et al.Loss of the mitochondrial phosphate carrier SLC25A3 induces remodeling of the cardiac mitochondrial protein acylome Am J Physiol Cell Physiol, 321 (3) (2021), pp. C519-C534

30 Y. Chen, R. Sprung, Y. Tang, et al.Lysine propionylation and butyrylation are novel post-translational modifications in histones Mol Cell Proteomics, 6 (5) (2007), pp. 812-819

31 X.F. Chen, X. Chen, X. TangShort-chain fatty acid, acylation and cardiovascular diseases Clin Sci (Lond), 134 (6) (2020), pp. 657-676

32 H. Xu, M. Wu, X. Ma, et al.Function and mechanism of novel histone posttranslational modifications in health and disease BioMed Res Int, 2021 (2021), Article 6635225

33 X. Li, Y. Yang, B. Zhang, et al.Lactate metabolism in human health and disease Signal Transduct Targeted Ther, 7 (1) (2022), p. 305

34 S. Zhao, X. Zhang, H. LiBeyond histone acetylation—writing and erasing histone acylations Curr Opin Struct Biol, 53 (2018), pp. 169-177

35 J. Han, C. Lachance, M.D. Ricketts, et al.The scaffolding protein JADE1 physically links the acetyltransferase subunit HBO1 with its histone H3-H4 substrate J Biol Chem, 293 (12) (2018), pp. 4498-4509

36 Y. Tao, C. Zhong, J. Zhu, et al.Structural and mechanistic insights into regulation of HBO1 histone acetyltransferase activity by BRPF2 Nucleic Acids Res, 45 (10) (2017), pp. 5707-5719

37 Y. Xiao, W. Li, H. Yang, et al.HBO1 is a versatile histone acyltransferase critical for promoter histone acylations Nucleic Acids Res, 49 (14) (2021), pp. 8037-8059

38 Y. Du, G. Hou, H. Zhang, et al.SUMOylation of the m6A-RNA methyltransferase METTL3 modulates its function Nucleic Acids Res, 46 (10) (2018), pp. 5195-5208

39 A.E. Ringel, C. WolbergerStructural basis for acyl-group discrimination by human Gcn5L2 Acta Crystallogr D Struct Biol, 72 (Pt 7) (2016), pp. 841-848

40 S. Biswas, C.M. RaoEpigenetic tools (The Writers, the Readers and the Erasers) and their implications in cancer therapy Eur J Pharmacol, 837 (2018), pp. 8-24

41 K. Tanabe, J. Liu, D. Kato, et al.LC-MS/MS-based quantitative study of the acyl group- and site-selectivity of human sirtuins to acylated nucleosomes Sci Rep, 8 (1) (2018), p. 2656

42 H.C. Chang, L. GuarenteSIRT1 and other sirtuins in metabolism Trends Endocrinol Metabol, 25 (3) (2014), pp. 138-145

43 B.C. Smith, J.M. DenuAcetyl-lysine analog peptides as mechanistic probes of protein deacetylases J Biol Chem, 282 (51) (2007), pp. 37256-37265

44 X. Xiong, T. Panchenko, S. Yang, et al.Selective recognition of histone crotonylation by double PHD fingers of MOZ and DPF2 Nat Chem Biol, 12 (12) (2016), pp. 1111-1118

45 E.M. Flynn, O.W. Huang, F. Poy, et al.A subset of human bromodomains recognizes butyryllysine and crotonyllysine histone peptide modifications Structure, 23 (10) (2015), pp. 1801-1814

46 F. Vollmuth, M. GeyerInteraction of propionylated and butyrylated histone H3 lysine marks with Brd4 bromodomains Angew Chem Int Ed Engl, 49 (38) (2010), pp. 6768-6772

47 Y. Li, B.R. Sabari, T. Panchenko, et al.Molecular coupling of histone crotonylation and active transcription by AF9 YEATS domain Mol Cell, 62 (2) (2016), pp. 181-193

48 D. Zhao, H. Guan, S. Zhao, et al.YEATS2 is a selective histone crotonylation reader Cell Res, 26 (5) (2016), pp. 629-632

49 F.H. Andrews, S.A. Shinsky, E.K. Shanle, et al.The Taf14 YEATS domain is a reader of histone crotonylation Nat Chem Biol, 12 (6) (2016), pp. 396-398

50 A. Goudarzi, D. Zhang, H. Huang, et al.Dynamic competing histone H4 K5K8 acetylation and butyrylation are hallmarks of highly active gene promoters Mol Cell, 62 (2) (2016), pp. 169-180

51 Z. Yang, M. He, J. Austin, et al.Histone H3K9 butyrylation is regulated by dietary fat and stress via an Acyl-CoA dehydrogenase short chain-dependent mechanism Mol Metabol, 53 (2021), Article 101249

52 H. Abou-Abbass, H. Abou-El-Hassan, H. Bahmad, et al.Glycosylation and other PTMs alterations in neurodegenerative diseases: current status and future role in neurotrauma Electrophoresis, 37 (11) (2016), pp. 1549-1561

53 J.T. O'Brien, A. ThomasVascular dementia Lancet, 386 (10004) (2015), pp. 1698-1706

54 L. Bryant, D. Li, S.G. Cox, et al.Histone H3.3 beyond cancer: Germline mutations in Histone 3 Family 3A and 3B cause a previously unidentified neurodegenerative disorder in 46 patients Sci Adv, 6 (49) (2020), Article eabc9207

55 C. IadecolaThe pathobiology of vascular dementia Neuron, 80 (4) (2013), pp. 844-866

56 P. Gareri, A.M. Cotroneo, G. Orsitto, et al.The CITIMEM study: a pilot study. Optimizing pharmacological treatment in dementia Arch Gerontol Geriatr, 89 (2020), Article 104073

57 N. Ghassab-Abdollahi, K. Mobasseri, A. Dehghani Ahmadabad, et al.The effects of Huperzine A on dementia and mild cognitive impairment: an overview of systematic reviews Phytother Res, 35 (9) (2021), pp. 4971-4987

58 J.F. Leijenaar, G.J. Groeneveld, E.S. Klaassen, et al.Methylphenidate and galantamine in patients with vascular cognitive impairment-the proof-of-principle study STREAM-VCI Alzheimer's Res Ther, 12 (1) (2020), p. 10

59 H. Wang, Y. Zong, Y. Han, et al.Compared of efficacy and safety of high-dose donepezil vs standard-dose donepezil among elderly patients with Alzheimer's disease: a systematic review and meta-analysis Expet Opin Drug Saf, 21 (3) (2022), pp. 407-415

60 H. Wang, J. Lu, W.C. Gao, et al.Donepezil down-regulates propionylation, 2-hydroxyisobutyrylation, butyrylation, succinylation, and crotonylation in the brain of bilateral common carotid artery occlusion-induced vascular dementia rats Clin Exp Pharmacol Physiol, 47 (10) (2020), pp. 1731-1739

61 C. Luís, R. Soares, P. Baylina, et al.Underestimated prediabetic biomarkers: are we blind to their strategy? Front Endocrinol, 13 (2022), Article 805837

62 C. Baradez, J. Liska, C. Brulle-Wohlhueter, et al.Brief digital solutions in behavior change interventions for type 2 diabetes mellitus: a literature review Diabetes Ther, 13 (4) (2022), pp. 635-649

63 X. Li, H. Qi, W. Cui, et al.Recent advances in targeted delivery of non-coding RNA-based therapeutics for atherosclerosis Mol Ther, 30 (10) (2022), pp. 3118-3132

64 X. Li, Y. Yang, Z. Wang, et al.Multistage-responsive nanocomplexes attenuate ulcerative colitis by improving the accumulation and distribution of oral nucleic acid drugs in the colon ACS Appl Mater Interfaces, 14 (1) (2022), pp. 2058-2070

65 Y. Yang, M. Li, Y. Liu, et al.The lncRNA punisher regulates apoptosis and mitochondrial homeostasis of vascular smooth muscle cells via targeting miR-664a-5p and OPA1 Oxid Med Cell Longev, 2022 (2022), Article 5477024

66 M. Li, Y. Yang, J. Zong, et al.MiR-564:a potential regulator of vascular smooth muscle cells and therapeutic target for aortic dissection J Mol Cell Cardiol, 170 (2022), pp. 100-114

67 A. Kadakol, V. Malek, S.K. Goru, et al.Telmisartan and esculetin combination ameliorates type 2 diabetic cardiomyopathy by reversal of H3, H2A, and H2B histone modifications Indian J Pharmacol, 49 (5) (2017), pp. 348-356

68 L. Nie, L. Shuai, M. Zhu, et al.The landscape of histone modifications in a high-fat diet-induced obese (DIO) mouse model Mol Cell Proteomics, 16 (7) (2017), pp. 1324-1334

69 C.J. Nolan, M.S. Madiraju, V. Delghingaro-Augusto, et al.Fatty acid signaling in the beta-cell and insulin secretion Diabetes, 55 (Suppl 2) (2006), pp. S16-S23

70 G.K. Bandyopadhyay, J.G. Yu, J. Ofrecio, et al.Increased malonyl-CoA levels in muscle from obese and type 2 diabetic subjects lead to decreased fatty acid oxidation and increased lipogenesis; thiazolidinedione treatment reverses these defects Diabetes, 55 (8) (2006), pp. 2277-2285

71 Z. Zhu, Z. Han, L. Halabelian, et al.Identification of lysine isobutyrylation as a new histone modification mark Nucleic Acids Res, 49 (1) (2021), pp. 177-189

72 Q.Q. Li, J.J. Hao, Z. Zhang, et al.Proteomic analysis of proteome and histone post-translational modifications in heat shock protein 90 inhibition-mediated bladder cancer therapeutics Sci Rep, 7 (1) (2017), p. 201

73 H.Z. Oo, R. Seiler, P.C. Black, et al.Post-translational modifications in bladder cancer: expanding the tumor target repertoire Urol Oncol Semin Orig Investig, 38 (12) (2020), pp. 858-866

74 A. Goudarzi, N. Hosseinmardi, S. Salami, et al.Starvation promotes histone lysine butyrylation in the liver of male but not female mice Gene, 745 (2020), Article 144647

75 J. Shi, A. Dong, W.H. ShenEpigenetic regulation of rice flowering and reproduction Front Plant Sci, 5 (2015), p. 803

76 Y. Lu, Q. Xu, Y. Liu, et al.Dynamics and functional interplay of histone lysine butyrylation, crotonylation, and acetylation in rice under starvation and submergence Genome Biol, 19 (1) (2018), p. 144

77 F. Yang, C. WangProfiling of post-translational modifications by chemical and computational proteomics Chem Commun, 56 (88) (2020), pp. 13506-13519

78 K. Zhang, Y. Chen, Z. Zhang, et al.Identification and verification of lysine propionylation and butyrylation in yeast core histones using PTMap software J Proteome Res, 8 (2) (2009), pp. 900-906

79 G. Huang, Y. Zheng, Y.Q. Wu, et al.An information entropy-based approach for computationally identifying histone lysine butyrylation Front Genet, 10 (2020), p. 1325

80 G. Xu, J. Wang, Z. Wu, et al.SAHA regulates histone acetylation, butyrylation, and protein expression in neuroblastoma J Proteome Res, 13 (10) (2014), pp. 4211-4219

81 Y. Zhao, X. Fang, Y. Wang, et al.Comprehensive analysis for histone acetylation of human colon cancer cells treated with a novel HDAC inhibitor Curr Pharmaceut Des, 20 (11) (2014), pp. 1866-1873

82 S. Santra, A. MacDonald, M.A. Preece, et al.Long-term outcome of isobutyryl-CoA dehydrogenase deficiency diagnosed following an episode of ketotic hypoglycaemia Mol Genet Metab Rep, 10 (2017), pp. 28-30

83 J.W. Yun, K.I. Jo, H.I. Woo, et al.A novel ACAD8 mutation in asymptomatic patients with isobutyryl-CoA dehydrogenase deficiency and a review of the ACAD8 mutation spectrum Clin Genet, 87 (2) (2015), pp. 196-198

84 G. Günes Günsel, T.M. Conlon, A. Jeridi, et al.The arginine methyltransferase PRMT7 promotes extravasation of monocytes resulting in tissue injury in COPD Nat Commun, 13 (1) (2022), p. 1303

85 S. Malebary, S. Rahman, O. Barukab, et al.iAcety-SmRF: identification of acetylation protein by using statistical moments and random forest Membranes, 12 (3) (2022), p. 265

86 M. Fiedler, W.H. Ip, H. Hofmann-Sieber, et al.Protein-protein interactions facilitate E4orf6-dependent regulation of E1B-55K SUMOylation in HAdV-C5 infection Viruses, 14 (3) (2022), p. 463

87 D. Huang, W.L. KrausThe expanding universe of PARP1-mediated molecular and therapeutic mechanisms Mol Cell, 82 (12) (2022), pp. 2315-2334

88 Y. Zhao, L. Zhang, C. Ju, et al.Quantitative multiplexed proteomics analysis reveals reshaping of the lysine 2-hydroxyisobutyrylome in Fusarium graminearum by tebuconazole BMC Genom, 23 (1) (2022), p. 145

89 B. Huo, Y. Liu, L. Li, et al.A chemical method for genome- and proteome-wide enrichment and O-GlcNAcylation profiling of chromatin-associated proteins Talanta, 241 (2022), Article 123167

90 S. Liu, G. Liu, P. Cheng, et al.Genome-wide profiling of histone lysine butyrylation reveals its role in the positive regulation of gene transcription in rice Rice, 12 (1) (2019), p. 86

91 E. González-Grandío, S. Álamos, Y. Zhang, et al.Chromatin changes in phytochrome interacting factor-regulated genes parallel their rapid transcriptional response to light Front Plant Sci, 13 (2022), Article 803441

92 P. Nounurai, A. Afifah, S. Kittisenachai, et al.Phosphorylation of CAD1, PLDdelta, NDT1, RPM1 proteins induce resistance in tomatoes infected by Ralstonia solanacearum Plants, 11 (6) (2022), p. 726

93 M.A. Carrillo-Sepulveda, N. Maddie, C.M. Johnson, et al.Vascular hyperacetylation is associated with vascular smooth muscle dysfunction in a rat model of non-obese type 2 diabetes Mol Med, 28 (2022), p. 30

94 L. Zou, Y. Yang, Z. Wang, et al.Lysine malonylation and its links to metabolism and diseases Aging Dis, 14 (1) (2023), pp. 84-98

95 Q. Xue, T. Yu, Z. Wang, et al.Protective effect and mechanism of ginsenoside Rg2 on atherosclerosis J Ginseng Res, 47 (2) (2023), pp. 237-245