1. Andersson C, Vasan RS. Epidemiology of cardiovascular disease in young individuals. Nat Rev Cardiol. 2018;15(4):230-40.
2. Petsophonsakul P, Furmanik M, Forsythe R, Dweck M, Schurink GW, Natour E, et al. Role of Vascular Smooth Muscle Cell Phenotypic Switching and Calcification in Aortic Aneurysm Formation. Arterioscler Thromb Vasc Biol. 2019;39(7):1351-68.
3. Gomez D, Owens GK. Smooth muscle cell phenotypic switching in atherosclerosis. Cardiovasc Res. 2012;95(2):156-64.
4. Owens GK, Kumar MS, Wamhoff BR. Molecular regulation of vascular smooth muscle cell differentiation in development and disease. Physiol Rev. 2004;84(3):767-801.
5. Kim DN, Schmee J, Baker JE, Lunden GM, Sheehan CE, Lee CS, et al. Dietary fish oil reduces microthrombi over atherosclerotic lesions in hyperlipidemic swine even in the absence of plasma cholesterol reduction. Exp Mol Pathol. 1993;59(2):122-35.
6. Cercek B, Sharifi B, Barath P, Bailey L, Forrester JS. Growth factors in pathogenesis of coronary arterial restenosis. Am J Cardiol. 1991;68(12):24C-33C.
7. Thyberg J, Ostman A, Backstrom G, Westermark B, Heldin CH. Localization of platelet-derived growth factor (PDGF) in CHO cells transfected with PDGF A- or B-chain cDNA: retention of PDGF-BB in the endoplasmic reticulum and Golgi complex. J Cell Sci. 1990;97 (Pt 2):219-29.
8. Heldin CH, Westermark B. Signal transduction by the receptors for platelet-derived growth factor. J Cell Sci. 1990;96 (Pt 2):193-6.
9. Kaplan-Albuquerque N, Van Putten V, Weiser-Evans MC, Nemenoff RA. Depletion of serum response factor by RNA interference mimics the mitogenic effects of platelet derived growth factor-BB in vascular smooth muscle cells. Circ Res. 2005;97(5):427-33.
10. Cain JA, Solis N, Cordwell SJ. Beyond gene expression: the impact of protein post-translational modifications in bacteria. J Proteomics. 2014;97:265-86.
11. Olsen JV, Mann M. Status of large-scale analysis of post-translational modifications by mass spectrometry. Mol Cell Proteomics. 2013;12(12):3444-52.
12. Zhao Y, Jensen ON. Modification-specific proteomics: strategies for characterization of post-translational modifications using enrichment techniques. Proteomics. 2009;9(20):4632-41.
13. Dong LH, Li L, Song Y, Duan ZL, Sun SG, Lin YL, et al. TRAF6-Mediated SM22alpha K21 Ubiquitination Promotes G6PD Activation and NADPH Production, Contributing to GSH Homeostasis and VSMC Survival In Vitro and In Vivo. Circ Res. 2015;117(8):684-94.
14. Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, et al. Regulation of cellular metabolism by protein lysine acetylation. Science. 2010;327(5968):1000-4.
15. Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, et al. Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol Cell. 2006;23(4):607-18.
16. Xie Z, Dai J, Dai L, Tan M, Cheng Z, Wu Y, et al. Lysine succinylation and lysine malonylation in histones. Mol Cell Proteomics. 2012;11(5):100-7.
17. Nakamura N. Ubiquitin System. Int J Mol Sci. 2018;19(4).
18. Peng C, Lu Z, Xie Z, Cheng Z, Chen Y, Tan M, et al. The first identification of lysine malonylation substrates and its regulatory enzyme. Mol Cell Proteomics. 2011;10(12):M111-12658.
19. Tan M, Luo H, Lee S, Jin F, Yang JS, Montellier E, et al. Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification. Cell. 2011;146(6):1016-28.
20. Yang XJ, Seto E. Lysine acetylation: codified crosstalk with other posttranslational modifications. Mol Cell. 2008;31(4):449-61.
21. Sabari BR, Tang Z, Huang H, Yong-Gonzalez V, Molina H, Kong HE, et al. Intracellular crotonyl-CoA stimulates transcription through p300-catalyzed histone crotonylation. Mol Cell. 2015;58(2):203-15.
22. Madsen AS, Olsen CA. Profiling of substrates for zinc-dependent lysine deacylase enzymes: HDAC3 exhibits decrotonylase activity in vitro. Angew Chem Int Ed Engl. 2012;51(36):9083-7.
23. Zhao D, Guan H, Zhao S, Mi W, Wen H, Li Y, et al. YEATS2 is a selective histone crotonylation reader. Cell Res. 2016;26(5):629-32.
24. Bao X, Wang Y, Li X, Li XM, Liu Z, Yang T, et al. Identification of 'erasers' for lysine crotonylated histone marks using a chemical proteomics approach. Elife. 2014;3.
25. Feldman JL, Baeza J, Denu JM. Activation of the protein deacetylase SIRT6 by long-chain fatty acids and widespread deacylation by mammalian sirtuins. J Biol Chem. 2013;288(43):31350-6.
26. Palacios OM, Carmona JJ, Michan S, Chen KY, Manabe Y, Ward JR, et al. Diet and exercise signals regulate SIRT3 and activate AMPK and PGC-1alpha in skeletal muscle. Aging (Albany NY). 2009;1(9):771-83.
27. Zhu J, Dong Q, Dong C, Zhang X, Zhang H, Chen Z. Global Lysine Crotonylation Alterations of Host Cell Proteins Caused by Brucella Effector BspF. Front Cell Infect Microbiol. 2020;10:603457.
28. Liu JF, Wu SF, Liu S, Sun X, Wang XM, Xu P, et al. Global Lysine Crotonylation Profiling of Mouse Liver. Proteomics. 2020;20(19-20):e2000049.
29. Chen W, Tang D, Xu Y, Zou Y, Sui W, Dai Y, et al. Comprehensive analysis of lysine crotonylation in proteome of maintenance hemodialysis patients. Medicine (Baltimore). 2018;97(37):e12035.
30. Xu W, Wan J, Zhan J, Li X, He H, Shi Z, et al. Global profiling of crotonylation on non-histone proteins. Cell Res. 2017;27(7):946-9.
31. Liu M, Yan M, Lv H, Wang B, Lv X, Zhang H, et al. Macrophage K63-Linked Ubiquitination of YAP Promotes Its Nuclear Localization and Exacerbates Atherosclerosis. Cell Rep. 2020;32(5):107990.
32. Dang F, Nie L, Wei W. Ubiquitin signaling in cell cycle control and tumorigenesis. Cell Death & Differentiation. 2021;28(2):427-38.
33. Chu Y, Kang Y, Yan C, Yang C, Zhang T, Huo H, et al. LUBAC and OTULIN regulate autophagy initiation and maturation by mediating the linear ubiquitination and the stabilization of ATG13. Autophagy. 2021;17(7):1684-99.
34. Dong LH, Wen JK, Miao SB, Jia Z, Hu HJ, Sun RH, et al. Baicalin inhibits PDGF-BB-stimulated vascular smooth muscle cell proliferation through suppressing PDGFRbeta-ERK signaling and increase in p27 accumulation and prevents injury-induced neointimal hyperplasia. Cell Res. 2010;20(11):1252-62.
35. Yin LM, Schnoor M, Jun CD. Structural Characteristics, Binding Partners and Related Diseases of the Calponin Homology (CH) Domain. Front Cell Dev Biol. 2020;8:342.
36. Xie X, Kang H, Liu W, Wang GL. Comprehensive profiling of the rice ubiquitome reveals the significance of lysine ubiquitination in young leaves. J Proteome Res. 2015;14(5):2017-25.
37. Guo J, Liu J, Wei Q, Wang R, Yang W, Ma Y, et al. Proteomes and Ubiquitylomes Analysis Reveals the Involvement of Ubiquitination in Protein Degradation in Petunias. Plant Physiol. 2017;173(1):668-87.
38. Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, et al. Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level. Mol Cell Proteomics. 2011;10(3):M110-3590.
39. Dong LH, Li L, Song Y, Duan ZL, Sun SG, Lin YL, et al. TRAF6-Mediated SM22alpha K21 Ubiquitination Promotes G6PD Activation and NADPH Production, Contributing to GSH Homeostasis and VSMC Survival In Vitro and In Vivo. Circ Res. 2015;117(8):684-94.
40. Harris AR, Belardi B, Jreij P, Wei K, Shams H, Bausch A, et al. Steric regulation of tandem calponin homology domain actin-binding affinity. Mol Biol Cell. 2019;30(26):3112-22.
41. Xiong W, Tang T, Littleton E, Karcini A, Lazar IM, Capelluto DGS. Preferential phosphatidylinositol 5-phosphate binding contributes to a destabilization of the VHS domain structure of Tom1. Sci Rep-Uk. 2019;9(1).
42. Lohi O, Poussu A, Mao Y, Quiocho F, Lehto V. VHS domain – a longshoreman of vesicle lines. Febs Lett. 2002;513(1):19-23.
43. Gowans GJ, Bridgers JB, Zhang J, Dronamraju R, Burnetti A, King DA, et al. Recognition of Histone Crotonylation by Taf14 Links Metabolic State to Gene Expression. Mol Cell. 2019;76(6):909-21.
44. Liu S, Yu H, Liu Y, Liu X, Zhang Y, Bu C, et al. Chromodomain Protein CDYL Acts as a Crotonyl-CoA Hydratase to Regulate Histone Crotonylation and Spermatogenesis. Mol Cell. 2017;67(5):853-66.
45. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, et al. Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009;325(5942):834-40.
46. Finkemeier I, Laxa M, Miguet L, Howden AJ, Sweetlove LJ. Proteins of diverse function and subcellular location are lysine acetylated in Arabidopsis. Plant Physiol. 2011;155(4):1779-90.
47. He D, Wang Q, Li M, Damaris RN, Yi X, Cheng Z, et al. Global Proteome Analyses of Lysine Acetylation and Succinylation Reveal the Widespread Involvement of both Modification in Metabolism in the Embryo of Germinating Rice Seed. J Proteome Res. 2016;15(3):879-90.
48. Lv L, Li D, Zhao D, Lin R, Chu Y, Zhang H, et al. Acetylation targets the M2 isoform of pyruvate kinase for degradation through chaperone-mediated autophagy and promotes tumor growth. Mol Cell. 2011;42(6):719-30.
49. Bhushan S, Meyer H, Starosta AL, Becker T, Mielke T, Berninghausen O, et al. Structural basis for translational stalling by human cytomegalovirus and fungal arginine attenuator peptide. Mol Cell. 2010;40(1):138-46.
50. Gamalinda M, Woolford JJ. Deletion of L4 domains reveals insights into the importance of ribosomal protein extensions in eukaryotic ribosome assembly. Rna. 2014;20(11):1725-31.
51. Singh N, Jindal S, Ghosh A, Komar AA. Communication between RACK1/Asc1 and uS3 (Rps3) is essential for RACK1/Asc1 function in yeast Saccharomyces cerevisiae. Gene. 2019;706:69-76.
52. Zhou X, Song N, Li D, Li X, Liu W. Systematic Analysis of the Lysine Crotonylome and Multiple Posttranslational Modification Analysis (Acetylation, Succinylation, and Crotonylation) in Candida albicans. Msystems. 2021;6(1).
53. Meng X, Mujahid H, Zhang Y, Peng X, Redoña ED, Wang C, et al. Comprehensive Analysis of the Lysine Succinylome and Protein Co-modifications in Developing Rice Seeds. Mol Cell Proteomics. 2019;18(12):2359-72.
54. Crespo M, Damont A, Blanco M, Lastrucci E, Kennani SE, Ialy-Radio C, et al. Multi-omic analysis of gametogenesis reveals a novel signature at the promoters and distal enhancers of active genes. Nucleic Acids Res. 2020;48(8):4115-38.
55. Pecci A, Ma X, Savoia A, Adelstein RS. MYH9: Structure, functions and role of non-muscle myosin IIA in human disease. Gene. 2018;664:152-67.
56. Ye G, Yang Q, Lei X, Zhu X, Li F, He J, et al. Nuclear MYH9-induced CTNNB1 transcription, targeted by staurosporin, promotes gastric cancer cell anoikis resistance and metastasis. Theranostics. 2020;10(17):7545-60.
57. Yang B, Liu H, Bi Y, Cheng C, Li G, Kong P, et al. MYH9 promotes cell metastasis via inducing Angiogenesis and Epithelial Mesenchymal Transition in Esophageal Squamous Cell Carcinoma. Int J Med Sci. 2020;17(13):2013-23.
58. Lin X, Li AM, Li YH, Luo RC, Zou YJ, Liu YY, et al. Silencing MYH9 blocks HBx-induced GSK3beta ubiquitination and degradation to inhibit tumor stemness in hepatocellular carcinoma. Signal Transduct Target Ther. 2020;5(1):13.