87. Duan L, Kim H, Suh Y, Ahn D, Kim S, Hyun J, Kwon Y, Seong J, Chung KY*. Interactions between β-Arrestin 1 and Gαs or Gαi1: Functional and structural insights. Nature Communications. accepted
86. Kim K, Ji JS, Kim HR, Choi Y, Lee HH, Inoue A*, Chung KY*. Molecular mechanism of β-arrestin 2 interaction with phosphorylated intracellular loop 3 of dopamine receptor D2. Communications Biology. 2025:8:1181. doi: 10.1038/s42003-025-08649-w
85. Ji JS, Yun Y, Stepniewski TM, Yoon H-J, Min K, Park JY, Chung C, Eceolaza MD, Chung KY, Selent J*, Lee HH*. An arginine switch drives the stepwise activation of β-arrestin by CXCR7. Plos Biology. 2025:23(8):e3003312. doi: 10.1371/journal.pbio.3003312
84. Kim K, Chung KY*. Protocol for measuring β-arrestin1-phosphorylated peptide interaction and analyzing conformational dynamics of β-arrestin1. Star Protocols. 2025:6(2):103823. doi:10.1016/j.xpro.2025.103823
83. Kim J, Chung KY*. Effects of Gα C-terminal deletion on the intrinsic GDP release/GTPase activity and conformational dynamics. Journal of Structural Biology. 2025:217(2):108182. doi:10.1016/j.jsb.2025.108182.
82. Sul JH, Shin S, Kim HK, Han J, Kim J, Son S, Lee J, Baek SH, Cho Y, Lee J, Park J, Ahn D, Park P, Palomera LF, Lim J, Kim J, Kim C, Han S, Chung KY, Lee S, Kam T, Lee Y, Kim J, Park JH, Jo D*. Dopamine-conjugated extracellular vesicles induce autophagy in Parkinson's disease. Journal of Extracellular Vesicles. 2024:13(12):e70018. doi: 10.1002/jev2.70018
81. Saha S, Khanppnavar B, Maharana J, Kim H, Carino CMC, Daly C, Houston S, Sharma S, Zaidi N, Dalal A, Mishra S, Ganguly M, Tiwari D, Kumari P, Jhingan GD, Yadav PN, Plouffe B, Inoue A, Chung KY, Banerjee R*, Korkhov VM*, Shukla AK*. Molecular mechanism of distinct chemokine engagement and functional divergence of the human Duffy antigen receptor. Cell. 2024:187(17):4751-4769.e25. doi: 10.1016/j.cell.2024.07.005
80. Kim K, Chung KY*. Molecular mechanism of β-arrestin-2 pre-activation by phosphatidylinositol 4,5-bisphosphate. EMBO reports. 2024:25(10):4190-4205. doi: 10.1038/s44319-024-00239-x
79. Ham D, Shihoya W, Nureki O, Inoue A*, Chung KY*. Molecular mechanism of the endothelin receptor type B interactions with Gs, Gi, and Gq. Structure. 2024:32(10):1632-1639.e4. doi: 10.1016/j.str.2024.06.020
78. Kim K, Ahim J, Ham D, Yu W*, Chung KY*. Roles of the gate loop in β-arrestin-1 conformational dynamics and phosphorylated receptor interaction. Structure. 2024:32(9):1358-1366.e3. doi: 10.1016/j.str.2024.05.014
77. Ham D, Inoue A*, Xu J, Du Y*, Chung KY*. Molecular Mechanism of muscarinic acetylcholine receptor M3 interaction with Gq. Communications Biology. 2024:7:362. doi: 10.1038/s42003-024-06056-1
76. Maharana J, Sano FK, Sarma P, Yadav MK, Duan L, Stepniewski TM, Chaturvedi M, Ranjan A, Singh V, Saha S, Mahajan G, Chami M, Shihoya W, Selent J, Chung KY, Banerjee R*, Nureki O*, Shukla AK*. Molecular insights into atypical modes of β-arrestin interaction with seven transmembrane receptors. Science. 2024:383(6678):101. doi: 10.1126/science.adj3347
75. Kang DH, Kim Y, Min S, Lee SY, Chung KY, Baek IJ, Kwon K, Jo H, Kang SW*. Blood flow patterns switch VEGFR2 activity through differential S-nitrosylation and S-oxidation. Cell Reports. 2023:42(11):113361. doi: 10.1016/j.celrep.2023.113361
74. Ham D, Ahn D, Chung C, Chung KY*. Isolation and conformational analysis of the Gα α-helical domain. Biochemical and Biophysical Research Communications. 2023:685:149153. doi: 10.1016/j.bbrc.2023.149153
73. Yun Y, Yoon H-J, Jeong Y, Choi Y, Jang S, Chung KY*, Lee HH*. GPCR targeting of E3 ubiquitin ligase MDM2 by inactive β-arrestin. Proceedings of the National Academy of Science USA. 2023:120(28):e2301934120. doi: 10.1073/pnas.2301934120
72. Ahn D, Provasi D, Duc NM, Xu J, Salas-Estrada L, Spasic A, Yun MW, Kang J, Gim D, Lee J, Du Y, Filizola M*, Chung KY*. Gαs slow conformational transition upon GTP binding and a novel Gαs Regulator. iScience. 2023:26(5):106603. doi: 10.1016/j.isci.2023.106603
71. Jeong Y, Chung KY*. Structural and Functional Implication of Natural Variants of Gαs. International Journal of Molecular Sciences. 2023:24(4):4064. doi: 10.3390/ijms24044064
70. Ahn D, Chung KY*. The Conformational Dynamics of Heterotrimeric G Proteins During GPCR-Mediated Activation. In: Harris, J.R., Marles-Wright, J. (eds) Macromolecular Protein Complexes IV. Subcellular Biochemistry, Springer, Cham. 2022:99:271-284. doi: 10.1007/978-3-031-00793-4_8
69. Kim HR, Ahn D, Jo JB, Chung KY*. Effect of alpha-helical domain of Gi/o alpha subunit on GDP/GTP turnover. Biochemical Journal. 2022:479(17):1843-1855. doi: 10.1042/BCJ20220163
68. Perry-Hauser NA, Hopkins JB, Zhuo Y, Zheng C, Peres I, Schultz KM, Vishnivetskiy SA, Kaya AI, Sharma P, Dalby K, Ching KY, Klug CS,Gurevish VV, Iverson TM. The two non-visual arrestins engage ERK2 differently. Journal of Molecular Biology. 2022:434(7):167465 doi: 10.1016/j.jmb.2022.167465
67. Kim K, Han Y, Duan L, Chung KY*. Scaffolding of mitogen-activated protein kinase signaling by beta-arrestins. International Journal of Molecular Sciences. 2022:23(2):1000. doi: 10.3390/ijms23021000
66. Qu C, Park JY, Yun MW, Yang F, He Q, Kim K, Ham D, Li R, Iverson TM, Gurevich VV, Sun, JP*, Chung KY*. Scaffolding mechanism of arrestin-2 in cRaf/MEK1/ERK signaling cascade. Proceedings of the National Academy of Science USA. 2021:118(37):e2026491118. doi: 10.1073/pnas.2026491118
65. Ahn D, Ham D, Chung KY*. The conformational transition during G protein-coupled receptor (GPCR) and G protein interaction. Current Opinion in Structural Biology. 2021:69:117-123. doi:10.1016/j.sbi.2021.03.013 Invited Review.
64. Seo MJ, Heo J, Kim K, Chung KY, Yu W. Coevolution underlies GPCR-G protein selectivity and functionality. Scientific Reports. 2021:11(1):7858. doi: 10.1038/s41598-021-87251-6
63. Jeong Y, Kim J, Choi H-J, Chung KY*. Conformational dynamics of Sclerostin-LRP6 complex analyzed by HDX-MS. Biomolecules & Therapeutics. 2021:29(5):527-535. doi: 10.4062/biomolther.2020.234
62. Ham D, Ahn D, Ashim J, Cho Y, Kim HR, Yu W*, Chung KY*. Conformational switch that induces GDP release from Gi. Journal of Structural Biology. 2021:213(1):107694. doi: 10.1016/j.jsb.2020.107694
61. Komolov KE, Sulon SM, Bhardwaj A, van Keulen SC, Duc NM, Laurinavichyute DK, Lou HJ, Turk BE, Chung KY, Dror RO, Benovic JL. Structure of a GRK5-calmodulin complex reveals molecular mechanism of GRK activation and substrate targeting. Molecular Cell. 2021:81(2):323-339. doi: 10.1016/j.molcel.2020.11.026
60. Yun MW, Kim K, Park JY, and Chung KY*. Conformational dynamics analysis of MEK1 using hydrogen/deuterium exchange mass spectrometry. Protein & Peptide Letters. 2021:28(5):481-488. doi: 10.2174/0929866527666201103152534
59. Kim K and Chung KY*. Many faces of the GPCR-arrestin interaction. Archives of Pharmacal Research. 2020:43(9):890-899. doi: 10.1007/s12272-020-01263-w
58. Kim HR, Xu J, Maeda S, Duc NM, Ahn D, Du Y*, and Chung KY*. Structural mechanism underlying primary and secondary coupling between GPCRs and the Gi/o family. Nature Communications. 2020:11:3160. doi: 10.1038/s41467-020-16975-2
57. Min K. Yoon H-J, Park JY, Baidya M, Dwivedi H, Maharana J, Chung KY*, Shukla AK*, and Lee HH*. Crystal structure of β-arrestin 2 in complex with CXCR7 phosphopeptide. Structure. 2020:28(9):1014-1023.e4. doi: 10.1016/j.str.2020.06.002
56. Kang H, Yang H-S, Ki AY, Ko S-B, Kim KW, Shim CY, Kim K, Choi H-J*, Chung KY*. Conformational dynamics and functional implications of phosphorylated beta-arrestins. Structure. 2020:28(3):314-323.e3. doi: 10.1016/j.str.2019.12.008
55. Lee S-M, Jeong Y, Simms J, Warner ML, Poyner DR, Chung KY, Pioszak AA. Calcitonin receptor N-glycosylation enhances peptide hormone affinity by controlling receptor dynamics. Journal of Molecular Biology. 2020:423(7):1996-2014. doi: 10.1016/j.jmb.2020.01.028
54. Ghosh E, Dwivedi H, Baidya M, Srivastava A, Kumari P, Stepniewski T, Kim HR, Lee M-H, Gstel J, Chaturvedi M, Roy D, Pandey S, Maharana J, Guixà‐Gonzàlez R, Luttrell LM, Chung KY, Dutta S, Selent J, Shukla AK. Conformational sensors and domain-swapping reveal structural and functional differences between the beta-arrestin isoforms. Cell Reports. 2019:28(13):3287-3299.e6. doi: 10.1016/j.celrep.2019.08.053
53. Du Y, Duc NM, Rasmussen SGF, Hilger D, Kubiak X, Wang L, Bohon J, Kim HR, Wegrecki M, Asuru A, Jeong KM, Lee JM, Chance MR, Lodowski DT*, Kobilka BK*, Chung KY*. Assembly of a GPCR-G protein complex. Cell. 2019:177(5):1232-1242.e11. doi: 10.1016/j.cell.2019.04.022
52. Park JY, Qu C, Li R, Yang F, Tian Z, Shen Y, Cai B, Yun Y, Sun J*, Chung KY*. Structural mechanism of the arrestin-3/JNK3 interaction. Structure. 2019:27(7):1162-1170e3. doi: 10.1016/j.str.2019.04.002
51. Yang H-S, Sun N, Zhao X, Kim HR, Park H-J, Kim K-M*, Chung KY*. Role of helix 8 in dopamine receptor signaling. Biomolecules & Therapeutics. 2019:27(6):514-521. doi: 10.4062/biomolther.2019.026
50. Ki AY, Park JY, Chung KY*. Conformational changes of JNK3 splice variants upon ATP binding. Biodesign. 2019:7(1):1-5.
49. Lisnyansky Bar-El M, Lee SY, Ki AY, Kapelushnik N, Loewenstein A, Chung KY, Schneidman-Duhovny D, Giladi M, Newman H, Haitin Y. Structural characterization of full-length human dehydrodolichyl diphosphate synthase using an integrative computational and experimental approach. Biomolecules. 2019:9:660 doi: 10.3390/biom9110660
48. Ham S, Kim H, Hwang S, Kang H, Yun SP, Kim S, Kim D, Kwon HS, Lee YS, Cho M, Shin HM, Choi H, Chung KY, Ko HS, Lee GH, Lee Y. Cell-Based Screen Using Amyloid Mimic β23 Expression Identifies Peucedanocoumarin III as a Novel Inhibitor of α-Synuclein and Huntingtin Aggregates. Molecules and Cells. 2019:42(6):480-494. doi: 10.14348/molcells.2019.0091
47. Park BB, Choi JW, Park Y, Choi D, Paek J, Kim HJ, Son S-Y, Mushtaq AU, Shin H, Kim SH, Zhou Y, Lim TH, Park JY, Baek J-Y, Kim K, Kwon H, Son SH, Chung KY, Jeong H-J, Kim H-M, Jung WY, Lee K, Lee K, Byun Y, Jeon YH. Structure-activity relationships of Baicalein and its analogs as novel TSLP inhibitors. Scientific Reports. 2019:9(1):8762. doi: 10.1038/s41598-019-44853-5
46. Jang S, Kang C, Yang H-S, Jung T, Hebert H, Chung KY, Hohng S, and Song J-J. Structural basis of recognition and destabilization of histone H2B ubiquitinated nucleosome by DOT1L histone H3 Lys79 methyltransferase. Genes & Development. 2019:33(11-22):620-625. doi: 10.1101/gad.323790.118
45. Giladi M, Lee SY, Refaeli B, Hiler R, Chung KY*, Khananshvili D*. Structure-dynamic and functional relationships in a Li+-transporting sodium-calcium exchanger mutant. BBA-Bioenergetics. 2019:1860(3):189-200. doi: 10.1016/j.bbabio.2018.11.015
44. Bang I, Kim HR, Beaven AH, Kima J, Ko SB, Lee GR, Lee H, Im W, Seok C, Chung KY*, Choi H-J*. Biophysical and functional characterization of Norrin signaling through Frizzled4. Proceedings of the National Academy of Science USA. 2018:115(35):8787-8792. doi: 10.1073/pnas.1805901115
43. Liu H, Kim HR, Deepak RNVK, Wan L, Chung KY, Fan H, Wei Z, and Zhang C. Orthosteric and allosteric action of the C5a receptor antagonists. Nature Structural and Molecular Biology. 2018:25(6):472-481. doi: 10.1038/s41594-018-0067-z
42. Zhang DL, Sun YJ, Ma ML, Wang YJ, Lin H, Li RR, Liang ZL, Gao Y, Yang Z, He DF, Lin A, Mo H, Lu YJ, Li MJ, Kong W, Chung KY, Yi F, Li JY, Qin YY, Li J, Thomsen ARB, Kahsai AW, Chen ZJ, Xu ZG, Liu M, Li D, Yu X, and Sun JP. Gq activity- and beta-arrestin-1 scaffolding-mediated ADGRG2/CFTR coupling are required for male fertility. Elife. 2018:7:e33432. doi: 10.7554/eLife.33432
41. Kim HR, Duc NM, and Chung KY*. Comprehensive analysis of non-synonymous natural variants of G protein-coupled receptors. Biomolecules & Therapeutics. 2018:26(2):101-108. doi: 10.4062/biomolther.2017.073
40. Park JY, Kim HR, and Chung KY*. Chapter 9. Localization of Conformational Dynamics of Arrestins by HDX-MS. The structural Basis of Arrestin Functions. (ISBN: 978-3-319-57552-0 (Print) 978-3-319-57553-7 (Online)) Invited book chapter. 10.1007/978-3-319-57553-7
39. Komolove KE, Du Y, Duc NM, Betz RM, Rodrigues JPGLM, Leib RD, Patra D, Skiniotis G, Adams CM, Dror R, Chung KY, Kobilka BK, and Benovic JL. Structural and functional analysis of b2-adrenergic receptor complex with GRK5. Cell. 2017:169(3):407-421. doi: 10.1016/j.cell.2017.03.047
38. Park JY, Yun Y, and Chung KY*. Conformations of JNK3α splice variants analyzed by hydrogen/deuterium exchange mass spectrometry. Journal of Structural Biology. 2017:197(3):271-278. doi: 10.1016/j.jsb.2016.12.005
37. Duc NM, Kim HR, and Chung KY*. Recent progress in understanding the conformational mechanism of heterotrimeric G protein activation. Biomolecules & Therapeutics. 2017:25(1):4-11. doi: 10.4062/biomolther.2016.169
36. Han SS, Min MK, Lee SY, Lim CW, Bhatnagar N, Lee Y, Shin D, Chung KY, Lee SC, Kim BG, and Lee S. Modulation of ABA Signaling by Altering VxGΦL Motif of PP2Cs in Oryza sativa. Molecular Plant. 2017:10(9):1190-1205. doi: 10.1016/j.molp.2017.08.003
35. Giladi M, Lee SY, Ariely Y, Teldan Y, Granit R, Strulevich R, Haitin Y, Chung KY*, and Khananshvili D*. Structure-based dynamic diversity in regulatory domains of sodium-calcium exchanger (NCX) isoforms. Scientific Reports. 2017:7:993. doi: 10.1038/s41598-017-01102-x
34. Lee SY, Yoo HS, Choi HS, Chung KY*, and Seo MD*. Structural and dynamic insights into the subtype-specific IP3 binding mechanism of IP3 receptor. Biochemical Journal. 2016:473(20):3533-3543. doi: 10.1042/BCJ20160539
33. Lee SY, Giladi M, Bohbot H, Hiller R, Chung KY*, and Khananshvili D*. Structure-dynamic basis of splicing dependent regulation in tissue-specific variants of the sodium-calcium exchanger (NCX1). FASEB Journal. 2016:30(3):1356-1366. doi: 10.1096/fj.15-282251
32. Lee KY, Choi HS, Choi HS, Chung KY, Lee BJ, Maeng HJ, and Seo MD. Quercetin directly interacts with vitamin D (VDR): Structural implication of VDR activation by quercetin. Biomolecules and Therapeutics. 2016:24(2):191-198. doi: 10.4062/biomolther.2015.122
31. Kim MH, Kim YJ, Kim HR, Chung KY*, and Kim MK*. Computational simulation of the activation cycle of Gα subunit in the G protein cycle using an elastic network model. Plos One. 2016:11(8):e0159528. doi: 10.1371/journal.pone.0159528
30. Park JY, Lee SY, Kim HR, Seo MD, and Chung KY*. Structural mechanism of GPCR-arrestin interaction: recent breakthroughs. Archives of Pharmacal Research. 2016:39(3):293-301. doi: 10.1007/s12272-016-0712-1
29. Lee SY, Yun Y, Kim HR, and Chung KY*. Conformational analysis of β-Arrestin2 pre-activated mutant p44 by hydrogen/deuterium exchange mass spectrometry. Biodesign. 2015:3(4):162-167.
28. Kim DK, Yun Y, Kim HR, Seo MD, and Chung KY*. Different Conformational Dynamics of Various Active States of β-Arrestin1 Analyzed by Hydrogen/Deuterium Exchange Mass Spectrometry. Journal of Structural Biology. 2015:190(2):250-9. doi: 10.1016/j.jsb.2015.04.006
27. Duc NM, Kim HR, and Chung KY*. Structural mechanism of G protein activation by G protein-coupled receptor. European Journal of Pharmacology. 2015:763(Pt B):214-222. (Invited review article) doi: 10.1016/j.ejphar.2015.05.016
26. Duc NM, Du Y, Thorsen TS, Lee SY, Zhang C, Kato H, Kobilka BK*, and Chung KY*. Effective Application of Bicelles for Conformational Analysis of G Protein-Coupled Receptors by Hydrogen/Deuterium Exchange Mass Spectrometry. Journal of the American Society for Mass Spectrometry. 2015:26(5):808-17. doi: 10.1007/s13361-015-1083-4
25. Li S, Lee SY, and Chung KY*. Conformational Analysis of G Protein-Coupled Receptor Signaling by Hydrogen/deuterium Exchange Mass Spectrometry. Methods in Enzymology. 2015:557:261-78. doi: 10.1016/bs.mie.2014.12.004
24. Yun Y. Kim DK, Kim KM, Seo MD, and Chung KY*. Different Conformational Dynamics of beta-Arrestin1 and beta-Arrestin2 Analyzed by Hydrogen/Deuterium Exchange Mass Spectrometry. Biochemical and Biophysical Research Communications. 2015:457(1):50-7. doi: 10.1016/j.bbrc.2014.12.079
23. Ko IY, Kim DK, and Chung KY*. Structural analysis of muscarinic acetylcholine receptor type 1 intracellular loop 3 by hydrogen/deuterium exchange mass spectrometry. Protein & Peptide Letters. 2015:22(1):94-100.
22. Lee YS, Yoon WS, Chung I, Chung KY, Won HS, and Seo MD. Backbone NMR assignments of an uncharacterized protein, SF1002 from Shigella flexneri 5a M90T. Journal of the Korean Magnetic Resonance Society. 2015:19:36-41.
21. Kim HN, Seok SH, Chung KY, Won HS, Son WS, and Seo MD. Expression, purification and structural characterization of the type 1-specific ATP binding site of IP3 receptor (IP3R1-ATPA). Process Biochemistry. 2015:50(10):1600-1606.
20. Giladi M, Lee SY, Hiller R, Chung KY* and Khananshvili D*. Structure-Dynamic Determinants Governing a Mode of Regulatory Response and Propagation of Allosteric Signal in Splice Variants of Na+/Ca2+ Exchange (NCX) Proteins. Biochemical Journal. 2015:465(3):489-501. doi: 10.1042/BJ20141036
19. Park JY, Duc NM, Kim DK, Lee SY, Li S, Seo MD, Woods VL Jr, and Chung KY*. Different Conformational Dynamics of PDZ1 and PDZ2 in Full-length EBP50 Analyzed by Hydrogen/Deuterium Exchange Mass Spectrometry. Biochemistry and Cell Biology. 2015:93(4):290-7. doi: 10.1139/bcb-2014-0145
18. Lee M, Park H, Jeon SW, Bang J, Chung KY, Choi DW, Kim E, and Lim KM. Novel anti-melanogenic hexapeptoids, PAL-10 and PAL-12. Archives of Dermatological Research. 2015:307(3):249-57. doi: 10.1007/s00403-015-1555-1
17. Chung KY*. Structural Aspects of GPCR-G Protein Coupling. Toxicological Research. 2013(29):149-55. (Reveiw article) doi: 10.5487/TR.2013.29.3.149
16. Kim TH, Chung KY, Manglik A, Hansen AL, Dror RO, Shaw DE, Kobilka BK, and Prosser RS. The Role of Ligands on the Equilibria Between Functional States of a G Protein-Coupled Receptor. Journal of the American Chemical Society. 2013:135(25):9465-74. doi: 10.1021/ja404305k
15. Chung KY*, Day PW, Vélez-Ruiz G, Sunahara RK, and Kobilka BK*. Identification of GPCR-Interacting Cytosolic Proteins Using HDL Particles and Mass Spectrometry-Based Proteomic Approach. Plos One. 2013:8(1):e54942. doi: 10.1371/journal.pone.0054942
14. Chung KY, Kim TH, Manglik A, Alvares R, Kobilka BK, and Prosser RS. The role of detergents on conformational exchange of a G protein-coulpled receptor. Journal of Biological Chemistry. 2012:287(43):36305-11. (Faculty of 1000 Recommended) doi: 10.1074/jbc.M112.406371
13. Kang M, Walker JW, and Chung KY*. Endothelin receptor overexpression alters diastolic function in cultured rat ventricular myocytes. Biomolecules and Therapeutics. 2012:20(4):386-392. doi: 10.4062/biomolther.2012.20.4.386
12. Kim K, Bae ON, Lim KM, Noh JY, Kang S, Chung KY, and Chung JH. Novel anti-platelet activity of protocatechuic acid through inhibition of high shear stress-induced aggregation. Journal of Pharmacology and Experimental Therapeutics. 2012:343(3):704-11. doi: 10.1124/jpet.112.198242
11. Kang M and Chung KY*. PKC-epsilon mediates multiple endothelin-1 actions on systolic Ca2+ and contractility in ventricular myocytes. Biochemical and Biophysical Research Communications. 2012:423(3):600-5. doi: 10.1016/j.bbrc.2012.06.024
10. Chung KY, Rasmussen SG, Liu T, Li S, DeVree BT, Chae PS, Calinski D, Kobilka BK, Woods VL Jr, and Sunahara RK. Conformational changes in the G protein Gs induced by the beta2 adrenergic receptor. Nature. 2011:477(7366):611-5. (2012 Nobel Chemistry) doi: 10.1038/nature10488
9. Rasmussen SG, DeVree BT, Zou Y, Kruse AC, Chung KY, Kobilka TS, Thian FS, Chae PS, Pardon E, Calinski D, Mathiesen JM, Shah ST, Lyons JA, Caffrey M, Gellman SH, Steyaert J, Skiniotis G, Weis WI, Sunahara RK, and Kobilka BK. Crystal structure of the beta2 adrenergic receptor-Gs protein complex. Nature. 2011:477(7366):549-55. (2012 Nobel Chemistry) doi: 10.1038/nature10361
8. Westfield GH, Rasmussen SG, Su M, Dutta S, DeVree BT, Chung KY, Calinski D, Velez-Ruiz G, Oleskie AN, Pardon E, Chae PS, Liu T, Li S, Woods VL Jr, Steyaert J, Kobilka BK, Sunahara RK, and Skiniotis G. Structural flexibility of the G{alpha}s {alpha}-helical domain in the {beta}2-adrenoceptor Gs complex. Proceedings of the National Academy of Science USA. 2011:108(38):16086-91. doi: 10.1073/pnas.1113645108
7. Chung KY, Kang M and Walker JW. Contractile regulation via ETA requires intact T-tubules in adult rat ventricular myocytes. American Journal of Physiology. 2008:294(5):H2391-9. doi: 10.1152/ajpheart.00011.2008
6. Lim KM, Kim JS, Bae ON, Noh JY, Chung SM, Chung KY, and Chung JH. Co-oxidation-mediated xenobiotic activation and cytotoxicity by 12-lipoxygenase in intact platelets. Toxicology. 2008:247(2-3):154-60. doi: 10.1016/j.tox.2008.02.015
5. Kang M, Chung KY, and Walker JW. G-protein coupled receptor signaling in myocardium: not for the faint of heart. Physiology (Bethesda). 2007:22:174-84. doi: 10.1152/physiol.00051.2006
4. Chung KY and Walker JW. Interaction and inhibitory cross-talk between endothelin and ErbB receptors in the adult heart. Molecular Pharmacology. 2007:71(6):1494-502. doi: 10.1124/mol.106.027599
3. Chung KY, Lim KM, Chung SM, Lee MY, Noh JY, Bae ON and Chung JH. Shear stress-induced pH increase in plasma is mediated by a decrease in P(CO(2)): the increase in pH enhances shear stress-induced P-selectin expression in platelets. Platelets. 2006:17(3):127-33. doi: 10.1080/09537100500437711
2. Chung KY, Lee SJ, Chung SM, Lee MY, Bae ON and Chung JH. Generation of free radical by interaction of iron with thiols in human plasma and its possible significance. Thrombosis Research. 2005:116(2):157-64. doi: 10.1016/j.thromres.2004.11.021
1. Bae ON, Lee JY, Chung GY, Chung SM, Lee MY, Yun YP, Kim YC, Moon CK and Chung JH. Enhanced menadione cytotoxicity in platelets isolated from streptozotocin-induced diabetic rats. Thrombosis Research. 2003:111(3):179-83. doi: 10.1016/j.thromres.2003.09.003