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Publications

 

2021

81. Byeon, I.L., Calero, G., Wu, Y., Byeon, C.H. Jung, J., DeLucia, M., Zhou, X., Weiss, S., Ahn, J., Hao, C., Skowronski, J., Gronenborn, A. M. Structure of HIV-1 Vpr in complex with the human nucleotide excision repair protein hHR23A. Nat. Commun. 12, 6864 (2021)

80. Ni, T., Zhu, Y., Yang, Z., Xu, C., Chaban, Y., Nesterova, T., Ning, J., Bocking, T., Parker, M. W. Monnie, C., Ahn, J., Perilla, J. R., Zhang, P., Structure of native HIV-1 cores and their interactions with IP6 and CypA. Sci. Adv. 7, eabj5715 (2021)

79. Li, M., Sun, W., Tyurin, V.A. DeLucia, M., Ahn, J., Kagan, V. E., and van der Wel PCA. Activation of Cytochrome C peroxidase function through corrdinated foldon loop dynamics upon interaction with anionic lipids. J. Mol. Biol. 433, 167057 (2021).

78. Zhong, Z., Ning, J., Boggs, E. A., Jang, S., Wallace, C., Telmer, C., Bruchez, M. P., Ahn, J., Engelman, A. N., Zhang, P., Watkins, S. C., Ambrose, Z. Cytoplasmic CPSF6 regulates HIV-1 capsid trafficking and infection in a cyclophilin A-dependent manner. mBio. 12, e013142-20 (2021)

77. Zhou, X., Monnie, C., DeLucia, M., Ahn, J. HIV-1 Vpr activates host CRL4-DCAF1 E3 ligase to degrade histone deacetylase SIRT7. Virol. J., 18, 48 (2021)

2020

76. Xu, C., Fischer, D. K., Rankovic, S., Li, W., Dick, R. A., Runge, B., Zadorozhnyi, R., Ahn, J., Aiken, C., Polenova, T., Engelman, A., N., Ambrose, Z., Rousso, I., Perilla, J. R. Permeability of the HIV-1 capsid to metabolites modulate viral DNA synthesis. PLoS Biol. 18, e3001015 (2020)

75. Byeon, I. L., Jung, J., Byeon, C. H. DeLucia, M., Ahn, J., Gronenborn, A. M. Complete 1H, 13C, 15N resonance assignemnts and secondary structure of the Vpr binding region of hHR23A (residues 223-363). Biomol. NMR Assign. 14, 13-17 (2020)

2019

74. Gupta, R., Zhang, H., Lu, M., Hou, G., Caporini, M., Rosay, M., Maas, W., Struppe, J., Ahn, J., Byeon, I. L., Oschkinat, H., Jaudzems, K., Barbet-Massin, E., Emsley, L., Pintacuda, G., Lesage, A., Gronenborn, A. M., Polenova, T. Dyanamic nuclear polarization magic-angle spinning nuclear magnetic resonance combined with molecular dynamics simulations permits detection of order and disorder in viral assemblies. J. Phys. Chem. 123, 5048-5058 (2019)

73. Bares, C. O. Wu, Y., Song, J., Lin, G., Baxter, E. L., Brewster, A. S., Nagarjan, V., Holmes, A., Soltis, S. M., Sauter, N. K., Ahn, J., Cohen, A. E., Calero, G. The crystal structure of dGTPase reveals the molecular basis of dGTP selectivity. Proc. Natl. Acad. Sci. USA 116, 9333-9339 (2019)

72. Li, M., Mandal, A., Tyurin, V. A., DeLucia, M., Ahn, J., Kagan, V.E. Van der Wel, P. C. A. Surface-binding to cardiolipin nanodomains triggers cytochrome c pro-apoptotic peroxidase activity via localized dynamics. Structure 27, 806-815 (2019)

2018

71. Yan, J., Shun, M.-S., Hao, C., Zhang, Y., Qian, J., Hrecka, K., DeLucia, M., Monnie, C. Ahn, J., Skowronski, J. HIV-1 Vpr reprograms CRL4-DCAF1 E3 ubiquitin ligase to antagonize exonuclease 1-mediated restriction of HIV-1 infection. mBio. 9:e01732-18 (2018)

70. Quinn, C. M., Wang, M., Fritz, M. P., Runge, B., Ahn, J., Xu, C., Perila, J. R., Gronenborn, A. M., Polenova, T. Dynamic regulation of HIV-1 capsid interaction with the restriction factor TRIM5a identified by magic-angle spinning NMR and molecular dynamics simulations, Proc. Natl. Acad. Sci. USA 115, 11519-11524 (2018)

2017

69. Zhou, X., Delucia, M., Hao, C., Hrecka, K., Monnie, C., Skowronski, J., Ahn, J. HIV-1 Vpr protein directly loads Helicase-like transcription factor (HLTF) onto the CRL4-DCAF1 E3 ubiquitin ligase. J. Biol. Chem. 292, 21117-21127 (2017)

2016

68. Zhang, H., Hou, G., Lu, M., Ahn, J., Byeon, I.-J. L., Langmead, C. J., Perilla, J. R., Hung, I., Gorkov, P. L., Gan, Z., Brey, W. W., Case, D. A., Schulten, K., Gronenborn, A. M., Polenova, T., HIV-1 Capsid Function is Regulated by Dynamics: Quantitative Atomic-Resolution Insights by Integrating Magic-Angle-Spinning NMR, QM/MM, and MD. J. Am. Chem. Soc. 138(42): 14066-14075 (2016)

67. Jang, S., Zhou, X., Ahn, J. Substrate specificity of SAMHD1 triphosphohydrolase activity is controlled by deoxyribonucleoside triphosphates and phosphorylation at Thr592. Biochemistry 55, 5635-5646 (2016)

66. Wu, Y., Zhou, X., Barnes, C.O., DeLucia, M., Cohen, A.E, Gronenborn, A.M#., Ahn, J.#, Calero, G#. The DDB1-DCAF1-Vpr-UNG2 crystal structure reveals how HIV-1 Vpr steers human UNG2 toward destruction. Nat Struct Mol Biol. 23, 933-940 (2016) #Correspondence

65. Hampp, S., Kiessling, T., Buechle, K., Mansilla, S.F., Thomale, J., Rall, M., Ahn, J., Pospiech, H., Gottifredi, V., Wiesmüller, L. DNA damage tolerance pathway involving DNA polymerase ι and the tumor suppressor p53 regulates DNA replication fork progression. Proc Natl Acad Sci U S A. 113, E4311-4319 (2016)

64. Zhou, X., DeLucia, M., Ahn, J. SLX4/SLX1 independent downregulation of MUS81/EME1 by HIV-1 Vpr. J. Biol. Chem. 291, 16936-16947 (2016) Selected as “a Paper of The Weeek”

63. Saito, A., Henning, M.S., Serrao, E., Dubose, B.N., Teng, S., Huang, J., Li, X., Saito, N., Roy, S.P., Siddiqui, M.A., Ahn, J., Tsuji, M., Hatziioannou, T., Engelman, A.N., Yamashita, M. The capsid-CPSF6 interaction is dispensable for HIV-1 replication in primary cells but is selected during virus passage in vivo. J Virol. 90, 6918-6935 (2016)

62. Beckerman, R., Yoh, K., Mattia-Sansobrino, M., Zupnick, A., Laptenko, O., Karni-Schmidt, O., Ahn, J., Byeon, I-J,, Keezer, S., Prives. C. Lysines in the tetramerization domain of p53 selectively modulate G1 arrest. Cell Cycle, 15, 1425-38 (2016)

61. Stevenson, H.P., Lin, G., Barnes, C.O., Sutkeviciute, I., Krzysiak, T., Weiss, S.C., Reynolds, S., Wu, Y., Nagarajan, V., Makhov, A.M., Lawrence, R., Lamm, E., Clark, L., Gardella, T.J., Hogue, B.G., Ogata, C.M., Ahn, J., Gronenborn, A.M., Conway, J.F., Vilardaga, J.P., Cohen, A.E., Calero, G. Transmission electron microscopy for the evaluation and optimization of crystal growth. Acta Crystallogr D Struct Biol. 72, 603-15 (2016)

60. Liu, C., Perilla, J.R., Ning J, Lu, M., Hou, G., Ramalho, R., Himes, B.A., Zhao, G., Bedwell, G.J., Byeon, I.J., Ahn, J., Gronenborn, A.M., Prevelige, P.E., Rousso, I., Aiken, C., Polenova, T., Schulten, K., Zhang, P.Cyclophilin A stabilizes the HIV-1 capsid through a novel non-canonical binding site. Nat. Commun.  7, 10714 (2016)

59. Gupta, R., Lu, M., Hou, G., Caporini, M. A., Rosay, M., Maas, W. E., Struppe, J. O., Suiter, C. L., Ahn, J., Byeon, I. L., Franks, W. T., Orwick-Rydmark, M., Bertarello, A., Oschkinat, H., Lesage, A., Pintacuda, G., Gronenborn, A. M., Polenova, T. E. Dynamic Nuclear Polarization Enhanced MAS NMR for Structural Analysis of HIV-1 Protein Assemblies. J. Phys. Chem. B. 120. 329-39 (2016)

58. Ahn, J. Functional organization of human SAMHD1 and mechanisms of HIV-1 restriction. Biol. Chem. 397, 373-379 (2016)

2015

57. Lu, M., Hou, G., Zhang, H., Suiter, C.L., Ahn, J., Byeon, I.-L., Perilla, J.R., Langmead, C.J., Hung, I., Gor’kov, P.L., Gan, Z., Brey, W., Aiken, C., Zhang, P., Schulten, K., Gronenborn, A.M., Polenova, T. Dynamic allostery governs cyclophilin A-HIV capsid interplay. Proc. Natl. Acad. Sci. USA 112, 14617-14622 (2015)

56. Mandal, A., Hoop, C.L., DeLucia, M., Kodali, R., Kagan, V.E., Ahn, J., and Van der Wel, P.C.A. Structural Changes and Proapoptotic Peroxidase Activity of Cardiolipin-Bound Mitochondrial Cytochrome c. Biophys. J. 109, 1873-1884 (2015)

55. Li W, Xin B, Yan J, Wu Y, Hu B, Liu L, Wang Y, Ahn J, Skowronski J, Zhang Z, Wang Y, Wang H., SAMHD1 Gene Mutations Are Associated with Cerebral Large-Artery Atherosclerosis. Biomed Res Int. 2015;2015:739586 (2015)

54. Slack RL, Spiriti J, Ahn J, Parniak MA, Zuckerman DM, Ishima R., Structural integrity of the ribonuclease H domain in HIV-1 reverse transcriptase. Proteins. 2015 Aug;83(8):1526-38 (2015)

53. Wu, Y*, Koharudin, L.*, Mehrens, J., DeLucia, M., Byeon, C.-H., Byeon, I.J., Calero, G., Ahn, J.#, and Gronenborn, A. M.#Structural basis of clade-specific engagement of SAMHD1 restriction factors by lentiviral Vpx virulence factors.. J. Biol. Chem. 290, 17935-45 (2105)  *Equal Contribution, #Correspondence

52. Yan J, Hao C, DeLucia M, Swanson S, Florens L, Washburn MP, Ahn J, Skowronski J.Cyclin A2 – CDK regulates SAMHD1 phosphohydrolase domain. J. Biol.Chem. 290, 13279-92. (2015)

2014

51. Koharudin, L.*, Wu, Y.*, DeLucia, M., Mehrens, J., Gronenborn, A. M.#, Ahn, J.Structural basis of allosteric activation of Sterile Alpha Motif and Histidine-Aspartate Domain containing protein 1 (SAMHD1) by nucleoside triphosphates.   J. Biol. Chem.  289, 32617-27. (2014) *Equal Contribution, #Correspondence

50. Vorontsov, I. I.*, Wu, Y.*, DeLucia, M., Minasov, G., Mehrens, M., Shuvalova, L., Anderson, W.F.#, Ahn, J.Mechanisms of allosteric activation and inhibition of the deoxyribonucleoside triphosphate triphosphohydrolase from Enterococcus faecalis. J. Biol. Chem. 289, 2815-2824 (2014)  *Equal Contribution, #Correspondence, “Paper of the Week” and featured as a COVER in Jan. 31, 2014 Print.

49. Jung J, Byeon IJ, Delucia M, Koharudin LM, Ahn J, Gronenborn AM.Binding of HIV-1 Vpr to the Human Homolog of the Yeast DNA Repair Protein RAD23 (hHR23A) Requires Its XPC Binding (XPCB) as Well as the Ubiquitin Associated 2 (UBA2) Domains. J. Biol. Chem. 289 2577-2588 (2014)

48. Mitra, M, Hercík, K, Byeon, IJ, Ahn, J, Hill, S, Hinchee-Rodriguez, K, Singer, D, Byeon, CH, Charlton, LM, Nam, G, Heidecker, G, Gronenborn, AM, Levin, JG. Structural determinants of human APOBEC3A enzymatic and nucleic acid binding properties. Nucleic Acids Res. 42, 1095-1110 (2014)

2013

47. Han, Y, Hou, G, Suiter, CL, Ahn, J, Byeon, IJ, Lipton, AS, Burton, SD, Hung, I, Gor’kov, PL, Gan, Z, Brey, WW, Rice, D, Gronenborn, AM, Polenova, TE. Magic Angle Spinning NMR Reveals Sequence-Dependent Structural Plasticity, Dynamics, and the Spacer Peptide 1 Conformation in HIV-1 Capsid Protein Assemblies. J Am Chem Soc. 135, 17793-17803 (2013)

46. Ji, X*, Wu, Y*, Yan, J*, Mehrens, J, Yang, H, Delucia, M, Hao, C, Gronenborn, AM, Skowronski, J, Ahn, J#, Xiong, Y#. Mechanism of allosteric activation of SAMHD1 by dGTP. Nat Struct Mol Biol. 20, 1304-1309 (2013) *Equal contribution, #Correspondence

45. Fregoso, O. I., Ahn, J., Wang, C., Mehrens, J., Skowronski, J.#, and Emerman, M.# Evolutionary toggling of Vpx/Vpr specificity results in divergent recognition of the restriction factor SAMHD1. PLoS Pathog.  9,  e1003496 (2013) #Correspondence

44. DeLucia, M.*, Mehrens, M.*, Wu, Y., and Ahn, JHIV-2 and SIVmac accessory virulence factor Vpx down-regulates SAMHD1 enzyme catalysis prior to proteasome-dependent degradation.  J. Biol. Chem. 288, 19116-19126 (2013) *Equal contribution

43. Zhao, G., Perilla, J. R., Yufenyuy, E. L., Meng, X., Chen, B., Ning, J., Ahn, J., Gronenborn, A. M., Schulten, K., Aiken, C., and Zhang, P. Mature HIV-1 capsid structure by cryo-electron microscopy and all-atom molecular dynamics. Nature 497, 643-646 (2013); Cited more than 100 times (Web of Science)

42. Byeon, I.-J. L., Ahn, J., Mitra, M., Byeon, C.-H., Hercik, K., Hritz, J., Charlton, L. M., Levin, J. G., and Gronenborn, A. M. NMR structure of human restriction factor APOBEC3A reveals substrate binding and enzyme specificity. Nat. Commun. 4, 1890 (2013)

41. Yan, J., Kaur, S., DeLucia, M., Hao, C., Mehrens, J., Wang, C., Golczak, M., Palczewski, K., Gronenborn, A.M. Ahn, J.#, Skowronski, J.# Tetramerization of SAMHD1 is required for biological activity and inhibition of HIV infection. J. Biol. Chem. 288, 10406-10417 (2013) #Correspondence; Cited more than 30 times (Web of Science)

40. Shah, V., Shi, K., Hout, D., Oztop, I., Krishnan, L., Ahn, J., Shotwell, M., Engelman, A., and Aiken, C. The host proteins transportin SR2/TNPO3 and cyclophilin A exert opposing effects on HIV-1 uncoating. J. Virol 87, 422-432 (2013); Cited more than 30 times (Web of Science)

2012
39. Hou, G., Byeon, I.-J., Ahn, J., Gronenborn, A. M. and Polenova, T. Recoupling of chemical shift anisotropy by R-symmetry sequences in magic angle spinning NMR spectroscopy. J. Chem. Phys. 132, 134201 (2012)

38. Meng, X., Zhao, G., Yufenyuy, E., Ke, D., Ning, J., DeLucia, M., Ahn, J., Gronenborn, A. M., Aiken, C., and Zhang, P. Protease cleavage leads to formation of mature trimer interface in HIV-1 capsid.PLOS Pathog. 8, e1002886 (2012)

37. Christen, M. T., Menon, L., Myshakina, N. A., Ahn, J., Parniak, M. A., and Ishima, R. Structural basis of the allosteric inhibitor interaction on the HIV-1 reverse transcriptase RNase H domain. Chem. Biol. Drug Des. 80, 706-716 (2012)

36. Yang, R., Shi, J., Byeon, I.-J., Ahn, J., Sheehan, J. H., Meiler, J., Gronenborn, A. M., and Aiken, C. Second-site suppressors of HIV-1 capsid mutations: restoration of intracellular activities without correction of intrinsic capsid stability defects. Retrovirology 9, 30 (2012)

35. Byeon, I.-J., Hou, G., Han, Y., Suiter, C., Ahn, J., Jung, J., Byeon, C.-H., Gronenborn, A. M., and Polenova, T. Motions on the millisecond time scale and multiple conformations of HIV-1 capsid protein: implications for structural polymorphism of CA assemblies. J. Am. Chem. Soc. 134, 6455-6466 (2012)

34. Ahn, J., Hao, C., Yan, J., DeLucia, M., Mehrens, J., Wang, C., Gronenborn, AM., and Skowronski, J. HIV/simian immunodeficiency virus (SIV) accessory virulence factor Vpx loads the host cell restriction factor SAMHD1 onto the E3 ubiquitin ligase complex CRL4DCAF1. J. Biol. Chem. 287, 12550-12558 (2012); Cited more than 30 times (Web of Science)

33. Sun, S., Han, Y., Paramasivam, S., Yan, S., Siglin, A.E., Williams, J.C., Byeon, I-J, Ahn, J., Gronenborn A.M., Polenova, T. Solid-state NMR spectroscopy of protein complexes. Methods Mol Biol. 831:303-31 (2012)

2011
32. Hou, G., Byeon, I-J, Ahn, J., Gronenborn A.M., and Polenova, T. 1H-13C/1H-15N heteronuclear dipolar recoupling by R-symmetry sequences under fast magic angle spinning for dynamics analysis of biological and organic solids. J Am Chem Soc. 133, 18645-18655 (2011)

31. Hou, G., Yan, S., Sun, S., Han, Y., Byeon, I-J, Ahn, J., Concel, J., Samoson, A., Gronenborn, A.M., and Polenova, T. Spin diffusion driven by R-symmetry sequences: applications to homonuclear correlation spectroscopy in MAS NMR of biological and organic solids. J Am Chem Soc. 133, 3943-3953 (2011)

30. Myint, W., Gong, Q., Ahn, J., and Ishima, R. Characterization of sarcoplasmic reticulum Ca2+ ATPase nucleotide binding domain mutants using NMR spectroscopy.Biochem Biophys Res Commun. 405, 19-23 (2011)

29. Zhao, G., Ke, D., Vu, T., Ahn, J., Shah, V.B., Yang, R., Aiken, C., Charlton, L.M., Gronenborn, A.M., and Zhang, P. Rhesus TRIM5α disrupts the HIV-1 capsid at the inter-hexamer interfaces. PLOS Pathog. e1002009 (2011); Cited more than 30 times (Web of Science)

28. Ahn, J.#, Novince, Z., Concel, J., Byeon, C-H, Makhov, A.M., Byeon, I-J, Zhang, P., and Gronenborn, A.M.# The Cullin-RING E3 ubiquitin ligase CRL4-DCAF1 complex dimerizes via a short helical region in DCAF1. Biochemistry 50, 1359-1367 (2011) #Correspondence

27. Jung, J., Byeon, I-J, Ahn, J., and Gronenborn, A.M. Structure, dynamics, and Hck interaction of full-length HIV-1 Nef. Proteins. 79, 1609-1622 (2011)

26. Du, S., Betts, L., Yang, R., Shi, H., Concel, J., Ahn, J., Aiken, C., Zhang, P, and Yeh, J.I. Structure of the HIV-1 full-length capsid protein in a conformationally trapped unassembled state induced by small-molecule binding. J. Mol. Biol. 406, 371-386 (2011)

25. Gong, Q., Menon, L., Ilina, T., Miller, L.G., Ahn, J., Parniak, M.A., and Ishima, R. Interaction of HIV-1 reverse transcriptase ribonuclease H with an acylhydrazone inhibitor. Chem. Biol. Drug Des. 77, 39-47 (2011)

2010
24. Ahn, J.#, Vu, T., Novince, Z., Guerrero-Santoro, J., Rapic-Otrin, V., and Gronenborn, A.M. HIV-1 Vpr loads uracil DNA glycosylase-2 onto DCAF1, a substrate recognition subunit of a cullin 4A-ring E3 ubiquitin ligase for proteasome-dependent degradation. J Biol Chem.;285:37333-41 (2010) #Correspondence; Cited more than 30 times (Web of Science)

23. Dikeakos, J.D., Atkins, K.M., Thomas, L., Emert-Sedlak, L., Byeon, I-J., Jung, J., Ahn, J., Wortmann, M.D., Kukull, B., Saito, M., Koizumi, H., Williamson, D.M., Hiyoshi, M., Barklis, E., Takiguchi, M., Suzu, S., Gronenborn, A.M., Smithgall, T.E., Thomas, G. Small molecule inhibition of HIV-1-induced MHC-I down-regulation identifies a temporally regulated switch in Nef action. Mol Biol Cell. 21:3279-92. (2010)

22. Poyurovsky, M.V., Katz, C., Laptenko, O., Beckerman, R., Lokshin, M., Ahn, J., Byeon, I-J., Gabizon, R., Mattia, M, Zupnick, A., Brown, L.M., Friedler, A., and Prives, C. The C terminus of p53 binds the N-terminal domain of MDM2. Nat. Struct. Mol. Biol. 8, 982-989 (2010); Cited more than 30 times (Web of Science)

21. Ahn, J., Byeon, I-J., Dharmasena, S., Huber, K., Concel, J., Gronenborn, A.M., and Sluis-Cremer, N. The RNA binding protein HuR does not interact directly with HIV-1 reverse transcriptase and does not affect reverse transcription in vitro. Retrovirology 7, 40 (2010)

20. Han, Y., Ahn, J., Concel, J., Byeon, I-J., Gronenborn, A.M., Yang, J., and Polenova, T. Solid-state NMR studies of HIV-1 capsid protein assemblies. J Am Chem Soc. 132, 1976-1987 (2010); Cited more than 50 times (Web of Science)

19. Jung, J, Byeon, I-J., Ahn, J., Concel, J., and Gronenborn, A.M. 1H, 15N and 13C assignments of the dimeric C-terminal domain of HIV-1 capsid protein. Biomol. NMR Assign. 4, 21-23 (2010)

2009
18. Byeon, I-J., Meng, X., Jung, J., Zhao, G., Yang, R., Ahn, J., Shi, J., Concel, J., Aiken, C., Gronenborn, A.M., and Zhang, P. Structural convergence between Cryo-EM and NMR reveals intersubunit interactions critical for HIV-1 capsid function. Cell 139, 780-790 (2009); Cited more than 50 times (Web of Science)

17. Hu, L.A., Zhou, T., Ahn, J., Wang, S., Zhou, J., Hu, Y., and Liu, Q. Human and mouse trace amine-associated receptor 1 have distinct pharmacology towards endogenous monoamines and imidazoline receptor ligands. Biochem J. 424, 39-45 (2009)

16. Ahn, J., Poyurovsky, M.V., Baptiste, N., Beckerman, R., Cain, C., Mattia, M., Mckinney, K., Zhou, J., Zupnick, A., Gottifredi, V., and Prives, C. Dissection of the sequence-specific DNA binding and exonuclease activities reveals a superactive yet apoptotically impaired mutant p53 protein. Cell Cycle 8, 1603-1615 (2009)

15. Ahn, J.*, Byeon, I-J.*, Byeon, C-H.*, and Gronenborn, A.M. Insight into the structural basis of pro- and antiapoptotic p53 modulation by ASPP proteins.  J Biol Chem. 284, 13812-22 (2009) Equal contribution; Cited more than 30 times (Web of Science)

1996-2008
14. Kass, E.M., Ahn, J., Tanaka, T., Freed-Pastor, W.A., Keezer, S., and Prives, C. Stability of checkpoint kinase 2 is regulated via phosphorylation at serine 456. J. Biol. Chem. 282, 30311- 30321 (2007)

13. Desgranges, Z.P., Ahn, J., Lazebnik, M.B., Ashworth, T., Lee, C., Pestell, R.C., Rosenberg, N., Prives, C., and Roy, A.L. Inhibition of TFII-I dependent cell cycle regulation by p53. Mol. Cell. Biol. 25, 10940-10952 (2005)

12. Ahn, J., Urist, M., and Prives, C. The Chk2 protein kinase. DNA Repair 3, 1039-1047 (2003); Cited more than 100 times(Web of Science)

11. Ahn, J., Urist, M., and Prives, C. Questioning the role of Chk2 in the p53 DNA damage response. J. Biol. Chem. 278, 20480-20489 (2003); Cited more than 50 times (Web of Science)

10. Ahn, J. and Prives, C. Chk2 monomers and dimers phosphorylates Cdc25C after DNA damage regardless of threonine-68 phosphorylation. J. Biol. Chem. 277, 48418-48426 (2002); Cited more than 50 times (Web of Science)

9. Ahn, J. and Prives, C. The C-terminus of p53: The more you learn the less you know. Nat. Struct. Biol. 8, 730-732 (2001)

8. Gaiddon, C., Lokshin, M., Ahn, J., Zhang, T., and Prives, C. A subset of tumor derived mutant forms of p53 down-regulate p63 and p73 through a direct interaction with the p53 core domain. Mol. Cell. Bio. 21, 1874-1887 (2001)

7. Zhou, J., Ahn, J., Wilson, S.H., and Prives, C, A role for p53 in base excision repair. EMBO. J. 20, 914-923 (2001); Cited more than 200 times (Web of Science)

6. Cain, C., Miller, S., Ahn, J., and Prives, C. The N-terminus of p53 regulates its dissociation from DNA. J. Biol. Chem. 275, 39944-39953 (2000); Cited more than 30 times (Web of Science)

5. Shieh, S-Y., Ahn, J., Tamai, K., Taya, Y., and Prives, C. The human homologs of check point kinases Chk1 and cds1(Chk2) phosphorylates p53 at multiple DNA damage-inducible sites. Genes&Dev. 14, 289-300 (2000); Cited more than 500 times  (Web of Science)

4. Ahn, J., Kraynov, V.S., Zhong, X., Werneburgh, B.G., and Tsai, M-D. DNA polymerase beta: Effects of gapped DNA substrates on DNA specificity, fidelity, processivity, and conformational changes. Biochem. J. 331, 79-87 (1998); Cited more than 50 times (Web of Science)

3. Kraynov, V.S, Werneburg, B.G., Zhong, X., Lee, H., Ahn, J., and Tsai, M-D. DNA polymerase beta: Contribution of Tyrosine-271 and Asparagine-279 to substrate specificity and fidelity of DNA replication. Biochem. J. 323, 103-111 (1997); Cited more than 50 times (Web of Science)

2. Ahn, J., Werneburgh.,B.G., and Tsai, M-D. DNA polymerase beat: Structure-fidelity relationship from pre-steady state kinetic analyses of all possible correct and incorrect base pairs for wild type and R283 mutants. Biochemistry 36, 1100-1107 (1997); Cited more than 100 times (Web of Science)

1. Werneburg, B.G., Ahn, J., Zhong, X., Hondal, R., Kraynov, V.S., and Tsai, M-D. A structural and functional characterization of rat DNA polymerase beta and R283 mutants. Biochemistry 35, 7041-7050 (1996); Cited more than 100 times (Web of Science)