Publications of Min Guo, Ph.D.
40. Doherty, J. R. and Guo, M. (2014). Nucleic Acid | tRNA. Encyclopedia of Cell Biology, Elsevier. [Book chapter, in press].
39. Naganuma, M., Sekine, S., Chong, Y., Guo, M, Yang, X.-L., Gamper, H., How, Y. M., Schimmel, P., and Yokoyma, S. (2014). The selective tRNA aminoacylation mechanism based on a single G·U pair. Nature 510: 507-511.
38. Lo, W. S., Gardiner, E., Xu, Z. W., Lau, C. F., Wang, F., Zhou, J., Mendlein, J. D., Nangle, L. A., Chian, K. P., Yang, X.-L., Au, K. F., Wong, W. H., Guo, M., Zhang, M., and Schimmel, P. (2014). Human tRNA synthetase catalytic nulls with diverse functions. Science 345: 328-332.
37. Kim, D. G., Lee, J. Y., Kwon, N. H., Fang, P., Zhang, Q., Wang, J., Young, N. L., Guo, M., Cho, H. Y., Mushtaq, A. U., Jeon, Y. H., Choi, J. W., Han, J.M., Kang, H. W., Joo, J. E., Hur, Y., Kang, W., Yang, H., Nam, D. H., Lee, M. S., Lee, J. W., Kim, E. S., Moon, A., Kim, K., Kim, D., Kang, E. J., Moon, Y., Rhee, K. H., Han, B. W., Yang, J. S., Han, G., Yang, W. S., Lee, C., Wang, M. W., and Kim, S. (2014). Chemical inhibition of prometastatic lysyl-tRNA synthetase-laminin receptor interaction. Nat. Chem. Biol. 10: 29-34.
36. Guo, M. and Yang, X.-L. (2014). Architecture and Metamorphosis. Top Curr. Chem. 344: 89-118.
35. Gonzalez, M., Mclaughlin, H., Houlden, H., Guo, M., Tsen, L. Y., Hadjivassilious, M., Speziani, F., Yang, X.-L., Antonellis, A., Reilly, M. M., and Zuchner, S. (2013). Exome sequencing identifies a loss-of-function mutation in methionyl-tRNA synthetase (MARS) in a family with CMT2. J. Neurol. Neurosurg. Psychiatry 84: 1247-1249.
34. Guo, M. and Schimmel, P. (2013). Essential nontranslational functions of tRNA synthetases. Nat. Chem. Biol. 9: 145-153.
33. Ofir-Birin, Y., Fang, P., Bennett, S. P., Zhang, H. M., Wang, J., Rachmin, I., Shapiro, R., Song, J., Dagan, A., Kim, S., Marshall, A. G., Schimmel, P., Yang, X.-L., Nechushtan, H., Razin, E., and Guo, M. (2013). Structural switch of lysyl-tRNA synthetase function between translation and transcription. Mol. Cell 49: 30-42.
32. Wang, J., Fang, P., Schimmel, P., and Guo, M. (2012). Side chain independent recognition of aminoacyl-adenylates by the Hint1 transcription suppressor. J. of Phys. Chem. B. 116: 6798-6805.
31. Guo, M. and Schimmel, P. (2012). Homeostatic mechanism by alternative forms of tRNA synthetases. Trends Biochem. Sci. 37: 401-403.
30. Park, M. C., Kang, T., Jin, D., Han, J. M., Kim, S. B., Park, Y. C., Cho, K., Park, Y. W., Guo, M., He, W., Yang, X.-L, Schimmel, P., and Kim, S. (2012). Secreted human Gly-tRNA synthetase implicated in defense against ERK-activated tumorigenesis. Proc. Natl. Acad. Sci. U S A. 109: E640-647.
29. Sajish, M., Zhou, Q., Kishi, S., Valdez, D. J., Kapoor, M., Guo, M., Kim, S., and Yang, X.-L. (2012). Trp-tRNA synthetase bridges DNA-PKcs to PARP-1 to link IFN-γ and p53 signaling. Nat. Chem. Biol.. 8: 547-554.
28. Xu, X., Shi, Y., Zhang, H.-M., Marshall, A. G., Guo, M., Kishi, S., and Yang, X.-L. (2012). Unique domain appended to vertebrate tRNA synthetase is essential for vascular development. Nat. Comm. 3: 681.
27. Guo, M. and Schimmel, P. (2012). Structural analyses clarify the complex control of mistranslation by tRNA synthetases. Curr. Opin. Struct. Biology. 22: 119-126.
26. Jones, J. E., Slack, J. L., Fang, P., Zhang, X., Subramanian, V., Causey, C. P., Coonrod, S. A., Guo, M., and Thompson, P. R. (2012). Synthesis and screening of a haloacetamidine containing library to identify PAD4 selective inhibitors. ACS Chem. Biol. 7: 160-165.
25. Kumar, A., Park, H., Fang, P., Parkesh, R., Guo, M., Nettles, K. W., Disney, M. D. (2011). Myotonic dystrophy type 1 RNA crystal structures reveal heterogeneous 1x1 nucleotide UU internal loop conformations. Biochemistry 50: 9928-9935.
24. He, W., Zhang, H.-M., Chong, Y. E., Guo, M., Marshall, A. G., and Yang, X.-L. (2011). Dispersed disease-causing neomorphic mutations on a single protein promote the same localized conformational opening. Proc. Natl. Acad. Sci. U S A. 108: 12307-12312.
23. Kumar, A., Fang, P., Park, H., Guo, M., Nettles, K. W., and Disney, M. D. (2011). A crystal structure of a model of the repeating r(CGG) transcript found in fragile X syndrome. Chembiochem. 12: 2140-2142.
22. Fang, P., Zhang, H.-M,, Shapiro, R., Marshall, A. G., Schimmel, P., Yang, X.-L.*, and Guo, M.* (2011). Structural context for mobilization of a human tRNA synthetase from its cytoplasmic complex. Proc. Natl. Acad. Sci. U S A. 108: 8239-8244 (*Co-corresponding author).
21. Guo, M., Shapiro, R., Morris, G. M., Yang, X.-L., and Schimmel, P. (2010). Packaging HIV virion components through dynamic equilibria of a human tRNA synthetase. J. Phys. Chem. B 114: 16273-16279.
20. Guo, M., Yang, X.-L., and Schimmel, P. (2010). New functions of tRNA synthetases beyond translation. Nat. Rev. Mol. Cell Biol. 11: 668-674.
19. Guo, M., Shapiro, R., Schimmel, P., and Yang, X.-L. (2010). Introduction of a leucine half-zipper engenders multiple high quality crystals of a recalcitrant tRNA synthetase. Acta Cryst. D. 66: 243-250.
18. Guo, M., Schimmel, P., and Yang, X.-L. (2010). Functional expansion of human tRNA synthetases achieved by structural inventions. FEBS Lett. 584: 434-442.
17. Zhou, Q., Kapoor, M., Guo, M., Belani, R., Xu, X., Kiosses, W. B., Hanan, M., Park, C., Armour, E., Do, M. H., Nangle, L. A., Schimmel, P., and Yang, X.-L. (2010). Orthogonal use of a human tRNA synthetase active site to achieve multifunctionality. Nat. Struct. Mol. Biol. 17: 57-61.
16. Guo, M., Chong, Y. E., Shapiro, R., Beebe, K., Yang, X.-L., and Schimmel, P. (2009). Paradox of mistranslation of serine for alanine caused by AlaRS recognition dilemma. Nature 462: 808-812.
15. Guo, R.T., Chong, Y. E., Guo, M., and Yang, X.-L. (2009). Crystal structures and biochemical analyses suggest unique mechanism and role for human GlyRS in Ap4A homeostasis. J. Biol. Chem. 284: 28968-28976.
14. Guo, M., Chong, Y. E., Beebe, K., Shapiro, R., Yang, X.-L., and Schimmel, P. (2009). The C-Ala domain brings together editing and aminoacylation functions on one tRNA. Science 325: 744-777.
13. Schimmel, P., and Guo, M. (2009). A tipping point for mistranslation and disease. Nat. Struct. Mol. Biol. 16: 348-349.
12. Schimmel, P., and Guo, M. (2009). Ancient tRNA synthetase meets modern structural biology. Structure 17: 315-317.
11. Guo, M., Ignatov, M., Musier-Forsyth, K., Schimmel, P., and Yang, X.-L. (2008). Crystal structure of tetrameric form of human lysyl-tRNA synthetase: Implications for multisynthetase complex formation. Proc. Natl. Acad. Sci. U S A. 105: 2331-2336.
10. Beebe, K., Waas, W., Druzina, Z., Guo, M., and Schimmel, P. (2007). A universal plate format for increased throughput of assays that monitor multiple aminoacyl transfer RNA synthetase activities. Anal Biochem. 368: 111-121.
9. Yang, X.-L., Guo, M., Kapoor, M., Ewalt, K. L., Otero, F. J., Skene, R. J., McRee, D. E., and Schimmel, P. (2007). Functional and crystal structure analysis of active site adaptations of a potent anti-angiogenic human tRNA synthetase. Structure 15: 793-805.
8. Fang, P., Wang, J., Li, X., Guo, M., Xing, L., Cao, X., Zhu, Y., Gao, Y., Niu, L., and Teng, M. (2009). Crystallization and preliminary X-ray analysis of Escherichia coli Rnase G. Acta Cryst. F. 65: 586-588.
7. Guo, M., Xu, F., Yamada, J., Egelhofer, T., Gao, Y., Hartzog, G. A., Teng, M., and Niu, L. (2008). Core structure of the yeast Spt4-Spt5 complex: A conserved module for regulation of transcription elongation. Structure 16: 1649-1658.
6. Li, X., Guo, M., Fan, J., Tang, W., Wang, D., Ge, H., Rong, H., Teng, M., Niu, L., Liu, Q., and Hao, Q. (2006). Crystal structure of 3-hydroxyanthranilic acid 3-4-dioxygenase from Sacchromyces cerevisiae: A special subgroup of the type III extradiol dioxygenases. Protein Sci. 15: 761-773.
5. Fan, J., Wang, D., Liang, Z., Guo, M., Teng, M., and Niu, L. (2006). Maize uroporphyrinogen III methyltransferase: Overexpression of the functional gene fragments in Escherichia coli and one-step purification. Protein Expr Purif. 46: 40-46.
4. Wang, J., Shen, B., Guo, M., Lou, X., Duan, Y., Cheng, X. P., Teng, M., Niu, L., Liu, Q., Huang, Q., and Hao, Q. (2005). Blocking effect and crystal structure of natrin toxin, a cysteine-rich secretory protein from Naja atra venom that targets the BKCa channel. Biochemistry 44: 10145-10152.
3. Wang, D., Guo, M., Liang, Z., Fan, J., Zhu, Z., Zang, J., Zhu, Z., Li, X., Teng, M., Niu, L., Dong, Y., and Liu, P. (2005). Crystal structure of human vacuolar protein sorting protein 29 reveals a phosphodiesterase/nuclease-like fold and two protein-protein interaction sites. J. Biol. Chem. 280: 22962 – 22967.
2. Guo, M., Teng, M., Niu, L., Liu, Q., Huang, Q., and Hao, Q. (2005). Crystal structure of cysteine-rich secretory protein stecrisp reveals the cysteine-rich domain has a K+-channel inhibitor-like fold. J. Biol. Chem. 280: 12405-12412.
1. Tu, X., Wang, J., Guo, M., Zheng, D., Teng, M., Niu, L., Liu, Q., Huang, Q., and Hao, Q. (2004). Purification, partial characterization, crystallization and preliminary X-ray diffraction of two cysteine-rich secretory proteins from Naja atra and Trimeresurus stejnegeri venoms. Acta Cryst. D. 60: 1108-1111.
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