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Hong Li (Orcid ID): 0000-0003-2046-9861

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Full list of publications

  • Ramia, N.F., Tang, L., Cocozaki, A.I. & Li, H. Staphylococcus epidermidis Csm1 is a 3′-5′ exonuclease. Nucleic acids research42, 1129-1138 (2014).
  • Ramia, N.F. et al. Essential structural and functional roles of the Cmr4 subunit in RNA cleavage by the Cmr CRISPR-Cas complex. Cell reports9, 1610-1617 (2014).
  • Peng, Y., Yu, G., Tian, S. & Li, H. Co-expression and co-purification of archaeal and eukaryal box C/D RNPs. PloS one9, e103096 (2014).
  • Hale, C.R., Cocozaki, A., Li, H., Terns, R.M. & Terns, M.P. Target RNA capture and cleavage by the Cmr type III-B CRISPR-Cas effector complex. Genes & development28, 2432-2443 (2014).
  • Spilman, M. et al. Structure of an RNA silencing complex of the CRISPR-Cas immune system. Molecular cell52, 146-152 (2013).
  • Shao, Y. & Li, H. Recognition and cleavage of a nonstructured CRISPR RNA by its processing endoribonuclease Cas6. Structure (London, England : 1993)21, 385-393 (2013).
  • Shao, Y. et al. Structure of the Cmr2-Cmr3 subcomplex of the Cmr RNA silencing complex. Structure (London, England : 1993)21, 376-384 (2013).
  • Wang, R., Zheng, H., Preamplume, G., Shao, Y. & Li, H. The impact of CRISPR repeat sequence on structures of a Cas6 protein-RNA complex. Protein science : a publication of the Protein Society21, 405-417 (2012).
  • Wang, R. & Li, H. The mysterious RAMP proteins and their roles in small RNA-based immunity. Protein science : a publication of the Protein Society21, 463-470 (2012).
  • Cocozaki, A.I. et al. Structure of the Cmr2 subunit of the CRISPR-Cas RNA silencing complex. Structure (London, England : 1993)20, 545-553 (2012).
  • Zhou, J., Liang, B. & Li, H. Structural and functional evidence of high specificity of Cbf5 for ACA trinucleotide. RNA (New York, N.Y.)17, 244-250 (2011).
  • Wang, R., Preamplume, G., Terns, M.P., Terns, R.M. & Li, H. Interaction of the Cas6 riboendonuclease with CRISPR RNAs: recognition and cleavage. Structure (London, England : 1993)19, 257-264 (2011).
  • Liang, B. & Li, H. Structures of ribonucleoprotein particle modification enzymes. Quarterly reviews of biophysics44, 95-122 (2011).
  • Zhou, J. et al. Glycosidic bond conformation preference plays a pivotal role in catalysis of RNA pseudouridylation: a combined simulation and structural study.Journal of molecular biology401, 690-695 (2010).
  • Zhou, J., Liang, B. & Li, H. Functional and structural impact of target uridine substitutions on the H/ACA ribonucleoprotein particle pseudouridine synthase. Biochemistry49, 6276-6281 (2010).
  • Xue, S. et al. Structural basis for substrate placement by an archaeal box C/D ribonucleoprotein particle. Molecular cell39, 939-949 (2010).
  • Mitchell, M. et al. Crystal structure and assembly of the functional Nanoarchaeum equitans tRNA splicing endonuclease. Nucleic acids research37, 5793-5802 (2009).
  • Liang, B. et al. Structure of a functional ribonucleoprotein pseudouridine synthase bound to a substrate RNA. Nature structural & molecular biology16, 740-746 (2009).
  • Liang, B. et al. Long-distance placement of substrate RNA by H/ACA proteins. RNA (New York, N.Y.)14, 2086-2094 (2008).
  • Li, H. Unveiling substrate RNA binding to H/ACA RNPs: one side fits all. Current opinion in structural biology18, 78-85 (2008).
  • Carte, J., Wang, R., Li, H., Terns, R.M. & Terns, M.P. Cas6 is an endoribonuclease that generates guide RNAs for invader defense in prokaryotes. Genes & development22, 3489-3496 (2008).
  • Calvin, K. & Li, H. RNA-splicing endonuclease structure and function. Cellular and molecular life sciences : CMLS65, 1176-1185 (2008).
  • Baker, D.L. et al. Determination of protein-RNA interaction sites in the Cbf5-H/ACA guide RNA complex by mass spectrometric protein footprinting. Biochemistry47, 1500-1510 (2008).
  • Phipps, K.R. & Li, H. Protein-RNA contacts at crystal packing surfaces. Proteins67, 121-127 (2007).
  • Oruganti, S. et al. Alternative conformations of the archaeal Nop56/58-fibrillarin complex imply flexibility in box C/D RNPs. Journal of molecular biology371, 1141-1150 (2007).
  • Min, D., Xue, S., Li, H. & Yang, W. ‘In-line attack’ conformational effect plays a modest role in an enzyme-catalyzed RNA cleavage: a free energy simulation study. Nucleic acids research35, 4001-4006 (2007).
  • Matera, A.G., Terns, R.M. & Terns, M.P. Non-coding RNAs: lessons from the small nuclear and small nucleolar RNAs. Nature reviews. Molecular cell biology8, 209-220 (2007).
  • Liang, B., Xue, S., Terns, R.M., Terns, M.P. & Li, H. Substrate RNA positioning in the archaeal H/ACA ribonucleoprotein complex. Nature structural & molecular biology14, 1189-1195 (2007).
  • Li, H. Complexes of tRNA and maturation enzymes: shaping up for translation. Current opinion in structural biology17, 293-301 (2007).
  • Calvin, K. & Li, H. Achieving specific RNA cleavage activity by an inactive splicing endonuclease subunit through engineered oligomerization. Journal of molecular biology366, 642-649 (2007).
  • Xue, S., Calvin, K. & Li, H. RNA recognition and cleavage by a splicing endonuclease. Science (New York, N.Y.)312, 906-910 (2006).
  • Trotta, C.R., Paushkin, S.V., Patel, M., Li, H. & Peltz, S.W. Cleavage of pre-tRNAs by the splicing endonuclease requires a composite active site. Nature441, 375-377 (2006).
  • Rashid, R. et al. Crystal structure of a Cbf5-Nop10-Gar1 complex and implications in RNA-guided pseudouridylation and dyskeratosis congenita. Molecular cell21, 249-260 (2006).
  • Randau, L. et al. The heteromeric Nanoarchaeum equitans splicing endonuclease cleaves noncanonical bulge-helix-bulge motifs of joined tRNA halves. Proceedings of the National Academy of Sciences of the United States of America102, 17934-17939 (2005).
  • Oruganti, S., Zhang, Y. & Li, H. Structural comparison of yeast snoRNP and spliceosomal protein Snu13p with its homologs. Biochemical and biophysical research communications333, 550-554 (2005).
  • Calvin, K., Hall, M.D., Xu, F., Xue, S. & Li, H. Structural characterization of the catalytic subunit of a novel RNA splicing endonuclease. Journal of molecular biology353, 952-960 (2005).
  • Zhang, Y. & Li, H. Structure determination of a truncated dimeric splicing endonuclease in pseudo-face-centered space group P2(1)2(1)2. Acta crystallographica. Section D, Biological crystallography60, 447-452 (2004).
  • Moore, T., Zhang, Y., Fenley, M.O. & Li, H. Molecular basis of box C/D RNA-protein interactions; cocrystal structure of archaeal L7Ae and a box C/D RNA. Structure (London, England : 1993)12, 807-818 (2004).
  • Aittaleb, M., Visone, T., Fenley, M.O. & Li, H. Structural and thermodynamic evidence for a stabilizing role of Nop5p in S-adenosyl-L-methionine binding to fibrillarin. The Journal of biological chemistry279, 41822-41829 (2004).
  • Rashid, R. et al. Functional requirement for symmetric assembly of archaeal box C/D small ribonucleoprotein particles. Journal of molecular biology333, 295-306 (2003).
  • Aittaleb, M. et al. Structure and function of archaeal box C/D sRNP core proteins. Nature structural biology10, 256-263 (2003).
  • Lima, S., Hildenbrand, J., Korostelev, A., Hattman, S. & Li, H. Crystal structure of an RNA helix recognized by a zinc-finger protein: an 18-bp duplex at 1.6 A resolution. RNA (New York, N.Y.)8, 924-932 (2002).
  • Story, R.M., Li, H. & Abelson, J.N. Crystal structure of a DEAD box protein from the hyperthermophile Methanococcus jannaschii. Proceedings of the National Academy of Sciences of the United States of America98, 1465-1470 (2001).
  • Li, H. & Abelson, J. Crystal structure of a dimeric archaeal splicing endonuclease. Journal of molecular biology302, 639-648 (2000).
  • Li, H., Trotta, C.R. & Abelson, J. Crystal structure and evolution of a transfer RNA splicing enzyme. Science (New York, N.Y.)280, 279-284 (1998).
  • Abelson, J., Trotta, C.R. & Li, H. tRNA splicing. The Journal of biological chemistry273, 12685-12688 (1998).
  • Li, H., Dunn, J.J., Luft, B.J. & Lawson, C.L. Crystal structure of Lyme disease antigen outer surface protein A complexed with an Fab. Proceedings of the National Academy of Sciences of the United States of America94, 3584-3589 (1997).
  • Li, H. & Lawson, C.L. Crystallization and preliminary X-ray analysis of Borrelia burgdorferi outer surface protein A (OspA) complexed with a murine monoclonal antibody Fab fragment. Journal of structural biology115, 335-337 (1995).
  • Li, H. et al. Crystallographic studies of isosteric NAD analogues bound to alcohol dehydrogenase: specificity and substrate binding in two ternary complexes. Biochemistry33, 11734-11744 (1994).
  • Li, H. et al. Crystallographic studies of two alcohol dehydrogenase-bound analogues of thiazole-4-carboxamide adenine dinucleotide (TAD), the active anabolite of the antitumor agent tiazofurin. Biochemistry33, 23-32 (1994).
  • Goldstein, B.M. et al. CNAD: a potent and specific inhibitor of alcohol dehydrogenase. Journal of medicinal chemistry37, 392-399 (1994).
  • Goldstein, B.M. et al. C-glycosyl bond conformation in oxazofurin: crystallographic and computational studies of the oxazole analogue of tiazofurin. Journal of medicinal chemistry37, 1684-1688 (1994).
  • Li, H., Kennedy, S.D. & Goldstein, B.M. Solid-state and solution conformations of isotiazofurin: crystallographic, computational and 1H NMR studies. Acta crystallographica. Section B, Structural science49 ( Pt 4), 729-738 (1993).
  • Li, H. & Goldstein, B.M. Carboxamide group conformation in the nicotinamide and thiazole-4-carboxamide rings: implications for enzyme binding. Journal of medicinal chemistry35, 3560-3567 (1992).
  • Mitchell, M.H. & Li, H. DNA and RNA Modification Enzymes, Structure, Mechanism, Functions, Cellular Interactions and Evolution.
  • Li, H. Protein-Nucleic Acid Interactions: Structural Biology.
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