Publications

For a full list of publications, please visit Google Scholars or PubMed.

Keane Lab Publications:

Selective deuteration of an RNA:RNA complex for structural analysis using small-angle scattering. Submitted (2024).

Munsayac A, Leite WC, Hopkins JB, Hall I, O’Neill HM, Keane SC*

bioRxiv: https://doi.org/10.1101/2024.09.09.612093

SASBDB: SASDUS8, SASDUT8, SASDUU8, SASDUV8, SASDUW8, SASDUX8


Use of steric blocking antisense oligonucleotides for the targeted inhibition of junction-containing precursor microRNAs. (2024). PMID: 38645194.

Ma S, Howden S, Keane SC*

bioRxiv: https://www.biorxiv.org/content/10.1101/2024.04.08.588531v1


Template switching enables chemical probing of native RNA structures. RNA 31: 113-125 (2025). PMID: 39438135. http://doi.org/10.1261/rna.079926.123

Hall I, O’Steen M, Gold S, Keane SC*, Weidmann CA*


Functional validation of SAM Riboswitch Element A from Listeria monocytogenes. Biochemistry 63, 20, 2621–2631 (2024). PMID: 39323220. https://doi.org/10.1021/acs.biochem.4c00247

Hall I, Zablock K, Sobetski R, Weidmann CA, Keane SC*

SASBDB: SASDSK9, SASDSL9


Structure of pre-miR-31 reveals an active role in Dicer-TRBP complex processing. PNAS 120(39):e2300527120 (2023). PMID: 37725636. doi: 10.1073/pnas.2300527120

Ma S#, Kotar A#, Grote S, Rouskin S, Keane SC*

PDB: 8FCS

BMRB: 31061, 51697, 51698

SASBDB: SASDRF9


Solution structure of NPSL2, a regulatory element in the oncomiR-1 RNA. JMB 434, 18, 187688 (2022). PMID: 35717998. doi: 10.1016/j.jmb.2022.167688

Liu Y, Munsayac A, Hall I, Keane SC*

PDB: 7UGA

BMRB: 51348, 51349, 51350

SASBDB: SASDNJ7


pH dependence of C•A, G•A and A•A mismatches in the stem of precursor microRNA-31. Biophys Chem. 283:106763 (2022). PMID: 35114594. doi: 10.1016/j.bpc.2022.106763

Kotar A, Ma S, Keane SC*

BMRB: 51129, 51134


NMR chemical shift assignments of RNA oligonucleotides to expand the RNA chemical shift database. Biomol NMR Assign. 15(2):479-490 (2021). PMID: 34449019. doi: 10.1007/s12104-021-10049-0

Liu Y#, Kotar A#, Hodges TL, Abdallah K, Taleb MH, Bitterman BA, Jaime S, Schaubroeck KJ, Mathew E, Morgenstern NW, Lohmeier A, Page JL, Ratanapanichkich M, Arhin G, Johnson BL, Cherepanov S, Moss SC, Zuniga G, Tilson NJ, Yeoh ZC, Johnson BA, Keane SC*

BMRB: 50933, 50932, 50931, 50930, 50929, 50928, 50927, 50926, 50925, 50924, 50923, 50922


A tale of two transitions: the unfolding mechanism of the prfA RNA thermosensor. Biochemistry 59(48):4533-4545 (2020). PMID: 33231432. doi: 10.1021/acs.biochem.0c00588

Zhang H, Hall I, Nissley AJ, Abdallah K, Keane SC*


Anomalous reverse transcription through chemical modifications in polyadenosine stretches. Biochemistry. 59, 23, 2154-2170 (2020). PMID: 32407625. doi: 10.1021/acs.biochem.0c00020

Kladwang W, Topkar VV, Liu B, Hodges TL, Keane SC, al-Hashimi H, Das R


Advanced approaches for elucidating structures of large RNAs using NMR spectroscopy and complementary methods. Methods. 183:93-107 (2020). PMID: 31972224. doi: 10.1016/j.ymeth.2020.01.009

Kotar, A, Foley, HN, Baughman, KM, Keane, SC* 


Structure of the zinc-finger antiviral protein in complex with RNA reveals a mechanism for selective targeting of CG-rich viral sequences. PNAS 116(48):25303-24309 (2019). PMID: 31719195. doi: 10.1073/pnas.1913232116

Meagher, JL, Takata, M, Gonçalves-Carneiro, D, Keane, SC, Rebendenne, A, Ong, H, Orr, VK, MacDonald, MR, Stuckey, JA, Bieniasz, PD*, Smith, JL*


Advances that facilitate the study of large RNA structure and dynamics by nuclear magnetic resonance spectroscopy. Wiley Interdiscip Rev RNA. 10(5):e1541 (2019). PubMed PMID: 31025514. doi: 10.1002/wrna.1541

Zhang, H and Keane, SC*


Papers published prior to the University of Michigan

Zhang, K.*, Keane, S.C.*, Su, Z., Irobalieva, R.N., Chen, M., Van, V., Sciandra, C.A., Marchant, J., Heng, X., Schmid, M.F., Case, D.A., Ludtke, S.J., Summers, M.F., Chiu, W. Structure of the 30 kDa HIV-1 RNA Dimerization Signal by a Hybrid Cryo-EM, NMR, and Molecular Dynamics Approach. Structure 26,490-498.e3 (2018)

Keane, S.C. and Summers, M.F. NMR studies of the structure and function of the HIV-1 5′-leader. Viruses 8; v8120338 (2016)

Keane, S.C., Van, V., Frank, H.M., Sciandra, C.A., McCowin, S., Santos, J., Heng, X., Summers, M.F. NMR detection of intermolecular interaction sites in the dimeric 5′-leader of the HIV-1 genome. PNAS 113, 13033-13038 (2016).

Carlson, L.A., Bai, Y., Keane, S.C., Doudna, J.A., Hurley, J.H. Reconstitution of selective HIV-1 RNA packaging in vitro by membrane-bound Gag assemblies. eLife 5:e14663 (2016)

Keane, S.C., Heng, X., Lu, K., Kharytonchyk, S., Ramakrishnan, V., Carter, G., Barton, S., Hosic, A., Florwick, A., Santos, J., Bolden, N.C., McCowin, S., Case, D.A., Johnson, B., Salemi, M., Telesnitsky, A., Summers, M.F. Structure of the HIV-1 RNA Packaging Signal. Science 348, 917-921 (2015).

Alvarado, L.J., LeBlanc, R.M., Longhini, A.P., Keane, S.C., Niyati, J., Yildiz, Z.F., Tolbert, B.S., D’Souza, V.M., Summers, M.F., Kreutz, C., Dayie, T.K. Regio-selective Chemical-Enzymatic Synthesis of Pyrimidine Nucleotides Facilitates RNA Structure and Dynamics Studies. ChemBioChem 15, 1573-1577 (2014).

Keane, S.C. and Giedroc, D.P. Solution Structure of Mouse Hepatitis Virus (MHV) nsp3a and Determinants of the Interaction with MHV Nucleocapsid (N) Protein. J. Virol. 87, 3502-3515 (2013).

Keane, S.C. and Giedroc, D.P. (1)H, (13)C, (15)N resonance assignments of murine hepatitis virus nonstructural protein 3a. Biomol NMR Assign. 8, 15-17 (2014).

Keane, S.C., Liu, P., Leibowitz, J.L., Giedroc, D.P. Functional transcriptional regulatory sequence (TRS) RNA binding and helix destabilizing determinants of murine hepatitis virus (MHV) nucleocapsid (N) protein. J. Biol. Chem. 287, 7063-7073 (2012).

Grossoehme, N.E., Li, L., Keane, S.C., Liu, P., Dann, C.E. 3rd, Leibowitz, J.L., Giedroc, D.P. Coronavirus N protein N-terminal domain (NTD) specifically binds the transcriptional regulatory sequence (TRS) and melts TRS-cTRS RNA duplexes. J. Mol. Biol. 394, 544-57 (2009)

Liu, P., Li, L., Keane, S.C., Yang, D., Leibowitz, J.L., Giedroc, D.P. Mouse hepatitis virus stem-loop 2 adopts a uYNMG(U)a-like tetraloop structure that is highly functionally tolerant of base substitutions. J. Virol. 83, 12084-12093 (2009).