Many of these publications can be viewed using the Pubmed links below. Undergraduate coauthors are underlined in the citations.
We have chosen to make select raw data from our publications freely available through the Penn State ScholarSphere service. This Data is provided for download with Open Access licensing; if it is helpful for your research, we request that you please cite the relevant publication in your work. If there is additional data that may help you with your research, please contact Dr. Showalter with your request.
Penn State Publications
- Fraser, O.A., Dewing, S.M., Usher, E.T., George, C., Showalter, S.A. A Direct Nuclear Magnetic Resonance Method to Investigate Lysine Acetylation of Intrinsically Disordered Proteins. Front. Mol. Biosci. 2022: 9, 1074743. PMCID: PMC9853081.
- Usher, E.T., Showalter S.A. Biophysical Insights into Glucose-Dependent Transcriptional Regulation by PDX1. J. Biol. Chem. 2022: 298, 102623. PMCID: PMC9691942.
- Usher, E.T., Namitz, K.E.W., Cosgrove, M.S., Showalter, S.A. Probing multiple enzymatic methylation events in real time with NMR spectroscopy. Biophys. J. 2021: 120, 4710-4721. PMCID: PMC8595733.
- Prieto V.A., Namitz, K.E.W., Showalter, S.A. Transient Electrostatic Interactions between Fcp1 and Rap74 Bias the Conformational Ensemble of the Complex with Minimal Impact on Binding Affinity. J. Phys. Chem. B. 2021: 125, 10917-10927. PMID:34550709.
- Usher, E.T., Sabri, N., Rohac, R., Boal, A.K., Mittag, T., Showalter, S.A. Intrinsically Disordered Substrates Dictate SPOP Subnuclear Localization and Ubiquitination Activity. J. Biol. Chem. 2021: 296, 100693. PMCID: PMC8138767.
- Usher, E.T., Showalter, S.A. Mapping Invisible Epitopes by NMR Spectroscopy. J. Biol. Chem. 2020: 295, 17411-17412. PMCID: PMC7762964.
- Morley, V.J., Kinnear, C.L., Sim, D.G., Olsen, S.N., Jackson, L., Hansen, E., Usher, G.A., Showalter, S.A., Pai, M.P., Woods, R.J., Read, A.F. An adjunctive therapy prevents enrichment of antibiotic-resistant clones of a colonizing opportunistic pathogen. eLife 2020: 9, e58147. PMCID: PMC770784.
- Pabit, S.A., Chen, Y.-L., Usher, E.T., Cook, E.C., Pollack, L., Showalter, S.A. Elucidating the Role of Microprocessor Protein DGCR8 in Bending RNA Structures. Biophys. J. 2020: 119, 2524-2536. PMCID: PMC7822732.
- Showalter, SA. Reviving Protein-Observed 19F Lineshape Analysis for Deep Insight into Protein-Ligand Binding Events. Biophys J. 2020: 118, 2333-2335. PMCID: PMC7231914.
- Sloand, JN, Nguyen, TT, Zinck, SA, Cook, EC, Zimudzi, TJ, Showalter, SA, Glick, AB, Simon, JC, Medina, SH. Ultrasound-Guided Cytosolic Protein Delivery via Transient Fluorous Masks. ACS Nano 2020: 14, 4061-4073. PMID: 32134630.
- Cook, EC, Sahu, D, Bastidas, M, Showalter, SA. The Solution Ensemble of the C-Terminal Domain from the Transcription Factor Pdx1 Resembles an Excluded Volume Polymer. J. Phys. Chem. B. 2019: 123, 106-116. PMID: 30525611.
Data: Download the raw SAXS data for this publication. - Cook, EC, Featherston, ER, Showalter, SA, Cotruvo, JA. Structural Basis for Rare Earth Element Recognition by Methylobacterium extorquens Lanmodulin. Biochemistry. 2019: 58, 120-125. PMID: 30352145.
- Cook, EC, Usher, GA, Showalter, SA. The use of 13C Direct-Detect NMR to Characterize Flexible and Disordered Proteins. Methods Enzymol. 2018: 611, 81-100. PMID: 30471706.
- Burkholder, NT, Medellin, B, Irani, S, Matthews, W, Showalter, SA, Zhang, YJ. Chemical Tools for Studying the Impact of cis/trans Prolyl Isomerization on RNA Polymerase II Phosphatase Activity and Specificity. Methods Enzymol. 2018: 607, 269-297. PMID: 30149861.
- Gibbs, E.B., Laremore, T.N., Usher, G.A., Portz, B., Cook, E.C., & Showalter, S.A. “Substrate Specificity of the Kinase P-TEFb Towards the RNA Polymerase II C-Terminal Domain.” Biophys J. 2017: 113, 1909-1911. PMID: PMC5685781
Data: Download all raw data for this publication. - Kranick, J.C., Chadalavada, D.M. Sahu, D., & Showalter, S.A. (2017) “Engineering Double-Stranded RNA Binding Activity into the Drosha Double-Stranded RNA Binding Domain Results in a Loss of MicroRNA Processing Function.” PLoS One, 12, e0182445. PMCID: PMC5549741
Data: Download all raw data for this publication. - Gibbs, E.B., Cook, E.C., & Showalter, S.A. (2017) “Application of NMR to Studies of Intrinsically Disordered Proteins.” Arch. Biochem. Biophys., 628, 57-70. PMID: 28502465
- Gibbs, E.B., Lu, F., Portz, B., Fisher, M.J., Medellin, B.P., Laremore, T.N., Zhang, Y.J., Gilmour, D.S., & Showalter, S.A. (2017) “Phosphorylation Induces Sequence-Specific Conformational Switches in the RNA Polymerase II C-Terminal Domain.” Nat. Commun., 8, 15233. PMCID: PMC5437310
Data: Download the raw SAXS data for this publication. - Portz, B., Lu, F., Gibbs, E.B., Mayfield, J.E., Mehaffey, M.R., Zhang, Y.J., Brodbelt, J.S., Showalter, S.A., & Gilmour, D.S. (2017) “Structural Heterogeneity in the Intrinsically Disordered RNA Polymerase II C-terminal Domain.” Nat. Commun., 8, 15231. PMCID: PMC5437306
- Gibbs, E.B., & Showalter, S.A. (2016) “Quantification of Compactness and Local Order in the Ensemble of the Intrinsically Disordered Protein FCP1.” J. Phys. Chem. B, 120, 8960-8969. PMID: 27551949
- Acevedo, R., Evans, D., Penrod, K.A., & Showalter, S.A. (2016) “Binding by TRBP-dsRBD2 does not Induce Bending of Double-Stranded RNA.” Biophys. J., 110, 2610-2617. PMCID: PMC4914420
- Sahu, D., Bastidas, M., Lawrence, C.W., Noid, W.G., & Showalter, S.A. (2016) “Assessing Coupled Protein Folding and Binding through Temperature-Dependent Isothermal Titration Calorimetry.” Methods Enzymol., 567, 23-45. PMCID: In Process
- Yennawar, N.H., Fecko, J.A., Showalter, S.A., & Bevilacqua, P.C. (2016) “A High-Throughput Biological Calorimetry Core – Steps to Startup, Run, and Maintain a Multi-User Facility.” Methods Enzymol., 567, 435-460. PMCID: In Process
- Bastidas, M., Gibbs, E.B., Sahu, D., & Showalter, S.A. (2015) “A Primer for Carbon-Detected NMR Applications to Intrinsically Disordered Proteins in Solution.” Con. Mag. Reson., 44, 54-66. PMCID: In Process
- Quarles, K.A., Chadalavada, D., & Showalter, S.A. (2015) “Deformability in the Cleavage Site of Primary MicroRNA is Not Sensed by the Double-Stranded RNA Binding Domains in the Microprocessor Component DGCR8.” Proteins: Struct. Funct. Bioinf., 83, 1165-1179. PMCID: PMC4446130
- Gibbs, E.B., & Showalter, S.A. (2015) “Quantitative Biophysical Characterization of Intrinsically Disordered Proteins.” Biochemistry, 54, 1314-1326. PMID: 25631161
- Acevedo, R., Orench-Rivera, N., Quarles, K.A., & Showalter, S.A. (2015) “Helical Defects in MicroRNA Influence Protein Binding by TAR RNA Binding Protein.” PLoS One, e0116749. PMCID: PMC4301919
Data: All raw data associated with this publication. - Cordek, D.G., Croom-Perez, T.J., Hwang, J., Hargittai, M.R.S., Subba-Reddy, C.V., Han, Q., Lodeiro, M.F., Ning, G., McCrory, T.S., Arnold, J.J., Koc, H., Lindenbach, B.D., Showalter, S.A., & Cameron, C.E. (2014) “Expanding the proteome of an RNA virus by phosphorylation of an intrinsically disordered viral protein.” J. Biol. Chem., 289, 24397-24416. PMCID: PMC4148867
- Showalter, S.A. (2014) “Intrinsically Disordered Proteins: Methods for Structure and Dynamics Studies.” eMagRes, 3, 181-190. (pdf)
- Lawrence, C.W., Kumar, S., Noid, W.G., & Showalter, S.A. (2014) “Role of Ordered Proteins in the Folding-Upon-Binding of Intrinsically Disordered Proteins.” J. Phys. Chem. Lett., 5, 833-838. PMID: 26274075
- Sahu, D., Bastidas, M., & Showalter, S.A. (2014) “Generating NMR Chemical Shift Assignments of Intrinsically Disordered Proteins Using Carbon-Detect NMR Methods.” Anal. Biochem., 449, 17-25. PMCID: PMC3944900
- Bastidas, M., & Showalter, S.A. (2013) “Thermodynamic and Structural Determinants of Differential Pdx1 Binding to Elements from the Insulin and IAPP Promoters.”J. Mol. Biol., 425, 3360-3377. PMCID: PMC3800017
- Kumar, S., Showalter, S.A., & Noid, W.G. (2013) “Native-Based Simulations of the Binding Interaction Between RAP74 and the Disordered FCP1 Peptide.” J. Phys. Chem. B, 117, 3074-3085. PMID: 23387368
- Quarles, K.A., Sahu, D., Havens, M.A., Forsyth, E.R., Wostenberg, C., Hastings, M.L., & Showalter, S.A. (2013) “Ensemble Analysis of Primary MicroRNA Structure Reveals an Extensive Capacity to Deform near the Drosha Cleavage Site.” Biochemistry, 52, 795-807. PMCID: PMC3565094
Data – Average SHAPE Intensity: pri-mir-16-1 pri-mir-30a pri-mir-107 - Wostenberg, C., Lary, J.W., Sahu, D., Acevedo, R., Quarles, K.A., Cole, J.L., & Showalter, S.A. (2012) “The Role of Human Dicer-dsRBD in Processing Small Regulatory RNAs.” PLoS One, 7, e51829. PMCID: PMC3521659
- Myers, C.P., Sun, S., Showalter, S.A., Miller, J.R., & Williams, M.E. (2012) “NMR Investigations of the Solution Structures of Ru-Zn Complexes Tethered by Oligo(aminoethylglycine) chains.” Polyhedron, 40, 118-124.
- Lawrence, C.W., & Showalter, S.A. (2012) “Carbon-Detected 15N NMR Spin Relaxation of an Intrinsically Disordered Protein: FCP1 Dynamics Unbound and in Complex with RAP74.” J. Phys. Chem. Lett., 3, 1409-1413. PMID: 26286791
- Wostenberg, C., Kumar, S., Noid, W.G., & Showalter, S.A. (2011) “Atomistic Simulations Reveal Structural Disorder in the RAP74-FCP1 Complex.” J. Phys. Chem. B, 115, 13731-13739. PMID: 21988473
- Lawrence, C.W., Bonny, A., & Showalter, S.A. (2011) “The Disordered C-Terminus of the RNA Polymerase II Phosphatase FCP1 is Partially Helical in the Unbound State.” Biochem. Biophys. Res. Comm., 410, 461-465. PMID: 21672523
- Wostenberg, C., Quarles, K.A., & Showalter, S.A. (2010) “Dynamic Origins of Differential RNA Binding Function in Two dsRBDs from the miRNA ‘Microprocessor’ Complex.” Biochemistry, 49, 10728-10736. PMCID: PMC3565223
- Wostenberg, C. & Showalter, S.A. (2010) “MD Simulations of the dsRBP DGCR8 Reveal Correlated Motions that may Facilitate pri-miRNA Binding.” Biophys. J., 99, 248-256. PMID: PMC2895372
- O’Hare, B., Benesi, A.J., & Showalter, S.A. (2009) “Incorporating 1H chemical shift determination into 13C-detected spectroscopy of intrinsically disordered proteins in solution.” J. Mag. Reson., 200, 354-358. PMID: 19648037
- Showalter, S.A. (2009) “NMR Assignment of the Intrinsically Disordered C-terminal Region of Homo sapiens FCP1 in the Unbound State.” Biomol. NMR Assign., 3, 179-181. PMID: 19888685
Data – FCP1 Chemical Shifts - Levine, L.A., Kirin, S.I., Myers, C.P., Showalter, S.A., & Williams, M.E. (2009) “Heterometallic Ferrocene-Rhenium Complexes Linked by an Aminoethylglycine Scaffold.” Eur. J. Inorg. Chem., 2009, 613-621.
Non-Penn State Papers
- Li, D.-W., Showalter, S.A., & Brüschweiler, R. (2010) “Entropy Localization in Proteins.” J. Phys. Chem. B, 114, 16036-16044.
- Markwick, P.R.L., Showalter, S.A., Bouvignies, G., Brüschweiler, R., & Blackledge, M. (2009) “Structural Dynamics of Protein Backbone φ Angles: Extended Molecular Dynamics Simulations versus Experimental 3J Scalar Couplings.” J. Biomol. NMR.,45, 17-21.
- Salmon, L., Bouvignies, G., Markwick, P., Lakomek, N., Showalter, S., Li, D.-W., Walter, K., Griesinger, C., Brüschweiler, R., & Blackledge, M. (2009) “Protein Conformational Flexibility from Structure-Free Analysis of NMR Dipolar Couplings: Quantitative and Absolute Determination of Backbone Motion in Ubiquitin.” Angew. Chem. Int. Ed., 48, 4154-4157.
- Showalter, S.A., Bruschweiler-Li, L., Johnson, E., Zhang, F., & Brüschweiler, R. (2008) “Quantitative Lid Dynamics of MDM2 Reveals Differential Ligand Binding Modes of the p53-Binding Cleft.” J. Am. Chem. Soc., 130, 6472-6478.
- Johnson, E., Showalter, S.A., & Brüschweiler, R. (2008) “A Multifaceted Approach to the Interpretation of NMR Order Parameters: A Case Study of a Dynamic α-Helix.” J. Phys. Chem. B, 112, 6203-6210.
- Johnson, E., Bruschweiler-Li, L., Showalter, S.A., Vuister, G., Zhang, F., & Brüschweiler, R. (2008) “Structure and Dynamics of Ca2+-Binding Domain 1 of the Na+/Ca2+ Exchanger In the Presence and in the Absence of Ca2+.“ J. Mol. Biol., 377, 945-955.
- Showalter, S.A., Johnson, E., Rance, M., & Brüschweiler, R. (2007) “Toward Quantitative Interpretation of Methyl-Side Chain Dynamics by Molecular Dynamics Simulations.” J. Am. Chem. Soc., 129, 14146-14147.
- Showalter, S.A., & Brüschweiler, R. (2007) “Quantitative Molecular Ensemble Interpretation of NMR Dipolar Couplings without Restraints.” J. Am. Chem. Soc., 129, 4158-4159.
- Showalter, S.A., & Brüschweiler, R. (2007) “Validation of Molecular Dynamics Simulations of Biomolecules Using NMR Spin Relaxation as Benchmarks: Application to the AMBER99SB Force Field.” J. Chem. Theory Comput., 3, 961-975.
- Showalter, S.A., & Hall, K.B. (2005) “Correlated Motions in the U1A snRNA Stem/Loop 2:U1A RBD1 Complex.” Biophys. J., 89, 2046-2058.
- Showalter, S.A., Baker, N.A., Tang, C., & Hall, K.B. (2005) “Iron Responsive Element RNA Flexibility Described by NMR and Isotropic Reorientational Eigenmode Dynamics.” J. Biomol. NMR. 32, 179-193.
- Showalter, S. A., & Hall, K.B. (2005) “Isotropic Reorientational Eigenmode Dynamics Compliments NMR Relaxation Measurements for RNA.” Methods Enzymol. 394, 465.
- Showalter, S.A., & Hall, K.B. (2004) “Altering the RNA-binding mode of the U1A RBD1 Protein.” J. Mol. Biol. 335, 465-480.
- Showalter, S.A., & Hall, K.B. (2002) “A Functional Role for Correlated Motion in the N-Terminal RNA Binding Domain of Human U1A Protein.” J. Mol. Biol. 322, 533-542.