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Return to DCDT+ description | List of users Below is a partial list of publications in which DCDT+ has been used (325 known), in reverse order by year. If you know of others, please send the citation to John Philo. 2024Kingsbury, J. S., Starr, C. G., and Gokarn, Y. R. (2024). A scaling relationship between thermodynamic and hydrodynamic interactions in protein solutions. Biophys. J., [online ahead of print]. 2023Klontz, E., Obi, J. O., Wang, Y., Glendening, G., Carr, J., Tsibouris, C., Buddula, S., Nallar, S., Soares, A. S., Beckett, D., Redzic, J. S., Eisenmesser, E., Palm, C., Schmidt, K., Scudder, A. H., Obiorah, T., Essuman, K., Milbrandt, J., Diantonio, A., Ray, K., Snyder, M. L. D., Deredge, D., and Snyder, G. A. (2023). The structure of NAD(+) consuming protein Acinetobacter baumannii TIR domain shows unique kinetics and conformations. J. Biol. Chem. 299, 105290 [free full text] Posey, A. E., Ross, K. A., Bagheri, M., Lanum, E. N., Khan, M. A., Jennings, C. E., Harwig, M. C., Kennedy, N. W., Hilser, V. J., Harden, J. L., and Hill, R. B. (2023). The variable domain from dynamin-related protein 1 promotes liquid-liquid phase separation that enhances its interaction with cardiolipin-containing membranes. Protein Sci. 32, e4787 [abstract} Yarawsky, A. E., Dinu, V., Harding, S. E., and Herr, A. B. (2023). Strong non-ideality effects at low protein concentrations: considerations for elongated proteins. Eur. Biophys. J.online ahead of print [abstract] [free preprint PDF] Kavran, J. M., Weingartner, K. A., Tran, T., and Tripp, K. W. (2023). Dimerization and autophosphorylation of the MST family of kinases are controlled by the same set of residues. bioRxiv 2023-03. [free preprint PDF] Devlin, T., Fleming, P. J., Loza, N., and Fleming, K. G. (2023). Generation of unfolded outer membrane protein ensembles defined by hydrodynamic properties. Eur. Biophys. J. 1-11. [abstract} Yarawsky, A. E., Ori, A. L., English, L. R., Whitten, S. T., and Herr, A. B. (2023). Convergent behavior of extended stalk regions from staphylococcal surface proteins with widely divergent sequence patterns. bioRxiv 2023-01.[free preprint PDF] Devlin, T., Marx, D. C., Roskopf, M. A., Bubb, Q. R., Plummer, A. M., and Fleming, K. G. (2023). FkpA enhances outer membrane protein folding using an extensive interaction surface. Biophys. J. 122, 152a [abstract] 2022Frampton, S. L., Sutcliffe, C., Baldock, C., and Ashe, H. L. (2022). Modelling the structure of Short Gastrulation and generation of a toolkit for studying its function in Drosophila. Biology Open. 11, bio059199 [free HTML] Davis, C. R., Backos, D., Morais, M. C., Churchill, M. E., and Catalano, C. E. (2022). Characterization of a Primordial Major Capsid-Scaffolding Protein Complex in Icosahedral Virus Shell Assembly. J. Mol. Biol. 434, 167719 [abstract] 2021Winzor, D. J., Dinu, V., Scott, D. J., and Harding, S. E. (2021). Quantifying the concentration dependence of sedimentation coefficients for globular macromolecules: a continuing age-old problem. Biophysical Reviews. 13, 273-288. [free HTML] Abraham, E. T., Oecal, S., Morgelin, M., Schmid, P. W., Buchner, J., Baumann, U., and Gebauer, J. M. (2021). Collagen's primary structure determines collagen: HSP47 complex stoichiometry. J. Biol. Chem, online ahead of print [free full text] Davis, G., York, A. J., Bacon, W. C., Lin, S. C., McNeal, M. M., Yarawsky, A. E., Maciag, J. J., Miller, J. L., Locker, K. C., and Bailey, M. (2021). Seroprevalence of SARS-CoV-2 Infection in Cincinnati Ohio USA from August to December 2020. medRxiv. [free PDF] Schmid, P. W., Lim, N. C., Peters, C., Back, K. C., Bourgeois, B., Pirolt, F., Richter, B., Peschek, J., Puk, O., and Amarie, O. V. (2021). Imbalances in the eye lens proteome are linked to cataract formation. Nature Structural. & Molecular. Biology. 1-9. [abstract] 2020Herrera, N. G., Morano, N. C., Celikgil, A., Georgiev, G. I., Malonis, R. J., Lee, J. H., Tong, K., Vergnolle, O., Massimi, A. B., and Yen, L. Y. (2020). Characterization of the SARS-CoV-2 S protein: biophysical, biochemical, structural, and antigenic analysis. ACS omega, preprint prior to publication [free full text] Lessen, H. J., Majumdar, A., and Fleming, K. G. (2020). Backbone hydrogen bond energies in membrane proteins are insensitive to large changes in local water concentration. Journal of the American. Chemical Society. 142, 6227-6235. [abstract} Badmalia, M. D., Siddiqui, M. Q., Mrozowich, T., Gemmill, D. L., and Patel, T. R. (2020). Analytical ultracentrifuge: an ideal tool for characterization of non-coding RNAs. Eur. Biophys. J. 49, 809-818. [abstract] Correia, J. J., Wright, R. T., Sherwood, P. J., and Stafford, W. F. (2020). Analysis of nonideality: insights from high concentration simulations of sedimentation velocity data. Eur. Biophys. J. 49, 687-700. [free PDF] Cui, H., Ali, M. Y., Goyal, P., ZHANG, K., Loh, J. Y., Trybus, K. M., and Solmaz, S. R. (2020). Coiled-coil registry shifts in the F684I mutant of Bicaudal D result in cargo-independent activation of dynein motility. Traffic. 21, 463-478. [abstract] Chaturvedi, S. K., Parupudi, A., Juul-Madsen, K., Nguyen, A., Vorup-Jensen, T., Dragulin-Otto, S., Zhao, H., Esfandiary, R., and Schuck, P. (2020). Measuring aggregates, self-association, and weak interactions in concentrated therapeutic antibody solutions. MAbs. 12, 1810488 [free full text] Kingsbury, J. S., Saini, A., Auclair, S. M., Fu, L., Lantz, M. M., Halloran, K. T., Calero-Rubio, C., Schwenger, W., Airiau, C. Y., and Zhang, J. (2020). A single molecular descriptor to predict solution behavior of therapeutic antibodies. Science Advances. 6, epub ahead of print [free full text] Brautigam, C. A., Tso, S. C., Deka, R. K., Liu, W. Z., and Norgard, M. V. (2020). Using modern approaches to sedimentation velocity to detect conformational changes in proteins. Eur. Biophys. J. (epub ahead of print) [abstract] Yarawsky, A. E. and Herr, A. B. (2020). The staphylococcal biofilm protein Aap forms a tetrameric species as a necessary intermediate before amyloidogenesis. J. Biol. Chem. (epub ahead of print) [free full text] Venkataramani, S., Ernst, R., Derebe, M. G., Wright, R., Kopenhaver, J., Jacobs, S. A., Singh, S., and Ganesan, R. (2020). In Pursuit of Stability Enhancement of a Prostate Cancer Targeting Antibody Derived from a Transgenic Animal Platform. Sci. Rep. 10, 9722 [free full text] Dolinska, M. B., Young, K. L., Kassouf, C., Dimitriadis, E. K., Wingfield, P. T., and Sergeev, Y. V. (2020). Protein Stability and Functional Characterization of Intra-Melanosomal Domain of Human Recombinant Tyrosinase-Related Protein 1. Int. J. Mol. Sci. 21, 331 [free full text] Fung, H. Y. J., McKibben, K. M., Ramirez, J., Gupta, K., and Rhoades, E. (2020). Structural Characterization of Tau in Fuzzy Tau:Tubulin Complexes. Structure 28, 378-384.[abstract] 2019Liu, N., Girvin, M. E., Brenowitz, M., and Lai, J. R. (2019). Conformational and lipid bilayer-perturbing properties of Marburg virus GP2 segments containing the fusion loop and membrane-proximal external region/transmembrane domain. Heliyon. 5, e03018 [free full text] Deshmukh, S. S., Kornblatt, M. J., and Kornblatt, J. A. (2019). The influence of truncating the carboxy-terminal amino acid residues of streptococcal enolase on its ability to interact with canine plasminogen. PLoS. One. 14, e0206338 [free full text] Wang, Q., Aleshintsev, A., Bolton, D., Zhuang, J., Brenowitz, M., and Gupta, R. (2019). Ca(II) and Zn(II) Cooperate To Modulate the Structure and Self-Assembly of S100A12. Biochemistry 58, 2269-2281. [Abstract] Bazilevsky, G. A., Affronti, H. C., Wei, X., Campbell, S. L., Wellen, K. E., and Marmorstein, R. (2019). ATP-citrate lyase multimerization is required for coenzyme-A substrate binding and catalysis. J. Biol. Chem. 294, 7259-7268. [Abstract] 2018Hartwick, E. W., Costantino, D. A., MacFadden, A., Nix, J. C., Tian, S., Das, R., and Kieft, J. S. (2018). Ribosome-induced RNA conformational changes in a viral 3'-UTR sense and regulate translation levels. Nat. Commun. 9, 5074 [free full text] Eren, E., Watts, N. R., Dearborn, A. D., Palmer, I. W., Kaufman, J. D., Steven, A. C., and Wingfield, P. T. (2018). Structures of Hepatitis B Virus Core-and e-Antigen Immune Complexes Suggest Multi-point Inhibition. Structure 26, 1314-26 [Abstract] Dearborn, A. D., Eren, E., Watts, N. R., Palmer, I. W., Kaufman, J. D., Steven, A. C., and Wingfield, P. T. (2018). Structure of an RNA Aptamer that Can Inhibit HIV-1 by Blocking Rev-Cognate RNA (RRE) Binding and Rev-Rev Association. Structure 26, 1187-95. [Abstract] Mucke, N., Kammerer, L., Winheim, S., Kirmse, R., Krieger, J., Mildenberger, M., Bassler, J., Hurt, E., Goldmann, W. H., Aebi, U., Toth, K., Langowski, J., and Herrmann, H. (2018). Assembly Kinetics of Vimentin Tetramers to Unit-Length Filaments: A Stopped-Flow Study. Biophys. J. 114, 2408-2418. [Abstract] Wright, R. T., Hayes, D. B., Stafford, W. F., Sherwood, P. J., and Correia, J. J. (2018). Characterization of therapeutic antibodies in the presence of human serum proteins by AU-FDS analytical ultracentrifugation. Anal. Biochem. 550, 72-83. [Abstract] Kunz, P., Zinner, K., Mucke, N., Bartoschik, T., Muyldermans, S., and Hoheisel, J. D. (2018). The structural basis of nanobody unfolding reversibility and thermoresistance. Sci. Rep. 8, 7934 [free PDF] P. Y. Chen, M. A. Funk, E. J. Brignole, and C. L. Drennan (2018). Disruption of an oligomeric interface prevents allosteric inhibition of Escherichia coli class Ia ribonucleotide reductase. J. Biol. Chem., epub ahead of print [PDF]. Shcherbakova, D. M., Cox Cammer, N., Huisman, T. M., Verkhusha, V. V., and Hodgson, L. (2018). Direct multiplex imaging and optogenetics of Rho GTPases enabled by near-infrared FRET. Nature Chemical Biology, epub ahead of print [abstract] 2017Plummer, A.M. (2017). The role of chaperones and BAMA in the outer membrane protein biogenesis pathway of Escherichia coli. Dissertation, Johns Hopkins University. [free PDF]. Ghosh, A., Ramagopal, U. A., Bonanno, J. B., Brenowitz, M. D., and Almo, S. C. (2017). Structures of the L27 domain of Disc Large homolog 1 protein illustrate a self-assembly module. Biochemistry 57, 1293-1305. [abstract] Puthenveetil, R., Kumar, S., Caimano, M. J., Dey, A., Anand, A., Vinogradova, O., and Radolf, J. D. (2017). The major outer sheath protein forms distinct conformers and multimeric complexes in the outer membrane and periplasm of Treponema denticola. Sci. Rep. 7, 13260 [free full text] Mayo, C. B. and Cole, J. L. (2017). Interaction of PKR with single-stranded RNA. Sci. Rep. 7, 3335. [free full text] Sauer, P. V., Timm, J., Liu, D., Sitbon, D., Boeri-Erba, E., Velours, C., Mucke, N., Langowski, J., chsenbein, F., lmouzni, G., and anne, D. (2017). Insights into the molecular architecture and histone H3-H4 deposition mechanism of yeast Chromatin assembly factor 1. eLife 6, e23474 [free full text] Blevitt, J. M., Hack, M. D., Herman, K. L., Jackson, P. F., Krawczuk, P. J., Lebsack, A. D., Liu, A. X., Mirzadegan, T., Nelen, M. I., and Patrick, A. N. (2017). Structural Basis of Small-Molecule Aggregate Induced Inhibition of a Protein-Protein Interaction. Journal of medicinal chemistry 60, 3511. [Abstract] Selcuk, H.B. (2017). Structural and functional studies of the regulation and inhibition of LuxO, a AAA+ ATPase. Thesis, Princeton University. [Abstract] 2016Boyaci, H., Shah, T., Hurley, A., Kokona, B., Li, Z., Ventocilla, C., Jeffrey, P. D., Semmelhack, M. F., Fairman, R., Bassler, B. L., and Hughson, F. M. (2016). Structure, Regulation, and Inhibition of the Quorum-Sensing Signal Integrator LuxO. PLoS. Biol. 14, e1002464 [free full text] Mayo, C. B., Wong, C. J., Lopez, P. E., Lary, J. W., and Cole, J. L. (2016). Activation of PKR by short stem-loop RNAs containing single-stranded arms. RNA 22, 1065-1075. [free full text] Vámosi, G., Mucke, N., Muller, G., Krieger, J. W., Curth, U., Langowski, J., and Toth, K. (2016). EGFP oligomers as natural fluorescence and hydrodynamic standards. Scientific Reports 6, article 33022. [free full text] Postel, S., Deredge, D., Bonsor, D. A., Yu, X., Diederichs, K., Helmsing, S., Vromen, A., Friedler, A., Hust, M., and Egelman, E. H. (2016). Bacterial flagellar capping proteins adopt diverse oligomeric states. eLife 5, e18857. [free full text] DiMattia, M. A., Watts, N. R., Cheng, N., Huang, R., Heymann, J. B., Grimes, J. M., Wingfield, P. T., Stuart, D. I., and Steven, A. C. (2016). The Structure of HIV-1 Rev Filaments Suggests a Bilateral Model for Rev-RRE Assembly. Structure 24, 1068. [free full text] Husain, B., Mayo, C., and Cole, J. L. (2016). Role of the Interdomain Linker in RNA-Activated Protein Kinase Activation. Biochemistry 55, 253-261. [Abstract] Chairatana, P., Chu, H., Castillo, P. A., Shen, B., Bevins, C. L., and Nolan, E. M. (2016). Proteolysis triggers self-assembly and unmasks innate immune function of a human +¦-defensin peptide. Chemical Science 7, 1738-1752. [free PDF] Kokona, B., Winesett, E. S., Nikolai von, K. A., Cryle, M. J., Fairman, R., and Charkoudian, L. K. (2016). Probing the selectivity of beta-hydroxylation reactions in non-ribosomal peptide synthesis using analytical ultracentrifugation. Anal. Biochem. 495, 42-51. [Abstract] 2015Bain, D. L., De Angelis, R. W., Connaghan, K. D., Yang, Q., Degala, G. D., and Lambert, J. R. (2015). Dissecting Steroid Receptor Function by Analytical Ultracentrifugation. Methods Enzymol. 562, 363-389. [Abstract] Tarasevich, B. J., Philo, J. S., Maluf, N. K., Krueger, S., Buchko, G. W., Lin, G., and Shaw, W. J. (2015). The leucine-rich amelogenin protein (LRAP) is primarily monomeric and unstructured in physiological solution. J Struct. Biol 190, 81-91. [Abstract] Chaton, C. T. and Herr, A. B. (2015). Elucidating Complicated Assembling Systems in Biology Using Size-and-Shape Analysis of Sedimentation Velocity Data. Methods Enzymol. 562, 187-204. [Abstract] Liu, N., Tao, Y., Brenowitz, M. D., Girvin, M. E., and Lai, J. R. (2015). Structural and Functional Studies on the Marburg Virus GP2 Fusion Loop. J. Infect. Dis. 212 Suppl 2, S146-S153 [Abstract] Yamniuk, A. P., Newitt, J. A., Doyle, M. L., Arisaka, F., Giannetti, A. M., Hensley, P., Myszka, D. G., Schwarz, F. P., Thomson, J. A., and Eisenstein, E. (2015). Development of a Model Protein Interaction Pair as a Benchmarking Tool for the Quantitative Analysis of 2-Site Protein-Protein Interactions. J. Biomol. Tech. 26, 125-141. [free PDF] Kokona, B., Winesett, E. S., Nikolai von, K. A., Cryle, M. J., Fairman, R., and Charkoudian, L. K. (2015). Probing the selectivity of beta-hydroxylation reactions in non-ribosomal peptide synthesis using analytical ultracentrifugation. Anal. Biochem., epub ahead of print [Abstract] Wu, S., Ding, Y., and Zhang, G. (2015). Mechanic Insight into Aggregation of Lysozyme by Ultrasensitive Differential Scanning Calorimetry and Sedimentation Velocity. J. Phys. Chem. B 119, 15789-15795 [Abstract] LoPiccolo, J., Kim, S. J., Shi, Y., Wu, B., Wu, H., Chait, B. T., Singer, R. H., Sali, A., Brenowitz, M., and Bresnick, A. R. (2015). Assembly and Molecular Architecture of the Phosphoinositide 3-Kinase p85a Homodimer. J. Biol. Chem. 290, 30390-30405 [free PDF] Premchandar, A., Kupniewska, A., Tarnowski, K., Mucke, N., Mauermann, M., Kaus-Drobek, M., Edelman, A., Herrmann, H., and Dadlez, M. (2015). Analysis of distinct molecular assembly complexes of keratin K8 and K18 by hydrogen-deuterium exchange. J. Struct. Biol. (epub ahead of print). [Abstract] De, S., Bubnys, A., Alonzo, F., III, Hyun, J., Lary, J. W., Cole, J. L., Torres, V. J., and Olson, R. (2015). The Relationship Between Glycan-Binding and Direct Membrane Interactions in Vibrio cholerae Cytolysin, a Channel-Forming Toxin. J. Biol. Chem. (epub ahead of print). [Abstract] Doll, T. A., Neef, T., Duong, N., Lanar, D. E., Ringler, P., Muller, S. A., and Burkhard, P. (2015). Optimizing the design of protein nanoparticles as carriers for vaccine applications. Nanomedicine 11, 1705-1713. [Abstract] Urbauer, J. L., Cowley, A. B., Broussard, H. P., Niedermaier, H. T., and Bieber Urbauer, R. J. (2015). Solution structure and properties of AlgH from Pseudomonas aeruginosa. Proteins 83, 1137-1150. [Abstract] Dai, Z., Tao, Y., Liu, N., Brenowitz, M. D., Girvin, M. E., and Lai, J. R. (2015). Conditional trimerization and lytic activity of HIV-1 gp41 variants containing the membrane-associated segments. Biochemistry 54, 1589-1599. [Abstract] Cao, Z. and Zhang, G. (2015). Dynamics of polyzwitterions in salt-free and salt solutions. Phys. Chem. Chem. Phys. 17, 27045-27051. [Abstract] Gaik, M., Flemming, D., von, A. A., Kastritis, P., Mucke, N., Fischer, J., Stelter, P., Ori, A., Bui, K. H., Bassler, J., Barbar, E., Beck, M., and Hurt, E. (2015). Structural basis for assembly and function of the Nup82 complex in the nuclear pore scaffold. J. Cell Biol. 208, 283-297. [Abstract] Launer-Felty, K., Wong, C. J., and Cole, J. L. (2015). Structural analysis of adenovirus VAI RNA defines the mechanism of inhibition of PKR. Biophys. J. 108, 748-757. [Abstract] Bonsor, D. A., Pham, K. T., Beadenkopf, R., Diederichs, K., Haas, R., Beckett, D., Fischer, W., and Sundberg, E. J. (2015). Integrin engagement by the helical RGD motif of the Helicobacter pylori CagL protein is regulated by pH-induced displacement of a neighboring helix. J. Biol. Chem., epub ahead of print [free PDF] Malashkevich, V. N., Higgins, C. D., Almo, S. C., and Lai, J. R. (2015). A Switch from Parallel to Antiparallel Strand Orientation in a Coiled-Coil X-Ray Structure via Two Core Hydrophobic Mutations. Peptide Science 104, 178-185. [free PDF] 2014Wowor, A. J., Yan, Y., Auclair, S. M., Yu, D., Zhang, J., May, E. R., Gross, M. L., Kendall, D. A., and Cole, J. L. (2014). Analysis of SecA dimerization in solution. Biochemistry 53, 3248-3260. [free PDF] Hao, Y. and Kieft, J. S. (2014). Diverse self-association properties within a family of phage packaging RNAs. RNA 20, 1759-1774. [Abstract] Bookwalter, C. S., Kelsen, A., Leung, J. M., Ward, G. E., and Trybus, K. M. (2014). A Toxoplasma gondii class XIV myosin, expressed in Sf9 cells with a parasite co-chaperone, requires two light chains for fast motility. J. Biol. Chem. 289, 30832-30841. [Abstract] Holley, A.C. (2014). Utilization of aqueous RAFT synthesized copolymers to improve anticancer drug efficacy. Ph.D. Thesis, U. Southern Mississippi [free PDF] Chairatana, P. and Nolan, E. M. (2014). Molecular basis for self-assembly of a human host-defense peptide that entraps bacterial pathogens. J. Am. Chem. Soc. 136, 13267-13276. [free PDF] Cao, Z and Zhang, G. (2014) Insight into dynamics of polyelectrolyte chains in salt-free solutions by laser light scattering and analytical ultracentrifugation. Polymer 55, 6789-6794. [Abstract] Lorenz, O. R., Freiburger, L., Rutz, D. A., Krause, M., Zierer, B. K., Alvira, S., Cuellar, J., Valpuesta, J. M., Madl, T., Sattler, M., and Buchner, J. (2014). Modulation of the Hsp90 chaperone cycle by a stringent client protein. Mol. Cell 53, 941-953. [Abstract] Khalil, S., Jaworski, I., and Pawelek, P. D. (2014). Identification of a surface glutamine residue (Q64) of Escherichia coli EntA required for interaction with EntE. Biochem. Biophys. Res. Commun. 453, 625-630. [Abstract] Reilly, S. M., Lyons, D. F., Wingate, S. E., Wright, R. T., Correia, J. J., Jameson, D. M., and Wadkins, R. M. (2014). Folding and Hydrodynamics of a DNA i-Motif from the c-MYC Promoter Determined by Fluorescent Cytidine Analogs. Biophys. J 107, 1703-1711. [Abstract] Holley, A., Parsons, K., Wan, W., Lyons, D., Bishop, R., Correia, J., Huang, F., and McCormick, C. (2014) Block ionomer complexes consisting of siRNA and aRAFT-synthesized hydrophilic-block-cationic copolymers: The influence of cationic block length on gene suppression. Polymer Chem., epub ahead of print [Abstract] Higgins, C. D., Malashkevich, V. N., Almo, S. C., and Lai, J. R. (2014). Influence of a heptad repeat stutter on the pH-dependent conformational behavior of the central coiled-coil from influenza hemagglutinin HA2. Proteins, April 21 2014, epub ahead of print [Abstract] Lyons, D. F., Le, V., Kramer, W. H., Bidwell, G. L., III, Lewis, E. A., Raucher, D., and Correia, J. J. (2014). Effect of basic cell-penetrating peptides on the structural, thermodynamic, and hydrodynamic properties of a novel drug delivery vector, ELP[V5G3A2-150]. Biochemistry 53, 1081-1091. [Abstract] Launer-Felty, K. and Cole, J. L. (2014). Domain interactions in adenovirus VAI RNA mediate high-affinity PKR binding. J. Mol. Biol. 426, 1285-1295. [free PDF] Padlan, C. S., Malashkevich, V. N., Almo, S. C., Levy, M., Brenowitz, M., and Girvin, M. E. (2014). An RNA aptamer possessing a novel monovalent cation-mediated fold inhibits lysozyme catalysis by inhibiting the binding of long natural substrates. RNA 20, 447-461. [Free PDF] Driggers, C. M., Dayal, P. V., Ellis, H. R., and Karplus, P. A. (2014). Crystal structure of Escherichia coli SsuE: Defining a General Catalytic Cycle for FMN reductases of the Flavodoxin-like Superfamily. Biochemistry, epub before print DOI: 10.1021/bi500314f [Free PDF] Mitra, S. (2014). Detecting RNA Tertiary Folding by Sedimentation Velocity Analytical Ultracentrifugation. In: RNA folding. (Methods in Molecular Biology vol. 1086). C.Waldsich, ed. Humana Press, pp. 265-288. [Abstract] 2013Taylor, M. S., Ruch, T. R., Hsiao, P. Y., Hwang, Y., Zhang, P., Dai, L., Huang, C. R., Berndsen, C. E., Kim, M. S., Pandey, A., Wolberger, C., Marmorstein, R., Machamer, C., Boeke, J. D., and Cole, P. A. (2013). Architectural organization of the metabolic regulatory enzyme ghrelin O-acyltransferase. J. Biol. Chem. 288, 32211-32228. [Free full text] Maquat, L.E. and Gong, C. (2012). Methods and compositions related to staufen 1 binding sites formed by duplexing alu elements. US Patent Application 13/984,709 [Free full text] DeBerg, H. A., Blehm, B. 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