85. Hennecker, C., Venegas, F., Wang, G., Stille, J., Milaczewska, A., Moitessier, N., & Mittermaier, A. (2025). Mechanistic Characterization of Covalent Enzyme Inhibition by Isothermal Titration Calorimetry Kinetic Competition (ITC-KC). Analytical Chemistry, 97(12), 6368–6381.
84. Alanagh, H. R., Sánchez-Sánchez, M. G., Wozny, M. R., Habibi, Y., Jarade, C., Sprules, T., Mittermaier, A. K., Hendricks, A. G., & Harrington, M. J. (2025). pH-sulfate synergy regulates processing and mechanics of mussel byssus protein condensates. Chemistry of Materials, 37(3), 925–938.
83. Rivera, M., Ayon, O. S., Diaconescu-Grabari, S., Pottel, J., Moitessier, N., Mittermaier, A., & McKeague, M. (2024). A sensitive and scalable fluorescence anisotropy single stranded RNA targeting approach for monitoring riboswitch conformational states. Nucleic Acids Research, 52(6), 3164–3179.
82. Wang, G., Venegas, F. A., Rueda, A. M., Weerasinghe, N. W., Uggowitzer, K. A., Thibodeaux, C. J., Moitessier, N., & Mittermaier, A. K. (2024). A naturally occurring G11S mutation in the 3C‐like protease from the SARS‐CoV‐2 virus dramatically weakens the dimer interface. Protein Science, 33(1), e4857.
81. Wang, G., Moitessier, N., & Mittermaier, A. K. (2023). Computational and biophysical methods for the discovery and optimization of covalent drugs. Chemical Communications, 59(73), 10866–10882.
80. Stille, J. K., Tjutrins, J., Wang, G., Venegas, F. A., Hennecker, C., Rueda, A. M., ... & Moitessier, N. (2022). Design, synthesis and in vitro evaluation of novel SARS-CoV-2 3CLpro covalent inhibitors. European Journal of Medicinal Chemistry, 229, 114046.
79. Plescia, J., Hédou, D., Pousse, M. E., Labarre, A., Dufresne, C., Mittermaier, A., & Moitessier, N. (2022). Modulating the selectivity of inhibitors for prolyl oligopeptidase inhibitors and fibroblast activation protein-α for different indications. European Journal of Medicinal Chemistry, 240, 114543.
78. Hennecker, C. D., Lachance-Brais, C., Sleiman, H., & Mittermaier, A. (2022). Using transient equilibria (TREQ) to measure the thermodynamics of slowly assembling supramolecular systems. Science Advances, 8(14), eabm8455.
77. Lachance-Brais, C., Hennecker, C. D., Alenaizan, A., Luo, X., Toader, V., Taing, M., Sherrill, C. D., Mittermaier, A. K., & Sleiman, H. F. (2021). Tuning DNA supramolecular polymers by the addition of small, functionalized nucleobase mimics. Journal of the American Chemical Society, 143(47), 19824–19833.
76. Falconer, R. J., Schuur, B., & Mittermaier, A. K. (2021). Applications of isothermal titration calorimetry in pure and applied research from 2016 to 2020. Journal of Molecular Recognition, 34(10), e2901.
75. Odette, W. L., Hennecker, C. D., Mittermaier, A. K., & Mauzeroll, J. (2021). EDTA-gradient loading of doxorubicin into ferrocene-containing liposomes: Effect of lipid composition and visualization of triggered release by cryo-TEM. Langmuir, 37(38), 11222–11232.
74. Wang, Y., & Mittermaier, A. K. (2021). Characterizing bi-substrate enzyme kinetics at high resolution by 2D-ITC. Analytical Chemistry, 93(37), 12723–12732.
73. Carrino, S., Hennecker, C. D., Murrieta, A. C., & Mittermaier, A. K. (2021). Frustrated folding of guanine quadruplexes in telomeric DNA. Nucleic Acids Research, 49(6), 3063–3076.
72. Harkness, R. W., Hennecker, C., Grün, J. T., Blümler, A., Heckel, A., Schwalbe, H., & Mittermaier, A. K. (2021). Parallel reaction pathways accelerate folding of a guanine quadruplex. Nucleic Acids Research, 49(3), 1247–1262.
71. Wang, Y., Wang, G., Moitessier, N., & Mittermaier, A. K. (2020). Enzyme kinetics by isothermal titration calorimetry: Allostery, inhibition, and dynamics. Frontiers in Molecular Biosciences, 7, 583826.
70. Payliss, B., & Mittermaier, A. (2020). Determination of pKa values in intrinsically disordered proteins. In Methods in Molecular Biology (Vol. 2141), Intrinsically Disordered Proteins: Methods and Protocols (pp. 319–336).
69. Prinzen, A. L., Saliba, D., Hennecker, C., Trinh, T., Mittermaier, A., & Sleiman, H. F. (2020). Amplified self-immolative release of small molecules by spatial isolation of reactive groups on DNA-minimal architectures. Angewandte Chemie International Edition, 59(31), 12900–12908.
68. Vahidi, S., Ripstein, Z. A., Juravsky, J. B., Rennella, E., Goldberg, A. L., Mittermaier, A. K., Rubinstein, J. L., & Kay, L. E. (2020). An allosteric switch regulates Mycobacterium tuberculosis ClpP1P2 protease function as established by cryo-EM and methyl-TROSY NMR. Proceedings of the National Academy of Sciences, 117(11), 5895–5906.
67. Grün, J. T., Hennecker, C., Klötzner, D. P., Harkness, R. W., Bessi, I., Heckel, A., Mittermaier, A. K., & Schwalbe, H. (2020). Conformational dynamics of strand register shifts in DNA G-quadruplexes. Journal of the American Chemical Society, 142, 264–273.
66. Plescia, J., Dufresne, C., Janmamode, N., Wahba, A. S., Mittermaier, A. K., & Moitessier, N. (2020). Discovery of covalent prolyl oligopeptidase boronic ester inhibitors. European Journal of Medicinal Chemistry, 185, 111783.
65. Wang, Y., Guan, J. M., Di Trani, J. M., Auclair, K., & Mittermaier, A. K. (2019). Inhibition and activation of kinases by reaction products: A reporter-free assay. Analytical Chemistry, 91, 11803–11811.
64. Plescia, J., De Cesco, S., Patrascu, M. B., Kurian, J., Di Trani, J., Dufresne, C., Wahba, A. S., Janmamode, N., Mittermaier, A. K., & Moitessier, N. (2019). Integrated synthetic, biophysical, and computational investigations of covalent inhibitors of prolyl oligopeptidase and fibroblast activation protein alpha. Journal of Medicinal Chemistry, 62, 7874–7884.
63. Antunes, V. U., Llontop, E. E., Vasconcelos, F. N. D., de los Santos, Y. L., Oliveira, R. J., Lincopan, N., Farah, C. S., Doucet, N., Mittermaier, A., & Favaro, D. C. (2019). Importance of the β5–β6 loop for the structure, catalytic efficiency, and stability of carbapenem-hydrolyzing class D β-lactamase subfamily OXA-143. Biochemistry, 58, 3604–3616.
62. Payliss, B., Vogel, J., & Mittermaier, A. (2019). Side chain electrostatic interactions and pH-dependent expansion of the intrinsically disordered, highly acidic carboxyl-terminus of γ-tubulin. Protein Science, 28, 1095–1105.
61. Di Trani, J., De Cesco, S., O'Leary, R., Plescia, J., Nascimento, C., Moitessier, N., & Mittermaier, A. (2018). Rapid measurement of inhibitor binding kinetics by isothermal titration calorimetry. Nature Communications, 9, 893.
60. Harkness, R. W., Avakyan, N., Sleiman, H. F., & Mittermaier, A. (2018). Mapping the energy landscapes of supramolecular assembly by thermal hysteresis. Nature Communications, 9, 3152.
59. Di Trani, J. M., Moitessier, N., & Mittermaier, A. K. (2018). Complete kinetic characterization of enzyme inhibition in a single isothermal titration calorimetric experiment. Analytical Chemistry, 90, 8430–8435.
58. El Turk, F., De Genst, E., Guilliams, T., Fauvet, B., Hejjaoui, M., Di Trani, J., Chiki, A., Mittermaier, A., Vendruscolo, M., Lashuel, H. A., & Dobson, C. M. (2018). Exploring the role of post-translational modifications in regulating α-synuclein interactions by studying the effects of phosphorylation on nanobody binding. Protein Science, 27, 1262–1274.
57. Harris, J., Shadrina, M., Oliver, C., Vogel, J., & Mittermaier, A. (2018). Concerted millisecond timescale dynamics in the intrinsically disordered carboxyl terminus of γ-tubulin induced by mutation of a conserved tyrosine residue. Protein Science, 27(2), 531–545.
56. Garci, A., Castor, K. J., Fakhoury, J., Do, J. L., Di Trani, J., Chidchob, P., Stein, R. S., Mittermaier, A. K., Friscic, T., & Sleiman, H. (2018). Efficient and rapid mechanochemical assembly of platinum(II) squares for guanine quadruplex targeting. Journal of the American Chemical Society, 139(46), 16913–16922.
55. Harkness, R. W., Johnson, P. E., & Mittermaier, A. K. (2017). Measuring biomolecular DSC profiles with thermolabile ligands to rapidly characterize folding and binding interactions. Journal of Visualized Experiments, 129, e55959.
54. De Cesco, S., Kurian, J., Dufresne, C., Mittermaier, A. K., & Moitessier, N. (2017). Covalent inhibitors design and discovery. European Journal of Medicinal Chemistry, 138, 96–114.
53. Harkness, R. W., & Mittermaier, A. K. (2017). G-quadruplex dynamics. Biochimica et Biophysica Acta (BBA) - General Subjects, 1865, 1544–1554.
52. Di Trani, J. M., Moitessier, N., & Mittermaier, A. K. (2017). Measuring rapid time-scale reaction kinetics using isothermal titration calorimetry. Analytical Chemistry, 89(13), 7022–7030.
51. Assi, H. A., Harkness, R. W., Martin-Pintado, N., Wilds, C. J., Campos-Olivas, R., Mittermaier, A. K., González, C., & Damha, M. J. (2016). Stabilization of i-motif structures by 2′β-fluorination of DNA. Nucleic Acids Research, 44(11), 4998–5009.
50. El-Turk, F., Newby, F. N., De Genst, E., Guilliams, T., Sprules, T., Mittermaier, A., Dobson, C. M., & Vendruscolo, M. (2016). Structural effects of two camelid nanobodies directed to distinct C-terminal epitopes on α-synuclein. Biochemistry, 55(22), 3116–3122.
49. Harkness, R. W., & Mittermaier, A. (2016). G-register exchange dynamics in guanine quadruplexes. Nucleic Acids Research, 44(8), 3481–3494.
48. Harkness, R. W., Slavkovic, S., Johnson, P. E., & Mittermaier, A. K. (2016). Rapid characterization of folding and binding interactions with thermolabile ligands by DSC. Chemical Communications, 52(92), 13471–13474.
47. Chong, P. A., Farber, P. J., Vernon, R. M., Hudson, R. P., Mittermaier, A. K., & Forman-Kay, J. D. (2015). Deletion of phenylalanine-508 in the first nucleotide binding domain of the cystic fibrosis transmembrane conductance regulator increases conformational exchange and inhibits dimerization. Journal of Biological Chemistry, 290, 22862–22878.
46. Mariaule, G., De Cesco, S., Airaghi, F., Kurian, J., Schiavini, P., Rocheleau, S., Huskić, I., Auclair, K., Mittermaier, A., & Moitessier, N. (2015). 3-Oxo-hexahydro-1H-isoindole-4-carboxylic acid as a drug chiral bicyclic scaffold: Structure-based design and preparation of conformationally constrained covalent and noncovalent prolyl oligopeptidase inhibitors. Journal of Medicinal Chemistry, 59(9), 4221–4234.
45. Miletti, T., Levros, L. C., Di Trani, J., & Mittermaier, A. (2015). Conformational plasticity surrounding the active site of NADH oxidase from Thermus thermophilus. Protein Science, 24, 1114–1128.
44. Farber, P. J., & Mittermaier, A. (2015). Relaxation dispersion NMR spectroscopy for the study of protein allostery. Biophysical Reviews, 7, 191–200.
43. Mittermaier, A. (2015). An enzyme cofactor with a split personality. Nature Structural & Molecular Biology, 22, 101–103.
42. Freiburger, L., Auclair, K., & Mittermaier, A. (2015). Global ITC fitting methods in studies of protein allostery. Methods, 76, 149–161.
41. Freiburger, L., Miletti, T., Zhu, S., Baettig, O., Berghuis, A., Auclair, K., & Mittermaier, A. (2014). Substrate-dependent switching of the allosteric binding mechanism of a dimeric enzyme. Nature Chemical Biology, 10, 937–942.
40. Meneses, E., & Mittermaier, A. (2014). Electrostatic interactions in the binding pathway of a transient protein complex studied by NMR and isothermal titration calorimetry. Journal of Biological Chemistry, 289, 27911–27923.
39. Castor, K., Liu, Z., Fakhoury, J., Hancock, M., Mittermaier, A., Autexier, C., Moitessier, N., & Sleiman, H. (2013). A platinum(II) phenylphenanthroimidazole with an extended side-chain exhibits slow dissociation from a c-kit G-quadruplex motif. Chemistry – A European Journal, 19, 17836–17845.
38. Mittermaier, A. (2013). ZZ-exchange. In G. Roberts (Ed.), Encyclopedia of Biophysics. Springer-Verlag.
37. Mittermaier, A., & Meneses, E. (2013). Analyzing protein-ligand interactions by dynamic NMR spectroscopy. In M. Williams & T. Daviter (Eds.), Methods in Molecular Biology/Springer Protocols (Vol. 1008, pp. 243–266). Humana Press.
36. Farber, P. J., Slager, J., & Mittermaier, A. (2012). Local folding and misfolding in the PBX homeodomain from a three-state analysis of CPMG relaxation dispersion NMR data. Journal of Physical Chemistry B, 116, 10317–10329.
35. De Cesco, S., Deslandes, S., Therrien, E., Levan, D., Cueto, M., Schmidt, R., Cantin, L. D., Mittermaier, A., Juillerat-Jeanneret, L., & Moitessier, N. (2012). Virtual screening and computational optimization for the discovery of covalent prolyl oligopeptidase inhibitors with activity in human cells. Journal of Medicinal Chemistry, 55, 6306–6315.
34. Castor, K., Kieltyka, R., Englebienne, P., Weill, N., Fakhoury, J., Mancini, J., Avakyan, N., Mittermaier, A., Autexier, C., Moitessier, N., & Sleiman, H. F. (2012). Platinum(II) phenanthroimidazoles for targeting telomeric G-quadruplexes. ChemMedChem, 7, 85–94.
33. Freiburger, L., Auclair, K., & Mittermaier, A. (2012). Van ’t Hoff global analyses of variable temperature isothermal titration calorimetry data. Acta Thermochimica, 527, 148–157.
32. Miletti, T., Farber, P. J., & Mittermaier, A. (2011). Active site dynamics in NADH oxidase from Thermus thermophilus studied by NMR spin relaxation. Journal of Biomolecular NMR, 51, 71–82.
31. Freiburger, L., Mittermaier, A., & Auclair, K. (2011). Collecting variable-concentration isothermal titration calorimetry datasets in order to determine binding mechanisms. Journal of Visualized Experiments, 50, e2529.
30. Farber, P. J., & Mittermaier, A. (2011). Concerted dynamics link allosteric sites in the PBX homeodomain. Journal of Molecular Biology, 405, 819–830.
29. Freiburger, L., Baettig, O. M., Berghuis, A. M., Sprules, T., Auclair, K., & Mittermaier, A. (2011). Competing allosteric mechanisms modulate substrate binding in a dimeric enzyme. Nature Structural & Molecular Biology, 18, 288–294.
28. Denisov, A., Kloser, E., Gray, D., & Mittermaier, A. (2010). Protein alignment using cellulose nanocrystals: Practical considerations and range of application. Journal of Biomolecular NMR, 47, 195–204.
27. Farber, P. J., Darmawan, H., Sprules, T., & Mittermaier, A. (2010). Analyzing protein folding cooperativity using NMR and DSC. Journal of the American Chemical Society, 132, 6214–6222.
26. Mittermaier, A., & Farber, P. J. (2010). NMR and calorimetry of biological systems. In S. Pascal & A. Dingely (Eds.), Advances in BioNMR Spectroscopy. IOS Press.
25. Freiburger, L. A., Auclair, K., & Mittermaier, A. K. (2009). Elucidating protein binding mechanisms by variable-c ITC. ChemBioChem, 10, 2871–2873.
24. Mittermaier, A., & Kay, L. E. (2009). Observing biological dynamics at atomic resolution using NMR. Trends in Biochemical Sciences, 34, 601–611.
23. Demers, J. P., & Mittermaier, A. (2009). Binding mechanism of an SH3 domain studied by NMR and ITC. Journal of the American Chemical Society, 131, 4355–4367.
22. Farber, P. J., & Mittermaier, A. (2008). Side chain burial and hydrophobic core packing in protein folding transition states. Protein Science, 17, 644–651.
21. Mittermaier, A., & Kay, L. E. (2006). New tools provide new insights in NMR studies of protein dynamics. Science, 312, 224–228.
20. Zarrine-Afsar, A., Mittermaier, A., Kay, L. E., & Davidson, A. R. (2005). Protein stabilization by specific binding of guanidinium to a functional arginine-binding surface on an SH3 domain. Protein Science, 15, 162–170.
19. Mittermaier, A., Korzhnev, D. M., & Kay, L. E. (2005). Side-chain interactions in the folding pathway of a Fyn SH3 domain mutant studied by relaxation dispersion NMR spectroscopy. Biochemistry, 44, 15430–15436.
18. Korzhnev, D. M., Neudecker, P., Mittermaier, A., Orekhov, V. Y., & Kay, L. E. (2005). Multiple-site exchange in proteins studied with a suite of six NMR relaxation dispersion experiments: An application to the folding of a Fyn SH3 domain mutant. Journal of the American Chemical Society, 127, 15602–15611.
17. Korzhnev, D. M., Mittermaier, A., & Kay, L. E. (2005). Cross-correlated spin relaxation effects in methyl ¹H CPMG-based relaxation dispersion experiments: Complications and simple solution. Journal of Biomolecular NMR, 4, 337–342.
16. Finerty, P. J. Jr., Mittermaier, A., Muhandiram, R., Kay, L. E., & Forman-Kay, J. D. (2005). NMR dynamics-derived insights into the binding properties of a peptide interacting with an SH2 domain. Biochemistry, 44, 694–703.
15. Mittermaier, A., & Kay, L. E. (2004). The response of internal dynamics to hydrophobic core mutations in the SH3 domain from the Fyn tyrosine kinase. Protein Science, 13, 1088–1099.
14. Mittermaier, A., Davidson, A. R., & Kay, L. E. (2003). Correlation between ²H NMR side-chain order parameters and sequence conservation in globular proteins. Journal of the American Chemical Society, 125, 9004–9005.
13. Millet, O., Mittermaier, A., Baker, D., & Kay, L. E. (2003). The effects of mutations on motions of side-chains in Protein L studied by ²H NMR dynamics and scalar couplings. Journal of Molecular Biology, 329, 551–563.
12. Mittermaier, A., & Kay, L. E. (2002). Effect of deuteration on some structural parameters of methyl groups in proteins as evaluated by residual dipolar couplings. Journal of Biomolecular NMR, 23, 35–45.
11. Mulder, F. A. A., Hon, B., Mittermaier, A., Dahlquist, F. W., & Kay, L. E. (2002). Slow internal dynamics in proteins: Application of NMR dispersion spectroscopy to methyl groups in a cavity mutant of T4 lysozyme. Journal of the American Chemical Society, 124(7), 1443–1451.
10. Davidson, A. R., Maxwell, K. L., Mittermaier, A. K., & Forman-Kay, J. D. (2002). Methods for in vivo selection of soluble protein domains. In M. P. Weiner & Q. Lu (Eds.), Gene Cloning and Expression Technologies. Eaton Publishing.
9. Mulder, F. A. A., Mittermaier, A., Hon, B., Dahlquist, F. W., & Kay, L. E. (2001). Studying excited states of proteins by NMR spectroscopy. Nature Structural Biology, 8(11), 932–935.
8. Evenäs, J., Mittermaier, A., Yang, D., & Kay, L. E. (2001). Measurement of ¹³Cα–¹³Cβ dipolar couplings in ¹⁵N, ¹³C, ²H-labeled proteins: Application to domain orientation in maltose binding protein. Journal of the American Chemical Society, 123(12), 2858–2864.
7. Mittermaier, A., & Kay, L. E. (2001). χ1 torsion angle dynamics in proteins from dipolar couplings. Journal of the American Chemical Society, 123(28), 6892–6903.
6. Mittermaier, A., & Kay, L. E. (1999). Measurement of methyl ²H quadrupolar couplings in oriented proteins: How uniform is the quadrupolar coupling constant? Journal of the American Chemical Society, 121(45), 10608–10613.
5. Mittermaier, A., Kay, L. E., & Forman-Kay, J. D. (1999). Analysis of deuterium relaxation-derived methyl axis order parameters and correlation with local structure. Journal of Biomolecular NMR, 13, 181–185.
4. Mittermaier, A., Varani, L., Muhandiram, D. R., Kay, L. E., & Varani, G. (1999). Changes in side chain and backbone dynamics identify determinants of specificity in RNA recognition by human U1A protein. Journal of Molecular Biology, 294, 967–979.
3. Maxwell, K. L., Mittermaier, A., Forman-Kay, J. D., & Davidson, A. R. (1999). A simple in vivo assay for increased protein solubility. Protein Science, 8, 1908–1911.
2. Yang, D., Mittermaier, A., Mok, Y. K., & Kay, L. E. (1998). A study of protein side chain dynamics from new ²H auto-correlation and ¹³C cross-correlation NMR experiments: Application to the N-terminal SH3 domain from drk. Journal of Molecular Biology, 276, 939–954.
1. Olive, J. E., De Abreu, D. M., Rastogi, T., Andersen, A., Mittermaier, A., Beattie, T., & Collins, R. A. (1995). Enhancement of Neurospora VS ribozyme cleavage by tuberactinomycin antibiotics. The EMBO Journal, 14, 3247–3251.