Carla Mattos Kearney, B. M., Schwabe, M., Marcus, K. C., Roberts, D. M., Dechene, M., Swartz, P., & Mattos, C. (2020). DRoP: Automated detection of conserved solvent-binding sites on proteins. PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 88(1), 152–165. https://doi.org/10.1002/prot.25781 Schwabe, M., Holzapfel, G., & Mattos, C. (2020, April). Exploring the Rap1A Active Site Through Accelerated Molecular Dynamic Simulations. FASEB JOURNAL, Vol. 34. https://doi.org/10.1096/fasebj.2020.34.s1.02775 Knihtila, R., Volmar, A. Y., Meilleur, F., & Mattos, C. (2019). Titration of ionizable groups in proteins using multiple neutron data sets from a single crystal: application to the small GTPase Ras. ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 75(2), 111–115. https://doi.org/10.1107/S2053230X18018125 Ashkar, R., Bilheux, H. Z., Bordallo, H., Briber, R., Callaway, D. J. E., Cheng, X., … Smith, J. C. (2018). Neutron scattering in the biological sciences: progress and prospects. ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 74, 1129–1168. https://doi.org/10.1107/S2059798318017503 Fetics, S. K., Guterres, H., Kearney, B. M., Buhrman, G., Ma, B., Nussinov, R., & Mattos, C. (2015). Allosteric Effects of the Oncogenic RasQ61L Mutant on Raf-RBD. STRUCTURE, 23(3), 505–516. https://doi.org/10.1016/j.str.2014.12.017 Knihtila, R., Holzapfel, G., Weiss, K., Meilleur, F., & Mattos, C. (2015). Neutron Crystal Structure of RAS GTPase Puts in Question the Protonation State of the GTP gamma-Phosphate. JOURNAL OF BIOLOGICAL CHEMISTRY, 290(52), 31025–31036. https://doi.org/10.1074/jbc.m115.679860 Kearney, B. N., Johnson, C. W., Roberts, D. M., Swartz, P., & Mattos, C. (2014). DRoP: A Water Analysis Program Identifies Ras-GTP-Specific Pathway of Communication between Membrane-Interacting Regions and the Active Site. JOURNAL OF MOLECULAR BIOLOGY, 426(3), 611–629. https://doi.org/10.1016/j.jmb.2013.10.036 Walters, J., Schipper, J. L., Swartz, P., Mattos, C., & Clark, A. C. (2012). Allosteric modulation of caspase 3 through mutagenesis. BIOSCIENCE REPORTS, 32(4), 401–411. https://doi.org/10.1042/bsr20120037 Holzapfel, G., Buhrman, G., & Mattos, C. (2012). Shift in the Equilibrium between On and Off States of the Allosteric Switch in Ras-GppNHp Affected by Small Molecules and Bulk Solvent Composition. BIOCHEMISTRY, 51(31), 6114–6126. https://doi.org/10.1021/bi300509j Gagnon, K. T., Biswas, S., Zhang, X., Brown, B. A., II, Wollenzien, P., Mattos, C., & Maxwell, E. S. (2012). Structurally Conserved Nop56/58 N-terminal Domain Facilitates Archaeal Box C/D Ribonucleoprotein-guided Methyltransferase Activity. JOURNAL OF BIOLOGICAL CHEMISTRY, 287(23), 19418–19428. https://doi.org/10.1074/jbc.m111.323253 Buhrman, G., Kumar, V. S. S., Cirit, M., Haugh, J. M., & Mattos, C. (2011). Allosteric Modulation of Ras-GTP Is Linked to Signal Transduction through RAF Kinase. JOURNAL OF BIOLOGICAL CHEMISTRY, 286(5), 3323–3331. https://doi.org/10.1074/jbc.m110.193854 Biswas, S., Buhrman, G., Gagnon, K., Mattos, C., Brown, B. A., II, & Maxwell, E. S. (2011). Comparative Analysis of the 15.5kD Box C/D snoRNP Core Protein in the Primitive Eukaryote Giardia lamblia Reveals Unique Structural and Functional Features. BIOCHEMISTRY, 50(14), 2907–2918. https://doi.org/10.1021/bi1020474 Walters, J., Swartz, P., Mattos, C., & Clark, A. C. (2011). Thermodynamic, enzymatic and structural effects of removing a salt bridge at the base of loop 4 in (pro)caspase-3. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 508(1), 31–38. https://doi.org/10.1016/j.abb.2011.01.011 Buhrman, G., Holzapfel, G., Fetics, S., & Mattos, C. (2010). Allosteric modulation of Ras positions Q61 for a direct role in catalysis. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 107(11), 4931–4936. https://doi.org/10.1073/pnas.0912226107 Walters, J., Pop, C., Scott, F. L., Drag, M., Swartz, P., Mattos, C., … Clark, A. C. (2009). A constitutively active and uninhibitable caspase-3 zymogen efficiently induces apoptosis. BIOCHEMICAL JOURNAL, 424, 335–345. https://doi.org/10.1042/bj20090825 Brenke, R., Kozakov, D., Chuang, G.-Y., Beglov, D., Hall, D., Landon, M. R., … Vajda, S. (2009). Fragment-based identification of druggable 'hot spots' of proteins using Fourier domain correlation techniques. BIOINFORMATICS, 25(5), 621–627. https://doi.org/10.1093/bioinformatics/btp036 Dechene, M., Wink, G., Smith, M., Swartz, P., & Mattos, C. (2009). Multiple solvent crystal structures of ribonuclease A: An assessment of the method. PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 76(4), 861–881. https://doi.org/10.1002/prot.22393 Mattos, C., & Clark, A. C. (2008). [Review of Minimizing frustration by folding in an aqueous environment]. Archives of Biochemistry and Biophysics, 469(1), 118–131. Milam, S. L., Nicely, N. I., Feeney, B., Mattos, C., & Clark, A. C. (2007). Rapid folding and unfolding of Apaf-1 CARD. JOURNAL OF MOLECULAR BIOLOGY, 369(1), 290–304. https://doi.org/10.1016/j.jmb.2007.02.105 Buhrman, G., Wink, G., & Mattos, C. (2007). Transformation efficiency of RasQ61 mutants linked to structural features of the switch regions in the presence of Raf. STRUCTURE, 15(12), 1618–1629. https://doi.org/10.1016/j.str.2007.10.011 Mattos, C., Bellamacina, C. R., Peisach, E., Pereira, A., Vitkup, D., Petsko, G. A., & Ringe, D. (2006). Multiple solvent crystal structures: Probing binding sites, plasticity and hydration. JOURNAL OF MOLECULAR BIOLOGY, 357(5), 1471–1482. https://doi.org/10.1016/j.jmb.2006.01.039 Feeney, B., Pop, C., Swartz, P., Mattos, C., & Clark, A. C. (2006). Role of loop bundle hydrogen bonds in the maturation and activity of (pro) caspase-3. BIOCHEMISTRY, 45(44), 13249–13263. https://doi.org/10.1021/bi0611964 Buhrman, G., Parker, B., Sohn, J., Rudolph, J., & Mattos, C. (2005). Structural mechanism of oxidative regulation of the phosphatase Cdc25B via an intramolecular disulfide bond. BIOCHEMISTRY, 44(14), 5307–5316. https://doi.org/10.1021/bi047449f Nicely, N. I., Kosak, J., Serrano, V., & Mattos, C. (2004). Crystal structures of Ral-GppNHp and Ral-GDP reveal two binding sites that are also present in Ras and Rap. STRUCTURE, 12(11), 2025–2036. https://doi.org/10.1016/j.str.2004.08.011 Mattos, C., Cohen, J. D., Green, D. F., Tidor, B., & Karplus, M. (2004). X-ray structural and simulation analysis of a protein mutant: The value of a combined approach. PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 55(3), 733–742. https://doi.org/10.1002/prot.20031 Buhrman, G., Serrano, V., & Mattos, C. (2003). Organic solvents order the dynamic switch II in Ras crystals. STRUCTURE, 11(7), 747–751. https://doi.org/10.1016/s0969-2126(03)00128-x Mattos, C. (2002). [Review of Protein-water interactions in a dynamic world]. Trends in Biochemical Sciences, 27(4), 203–208. Mattos, C., & Ringe, D. (2001). Proteins in organic solvents. CURRENT OPINION IN STRUCTURAL BIOLOGY, 11(6), 761–764. https://doi.org/10.1016/S0959-440X(01)00278-0