Postdoctoral Fellow - University of Utrecht, The Netherlands
PhD - Institut Curie, Paris, France
BS - University of Ioannina, Greece
Honors & Awards
- 2020 Biophysical Society Fellow Award
- 2017 The Raymond and Beverly Sackler International Prize in the Physical Sciences
- 2017 Henry A. Lardy Distinguished Lecturer
- 2013 Stig Sunner Young Investigator Award
- 2011 Biophysical Society Michael and Kate Bárány Young Investigator Award
- 2011 New York Academy of Sciences Blavatnik Young Investigator Award
- 2010 Protein Society Young Investigator Award
My lab works on the determination of the structural and dynamic basis for the function and operation of complex protein machineries that are involved in key biological processes. We aim to understand at the atomic level how these machineries work inside the cell. We combine high-resolution NMR spectroscopy with other structural biology approaches to gain unprecedented insights into the sophisticated mechanisms of action of the following protein systems:
- Protein kinases, such as the Bcr-Abl causing chronic myelogenous leukemia
- Molecular chaperones, such as the Hsp90 and Hsp70/40 families involved in cancer
- The injectisome and the flagellum machineries in pathogenic bacteria involved in infectious diseases
- Membrane transporter proteins in pathogenic bacteria
Jiang, Y, Rossi, P, Kalodimos CG. Structural basis for client recognition and activity of Hsp40 chaperones. Science 365:1313-1319, 2019.
Saleh T, Rossi P, Kalodimos CG. Atomic view of the energy landscape in the allosteric regulation of Abl kinase. Nat Struct Mol Biol Nov;24:893-901, 2017.
Saleh T, Kalodimos CG. Enzymes at work are enzymes in motion. Science 355:247-248, 2017.
Huang C, Saio T, Rossi P, Kalodimos CG. Structural basis for the antifolding activity of a molecular Chaperone. Nature 537:202-206, 2016.
Khanra N, Rossi P, Economou A, Kalodimos CG. Recognition and targeting mechanisms by chaperones in flagellum assembly and operation. Proceedings of the National Academy of Sciences of USA 113:9798-9803, 2016.
Saleh T, Jankowski W, Sriram G, Rossi P, Shah S, Lee KB, Cruz LA, Rodriguez AJ, Birge RB, Kalodimos CG. Cyclophilin A promotes cell migration via the Abl-Crk signaling pathway. Nature Chemical Biology 12:117-123, 2016.
Saio T, Guan X, Rossi P, Economou A, Kalodimos CG. Structural basis for protein anti-aggregation activity of the Trigger Factor Chaperone. Science 344:1250494-13, 2014.
Tzeng H-S, Kalodimos CG. Allosteric inhibition through suppression of transient conformational states. Nature Chemical Biology 9:462-465, 2013.
Chen L, Ai X, Portaliou A, Remeta D, Menetti C, Economou A, Kalodimos CG. Substrate-activated conformational switch on chaperones encodes a targeting signal in type III secretion. Cell Reports 3:709-715, 2013.
Tinberg CE, Khare SD, Dou J, Doyle L, Nelson JW, Schena A, Jankowski W, Kalodimos CG, Johnsson K, Stoddard BL, Baker D. Computational Design of Ligand Binding Proteins with High Affinity and Selectivity. Nature 501:212-216, 2013.
Saio T, Kalodimos CG. NMR disentangles a dynamic disaggregase machinery. Nature Structural & Molecular Biology 20:409-410, 2013.
Tzeng H-S, Kalodimos CG. Protein activity regulation by conformational entropy. Nature 488:236-240, 2012.
Jankowski W, Saleh T, Pai M-T, Sriram G, Birge RB, Kalodimos CG. Domain organization differences explain Bcr-Abl’s preference for CrkL over CrkII. Nature Chemical Biology 8:590-596, 2012.
Chen L, Balabanidou V, Remeta D, Menetti C, Economou A, Kalodimos CG. Structural instability tuning as a regulatory mechanism in protein-protein interactions. Molecular Cell 44:734-744, 2011.
Sarkar P, Saleh T, Tzeng H-S, Birge RB, Kalodimos CG. Structural basis for regulation of the Crk signaling protein. Nature Chemical Biology 7:51-57, 2011.
Pai M-T, Kalodimos CG. Dynamic fluctuations lubricate the circadian clock. Proceedings of the National Academy of Sciences of USA 108:14377-14378, 2011.
Tzeng H-S, Kalodimos CG. Dynamic activation of an allosteric regulatory protein. Nature 462:368-372, 2009.
Gouridis G, Karamanou S, Gelis I, Kalodimos CG, Economou A. Signal sequences are allosteric activators of the protein translocase. Nature 462:363-367, 2009.
Popovych N, Tzeng H-S, Tonelli M, Ebright RH, Kalodimos CG. Structural basis for cAMP-mediated allosteric control of the catabolite activator protein. Proceedings of the National Academy of Sciences of USA 106:6927-6932, 2009.
Gelis I, Bonvin A, Keramisanou D, Economou A, Kalodimos CG. Structural basis for signal sequence recognition by the 204-kDa translocase motor SecA determined by NMR. Cell 131:756-769, 2007.
Sarkar P, Reichman C, Saleh T, Birge RB, Kalodimos CG. Proline cis-trans isomerization controls autoinhibition of a signaling protein. Molecular Cell 25:413-426, 2007.
Popovych N, Sun S, Ebright RH, Kalodimos CG. Dynamically driven protein allostery. Nature Structural & Molecular Biology 13:831-838, 2006.
Keramisanou D, Biris N, Gelis I, Sianidis G, Karamanou S, Economou A, Kalodimos CG. Disorder-order transitions underlie catalysis of the helicase motor of SecA. Nature Structural & Molecular Biology 13:594-602, 2006.
Kalodimos CG, Biris N, Bonvin AMJJ, Levandoski M, Guennuegues M, Boelens R, Kaptein R. Structure and Flexibility Adaptation in Nonspecific and Specific Protein-DNA Complexes. Science 305:386-389, 2004.
Kalodimos CG, Bonvin AMJJ, Salinas RK, Weschelberger R, Boelens R, Kaptein R. Plasticity in Protein-DNA recognition: lac Repressor Recognizes its Natural Operator with Alternative Conformations of its DNA-Binding Domain. The EMBO Journal 21:2866-2876, 2002.
Kalodimos CG, Boelens R, Kaptein R. A Residue-Specific View of the Association and Dissociation Pathway in Protein-DNA Recognition. Nature Structural Biology 9:193-197, 2002.
Kalodimos CG, Folkers G, Boelens R, Kaptein R. Strong DNA Binding by Covalently-Linked Lac Headpiece: The Crucial Role of Hinge Helices. Proceedings of the National Academy of Sciences of USA 98:6039-6044, 2001.
Last update: October 2019