- Javier Coloma
- Ana I. Hernández
- María Ibarra
- Andrés López
- Ángel Rivera
- Marina Serna
- Sofía Cabezudo
- Alba Ruiz
- Natalia Cuervo
- Carlos Fernández
- Ana González
Our key mission is to provide in-depth structural and molecular understanding of how macromolecular complexes implicated in cancer work. This information is essential to comprehend why and how some proteins are involved in the development of cancer. This fundamental knowledge is the basis to start the search for potential strategies to interfere with the function of these macromolecules. To accomplish this, we make use of several biochemical and molecular biology tools in combination with cryo-electron microscopy (cryo-EM). Cryo-EM is used to visualise large macromolecular complexes, and to observe their motions. Two main objectives drive our current research: (i) the study of macromolecular complexes that function in the cellular response to DNA damage; and (ii) an HSP90 co-chaperone network implicated in the assembly, activation and regulation of several complexes that are essential for cancer progression. In addition, we also address other relevant questions about human disease, in collaboration with other groups.
- (2020). RPAP3 C-Terminal Domain: A Conserved Domain for the Assembly of R2TP Co-Chaperone Complexes. Cells 9, E1139. CNIO Publication.
- (2020). Modeling of a 14 kDa RUVBL2-Binding Domain with Medium Resolution Cryo-EM Density.. J Chem Inf Model (in press). CNIO Publication.
- (2019). Architecture of the mycobacterial type VII secretion system. Nature 576, 321-325. CNIO Publication.
- (2019). Hands on Methods for High Resolution Cryo-Electron Microscopy Structures of Heterogeneous Macromolecular Complexes.. Front Mol Biosci 6, 33. CNIO Publication. Open Access
- (2019). Editorial: Technical Advances in Cryo-Electron Microscopy.. Front Mol Biosci 6, 72. CNIO Publication. Open Access
- (2019). Structural mechanism for regulation of the AAA-ATPases RUVBL1-RUVBL2 in the R2TP co-chaperone revealed by cryo-EM. Sci Adv 5, eaaw1616. CNIO Publication. Open Access
- (2018). CryoEM reveals how the complement membrane attack complex ruptures lipid bilayers. Nat Commun 9, 5316. CNIO Publication. Open Access
- (2018). RPAP3 provides a flexible scaffold for coupling HSP90 to the human R2TP co-chaperone complex. Nat Commun 9, 1501. CNIO Publication. Open Access
- (2018). How novel structures inform understanding of complement function. Semin Immunopathol 40, 3-14. CNIO Publication.
- (2018). Advances on the Structure of the R2TP/Prefoldin-like Complex. Adv Exp Med Biol 1106, 73-83. CNIO Publication.
- (2017). The structure of the R2TP complex defines a platform for recruiting diverse client proteins to the HSP90 molecular chaperone system.. Structure 25, 1145-1152. Publication in other institutions.
- (2017). Functional and structural characterization of four mouse monoclonal antibodies to complement C3 with potential therapeutic and diagnostic applications. Eur J Immunol 47, 504-515. Publication in other institutions.
- (2017). Self-Organization of FtsZ Polymers in Solution Reveals Spacer Role of the Disordered C-Terminal Tail.. Biophys J 113, 1831-1844. CNIO Publication.
- (2017). Ionic tethering contributes to the conformational stability and function of complement C3b.. Mol Immunol 85, 137-147. Publication in other institutions.
- (2017). Transmission Cryo-electron Microscopy in Drug Discovery.Royal Society of Biochemistry.. Biophysical Techniques in Drug Discovery (in press). CNIO Publication.
- (2016). The RNA helicase DHX34 functions as a scaffold for SMG1-mediated UPF1 phosphorylation.. Nat Communications 7, 10585. Publication in other institutions.
- (2016). Human nonsense-mediated mRNA decay factor UPF2 interacts directly with eRF3 and the SURF complex.. Nucleic Acids Res 44, 1909-1923. Publication in other institutions.
- (2015). Amyloidogenesis of bacterial prionoid RepA-WH1 recapitulates dimer to monomer transitions of RepA in DNA replication initiation.. Structure 23, 183-189. Publication in other institutions.
- (2015). Structural insights on complement activation.. FEBS J 282, 3883-3891. Publication in other institutions.
- (2015). Structure and Assembly of the PI3K-like Protein Kinases (PIKKs) Revealed by Electron Microscopy .. AIMS BIOPHYSICS 2, 36-57. Publication in other institutions.