Maria Carrondo

Head of the ITQB-UNL MX Unit, Vice-Rector of UNL

Universidade Nova de Lisboa

Innate ImmunityTLRsNLRsprotein-protein interactions
Maria Arménia Carrondo Maria Arménia Carrondo, born in 31.07.1948 in Portugal, is the leader for the Portuguese National Affiliate Centre and has coordinated all the process leading to the application of the Portuguese membership to Instruct. The Portuguese scientific community related with the mission of INSTRUCT agreed that there is great interest from the different areas of research already established in Portugal to participate in INSTRUCT since this would constitute a clear impact to Portuguese research in Structural Biology and related methodologies. The existing know-how should be the basis for the establishment of a large network of Centers in the form of a National Centre. diffraction, Mass Spectrometry, other Biophysical Methods, Protein Production and Light Microscopy. The goal is to strengthen the current Portuguese infrastructure by providing a platform to promote the integration of the various techniques and develop current projects taking advantage of the European facilities. MAC is currently the representative of ITQB as a partner of the BioStruct-X, a project of translational access and enhancement of integrated Biological Structure determination at synchrotron X-ray facilities. Maria Arménia Carrondo (MAC) is Vice-Rector of the Universidade Nova de Lisboa (UNL) since 2007 and Professor at Instituto de Tecnologia Química e Biológica (ITQB), UNL, where she was Vice-Director between 1996 and 2005. MAC is the coordinator of the Macromolecular Crystallography Unit at ITQB, was elected EMBO member in 2000 and awarded the European Medal for Bio-Inorganic Chemistry in 2004. MAC was the representative of the Portuguese Government at the ESRF Council (1998-2002) and coordinator at the national level of the process that led to the Portuguese membership of ESRF in 1998. MAC has for a long time been involved with European Synchrotrons panels, namely as a member of the Scientific Advisory Committee of ESRF since 2012, a member of the Review Panel of the EMBL Hamburg Outstation in 2011 and 2003, a member of the Scientific Advisory Board of the EMBL-PETRAIII project since 2008, a member of the Review Panel for the MAX laboratory in Lund between 2009- 2011. Between 2009 and 2011, MAC was one of the user representatives in the I3 ELISA project, the world´s largest network of research facilities. MAC has also served as a member of the Priorities Committee of the EMBL Hamburg Outstation between 1999 and 2011 2005 as a member of the ESRF Review Committee in Life Sciences - Protein Crystallography (2000-2003). MAC was the coordinator for the ITQB participation as partner of the EU integrated project SPINE2-Complexes, the Specific Support Action TEACH-SG, the EU Infrastructure Cooperation Network MAX-INF2 and associated TID centre to the EU integrated project BIOXHIT. MAC was co-Director of the Erice 2010 “Structure and Function from Macromolecular Crystallography: Organisation in Space and Time” and organizer of the BioCrys courses on “Fundamentals of modern methods in Biocrystallography”, held at ITQB, in 2002, 2004, 2006, 2008 and 2010. MAC scientific interests currently focus on structural studies of protein and protein complexes implicated in health sciences, in particular proteins of the innate immune system, and also metalloproteins and metalloenzymes. MAC has currently 149 publications in international refereed journals included in the web of science, with 3728 citations and an h-index of 35. Selected List of Publications • P.M. Matias, P. Donner, R. Coelho, M. Thomaz, C. Peixoto, S. Macedo, N. Otto, S. Joschko, P. Scholz, A. Wegg, S. Bäsler, M. Schäfer, U. Egner and M.A. Carrondo, “Structural evidence for ligand specificity in the binding domain of the human Androgen receptor : implications for phatogenic gene mutations” J. Biol. Chem. (2000) 275: 26164-26171, First structure of the LBD of the Androgen receptor subsequently used for drug discovery , Times cited: 321 • C. Frazão, G. Silva, C. M. Gomes, P. Matias, R. Coelho, L. Sieker, S. Macedo, M. Y. Liu, S. Oliveira, M. Teixeira, A. V. Xavier, C. Rodrigues-Pousada, M. A. Carrondo, and J. Le Gall, “Structure of a dioxygen reduction enzyme from Desulfovibrio gigas”, Nature Struct. Biol. (2000) 7: 1041-1045, Times cited: 129. • P.M. Matias, C. M. Soares, L. M. Saraiva, R. Coelho, J. Morais, J. Le Gall and M.A. Carrondo, “[NiFe] Hydrogenase from Desulfovibrio desulfuricans ATCC 27774: Gene sequencing, three-dimensional structure determination and refinement at 1.8 Å and modelling studies of its interaction with the tetra-haem cytochrome c3 “, J. Biol. Inorg. Chem., (2001) 6: 63-81, Times cited: 111. • M. A. Carrondo “Ferritins, Iron Uptake and Storage from the Bacterioferritin Viewpoint” EMBO J. (2003), 22, 1959-1968, Times cited: 90. • S. Macedo, C. V. Romão, E. Mitchell , P. M. Matias, M. Y. Liu , A. V. Xavier , J. LeGall , M. Teixeira, P. Lindley and M. A. Carrondo “The nature of the di-iron site in the bacterioferritin from Desulfovibrio desulfuricans” Nature Struct. Biol (2003), 10, 285-290, Times cited: 50. • I. Bento, L. O. Martins, G. G. Lopes, M. A. Carrondo and P. F. Lindley “Dioxygen reduction by multi-copper oxidases; a structural perspective”, Roy. Soc. Chem. Dalton Trans. (2005), 3507-3513, Times cited : 46. • C. Frazão, C. E. McVey, M. Amblar, A. Barbas, C. Vonrhein, C. M. Arraiano and M.A. Carrondo “Unravelling the dynamics of RNA degradation by RNAse II and its RNA- bound complex”, Nature (2006), 443, 110-114, Times cited: 72. • P. M. Matias, S. Gorynia, P. Donner, M. A. Carrondo, “Crystal Structure of the Human AAA+ Protein RuvBL1”, J. Biol. Chem. (2006) 281, 38918-38929. Times cited: 29. • M de Rosa, D. de Sanctis, M. Archer, A. Rich, A. Athanasiadis and M. A. Carrondo “Crystal structure of a junction between two Z-DNA helices" PNAS (2010), 107, 9088-9092. Times cited: 2 • S. Gorynia, T. M. Bandeiras, F. G. Pinho, C. E. McVey, C. Vonrhein, A. Round, D. I. Svergun, P. Donner, P. M. Matias and M. A. Carrondo “Structural and functional insights into a dodecameric molecular machine – The RuvBL1/RuvBL2 complex”,