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Antonio Artigues-Serra, PhD

Antonio Artigues-Serra portrait
Research Professor, Biochemistry and Molecular Biology

Director of the Mass Spectrometry/Proteomics Core Facility, Director, SOM-Kansas City

Professional Background

Virginia Commonwealth University, Postdoctoral Fellow, 1988-90
University of Alicante, Fellow, 1991
University of Missouri-Kansas City, Research Instructor, 1992-1996
University of Missouri-Kansas City, Supervisor of Macromolecular Analysis Core Facilities, 1996-2001
University of Missouri-Kansas City, Research Assistant Professor and Deputy Director for Research Development, 2001-2004
University of Kansas Medical Center, Research Assistant Professor and Director of the Mass Spectrometry Laboratory, 2004-2009
University of Kansas Medical Center, Research Associate Professor and Director of the Mass Spectrometry Laboratory, 2009-present

Education and Training
  • MS, Edaphology, Univ. of Navarra, Pampona, Navarra
  • MS, Neurochemistry, Univ. of Navarra, Pamplona, Navarra
  • PhD, Neurochemistry, Univ of Balearic Islands, Palma de Mallorc, Baleares
  • Post Doctoral Fellowship, Protein degratation and aging, Medical College of Virginia - Virginia Comonweath University, Richmond, VA
  • Post Doctoral Fellowship, Neurochemistry, University of Alicante, Alicante, Alicante
  • Post Doctoral Fellowship, Protein Folding, School of Biological Sciences - University of Missouri Kansas City, Kansas City, MO



Research Areas of Interest
Protein-protein interactions
Enzyme structure and relationship of enzyme structure to function
Protein folding
Mechanisms of Protein transport across membranes

Current Interest
Newly made proteins must achieve their native configuration before they can play their physiological roles in the cell. These processes are of particular importance for mitochondria. Of the roughly 1100 different proteins present in the mitochondrion only 13 are encoded by the mitochondrial DNA and synthesized in the mitochondrial matrix. The remaining proteins are encoded by the nuclear genome, transcribed in the nucleus, translated in the cytoplasm and imported into the mitochondrion, where they fold to their native structure. Understanding these processes at the molecular level is of the utmost importance because alterations in protein folding or mitochondrial protein translocation cause disease.

The model system used to study this process is the eukaryotic isoenzymes of aspartate aminotransferase. Two isoenzymes, one cytosolic, the other mitochondrial, exist in all eukaryotic cells. These proteins have extensive amino acid similarity, an almost identical three dimensional structure, are encoded by the genomic DNA, and are synthesized in the cytoplasm. Despite these similarities the mature proteins have different folding kinetics and different sub-cellular locations. Our main goals are to understand; (a) the molecular basis for the distinct folding behavior of these homologous proteins, and (b) to elucidate the mechanisms for the differences observed in their interactions with the cellular machineries in charge of protein sorting, import and folding.