- Cristovao, J. S., Morris, V. K., Cardoso, I., and Leal, S. S. (2018) The neuronal S100B protein is a calcium-tuned suppressor of amyloid-beta aggregation. Science Advances 4(6) eaaq1702. (10.1126/sciadv.aaq1702)
- Hagmeyer S, Cristóvão JS, Mulvihill JJE, Boeckers TM, Gomes CM, Grabrucker AM. Zinc Binding to S100B Affords Regulation of Trace Metal Homeostasis and Excitotoxicity in the Brain. Front Mol Neurosci. (2018) 10:456. doi: 10.3389/fnmol.2017.00456
- Cristóvão, J.S., Santos, R., Gomes, C.M. Metals and neuronal metal binding proteins implicated in Alzheimer’s disease. Oxidative Medicine and Cellular Longevity (2016) Article ID 9812178 (10.1155/2016/9812178)
- Leal, S.S., Cardoso, I., Valentine, J.S. and Gomes, C.M. Calcium ions promote superoxide dismutase 1 (SOD1) aggregation into non fibrillar amyloid: a link to toxic effects of calcium overload in amyotrophic lateral sclerosis (ALS)? J. Biol. Chem. (2013) 288(35):25219-28
- Leal, S.S., Botelho, H. M., Gomes, C.M. Metal ions as modulators of protein conformation and misfolding in neurodegeneration Coordination Chemistry Reviews (2012) 256(19-20): 2253-2270
Cláudio M. Gomes
ContactosInstituto de Biosistemas e Ciências Integrativas
Ext. Principal 28537 Ext. Alt 28556
Telefone Direto 217500971
Carreira Docente Universitário
Categoria Professor Associado
The scientific activity of my laboratory (http://folding.fc.ul.pt/) focuses on research on the structural biochemistry and molecular biophysics of protein folding.
Our mission is to contribute to the molecular understanding of the mechanisms underlying protein misfolding and aggregation that occur in numerous protein folding diseases, and to establish the contribution of chemical and biochemical factors that are present in the cellular environments in which these processes develop.
For instance, we are studying how amyloid formation in neurodegenerative diseases such as Alzheimer's Disease and Amyotrophic Lateral Sclerosis is regulated by neuronal metal ions and by regulatory alarmin proteins that are highly abundant in the nervous systems in response to neuroinflammation.
In another example, we are investigating the folding of mitochondrial enzymes involved in metabolic disease in connection with accumulating metabolites that promote protein post translational modifications, whose role in pathophysiology we seek to uncover.
Experimentally, we have the resources to undertake a comprehensive experimental approach, combining molecular, cellular and biochemical methodologies, including spectroscopic and biophysical techniques for protein structural and functional analysis on which we have a unique track record and experience. Through collaboration with colleagues from different areas, from clinicians to physicists, we greatly expand our experimental toolbox and gain access to biological materials (including patient derived cells and tissues) and methodological resources that allow us to undertake a global multidisciplinary approach to tackle our research question, in an integrated perspective from molecules, to cells to organisms.
The Protein Folding and Misfolding Laboratory is a vibrant workplace with members from different backgrounds and training levels, committed to engage into multidisciplinary and collaborative research. For more information and details visit http://folding.fc.ul.pt/