Cláudio M. Gomes


Instituto de Biosistemas e Ciências Integrativas

Sala/Gabinete 8.5.37
Ext. Principal 28537 Ext. Alt 28556
Telefone Direto 217500971
Página Pessoal

Carreira Docente Universitário
Categoria Professor Associado


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Scientific Interests

I coordinate the Protein Misfolding and Amyloids in Biomedicine research laboratory, and my research at ULisboa aims to decipher molecular mechanisms underlying protein misfolding and aggregation in human disease, with a focus on amyloid formation in neurodegenerative diseases.

We investigate novel anti-aggregation chaperones in Alzheimer's Disease and how metal ions in the brain influence amyloid formation. We also research on protein misfolding in mitochondrial metabolic and neurological diseases. Experimentally, my laboratory combines molecular, cellular and biochemical approaches to investigate protein structure and self-assembly in vitro and in cells.

More details about our research, publications and current research team at

Publicações selecionadas
  • 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
  • Cristovao, J. S., Figueira, A. J., Carapeto, A. P., Rodrigues, M. S., Cardoso, I., and Gomes, C. M. (2020) The S100B Alarmin Is a Dual-Function Chaperone Suppressing Amyloid-beta Oligomerization through Combined Zinc Chelation and Inhibition of Protein Aggregation, ACS chemical neuroscience 11, 2753-2760.
  • Cristóvão, J. S., and Gomes, C. M. (2019) S100 Proteins in Alzheimer’s Disease. Frontiers in Neuroscience 13
  • 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

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