A.C.D. Plufck, D.P.C. de Barros, L.P. Fonseca, E.P. Melo* (2018) Stability of lipases in miniemulsion systems: Correlation between secondary structure and activity”, Enz. Microbiol. Technol. 114: 7-14.
E.P. Melo, C. Lopes, P. Gollwitzer, S. Lortz, S. Lenzen, I. Mehmeti, C. F. Kaminski, D. Ron, E. Avezov (2017) “Triper, an optical probe tuned to the endoplasmic reticulum tracks changes in luminal H2O2”, BMC Biology 15: 24.
Macedo, J.A., D. Schrama, I. Duarte, E. Tavares, J. Renault, M.E. Futschik, P.M. Rodrigues, E.P. Melo* (2017) “Membrane-enriched proteome changes and prion protein expression during neural differentiation and in neuroblastoma cells.” BMC Genomics 18: 319.
Anjos, L., I. Morgado, M. Guerreiro, J. C. Cardoso, E. P. Melo, D. M. Power (2017) “Cartilage Acidic Protein 1 (CRTAC1), a new member of the beta-propeller protein family with amyloid propensity”, Proteins 85: 242-255.
Konno, K., E. P. Melo, C. Lopes, C. F. Kaminski, I. Mehmeti, S. Lenzen, D. Ron, E. Avezov (2015) “ERO1-independent production of H2O2 within the endoplasmic reticulum fuels Prdx4 mediated oxidative protein folding”, J. Cell Biol. 211: 253-259.
Estrela, N., H. G. Franquelim, C. Lopes, E. Tavares, J. A. Macedo, G. Christiansen, D. E. Otzen, E. P. Melo* (2015) “Sucrose prevents protein fibrillation through compaction of the tertiary structure but hardly affects the secondary structure”
Proteins 83: 2039-2051.
Avezov, E., T. Konno, A. Zyryanova, W. Chen, R. Laine, A. Crespillo-Casada, E. P. Melo, R. Ushioda, K. Nagata, C. F. Kaminski, H. P. Harding, D. Ron (2015) “Retarded PDI diffusion and a reductive shift in poise of the calcium depleted endoplasmic reticulum”
BMC Biology 13: 2.
Tsunoda, S., E. Avezov, A. Zyryanova, T. Konno, L. Mendes-Silva, E. P. Melo, H. P. Harding, D. Ron (2014) “Intact protein folding in the glutathione-depleted endoplasmic reticulum implicates alternative protein thiol reductants”
eLife 3: e03421.
Tavares, E., J. A. Macedo, P. M. R. Paulo, C. Tavares, C. Lopes, E. P. Melo* (2014) “Live-cell FRET imaging reveals clustering of the prion protein at the cell surface induced by infectious prions” Biochim. Biophys. Acta – Molecular Basis of Disease 11: 744-751.
Brissos, V., N. Gonçalves, E. P. Melo, L. O. Martins (2014) “Directed evolution leads to aggregation-resistant variants with improved stability” PLOS One 9: e87209.
Rosa, M., C. Lopes, E. P. Melo, S. K. Singh, V. Geraldes, M. A. Rodrigues (2013). Measuring and modelling hemoglobin aggregation below freezing temperature J. Phys. Chem. B 117 8939 8946
Avezov, E., B. C. S. Cross, G. S. K. Schierle, M. Winters, H. P. Harding, E.P. Melo, C. F. Kaminski, D. (2013) Ron Lifetime imaging of a fluorescent protein sensor tracks ER thiol redox revealing its surprising stability J. Cell Biol. 201 337 349
Anjos, L., A. S. Gomes, E.P. Melo, A. V. M. Canário, D. M. Power. (2013) Cartilage acidic protein 2 a hyperthermostable, high affinity calcium-binding protein Biochim. Biophys. Acta – Proteins and Proteomics 1834 642 650
Fernandes, A.T., C. Lopes, L. O. Martins and E.P. Melo* (2012) Unfolding pathway of CotA-laccase and the role of cooper on the prevention of refolding through aggregation of the unfolded state Biochem. Biophys. Res. Commun 422 442 446
Fernandes, A.T., M. M. Pereira, C. S. Silva, P. F. Lindley, I. Bento, E. P. Melo* and L. O. Martins* (2011) “The removal of a disulfide bridge of CotA-laccase changes the slower motion dynamics involved in copper binding but has no effect on the thermodynamic stability” J. Biol. Inorg. Chem. 16: 641-651.
Melo, E.P., N. Estrela, C. Lopes, A. C. Matias, E. Tavares and V. Ochoa-Mendes (2010) “Compacting proteins: Pros and Cons od osmolyte-induced folding” Curr. Prot. Pep. Science 11: 744-751.
Zito, E., E.P. Melo, Y.Yang, Å. Wahlander, T.A. Neubert and D. Ron (2010) “Oxidative protein folding by an endoplasmic reticulum localized peroxiredoxin. Molec. Cell 40: 787-797.
Madeira, C. Estrela N., Ferreira JAB., Andrade SM., Costa, SMB., Melo EP. (2009), “Fluorescence lifetime imaging microscopy and fluorescence resonance energy transfer from cyan to yellow fluorescent protein validates a novel method to cluster proteins on solid surfaces”, Journal of Biomed Optics, 14(4):044035.
Morgado, I., Fernandes, AT; Martins, LO; Melo, EP (2009) “The hyperthermophilic nature of the metallo-oxidase from Aquifex aeolicus”, Biochim. Biophys. Acta- Proteins and Proteiomics 1794(1): 75-83.
E.P. Melo, E. Lundberg, N.L. Estrela, A.E. Samer-Eriksson and D. Power (2008) “Piscine transthyretin hormone affinity and fibril formation: The role of the N-terminal”, Mol. Cell. Endocrinol. 295: 48-58.
Brissos, V., E.P. Melo, J.M.G. Martinho and J.M.S. Cabral (2008) “Biochemical and Structural Characterisation of Cutinase Mutants in the Presence of the Anionic Surfactant AOT”, Biochim. Biophys. Acta 1784: 1326-1334.
Baptista, R.P., S.H. Pedersen, G.J.M. Cabrita, D.E. Otzen, J.M.S. Cabral and E.P. Melo(2008) “Thermodynamics and Mechanism of Cutinase Stabilization by Trehalose” Biopolymers 89(6):538-547.
Durão, P., Z. Chen, A.T. Fernandes, M.M. Pereira, E.P. Melo, and L.O. Martins (2008) “Copper Incorporation Into Recombinant CotA-laccase from Bacillus subtilis: Characterization of Cu Full-Loaded Enzymes”. J. Biol. Inorg. Chem. 13 (2):183-193.