E
Eduardo P. Melo
Researcher at University of the Algarve
Publications - 80
Citations - 2193
Eduardo P. Melo is an academic researcher from University of the Algarve. The author has contributed to research in topics: Cutinase & Endoplasmic reticulum. The author has an hindex of 25, co-authored 76 publications receiving 1962 citations. Previous affiliations of Eduardo P. Melo include New York University & University of Cambridge.
Papers
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Journal ArticleDOI
Oxidative protein folding by an endoplasmic reticulum localized peroxiredoxin
Ester Zito,Eduardo P. Melo,Eduardo P. Melo,Yun Yang,Asa Wahlander,Thomas A. Neubert,David Ron +6 more
TL;DR: Observations implicate ER-localized PRDX4 in a previously unanticipated, parallel, ERO1-independent pathway that couples hydroperoxide production to oxidative protein folding in mammalian cells.
Journal ArticleDOI
Copper incorporation into recombinant CotA laccase from Bacillus subtilis: characterization of fully copper loaded enzymes.
Paulo Durão,Zhenjia Chen,André T. Fernandes,Peter Hildebrandt,Daniel H. Murgida,Smilja Todorovic,Manuela M. Pereira,Eduardo P. Melo,Eduardo P. Melo,Lígia O. Martins +9 more
TL;DR: EPR and resonance Raman data indicate that, presumably, folding in the presence of copper is indispensable for the correct structure of the trinuclear copper-containing site.
Journal ArticleDOI
Perturbations of the T1 copper site in the CotA laccase from Bacillus subtilis: structural, biochemical, enzymatic and stability studies.
Paulo Durão,Isabel Bento,André T. Fernandes,Eduardo P. Melo,Peter F. Lindley,Lígia O. Martins +5 more
TL;DR: X-ray structural comparison of M502L and M502F mutants with the wild-type CotA shows that the geometry of the T1 copper site is maintained as well as the overall fold of the proteins, indicating a key role in the regulation of CotA laccase activity.
Book ChapterDOI
Reverse micelles and protein biotechnology.
TL;DR: For biocatalysis the presence of a bulk organic solvent allow synthetic reactions to be performed via the control of water content and the solubilization of hydrophobic substrates, minimizing mass transfer problems.
Journal ArticleDOI
Lifetime imaging of a fluorescent protein sensor reveals surprising stability of ER thiol redox
Edward Avezov,Benedict C. S. Cross,Gabriele S. Kaminski Schierle,Mikael U. Winters,Heather P. Harding,Eduardo P. Melo,Clemens F. Kaminski,David Ron +7 more
TL;DR: Fluorescent lifetime imaging of an ER-tuned redox-responsive probe revealed an unanticipated stability of ER thiol redox to fluctuations in unfolded protein load, in contrast with sensitivity to lumenal calcium.