Eduardo P. Melo

2.6k total citations
70 papers, 2.2k citations indexed

About

Eduardo P. Melo is a scholar working on Molecular Biology, Cell Biology and Plant Science. According to data from OpenAlex, Eduardo P. Melo has authored 70 papers receiving a total of 2.2k indexed citations (citations by other indexed papers that have themselves been cited), including 52 papers in Molecular Biology, 18 papers in Cell Biology and 13 papers in Plant Science. Recurrent topics in Eduardo P. Melo's work include Protein Structure and Dynamics (15 papers), Enzyme-mediated dye degradation (12 papers) and Protein purification and stability (11 papers). Eduardo P. Melo is often cited by papers focused on Protein Structure and Dynamics (15 papers), Enzyme-mediated dye degradation (12 papers) and Protein purification and stability (11 papers). Eduardo P. Melo collaborates with scholars based in Portugal, Denmark and United Kingdom. Eduardo P. Melo's co-authors include Joaquim M. S. Cabral, M. Raquel Aires‐Barros, Lı́gia O. Martins, David Ron, Edward Avezov, André Fernandes, Sı́lvia M. B. Costa, Paulo Durão, Åsa Wåhlander and Ricardo P. Baptista and has published in prestigious journals such as Nature Communications, The Journal of Cell Biology and Molecular Cell.

In The Last Decade

Eduardo P. Melo

69 papers receiving 2.1k citations

Peers — A (Enhanced Table)

Peers by citation overlap · career bar shows stage (early→late) cites · hero ref

Name h Career Trend Papers Cites
Eduardo P. Melo Portugal 26 1.2k 497 483 322 238 70 2.2k
Luı́s Gales Portugal 32 905 0.7× 307 0.6× 181 0.4× 362 1.1× 467 2.0× 112 2.8k
Yajun Wang China 29 1.9k 1.5× 274 0.6× 154 0.3× 182 0.6× 226 0.9× 163 3.1k
Giuseppe Manco Italy 36 2.6k 2.2× 563 1.1× 135 0.3× 216 0.7× 500 2.1× 125 3.9k
Thorsten Selmer Germany 26 1.5k 1.2× 117 0.2× 205 0.4× 173 0.5× 302 1.3× 54 2.5k
Scott A. White United Kingdom 29 1.5k 1.2× 161 0.3× 238 0.5× 111 0.3× 606 2.5× 81 2.5k
Jesper Vind Denmark 23 1.3k 1.1× 337 0.7× 107 0.2× 337 1.0× 175 0.7× 45 1.9k
Pierre Briozzo France 24 994 0.8× 814 1.6× 169 0.3× 331 1.0× 246 1.0× 53 2.0k
Isabel Bento Portugal 24 791 0.7× 643 1.3× 174 0.4× 393 1.2× 258 1.1× 60 2.0k
M H Emptage United States 27 1.9k 1.5× 249 0.5× 237 0.5× 147 0.5× 603 2.5× 41 3.5k
Vladimir O. Popov Russia 27 2.2k 1.8× 323 0.6× 148 0.3× 150 0.5× 1.0k 4.3× 269 3.6k

Countries citing papers authored by Eduardo P. Melo

Since Specialization
Citations

This map shows the geographic impact of Eduardo P. Melo's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by Eduardo P. Melo with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Eduardo P. Melo more than expected).

Fields of papers citing papers by Eduardo P. Melo

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Eduardo P. Melo. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by Eduardo P. Melo. The network helps show where Eduardo P. Melo may publish in the future.

Co-authorship network of co-authors of Eduardo P. Melo

This figure shows the co-authorship network connecting the top 25 collaborators of Eduardo P. Melo. A scholar is included among the top collaborators of Eduardo P. Melo based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with Eduardo P. Melo. Eduardo P. Melo is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

20 of 20 papers shown
1.
Melo, Eduardo P., et al.. (2024). A Conformational-Dependent Interdomain Redox Relay at the Core of Protein Disulfide Isomerase Activity. Antioxidants and Redox Signaling. 41(4-6). 181–200. 1 indexed citations
2.
Lucas, Maria Fátima, Carlos Frazão, Eduardo P. Melo, et al.. (2023). Mechanistic insights into glycoside 3-oxidases involved in C-glycoside metabolism in soil microorganisms. Nature Communications. 14(1). 7289–7289. 12 indexed citations
3.
Melo, Eduardo P., Tasuku Konno, Adrienne W. Paton, et al.. (2022). Stress-induced protein disaggregation in the endoplasmic reticulum catalysed by BiP. Nature Communications. 13(1). 2501–2501. 21 indexed citations
4.
Melo, Eduardo P., et al.. (2020). Fluorescent dye nano-assemblies by thiol attachment directed to the tips of gold nanorods for effective emission enhancement. Nanoscale. 12(11). 6334–6345. 17 indexed citations
5.
Anjos, Liliana, et al.. (2016). Cartilage acidic protein 1, a new member of the beta-propeller protein family with amyloid propensity. Proteins Structure Function and Bioinformatics. 85(2). 242–255. 19 indexed citations
6.
Macedo, Joana A., et al.. (2014). Live-cell FRET imaging reveals clustering of the prion protein at the cell surface induced by infectious prions. Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1842(7). 981–991. 8 indexed citations
7.
Brissos, Vânia, et al.. (2014). Improving Kinetic or Thermodynamic Stability of an Azoreductase by Directed Evolution. PLoS ONE. 9(1). e87209–e87209. 31 indexed citations
8.
Tsunoda, Satoshi, Edward Avezov, Alisa Zyryanova, et al.. (2014). Intact protein folding in the glutathione-depleted endoplasmic reticulum implicates alternative protein thiol reductants. eLife. 3. e03421–e03421. 63 indexed citations
9.
Avezov, Edward, Benedict C. S. Cross, Gabriele S. Kaminski Schierle, et al.. (2013). Lifetime imaging of a fluorescent protein sensor reveals surprising stability of ER thiol redox. The Journal of Cell Biology. 201(2). 337–349. 86 indexed citations
10.
Fernandes, André, Manuela M. Pereira, Catarina S. Silva, et al.. (2011). The removal of a disulfide bridge in CotA-laccase changes the slower motion dynamics involved in copper binding but has no effect on the thermodynamic stability. JBIC Journal of Biological Inorganic Chemistry. 16(4). 641–651. 14 indexed citations
11.
Carvalho, Clayton Moura de, et al.. (2008). Resposta dos parâmetros tecnológicos da terceira folha de cana-de-açúcar submetida a diferentes níveis de irrigação. Revista Brasileira de Ciências Agrárias - Brazilian Journal of Agricultural Sciences. 3(4). 337–342. 13 indexed citations
12.
Chen, Zhenjia, Paulo Durão, Peter Hildebrandt, et al.. (2008). Copper incorporation into recombinant CotA-laccase from Bacillus subtilis: Characterization of fully copper loaded enzymes. Journal of Biotechnology. 136. S320–S320. 3 indexed citations
13.
Melo, Eduardo P., et al.. (2007). Insight into stability of CotA laccase from the spore coat of Bacillus subtilis. Biochemical Society Transactions. 35(6). 1579–1582. 27 indexed citations
14.
Rodrigues, Maria Luı́sa, Margarida Archer, Paulo Martel, et al.. (2005). Crystal structures of the free and sterol-bound forms of β-cinnamomin. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1764(1). 110–121. 29 indexed citations
15.
Chen, Luyang, Gonçalo J. M. Cabrita, Daniel E. Otzen, & Eduardo P. Melo. (2005). Stabilization of the Ribosomal Protein S6 by Trehalose is Counterbalanced by the Formation of a Putative Off-pathway Species. Journal of Molecular Biology. 351(2). 402–416. 20 indexed citations
16.
Carvalho, Ana Sofía, Maria Teresa Neves‐Petersen, Steffen B. Petersen, M. Raquel Aires‐Barros, & Eduardo P. Melo. (2004). Formation of a misfolded conformation during refolding of HRPA1 in the presence of calcium. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1747(1). 99–107. 4 indexed citations
17.
Carvalho, Ana Sofía, et al.. (2004). Conformational states of HRPA1 induced by thermal unfolding: Effect of low molecular weight solutes. Biopolymers. 75(2). 173–186. 8 indexed citations
18.
Carvalho, Ana Sofía, Eduardo P. Melo, Bruno Sommer Ferreira, et al.. (2003). Heme and pH-dependent stability of an anionic horseradish peroxidase. Archives of Biochemistry and Biophysics. 415(2). 257–267. 49 indexed citations
19.
Baptista, Ricardo P., Joaquim M. S. Cabral, & Eduardo P. Melo. (2000). Trehalose delays the reversible but not the irreversible thermal denaturation of cutinase. Biotechnology and Bioengineering. 70(6). 699–703. 44 indexed citations
20.
Setti, Leonardo, Pedro Fevereiro, Eduardo P. Melo, et al.. (1995). Superactivity of peroxidase solubilized in reversed micellar systems. Applied Biochemistry and Biotechnology. 55(3). 207–218. 23 indexed citations

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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