Fabiola Pazos

1.3k total citations
47 papers, 1.1k citations indexed

About

Fabiola Pazos is a scholar working on Paleontology, Molecular Biology and Environmental Chemistry. According to data from OpenAlex, Fabiola Pazos has authored 47 papers receiving a total of 1.1k indexed citations (citations by other indexed papers that have themselves been cited), including 41 papers in Paleontology, 22 papers in Molecular Biology and 15 papers in Environmental Chemistry. Recurrent topics in Fabiola Pazos's work include Marine Invertebrate Physiology and Ecology (41 papers), Lipid Membrane Structure and Behavior (17 papers) and Marine Toxins and Detection Methods (15 papers). Fabiola Pazos is often cited by papers focused on Marine Invertebrate Physiology and Ecology (41 papers), Lipid Membrane Structure and Behavior (17 papers) and Marine Toxins and Detection Methods (15 papers). Fabiola Pazos collaborates with scholars based in Cuba, Brazil and Chile. Fabiola Pazos's co-authors include María E. Lanio, Diana Martínez Hernández, Mayra Tejuca, Carlos Álvarez, Carlos Álvarez, E. A. Lissi, Shirley Schreier, Vivian Morera, Gianfranco Menestrina and Juan José Rodríguez Herrera and has published in prestigious journals such as The Journal of Immunology, Langmuir and Scientific Reports.

In The Last Decade

Fabiola Pazos

46 papers receiving 1.1k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Fabiola Pazos Cuba 19 680 639 279 237 204 47 1.1k
Diana Martínez Hernández Cuba 18 631 0.9× 552 0.9× 229 0.8× 222 0.9× 199 1.0× 38 975
Mayra Tejuca Cuba 19 766 1.1× 674 1.1× 292 1.0× 259 1.1× 216 1.1× 28 1.1k
Carlos Álvarez Cuba 22 681 1.0× 721 1.1× 263 0.9× 243 1.0× 203 1.0× 65 1.3k
Petra Malovrh Slovenia 7 292 0.4× 392 0.6× 106 0.4× 108 0.5× 98 0.5× 7 585
Carlos Álvarez Cuba 12 285 0.4× 303 0.5× 104 0.4× 111 0.5× 96 0.5× 21 505
Katarina Kristan Slovenia 8 289 0.4× 335 0.5× 102 0.4× 108 0.5× 103 0.5× 10 565
Dessislava Georgieva Germany 18 172 0.3× 671 1.1× 68 0.2× 41 0.2× 6 0.0× 47 1.1k
Ivan I. Kaiser United States 24 154 0.2× 1.2k 1.8× 18 0.1× 91 0.4× 24 0.1× 67 1.8k
Juliana Mozer Sciani Brazil 20 64 0.1× 349 0.5× 40 0.1× 33 0.1× 17 0.1× 83 1.1k
André Lopes Fuly Brazil 24 371 0.5× 786 1.2× 179 0.6× 48 0.2× 3 0.0× 80 1.7k

Countries citing papers authored by Fabiola Pazos

Since Specialization
Citations

This map shows the geographic impact of Fabiola Pazos'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 Fabiola Pazos with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Fabiola Pazos more than expected).

Fields of papers citing papers by Fabiola Pazos

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Fabiola Pazos. 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 Fabiola Pazos. The network helps show where Fabiola Pazos may publish in the future.

Co-authorship network of co-authors of Fabiola Pazos

This figure shows the co-authorship network connecting the top 25 collaborators of Fabiola Pazos. A scholar is included among the top collaborators of Fabiola Pazos 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 Fabiola Pazos. Fabiola Pazos 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.
Nogueira, Catarina V., Audry Fernández, Circe Mesa, et al.. (2021). Sticholysins, pore-forming proteins from a marine anemone can induce maturation of dendritic cells through a TLR4 dependent-pathway. Molecular Immunology. 131. 144–154. 5 indexed citations
2.
Klare, Johann P., et al.. (2019). Architecture of the pore forming toxin sticholysin I in membranes. Journal of Structural Biology. 208(1). 30–42. 8 indexed citations
3.
Soto, Carmen, Rancés Blanco, Uris Ros, et al.. (2018). Sticholysin II-mediated cytotoxicity involves the activation of regulated intracellular responses that anticipates cell death. Biochimie. 148. 18–35. 13 indexed citations
4.
Barbosa, J.A.R.G., et al.. (2018). Self-homodimerization of an actinoporin by disulfide bridging reveals implications for their structure and pore formation. Scientific Reports. 8(1). 6614–6614. 7 indexed citations
5.
Ros, Uris, Joana Paulino, Edson Crusca, et al.. (2018). Self-association and folding in membrane determine the mode of action of peptides from the lytic segment of sticholysins. Biochimie. 156. 109–117. 7 indexed citations
6.
Álvarez, Carlos, Uris Ros, Lohans Pedrera, et al.. (2017). Biophysical and biochemical strategies to understand membrane binding and pore formation by sticholysins, pore-forming proteins from a sea anemone. Biophysical Reviews. 9(5). 529–544. 18 indexed citations
7.
Ahumada, Manuel, et al.. (2017). The pore forming capacity of Sticholysin I in dipalmitoyl phosphatidyl vesicles is tuned by osmotic stress. Chemistry and Physics of Lipids. 203. 87–93. 2 indexed citations
8.
Lanio, María E., et al.. (2015). The multigene families of actinoporins (part I): Isoforms and genetic structure. Toxicon. 103. 176–187. 29 indexed citations
9.
Lissi, E. A., et al.. (2014). Inactivation of the Pore-Forming Toxin Sticholysin I by Peroxynitrite: Protection by Cys Groups Incorporated in the Toxin. The Protein Journal. 33(5). 493–501. 1 indexed citations
10.
González, Gustavo, et al.. (2013). Effect of Human Serum Albumin Upon the Permeabilizing Activity of Sticholysin II, a Pore Forming Toxin from Stichodactyla heliantus. The Protein Journal. 32(8). 593–600. 2 indexed citations
11.
Pentón, David, Isabel Dı́az, Javier Campos, et al.. (2011). Validation of a mutant of the pore-forming toxin sticholysin-I for the construction of proteinase-activated immunotoxins. Protein Engineering Design and Selection. 24(6). 485–493. 18 indexed citations
12.
13.
González, Gustavo, E. A. Lissi, Diana Martínez Hernández, et al.. (2009). Effect of calcium on the hemolytic activity of Stichodactyla helianthus toxin sticholysin II on human erythrocytes. Toxicon. 54(6). 845–850. 10 indexed citations
14.
Herrera, Juan José Rodríguez, et al.. (2007). Adhesion and detachment kinetics of several strains of Staphylococcus aureus subsp. aureus under three different experimental conditions. Food Microbiology. 24(6). 585–591. 83 indexed citations
15.
Lanio, María E., Carlos Álvarez, Uris Ros, et al.. (2007). Sticholysins I and II interaction with cationic micelles promotes toxins’ conformational changes and enhanced hemolytic activity. Toxicon. 50(6). 731–739. 9 indexed citations
16.
Hernández, Diana Martínez, et al.. (2006). Los lípidos de la membrana actúan como moduladores de la actividad permeabilizante de Sticholisina II, una toxina formadora de poros con aplicaciones biomédicas. Biotecnología aplicada. 23(3). 251–254. 1 indexed citations
17.
Pazos, Fabiola, Diana Martínez Hernández, Lesly Calderón, et al.. (2006). Structural and functional characterization of a recombinant sticholysin I (rSt I) from the sea anemone Stichodactyla helianthus. Toxicon. 48(8). 1083–1094. 26 indexed citations
18.
Lanio, María E., Carlos Álvarez, Fabiola Pazos, et al.. (2002). Effects of sodium dodecyl sulfate on the conformation and hemolytic activity of St I and St II, two isotoxins purified from Stichodactyla helianthus. Toxicon. 41(1). 65–70. 15 indexed citations
19.
Lanio, María E., Vivian Morera, Carlos Álvarez, et al.. (2001). Purification and characterization of two hemolysins from Stichodactyla helianthus. Toxicon. 39(2-3). 187–194. 109 indexed citations
20.
Pazos, Fabiola, Carlos Álvarez, María E. Lanio, et al.. (1998). Modification of sticholysin II hemolytic activity by free radicals. Toxicon. 36(10). 1383–1393. 24 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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