Uris Ros

1.6k total citations · 1 hit paper
39 papers, 1.2k citations indexed

About

Uris Ros is a scholar working on Molecular Biology, Paleontology and Environmental Chemistry. According to data from OpenAlex, Uris Ros has authored 39 papers receiving a total of 1.2k indexed citations (citations by other indexed papers that have themselves been cited), including 27 papers in Molecular Biology, 20 papers in Paleontology and 8 papers in Environmental Chemistry. Recurrent topics in Uris Ros's work include Marine Invertebrate Physiology and Ecology (20 papers), Lipid Membrane Structure and Behavior (16 papers) and Erythrocyte Function and Pathophysiology (8 papers). Uris Ros is often cited by papers focused on Marine Invertebrate Physiology and Ecology (20 papers), Lipid Membrane Structure and Behavior (16 papers) and Erythrocyte Function and Pathophysiology (8 papers). Uris Ros collaborates with scholars based in Germany, Cuba and Brazil. Uris Ros's co-authors include Ana J. García‐Sáez, Lohans Pedrera, Hector Flores‐Romero, María E. Lanio, Carlos Álvarez, Stephan Hailfinger, Jenny Stroh, Katia Cosentino, Anja Schmitt and Rafael A. Espiritu and has published in prestigious journals such as Journal of Biological Chemistry, SHILAP Revista de lepidopterología and The Journal of Cell Biology.

In The Last Decade

Uris Ros

37 papers receiving 1.2k citations

Hit Papers

Ferroptotic pores induce Ca2+ fluxes and ESCRT-III activa... 2020 2026 2022 2024 2020 50 100 150 200

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Uris Ros Germany 20 788 264 208 173 167 39 1.2k
Herbert J. Evans United States 25 1.1k 1.4× 236 0.9× 59 0.3× 80 0.5× 66 0.4× 34 1.9k
M.C.M. Chung Singapore 17 621 0.8× 152 0.6× 19 0.1× 134 0.8× 40 0.2× 42 1.0k
Vladimir Besada Cuba 23 921 1.2× 144 0.5× 13 0.1× 186 1.1× 33 0.2× 87 1.5k
Wen‐guey Wu Taiwan 22 858 1.1× 107 0.4× 25 0.1× 89 0.5× 24 0.1× 58 1.3k
Silvia E. Hajos Argentina 20 624 0.8× 38 0.1× 67 0.3× 251 1.5× 150 0.9× 71 1.2k
Carlos Álvarez Cuba 22 721 0.9× 681 2.6× 8 0.0× 213 1.2× 25 0.1× 65 1.3k
Sergey I. Kovalchuk Russia 21 867 1.1× 42 0.2× 25 0.1× 115 0.7× 110 0.7× 78 1.3k
José V. Ordóñez United States 19 800 1.0× 24 0.1× 63 0.3× 195 1.1× 126 0.8× 42 1.4k
Alexandra V. Andreeva United States 19 635 0.8× 21 0.1× 158 0.8× 80 0.5× 63 0.4× 41 1.1k
Natàlia Jiménez Spain 19 386 0.5× 27 0.1× 213 1.0× 190 1.1× 137 0.8× 47 906

Countries citing papers authored by Uris Ros

Since Specialization
Citations

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

Fields of papers citing papers by Uris Ros

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Uris Ros

This figure shows the co-authorship network connecting the top 25 collaborators of Uris Ros. A scholar is included among the top collaborators of Uris Ros 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 Uris Ros. Uris Ros 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.
Ros, Uris, et al.. (2025). Mitochondrial dynamics and pore formation in regulated cell death pathways. Trends in Biochemical Sciences. 50(11). 1001–1014. 1 indexed citations
2.
Schreier, Shirley, Joana Paulino, Leandro R.S. Barbosa, et al.. (2024). Extension of sticholysins N-terminal α-helix signals membrane lipids to acquire curvature for toroidal pore formation. Biochemical and Biophysical Research Communications. 742. 151071–151071.
3.
Pedrera, Lohans, Uris Ros, María Laura Fanani, et al.. (2023). The Important Role of Membrane Fluidity on the Lytic Mechanism of the α-Pore-Forming Toxin Sticholysin I. Toxins. 15(1). 80–80. 1 indexed citations
4.
Pedrera, Lohans, Uris Ros, & Ana J. García‐Sáez. (2023). Calcium as a master regulator of ferroptosis and other types of regulated necrosis. Cell Calcium. 114. 102778–102778. 27 indexed citations
5.
Wang, Xin, Uris Ros, Julia Slotta‐Huspenina, et al.. (2021). MLKL promotes cellular differentiation in myeloid leukemia by facilitating the release of G-CSF. Cell Death and Differentiation. 28(12). 3235–3250. 12 indexed citations
6.
Ros, Uris, Lohans Pedrera, & Ana J. García‐Sáez. (2021). Techniques for studying membrane pores. Current Opinion in Structural Biology. 69. 108–116. 5 indexed citations
7.
Pedrera, Lohans, Rafael A. Espiritu, Uris Ros, et al.. (2020). Ferroptotic pores induce Ca2+ fluxes and ESCRT-III activation to modulate cell death kinetics. Cell Death and Differentiation. 28(5). 1644–1657. 224 indexed citations breakdown →
8.
Flores‐Romero, Hector, Uris Ros, & Ana J. García‐Sáez. (2019). A lipid perspective on regulated cell death. International review of cell and molecular biology. 351. 197–236. 19 indexed citations
9.
Valiente, Pedro A., Mario E. Valdés‐Tresanco, Raquel F. Epand, et al.. (2019). Membrane Remodeling by the Lytic Fragment of SticholysinII: Implications for the Toroidal Pore Model. Biophysical Journal. 117(9). 1563–1576. 12 indexed citations
10.
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
11.
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
12.
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
13.
Ros, Uris, Aida Peña‐Blanco, Kay Hänggi, et al.. (2017). Necroptosis Execution Is Mediated by Plasma Membrane Nanopores Independent of Calcium. Cell Reports. 19(1). 175–187. 113 indexed citations
14.
Ho, Sylvia, et al.. (2017). Damage of eukaryotic cells by the pore-forming toxin sticholysin II: Consequences of the potassium efflux. Biochimica et Biophysica Acta (BBA) - Biomembranes. 1859(5). 982–992. 38 indexed citations
15.
Pedrera, Lohans, et al.. (2014). Isolation and partial purification of a hemolytic sphingomyelin-inhibitable fraction from the sea anemone Anthopleura nigrescens. SHILAP Revista de lepidopterología. 31(1). 53–56. 5 indexed citations
16.
Pedrera, Lohans, María Laura Fanani, Uris Ros, et al.. (2014). Sticholysin I–membrane interaction: An interplay between the presence of sphingomyelin and membrane fluidity. Biochimica et Biophysica Acta (BBA) - Biomembranes. 1838(7). 1752–1759. 37 indexed citations
17.
Ros, Uris, A. Michelle Edwards, Richard M. Epand, et al.. (2013). The sticholysin family of pore-forming toxins induces the mixing of lipids in membrane domains. Biochimica et Biophysica Acta (BBA) - Biomembranes. 1828(11). 2757–2762. 32 indexed citations
18.
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
19.
Cilli, Eduardo Maffud, Edson Crusca, Uris Ros, et al.. (2007). Correlations between differences in amino-terminal sequences and different hemolytic activity of sticholysins. Toxicon. 50(8). 1201–1204. 27 indexed citations
20.
Ros, Uris, David Pentón, Mayra Tejuca, et al.. (2005). Model peptides mimic the structure and function of the N‐terminus of the pore‐forming toxin sticholysin II. Biopolymers. 84(2). 169–180. 48 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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