Elisa Iniesto

1.4k total citations
11 papers, 816 citations indexed

About

Elisa Iniesto is a scholar working on Molecular Biology, Plant Science and Immunology and Allergy. According to data from OpenAlex, Elisa Iniesto has authored 11 papers receiving a total of 816 indexed citations (citations by other indexed papers that have themselves been cited), including 7 papers in Molecular Biology, 5 papers in Plant Science and 4 papers in Immunology and Allergy. Recurrent topics in Elisa Iniesto's work include Plant Molecular Biology Research (5 papers), Food Allergy and Anaphylaxis Research (4 papers) and Plant Stress Responses and Tolerance (3 papers). Elisa Iniesto is often cited by papers focused on Plant Molecular Biology Research (5 papers), Food Allergy and Anaphylaxis Research (4 papers) and Plant Stress Responses and Tolerance (3 papers). Elisa Iniesto collaborates with scholars based in Spain, Belgium and China. Elisa Iniesto's co-authors include Vicente Rubio, Joachim F. Uhrig, Alexander G. Maier, Leonie Kokkelink, Ute Hoecker, Andrea Schrader, Martin Hülskamp, Geert De Jaeger, Ning Wei and María Luisa Irigoyen and has published in prestigious journals such as Proceedings of the National Academy of Sciences, The Plant Cell and Journal of Agricultural and Food Chemistry.

In The Last Decade

Elisa Iniesto

11 papers receiving 809 citations

Peers

Elisa Iniesto
Elisa Iniesto
Citations per year, relative to Elisa Iniesto Elisa Iniesto (= 1×) peers Giulia Pagliarani

Countries citing papers authored by Elisa Iniesto

Since Specialization
Citations

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

Fields of papers citing papers by Elisa Iniesto

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Elisa Iniesto

This figure shows the co-authorship network connecting the top 25 collaborators of Elisa Iniesto. A scholar is included among the top collaborators of Elisa Iniesto 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 Elisa Iniesto. Elisa Iniesto is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

11 of 11 papers shown
1.
Martínez, Cristina, Elisa Iniesto, Sandra Fonseca, et al.. (2024). Hormone-mediated disassembly and inactivation of a plant E3 ubiquitin ligase complex. Cell Reports. 43(10). 114802–114802. 3 indexed citations
2.
Iniesto, Elisa, et al.. (2018). Tandem Affinity Purification of Protein Complexes from Arabidopsis Cell Cultures. Methods in molecular biology. 1794. 297–309. 3 indexed citations
3.
Park, Junghoon, Chae Jin Lim, Mingzhe Shen, et al.. (2018). Epigenetic switch from repressive to permissive chromatin in response to cold stress. Proceedings of the National Academy of Sciences. 115(23). E5400–E5409. 164 indexed citations
4.
Perea-Resa, Carlos, Miguel Ángel Rodríguez-Milla, Elisa Iniesto, Vicente Rubio, & Julio Salinas. (2017). Prefoldins Negatively Regulate Cold Acclimation in Arabidopsis thaliana by Promoting Nuclear Proteasome-Mediated HY5 Degradation. Molecular Plant. 10(6). 791–804. 33 indexed citations
5.
Linacero, Rosario, Isabel Ballesteros, África Sanchiz, et al.. (2016). Detection by real time PCR of walnut allergen coding sequences in processed foods. Food Chemistry. 202. 334–340. 29 indexed citations
6.
Durand, Astrid Nagels, Sabrina Iñigo, Andrés Ritter, et al.. (2016). The Arabidopsis Iron–Sulfur Protein GRXS17 is a Target of the Ubiquitin E3 Ligases RGLG3 and RGLG4. Plant and Cell Physiology. 57(9). 1801–1813. 15 indexed citations
7.
Burbano, Carmen, Elisa Iniesto, Julia Rodríguez, et al.. (2014). A Novel Proteomic Analysis of the Modifications Induced by High Hydrostatic Pressure on Hazelnut Water-Soluble Proteins. Foods. 3(2). 279–289. 16 indexed citations
8.
Irigoyen, María Luisa, Elisa Iniesto, Lesia Rodríguez, et al.. (2014). Targeted Degradation of Abscisic Acid Receptors Is Mediated by the Ubiquitin Ligase Substrate Adaptor DDA1 in Arabidopsis. The Plant Cell. 26(2). 712–728. 153 indexed citations
9.
Iniesto, Elisa, Carmen Burbano, Beatriz Cabanillas, et al.. (2014). Detection of Almond Allergen Coding Sequences in Processed Foods by Real Time PCR. Journal of Agricultural and Food Chemistry. 62(24). 5617–5624. 24 indexed citations
10.
Maier, Alexander G., Andrea Schrader, Leonie Kokkelink, et al.. (2013). Light and the E3 ubiquitin ligase COP1/SPA control the protein stability of the MYB transcription factors PAP1 and PAP2 involved in anthocyanin accumulation in Arabidopsis. The Plant Journal. 74(4). 638–651. 337 indexed citations
11.
Iniesto, Elisa, Beatriz Cabanillas, Carmen Burbano, et al.. (2012). Real Time PCR to detect hazelnut allergen coding sequences in processed foods. Food Chemistry. 138(2-3). 1976–1981. 39 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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