Wilber Romero‐Fernandez

2.5k total citations
51 papers, 1.7k citations indexed

About

Wilber Romero‐Fernandez is a scholar working on Molecular Biology, Cellular and Molecular Neuroscience and Social Psychology. According to data from OpenAlex, Wilber Romero‐Fernandez has authored 51 papers receiving a total of 1.7k indexed citations (citations by other indexed papers that have themselves been cited), including 42 papers in Molecular Biology, 29 papers in Cellular and Molecular Neuroscience and 5 papers in Social Psychology. Recurrent topics in Wilber Romero‐Fernandez's work include Receptor Mechanisms and Signaling (33 papers), Neuropeptides and Animal Physiology (17 papers) and Neurotransmitter Receptor Influence on Behavior (9 papers). Wilber Romero‐Fernandez is often cited by papers focused on Receptor Mechanisms and Signaling (33 papers), Neuropeptides and Animal Physiology (17 papers) and Neurotransmitter Receptor Influence on Behavior (9 papers). Wilber Romero‐Fernandez collaborates with scholars based in Sweden, Spain and Italy. Wilber Romero‐Fernandez's co-authors include Dasiel O. Borroto‐Escuela, Kjell Fuxé, Luigi F. Agnati, Alexander O. Tarakanov, Francisco Ciruela, Manuel Narváez, Pere Garriga, Luca Ferraro, Zaida Dı́az-Cabiale and Sergio Tanganelli and has published in prestigious journals such as Nature Communications, Nature Neuroscience and Journal of Molecular Biology.

In The Last Decade

Wilber Romero‐Fernandez

50 papers receiving 1.7k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Wilber Romero‐Fernandez Sweden 24 1.1k 1.1k 179 149 126 51 1.7k
Anton Terasmaa Estonia 20 1.1k 1.0× 1.1k 1.1× 558 3.1× 142 1.0× 181 1.4× 43 2.1k
Giuseppina Leo Italy 30 1.4k 1.2× 1.2k 1.1× 214 1.2× 161 1.1× 219 1.7× 72 2.5k
Zaida Dı́az-Cabiale Spain 28 1.3k 1.2× 1.8k 1.7× 124 0.7× 326 2.2× 163 1.3× 80 2.3k
Philippe Fossier France 20 1.0k 0.9× 884 0.8× 138 0.8× 65 0.4× 153 1.2× 34 1.7k
Kazuhisa Kohda Japan 28 1.6k 1.5× 1.5k 1.4× 85 0.5× 68 0.5× 152 1.2× 50 2.6k
Davide Pozzi Italy 24 772 0.7× 769 0.7× 218 1.2× 55 0.4× 232 1.8× 43 1.9k
Jianhua Xu United States 22 1.1k 1.0× 943 0.9× 116 0.6× 81 0.5× 231 1.8× 38 2.2k
Christian Lohr Germany 26 683 0.6× 941 0.9× 173 1.0× 94 0.6× 170 1.3× 75 1.9k
Jayne Cartmell United States 18 989 0.9× 1.5k 1.5× 125 0.7× 116 0.8× 170 1.3× 24 1.8k
Sukumar Vijayaraghavan United States 23 1.7k 1.5× 1.1k 1.1× 71 0.4× 128 0.9× 114 0.9× 36 2.3k

Countries citing papers authored by Wilber Romero‐Fernandez

Since Specialization
Citations

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

Fields of papers citing papers by Wilber Romero‐Fernandez

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Wilber Romero‐Fernandez. 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 Wilber Romero‐Fernandez. The network helps show where Wilber Romero‐Fernandez may publish in the future.

Co-authorship network of co-authors of Wilber Romero‐Fernandez

This figure shows the co-authorship network connecting the top 25 collaborators of Wilber Romero‐Fernandez. A scholar is included among the top collaborators of Wilber Romero‐Fernandez 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 Wilber Romero‐Fernandez. Wilber Romero‐Fernandez 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.
O’Brown, Natasha M., Emma H. Neal, Alexander G. Sorets, et al.. (2025). IQGAP2 regulates blood-brain barrier immune dynamics. iScience. 28(3). 111994–111994. 2 indexed citations
2.
Wang, Yongchao, et al.. (2024). Phospholipase D3 (PLD3) Regulates Lysosomal Biogenesis. Alzheimer s & Dementia. 20(S1). e087739–e087739.
3.
Rios, R. R., Geoffroy Venton, Sara Sánchez‐Redondo, et al.. (2020). Dual disruption of aldehyde dehydrogenases 1 and 3 promotes functional changes in the glutathione redox system and enhances chemosensitivity in nonsmall cell lung cancer. Oncogene. 39(13). 2756–2771. 41 indexed citations
4.
Borroto‐Escuela, Dasiel O., Manuel Narváez, Wilber Romero‐Fernandez, et al.. (2019). Acute Cocaine Enhances Dopamine D2R Recognition and Signaling and Counteracts D2R Internalization in Sigma1R-D2R Heteroreceptor Complexes. Molecular Neurobiology. 56(10). 7045–7055. 8 indexed citations
5.
Borroto‐Escuela, Dasiel O., Wilber Romero‐Fernandez, Karolina Wydra, et al.. (2019). OSU-6162, a Sigma1R Ligand in Low Doses, Can Further Increase the Effects of Cocaine Self-Administration on Accumbal D2R Heteroreceptor Complexes. Neurotoxicity Research. 37(2). 433–444. 8 indexed citations
6.
Borroto‐Escuela, Dasiel O., Karolina Wydra, Wilber Romero‐Fernandez, et al.. (2019). A2AR Transmembrane 2 Peptide Administration Disrupts the A2AR-A2AR Homoreceptor but Not the A2AR-D2R Heteroreceptor Complex: Lack of Actions on Rodent Cocaine Self-Administration. International Journal of Molecular Sciences. 20(23). 6100–6100. 10 indexed citations
7.
Fuxé, Kjell, Karolina Wydra, Krystyna Gołembiowska, et al.. (2014). Abstracts from Purines 2014, an International Conference on Nucleotides, Nucleosides and Nucleobases, held in Bonn, Germany, from July 23–27, 2014. Purinergic Signalling. 10(4). 657–854. 2 indexed citations
8.
Fuxé, Kjell, Dasiel O. Borroto‐Escuela, Alexander O. Tarakanov, et al.. (2014). Dopamine D2 heteroreceptor complexes and their receptor–receptor interactions in ventral striatum. Progress in brain research. 211. 113–139. 37 indexed citations
9.
Borroto‐Escuela, Dasiel O., Manuel Narváez, Wilber Romero‐Fernandez, et al.. (2014). P.1.g.067 The GalR1–GalR2 heteroreceptor complex can be the receptor for galanin fragment 1–15. European Neuropsychopharmacology. 24. S242–S243. 1 indexed citations
10.
Fuxé, Kjell, Alexander O. Tarakanov, Wilber Romero‐Fernandez, et al.. (2014). Diversity and Bias through Receptor–Receptor Interactions in GPCR Heteroreceptor Complexes. Focus on Examples from Dopamine D2 Receptor Heteromerization. Frontiers in Endocrinology. 5. 71–71. 43 indexed citations
11.
Borroto‐Escuela, Dasiel O., Wilber Romero‐Fernandez, Pere Garriga, et al.. (2013). G Protein–Coupled Receptor Heterodimerization in the Brain. Methods in enzymology on CD-ROM/Methods in enzymology. 521. 281–294. 94 indexed citations
12.
Borroto‐Escuela, Dasiel O., et al.. (2013). Hallucinogenic 5-HT2AR agonists LSD and DOI enhance dopamine D2R protomer recognition and signaling of D2-5-HT2A heteroreceptor complexes. Biochemical and Biophysical Research Communications. 443(1). 278–284. 61 indexed citations
13.
Fuxé, Kjell, Dasiel O. Borroto‐Escuela, Wilber Romero‐Fernandez, Weibo Zhang, & Luigi F. Agnati. (2013). Volume transmission and its different forms in the central nervous system. Chinese Journal of Integrative Medicine. 19(5). 323–329. 56 indexed citations
14.
Fuxé, Kjell, Dasiel O. Borroto‐Escuela, Wilber Romero‐Fernandez, et al.. (2012). On the role of volume transmission and receptor–receptor interactions in social behaviour: Focus on central catecholamine and oxytocin neurons. Brain Research. 1476. 119–131. 66 indexed citations
15.
Borroto‐Escuela, Dasiel O., Wilber Romero‐Fernandez, Patricia Correia, et al.. (2011). Dissecting the Conserved NPxxY Motif of the M<sub>3</sub> Muscarinic Acetylcholine Receptor: Critical Role of Asp-7.49 for Receptor Signaling and Multiprotein Complex Formation. Cellular Physiology and Biochemistry. 28(5). 1009–1022. 16 indexed citations
16.
Romero‐Fernandez, Wilber, Dasiel O. Borroto‐Escuela, Alexander O. Tarakanov, et al.. (2011). Agonist-induced formation of FGFR1 homodimers and signaling differ among members of the FGF family. Biochemical and Biophysical Research Communications. 409(4). 764–768. 21 indexed citations
17.
Alea, Mileidys Perez, Dasiel O. Borroto‐Escuela, Wilber Romero‐Fernandez, Kjell Fuxé, & Pere Garriga. (2011). Differential expression of muscarinic acetylcholine receptor subtypes in Jurkat cells and their signaling. Journal of Neuroimmunology. 237(1-2). 13–22. 6 indexed citations
18.
Borroto‐Escuela, Dasiel O., Wilber Romero‐Fernandez, Alexander O. Tarakanov, et al.. (2011). On the Existence of a Possible A2A–D2–β-Arrestin2 Complex: A2A Agonist Modulation of D2 Agonist-Induced β-Arrestin2 Recruitment. Journal of Molecular Biology. 406(5). 687–699. 72 indexed citations
19.
Borroto‐Escuela, Dasiel O., Kathleen Van Craenenbroeck, Wilber Romero‐Fernandez, et al.. (2010). Dopamine D2 and D4 receptor heteromerization and its allosteric receptor–receptor interactions. Biochemical and Biophysical Research Communications. 404(4). 928–934. 78 indexed citations
20.
Borroto‐Escuela, Dasiel O., Wilber Romero‐Fernandez, Alexander O. Tarakanov, et al.. (2010). Dopamine D2 and 5-hydroxytryptamine 5-HT2A receptors assemble into functionally interacting heteromers. Biochemical and Biophysical Research Communications. 401(4). 605–610. 72 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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