Carme Espinet

1.0k total citations
28 papers, 881 citations indexed

About

Carme Espinet is a scholar working on Molecular Biology, Cellular and Molecular Neuroscience and Developmental Neuroscience. According to data from OpenAlex, Carme Espinet has authored 28 papers receiving a total of 881 indexed citations (citations by other indexed papers that have themselves been cited), including 18 papers in Molecular Biology, 10 papers in Cellular and Molecular Neuroscience and 6 papers in Developmental Neuroscience. Recurrent topics in Carme Espinet's work include Nerve injury and regeneration (7 papers), Neurogenesis and neuroplasticity mechanisms (6 papers) and Fungal and yeast genetics research (4 papers). Carme Espinet is often cited by papers focused on Nerve injury and regeneration (7 papers), Neurogenesis and neuroplasticity mechanisms (6 papers) and Fungal and yeast genetics research (4 papers). Carme Espinet collaborates with scholars based in Spain, United States and Germany. Carme Espinet's co-authors include Joaquim Egea, Joan X. Comella, Isidró Ferrer, Martí Aldea, Enrique Herrero, Petar Podlesniy, María Ángeles de la Torre-Ruiz, S.J. Pilkis, Aksel Lange and Noemí Vidal and has published in prestigious journals such as Journal of Biological Chemistry, Journal of Neuroscience and The Journal of Cell Biology.

In The Last Decade

Carme Espinet

28 papers receiving 862 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Carme Espinet Spain 15 506 317 161 122 88 28 881
Joanna Fombonne France 17 575 1.1× 230 0.7× 283 1.8× 133 1.1× 109 1.2× 22 1.0k
Koji Shimoke Japan 19 464 0.9× 413 1.3× 84 0.5× 143 1.2× 186 2.1× 34 907
Jahan Ara United States 15 373 0.7× 300 0.9× 287 1.8× 129 1.1× 77 0.9× 35 1.1k
Marguerite Lucas France 18 710 1.4× 263 0.8× 194 1.2× 67 0.5× 114 1.3× 35 1.1k
Shoshona S. Le United States 11 615 1.2× 205 0.6× 82 0.5× 67 0.5× 97 1.1× 11 898
Miyahiko Murata Japan 9 646 1.3× 173 0.5× 67 0.4× 103 0.8× 69 0.8× 15 974
Monika Poppe Germany 14 787 1.6× 395 1.2× 124 0.8× 122 1.0× 219 2.5× 15 1.2k
Shlomit Erlich Israel 12 593 1.2× 174 0.5× 128 0.8× 56 0.5× 136 1.5× 13 1.2k
O. H. Lowry United States 8 647 1.3× 425 1.3× 97 0.6× 109 0.9× 107 1.2× 10 968
Alfredo J. Miñano‐Molina Spain 15 459 0.9× 365 1.2× 246 1.5× 49 0.4× 191 2.2× 18 911

Countries citing papers authored by Carme Espinet

Since Specialization
Citations

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

Fields of papers citing papers by Carme Espinet

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Carme Espinet

This figure shows the co-authorship network connecting the top 25 collaborators of Carme Espinet. A scholar is included among the top collaborators of Carme Espinet 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 Carme Espinet. Carme Espinet 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.
Roy, R., et al.. (2023). Altered ureido protein modification profiles in seminal plasma extracellular vesicles of non-normozoospermic men. Frontiers in Endocrinology. 14. 1113824–1113824. 11 indexed citations
2.
Cuesta‐Sancho, Sara, Carlos Anerillas, Anna Macià, et al.. (2022). A dominant negative mutation uncovers cooperative control of caudal Wolffian duct development by Sprouty genes. Cellular and Molecular Life Sciences. 79(10). 514–514. 2 indexed citations
3.
Toro, Daniel del, et al.. (2021). FLRT2 and FLRT3 cooperate in maintaining the tangential migratory streams of cortical interneurons during development. Journal of Neuroscience. 41(35). JN–RM. 13 indexed citations
4.
5.
Espinet, Carme, et al.. (2015). Oxidative Stress and Neurodegenerative Diseases: A Neurotrophic Approach. Current Drug Targets. 16(1). 20–30. 39 indexed citations
6.
Real, Sebastián, Lília Espada, Carme Espinet, Antonio F. Santidrián, & Albert Tauler. (2010). Study of the in vivo phosphorylation of E2F1 on Ser403. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1803(8). 912–918. 14 indexed citations
7.
Kichev, Anton, Ekaterina V. Ilieva, Gerard Piñol‐Ripoll, et al.. (2009). Cell Death and Learning Impairment in Mice Caused by in Vitro Modified Pro-NGF Can Be Related to Its Increased Oxidative Modifications in Alzheimer Disease. American Journal Of Pathology. 175(6). 2574–2585. 24 indexed citations
8.
Espada, Lília, et al.. (2007). Apoptotic action of E2F1 requires glycogen synthase kinase 3‐β activity in PC12 cells. Journal of Neurochemistry. 102(6). 2020–2028. 10 indexed citations
9.
Podlesniy, Petar, Anton Kichev, Carlos Pedraza, et al.. (2006). Pro-NGF from Alzheimer's Disease and Normal Human Brain Displays Distinctive Abilities to Induce Processing and Nuclear Translocation of Intracellular Domain of p75NTR and Apoptosis. American Journal Of Pathology. 169(1). 119–131. 64 indexed citations
10.
Pedraza, Carlos E., Petar Podlesniy, Noemí Vidal, et al.. (2005). Pro-NGF Isolated from the Human Brain Affected by Alzheimer's Disease Induces Neuronal Apoptosis Mediated by p75NTR. American Journal Of Pathology. 166(2). 533–543. 130 indexed citations
11.
Egea, Joaquim, Carme Espinet, Rosa M. Soler, et al.. (2001). Neuronal survival induced by neurotrophins requires calmodulin. The Journal of Cell Biology. 154(3). 585–598. 50 indexed citations
12.
Egea, Joaquim, Carme Espinet, Rosa M. Soler, et al.. (2000). Nerve Growth Factor Activation of the Extracellular Signal-Regulated Kinase Pathway Is Modulated by Ca 2+ and Calmodulin. Molecular and Cellular Biology. 20(6). 1931–1946. 47 indexed citations
13.
Espinet, Carme, et al.. (2000). Combined use of the green and yellow fluorescent proteins and fluorescence-activated cell sorting to select populations of transiently transfected PC12 cells. Journal of Neuroscience Methods. 100(1-2). 63–69. 9 indexed citations
14.
Egea, Joaquim, Carme Espinet, & Joan X. Comella. (1999). Calcium Influx Activates Extracellular-regulated Kinase/Mitogen-activated Protein Kinase Pathway through a Calmodulin-sensitive Mechanism in PC12 Cells. Journal of Biological Chemistry. 274(1). 75–85. 91 indexed citations
15.
Egea, Joaquim, Carme Espinet, & Joan X. Comella. (1998). Calmodulin Modulates Mitogen‐Activated Protein Kinase Activation in Response to Membrane Depolarization in PC12 Cells. Journal of Neurochemistry. 70(6). 2554–2564. 30 indexed citations
16.
Casas, Cèlia, Martí Aldea, Carme Espinet, et al.. (1997). TheAFT1 Transcriptional Factor is Differentially Required for Expression of High-Affinity Iron Uptake Genes inSaccharomyces cerevisiae. Yeast. 13(7). 621–637. 73 indexed citations
17.
Casas, Cèlia, Martí Aldea, Carme Espinet, et al.. (1997). The AFT1 Transcriptional Factor is Differentially Required for Expression of High‐Affinity Iron Uptake Genes in Saccharomyces cerevisiae. Yeast. 13(7). 621–637. 2 indexed citations
18.
Espinet, Carme, María Ángeles de la Torre-Ruiz, Martí Aldea, & Enrique Herrero. (1995). An efficient method to isolate yeast genes causing overexpression‐mediated growth arrest. Yeast. 11(1). 25–32. 62 indexed citations
19.
Espinet, Carme, Ramón Bartrons, & Josep Carreras. (1989). Effect of adenosine on fructose 2,6‐bisphosphate levels and glucose metabolization by chicken erythrocytes. FEBS Letters. 258(1). 143–146. 3 indexed citations
20.
Espinet, Carme, Ramón Bartrons, & Josep Carreras. (1988). Effects of fructose 2,6-bisphosphate and glucose 1,6-bisphosphate on phosphofructokinase from chicken erythrocytes. Comparative Biochemistry and Physiology Part B Comparative Biochemistry. 90(2). 453–457. 2 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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