Aurora Martı́nez

7.6k total citations
181 papers, 5.9k citations indexed

About

Aurora Martı́nez is a scholar working on Molecular Biology, Clinical Biochemistry and Materials Chemistry. According to data from OpenAlex, Aurora Martı́nez has authored 181 papers receiving a total of 5.9k indexed citations (citations by other indexed papers that have themselves been cited), including 130 papers in Molecular Biology, 75 papers in Clinical Biochemistry and 35 papers in Materials Chemistry. Recurrent topics in Aurora Martı́nez's work include Metabolism and Genetic Disorders (74 papers), Enzyme Structure and Function (34 papers) and Biochemical and Molecular Research (22 papers). Aurora Martı́nez is often cited by papers focused on Metabolism and Genetic Disorders (74 papers), Enzyme Structure and Function (34 papers) and Biochemical and Molecular Research (22 papers). Aurora Martı́nez collaborates with scholars based in Norway, Spain and United States. Aurora Martı́nez's co-authors include Jan Haavik, Torgeir Flatmark, Ángel L. Pey, Knut Teigen, Per M. Knappskog, Marte I. Flydal, Øyvind Halskau, Arturo Muga, Stein Ove Døskeland and Lars Skjærven and has published in prestigious journals such as Proceedings of the National Academy of Sciences, The Lancet and Journal of the American Chemical Society.

In The Last Decade

Aurora Martı́nez

178 papers receiving 5.8k citations

Author Peers

Peers are selected by citation overlap in the author's most active subfields. citations · hero ref

Author Last Decade Papers Cites
Aurora Martı́nez 4.0k 1.8k 797 683 634 181 5.9k
Torgeir Flatmark 5.0k 1.2× 2.0k 1.1× 756 0.9× 1.3k 1.9× 1.5k 2.3× 231 7.8k
Ian M. Fearnley 9.0k 2.2× 1.6k 0.9× 401 0.5× 1.5k 2.1× 753 1.2× 128 11.1k
Hiroyuki Kagamiyama 4.8k 1.2× 879 0.5× 1.7k 2.2× 509 0.7× 532 0.8× 164 7.0k
Ilka Wittig 7.5k 1.9× 1.2k 0.6× 263 0.3× 974 1.4× 660 1.0× 190 9.6k
Yasuo Kagawa 5.9k 1.5× 865 0.5× 477 0.6× 883 1.3× 394 0.6× 227 8.5k
Youssef Hatefi 9.3k 2.3× 1.5k 0.8× 661 0.8× 1.1k 1.5× 814 1.3× 190 11.6k
Peter L. Pedersen 12.0k 3.0× 1.5k 0.8× 476 0.6× 1.4k 2.0× 901 1.4× 213 15.7k
Roger J.W. Truscott 6.7k 1.7× 1.9k 1.0× 440 0.6× 2.1k 3.1× 641 1.0× 202 9.0k
Santiago Grisolı́a 3.9k 1.0× 1.7k 0.9× 650 0.8× 1.3k 2.0× 902 1.4× 295 6.8k
Cesare Indiveri 4.7k 1.2× 2.6k 1.4× 288 0.4× 627 0.9× 452 0.7× 211 7.3k

Countries citing papers authored by Aurora Martı́nez

Since Specialization
Citations

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

Fields of papers citing papers by Aurora Martı́nez

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Aurora Martı́nez

This figure shows the co-authorship network connecting the top 25 collaborators of Aurora Martı́nez. A scholar is included among the top collaborators of Aurora Martı́nez 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 Aurora Martı́nez. Aurora Martı́nez 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.
Flydal, Marte I., César Santiago, Fernando Moro, et al.. (2025). Structural recognition and stabilization of tyrosine hydroxylase by the J-domain protein DNAJC12. Nature Communications. 16(1). 2755–2755. 2 indexed citations
2.
Sánchez‐Hernández, Javier, Aurora Martı́nez, & Cayetano Gutiérrez‐Cánovas. (2024). Feeding patterns of Atlantic salmon (Salmo salar) parr are better explained by local drivers than by macroecological drivers. Journal of Fish Biology. 105(3). 1031–1035.
3.
Thöny, Beat, Joanne Ng, Manju A. Kurian, Philippa B. Mills, & Aurora Martı́nez. (2024). Mouse models for inherited monoamine neurotransmitter disorders. Journal of Inherited Metabolic Disease. 47(3). 533–550. 2 indexed citations
4.
Martín-Malpartida, Pau, et al.. (2024). TPPU_DSF: A Web Application to Calculate Thermodynamic Parameters Using DSF Data. Journal of Molecular Biology. 436(17). 168519–168519. 1 indexed citations
5.
Cuéllar, Jorge, Marte I. Flydal, César Santiago, et al.. (2022). Structural mechanism for tyrosine hydroxylase inhibition by dopamine and reactivation by Ser40 phosphorylation. Nature Communications. 13(1). 74–74. 55 indexed citations
6.
Shi, Tiejun, Ming Ying, Ann Kari Grindheim, et al.. (2021). The Pah-R261Q mouse reveals oxidative stress associated with amyloid-like hepatic aggregation of mutant phenylalanine hydroxylase. Nature Communications. 12(1). 2073–2073. 19 indexed citations
7.
Lyu, Chao, et al.. (2020). G Protein-Gated Inwardly Rectifying Potassium Channel Subunit 3 Is Upregulated in Rat DRGs and Spinal Cord After Peripheral Nerve Injury. SHILAP Revista de lepidopterología. 1 indexed citations
8.
Flydal, Marte I., Siseth Martínez‐Caballero, Lars Skjærven, et al.. (2019). Structure of full-length human phenylalanine hydroxylase in complex with tetrahydrobiopterin. Proceedings of the National Academy of Sciences. 116(23). 11229–11234. 43 indexed citations
9.
Ji, Jianxiong, Ran Xu, Kaikai Ding, et al.. (2019). Long Noncoding RNA SChLAP1 Forms a Growth-Promoting Complex with HNRNPL in Human Glioblastoma through Stabilization of ACTN4 and Activation of NF-κB Signaling. Clinical Cancer Research. 25(22). 6868–6881. 55 indexed citations
10.
Scherer, Tanja, Gabriella Allegri, Christineh N. Sarkissian, et al.. (2018). Tetrahydrobiopterin treatment reduces brain L‐Phe but only partially improves serotonin in hyperphenylalaninemic ENU1/2 mice. Journal of Inherited Metabolic Disease. 41(4). 709–718. 10 indexed citations
11.
Martı́nez, Aurora, et al.. (2016). FRECUENCIA DEL VIRUS LINFOTROPICO DE LAS CÉLULAS T HUMANAS TIPO I/II EN PACIENTES QUE ASISTEN A LA UNIDAD PROGRAMÁTICA REGIONAL DE INMUNOLOGÍA CLÍNICA DEL ESTADO ARAGUA, VENEZUELA, 2012. Redalyc (Universidad Autónoma del Estado de México). 28(1). 83–89. 3 indexed citations
12.
Kleppe, Rune, et al.. (2016). Tyrosine and tryptophan hydroxylases as therapeutic targets in human disease. Expert Opinion on Therapeutic Targets. 21(2). 167–180. 52 indexed citations
13.
Hritz, Jozef, et al.. (2014). Dissection of Binding between a Phosphorylated Tyrosine Hydroxylase Peptide and 14-3-3ζ: A Complex Story Elucidated by NMR. Biophysical Journal. 107(9). 2185–2194. 20 indexed citations
14.
Teigen, Knut, Vidar R. Jensen, & Aurora Martı́nez. (2005). The Reaction Mechanism of Phenylalanine Hydroxylase. – A Question of Coordination. Pteridines. 16(1). 27–34. 3 indexed citations
15.
Halskau, Øyvind, et al.. (2005). α-Lactalbumin binding and membrane integrity—effect of charge and degree of unsaturation of glycerophospholipids. Biochimica et Biophysica Acta (BBA) - Biomembranes. 1717(1). 11–20. 29 indexed citations
16.
Thöny, Beat, Zhaobing Ding, & Aurora Martı́nez. (2004). Tetrahydrobiopterin protects phenylalanine hydroxylase activity in vivo: Implications for tetrahydrobiopterin‐responsive hyperphenylalaninemia. FEBS Letters. 577(3). 507–511. 54 indexed citations
17.
Setti, Alberto G., et al.. (1998). JAZ volume 64 issue 1 Cover and Front matter. Journal of the Australian Mathematical Society Series A Pure Mathematics and Statistics. 64(1). f1–f3. 1 indexed citations
18.
Martı́nez, Aurora, et al.. (1998). Proton NMR Studies on the Conformation of the Pterin Cofactor Bound at the Active Site of Recombinant Human Tyrosine Hydroxylase. Pteridines. 9(1). 44–52. 12 indexed citations
19.
Martı́nez, Aurora. (1995). Evidence for a functionally important histidine residue in human tyrosine hydroxylase. Amino Acids. 9(3). 285–292. 16 indexed citations
20.
Haavik, Jan, et al.. (1990). pH‐dependent release of catecholamines from tyrosine hydroxylase and the effect of phosphorylation of Ser‐40. FEBS Letters. 262(2). 363–365. 61 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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