A. Cousido-Siah

1.9k total citations · 1 hit paper
51 papers, 1.5k citations indexed

About

A. Cousido-Siah is a scholar working on Molecular Biology, Cell Biology and Materials Chemistry. According to data from OpenAlex, A. Cousido-Siah has authored 51 papers receiving a total of 1.5k indexed citations (citations by other indexed papers that have themselves been cited), including 37 papers in Molecular Biology, 16 papers in Cell Biology and 9 papers in Materials Chemistry. Recurrent topics in A. Cousido-Siah's work include Aldose Reductase and Taurine (14 papers), Enzyme Structure and Function (9 papers) and Heme Oxygenase-1 and Carbon Monoxide (9 papers). A. Cousido-Siah is often cited by papers focused on Aldose Reductase and Taurine (14 papers), Enzyme Structure and Function (9 papers) and Heme Oxygenase-1 and Carbon Monoxide (9 papers). A. Cousido-Siah collaborates with scholars based in France, Argentina and United States. A. Cousido-Siah's co-authors include A. Podjarny, A. Mitschler, Francesc X. Ruiz, Gilles Travé, Murielle Masson, Juline Poirson, Katia Zanier, Anne Förster, Juan Antonio Ortega and Scott Vande Pol and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

A. Cousido-Siah

49 papers receiving 1.5k citations

Hit Papers

Structure of the E6/E6AP/p53 complex required for HPV-med... 2016 2026 2019 2022 2016 100 200 300

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
A. Cousido-Siah France 23 851 257 256 256 202 51 1.5k
Francesc X. Ruiz United States 23 876 1.0× 235 0.9× 269 1.1× 521 2.0× 179 0.9× 49 1.7k
Carlos A. Castañeda United States 26 2.1k 2.5× 203 0.8× 147 0.6× 209 0.8× 259 1.3× 70 2.5k
Oliver Ohlenschläger Germany 29 1.4k 1.7× 126 0.5× 127 0.5× 145 0.6× 159 0.8× 102 2.1k
Tao Peng China 25 774 0.9× 242 0.9× 155 0.6× 113 0.4× 126 0.6× 59 1.5k
Irene Luque Spain 27 1.4k 1.7× 151 0.6× 70 0.3× 208 0.8× 169 0.8× 65 2.2k
Thilo Werner Germany 21 2.8k 3.2× 347 1.4× 101 0.4× 311 1.2× 326 1.6× 25 3.5k
Siddhartha Roy India 33 2.3k 2.8× 192 0.7× 140 0.5× 269 1.1× 501 2.5× 136 3.1k
Roland H. Stote France 24 1.1k 1.3× 156 0.6× 133 0.5× 170 0.7× 203 1.0× 59 1.9k
Paul D. Kirchhoff United States 23 1.1k 1.3× 257 1.0× 209 0.8× 101 0.4× 171 0.8× 39 1.7k
Warren J. Rocque United States 21 1.6k 1.9× 311 1.2× 125 0.5× 223 0.9× 395 2.0× 28 2.0k

Countries citing papers authored by A. Cousido-Siah

Since Specialization
Citations

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

Fields of papers citing papers by A. Cousido-Siah

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by A. Cousido-Siah. 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 A. Cousido-Siah. The network helps show where A. Cousido-Siah may publish in the future.

Co-authorship network of co-authors of A. Cousido-Siah

This figure shows the co-authorship network connecting the top 25 collaborators of A. Cousido-Siah. A scholar is included among the top collaborators of A. Cousido-Siah 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 A. Cousido-Siah. A. Cousido-Siah 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.
Delalande, François, Søren Østergaard, Gergő Gógl, et al.. (2025). Holdup Multiplex Assay for High-Throughput Measurement of Protein–Ligand Affinity Constants Using a Mass Spectrometry Readout. Journal of the American Chemical Society. 147(13). 10886–10902. 1 indexed citations
2.
Gógl, Gergő, S. Betzi, A. Cousido-Siah, et al.. (2023). PDZome-wide and structural characterization of the PDZ-binding motif of VANGL2. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1872(3). 140989–140989. 1 indexed citations
3.
Lilie, Hauke, et al.. (2023). Evidence for direct interaction between the oncogenic proteins E6 and E7 of high-risk human papillomavirus (HPV). Journal of Biological Chemistry. 299(8). 104954–104954. 6 indexed citations
4.
Gógl, Gergő, A. Cousido-Siah, Bastien Morlet, et al.. (2022). Quantitative fragmentomics allow affinity mapping of interactomes. Nature Communications. 13(1). 5472–5472. 25 indexed citations
5.
Poirson, Juline, Marie‐Laure Straub, A. Cousido-Siah, et al.. (2022). High-Risk Mucosal Human Papillomavirus 16 (HPV16) E6 Protein and Cutaneous HPV5 and HPV8 E6 Proteins Employ Distinct Strategies To Interfere with Interferon Regulatory Factor 3-Mediated Beta Interferon Expression. Journal of Virology. 96(10). e0187521–e0187521. 18 indexed citations
6.
Cousido-Siah, A., et al.. (2022). A scalable strategy to solve structures of PDZ domains and their complexes. Acta Crystallographica Section D Structural Biology. 78(4). 509–516. 4 indexed citations
7.
Gógl, Gergő, A. Cousido-Siah, Murielle Masson, et al.. (2020). Structure of High-Risk Papillomavirus 31 E6 Oncogenic Protein and Characterization of E6/E6AP/p53 Complex Formation. Journal of Virology. 95(2). 20 indexed citations
8.
Gógl, Gergő, Jožica Dolenc, Judit Ősz, et al.. (2020). Conformational editing of intrinsically disordered protein by α-methylation. Chemical Science. 12(3). 1080–1089. 10 indexed citations
9.
Gógl, Gergő, Célia Caillet‐Saguy, A. Cousido-Siah, et al.. (2020). Dual Specificity PDZ- and 14-3-3-Binding Motifs: A Structural and Interactomics Study. Structure. 28(7). 747–759.e3. 28 indexed citations
10.
Celegato, Marta, Laura Goracci, Beatrice Mercorelli, et al.. (2019). A novel small-molecule inhibitor of the human papillomavirus E6-p53 interaction that reactivates p53 function and blocks cancer cells growth. Cancer Letters. 470. 115–125. 50 indexed citations
11.
Noguera, Martín E., Ernesto A. Román, A. Cousido-Siah, et al.. (2015). Structural characterization of metal binding to a cold-adapted frataxin. JBIC Journal of Biological Inorganic Chemistry. 20(4). 653–664. 9 indexed citations
12.
Giménez-Dejoz, Joan, Michal H. Kolář, Francesc X. Ruiz, et al.. (2015). Substrate Specificity, Inhibitor Selectivity and Structure-Function Relationships of Aldo-Keto Reductase 1B15: A Novel Human Retinaldehyde Reductase. PLoS ONE. 10(7). e0134506–e0134506. 23 indexed citations
13.
Zhao, Yuguang, Raúl E. Cachau, A. Cousido-Siah, et al.. (2015). New insights into the enzymatic mechanism of human chitotriosidase (CHIT1) catalytic domain by atomic resolution X-ray diffraction and hybrid QM/MM. Acta Crystallographica Section D Biological Crystallography. 71(7). 1455–1470. 26 indexed citations
14.
Cousido-Siah, A., Francesc X. Ruiz, A. Mitschler, et al.. (2014). Identification of a novel polyfluorinated compound as a lead to inhibit the human enzymes aldose reductase and AKR1B10: structure determination of both ternary complexes and implications for drug design. Acta Crystallographica Section D Biological Crystallography. 70(3). 889–903. 30 indexed citations
15.
Cousido-Siah, A., Francesc X. Ruiz, Isidro Crespo, et al.. (2014). Structural analysis of sulindac as an inhibitor of aldose reductase and AKR1B10. Chemico-Biological Interactions. 234. 290–296. 22 indexed citations
16.
Gołȩbiowski, Adam, Darren L. Whitehouse, R. Paul Beckett, et al.. (2013). Synthesis of quaternary α-amino acid-based arginase inhibitors via the Ugi reaction. Bioorganic & Medicinal Chemistry Letters. 23(17). 4837–4841. 33 indexed citations
17.
Petrova, T., Vladimir Y. Lunin, Stephan L. Ginell, et al.. (2012). X-ray-induced overall structural changes in a protein molecule at cryogenic temperatures. Acta Crystallographica Section A Foundations of Crystallography. 68(a1). s266–s266. 2 indexed citations
18.
Cousido-Siah, A., Daniel Ayoub, Graciela Berberián, et al.. (2012). Structural and functional studies of ReP1-NCXSQ, a protein regulating the squid nerve Na+/Ca2+exchanger. Acta Crystallographica Section D Biological Crystallography. 68(9). 1098–1107. 8 indexed citations
19.
Petrova, T., Stephan L. Ginell, A. Mitschler, et al.. (2010). X-ray-induced deterioration of disulfide bridges at atomic resolution. Acta Crystallographica Section D Biological Crystallography. 66(10). 1075–1091. 18 indexed citations
20.
Hazemann, Isabelle, A. Cousido-Siah, A. Joachimiak, et al.. (2007). The atomic resolution structure of human aldose reductase reveals that rearrangement of a bound ligand allows the opening of the safety-belt loop. Acta Crystallographica Section D Biological Crystallography. 63(6). 665–672. 12 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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