Benedetta Bolognesi

2.3k total citations
31 papers, 1.3k citations indexed

About

Benedetta Bolognesi is a scholar working on Molecular Biology, Physiology and Oncology. According to data from OpenAlex, Benedetta Bolognesi has authored 31 papers receiving a total of 1.3k indexed citations (citations by other indexed papers that have themselves been cited), including 27 papers in Molecular Biology, 16 papers in Physiology and 4 papers in Oncology. Recurrent topics in Benedetta Bolognesi's work include Alzheimer's disease research and treatments (16 papers), Prion Diseases and Protein Misfolding (11 papers) and Protein Structure and Dynamics (9 papers). Benedetta Bolognesi is often cited by papers focused on Alzheimer's disease research and treatments (16 papers), Prion Diseases and Protein Misfolding (11 papers) and Protein Structure and Dynamics (9 papers). Benedetta Bolognesi collaborates with scholars based in Spain, United Kingdom and Italy. Benedetta Bolognesi's co-authors include Gian Gaetano Tartaglia, Ben Lehner, Christopher M. Dobson, Davide Cirillo, Nieves Lorenzo-Gotor, Federico Agostini, Marta Baldrighi, Riddhiman Dhar, Priyanka Narayan and Richard W. Clarke and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Nucleic Acids Research and Journal of Biological Chemistry.

In The Last Decade

Benedetta Bolognesi

31 papers receiving 1.3k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Benedetta Bolognesi Spain 19 982 467 145 106 103 31 1.3k
David W. Colby United States 21 2.2k 2.2× 672 1.4× 237 1.6× 96 0.9× 132 1.3× 23 2.6k
Olga V. Bocharova Russia 25 1.9k 1.9× 648 1.4× 73 0.5× 133 1.3× 112 1.1× 59 2.2k
Isabelle Huvent France 21 779 0.8× 489 1.0× 47 0.3× 98 0.9× 163 1.6× 38 1.2k
Greet De Baets Belgium 16 772 0.8× 232 0.5× 179 1.2× 38 0.4× 73 0.7× 18 1.0k
Francesco Bemporad Italy 19 939 1.0× 628 1.3× 108 0.7× 42 0.4× 191 1.9× 45 1.2k
François‐Xavier Cantrelle France 23 929 0.9× 549 1.2× 58 0.4× 45 0.4× 228 2.2× 71 1.4k
Catherine K. Xu United Kingdom 17 466 0.5× 465 1.0× 276 1.9× 34 0.3× 77 0.7× 29 1.0k
Maja Debulpaep Belgium 8 723 0.7× 629 1.3× 39 0.3× 53 0.5× 79 0.8× 10 1.1k
Brian O’Nuallain United States 17 1.0k 1.1× 1.2k 2.5× 92 0.6× 80 0.8× 92 0.9× 22 1.6k
Amanda Penco Italy 17 471 0.5× 269 0.6× 171 1.2× 41 0.4× 88 0.9× 23 772

Countries citing papers authored by Benedetta Bolognesi

Since Specialization
Citations

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

Fields of papers citing papers by Benedetta Bolognesi

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Benedetta Bolognesi

This figure shows the co-authorship network connecting the top 25 collaborators of Benedetta Bolognesi. A scholar is included among the top collaborators of Benedetta Bolognesi 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 Benedetta Bolognesi. Benedetta Bolognesi 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.
Bolognesi, Benedetta, et al.. (2025). Massive mutagenesis reveals an incomplete amyloid motif in Bri2 that turns amyloidogenic upon C-terminal extension. Proceedings of the National Academy of Sciences. 122(18). e2415521122–e2415521122. 1 indexed citations
2.
Thompson, Michael, et al.. (2025). Massive experimental quantification allows interpretable deep learning of protein aggregation. Science Advances. 11(18). eadt5111–eadt5111. 4 indexed citations
3.
Arutyunyan, Anna, et al.. (2025). Massively parallel genetic perturbation suggests the energetic structure of an amyloid-β transition state. Science Advances. 11(24). eadv1422–eadv1422. 3 indexed citations
4.
Claussnitzer, Melina, Victoria N. Parikh, Alex H. Wagner, et al.. (2024). Minimum information and guidelines for reporting a multiplexed assay of variant effect. Genome biology. 25(1). 100–100. 8 indexed citations
5.
Lehner, Ben, et al.. (2022). An atlas of amyloid aggregation: the impact of substitutions, insertions, deletions and truncations on amyloid beta fibril nucleation. Nature Communications. 13(1). 7084–7084. 28 indexed citations
6.
Bolognesi, Benedetta, et al.. (2022). Understanding and evolving prions by yeast multiplexed assays. Current Opinion in Genetics & Development. 75. 101941–101941. 1 indexed citations
7.
8.
Bolognesi, Benedetta, et al.. (2021). Assembling the right type of switch: Protein condensation to signal cell death. Current Opinion in Cell Biology. 69. 55–61. 1 indexed citations
9.
Arndt, Verena, Benedetta Bolognesi, Shu Liu, et al.. (2019). Fibril-induced glutamine-/asparagine-rich prions recruit stress granule proteins in mammalian cells. Life Science Alliance. 2(4). e201800280–e201800280. 7 indexed citations
10.
Bolognesi, Benedetta, et al.. (2019). The mutational landscape of a prion-like domain. Nature Communications. 10(1). 4162–4162. 101 indexed citations
11.
Bolognesi, Benedetta, Nieves Lorenzo-Gotor, Riddhiman Dhar, et al.. (2016). A Concentration-Dependent Liquid Phase Separation Can Cause Toxicity upon Increased Protein Expression. Cell Reports. 16(1). 222–231. 210 indexed citations
12.
Porcari, Riccardo, Christos Proukakis, Christopher A. Waudby, et al.. (2014). The H50Q Mutation Induces a 10-fold Decrease in the Solubility of α-Synuclein. Journal of Biological Chemistry. 290(4). 2395–2404. 63 indexed citations
13.
Bolognesi, Benedetta & Gian Gaetano Tartaglia. (2013). Physicochemical Principles of Protein Aggregation. Progress in molecular biology and translational science. 117. 53–72. 19 indexed citations
14.
Narayan, Priyanka, Ángel Orte, Richard W. Clarke, et al.. (2012). The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-beta 1-40 peptide. Research Online (University of Wollongong). 7 indexed citations
15.
Mossuto, Maria F., Benedetta Bolognesi, Anne Dhulesia, et al.. (2011). Disulfide Bonds Reduce the Toxicity of the Amyloid Fibrils Formed by an Extracellular Protein. Angewandte Chemie International Edition. 50(31). 7048–7051. 52 indexed citations
16.
Narayan, Priyanka, Ángel Orte, Richard W. Clarke, et al.. (2011). The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β1−40 peptide. Nature Structural & Molecular Biology. 19(1). 79–83. 233 indexed citations
17.
Bolognesi, Benedetta, Thomas R. Jahn, Ann‐Christin Brorsson, et al.. (2010). The N-terminus of amyloid-beta plays a crucial role in its aggregation and toxicity. Research Online (University of Wollongong). 1 indexed citations
18.
Brorsson, Ann‐Christin, Benedetta Bolognesi, Gian Gaetano Tartaglia, et al.. (2010). Intrinsic Determinants of Neurotoxic Aggregate Formation by the Amyloid β Peptide. Biophysical Journal. 98(8). 1677–1684. 42 indexed citations
19.
Lendel, Christofer, Benedetta Bolognesi, Anna Wahlström, Christopher M. Dobson, & Astrid Gräslund. (2010). Detergent-like Interaction of Congo Red with the Amyloid β Peptide. Biochemistry. 49(7). 1358–1360. 63 indexed citations
20.
Esposito, Gennaro, Stéfano Ricagno, Alessandra Corazza, et al.. (2008). The Controlling Roles of Trp60 and Trp95 in β2-Microglobulin Function, Folding and Amyloid Aggregation Properties. Journal of Molecular Biology. 378(4). 887–897. 73 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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