Vito Foderà

2.1k total citations
76 papers, 1.7k citations indexed

About

Vito Foderà is a scholar working on Molecular Biology, Physiology and Food Science. According to data from OpenAlex, Vito Foderà has authored 76 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 Physiology and 20 papers in Food Science. Recurrent topics in Vito Foderà's work include Alzheimer's disease research and treatments (29 papers), Proteins in Food Systems (20 papers) and Protein Structure and Dynamics (16 papers). Vito Foderà is often cited by papers focused on Alzheimer's disease research and treatments (29 papers), Proteins in Food Systems (20 papers) and Protein Structure and Dynamics (16 papers). Vito Foderà collaborates with scholars based in Denmark, Italy and United Kingdom. Vito Foderà's co-authors include Valeria Vetri, Maurizio Leone, Marco van de Weert, Fabio Librizzi, Bente Vestergaard, Minna Groenning, Athene M. Donald, Valeria Militello, Giuseppe Sancataldo and Hanne Mørck Nielsen and has published in prestigious journals such as Journal of the American Chemical Society, Physical Review Letters and Nature Communications.

In The Last Decade

Vito Foderà

75 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
Vito Foderà Denmark 24 929 518 397 254 244 76 1.7k
Donatella Bulone Italy 30 1.1k 1.2× 447 0.9× 443 1.1× 313 1.2× 576 2.4× 92 2.5k
Valeria Vetri Italy 28 1.2k 1.3× 588 1.1× 389 1.0× 360 1.4× 331 1.4× 81 2.4k
Valeria Militello Italy 28 1.3k 1.4× 497 1.0× 253 0.6× 351 1.4× 446 1.8× 67 2.3k
Ibrahim Javed Australia 28 862 0.9× 802 1.5× 732 1.8× 610 2.4× 91 0.4× 71 2.4k
Brian S. Vad Denmark 20 861 0.9× 416 0.8× 164 0.4× 77 0.3× 95 0.4× 32 1.5k
Kexin Li China 21 500 0.5× 173 0.3× 240 0.6× 254 1.0× 63 0.3× 75 1.5k
Marc Sutter France 15 930 1.0× 221 0.4× 252 0.6× 233 0.9× 132 0.5× 18 1.8k
Li Fan China 24 748 0.8× 147 0.3× 601 1.5× 218 0.9× 49 0.2× 57 1.8k
Jianhong Chen China 25 738 0.8× 133 0.3× 136 0.3× 294 1.2× 64 0.3× 70 1.9k

Countries citing papers authored by Vito Foderà

Since Specialization
Citations

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

Fields of papers citing papers by Vito Foderà

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Vito Foderà

This figure shows the co-authorship network connecting the top 25 collaborators of Vito Foderà. A scholar is included among the top collaborators of Vito Foderà 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 Vito Foderà. Vito Foderà 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.
Lenton, Samuel, et al.. (2025). A low-complexity linker as a driver of intra- and intermolecular interactions in DNAJB chaperones. Nature Communications. 16(1). 5070–5070. 1 indexed citations
2.
Stie, Mai Bay, et al.. (2024). Disassembly and in vitro cell compatibility of α-lactalbumin particulates under physiologically relevant conditions. European Journal of Pharmaceutical Sciences. 204. 106962–106962. 2 indexed citations
3.
Arnous, Anis, et al.. (2024). Investigating the influence of protein secondary structure on the dissolution behavior of β-lactoglobulin-based amorphous solid dispersions. International Journal of Pharmaceutics. 653. 123887–123887. 5 indexed citations
4.
Ciavatti, Andrea, et al.. (2024). Radiation Hardness and Defects Activity in PEA2PbBr4 Single Crystals. Advanced Functional Materials. 34(46). 4 indexed citations
5.
Guo, Xiong, Hriday Bera, Peixin Liu, et al.. (2023). Unleashing the healing potential: Exploring next-generation regenerative protein nanoscaffolds for burn wound recovery. Asian Journal of Pharmaceutical Sciences. 18(6). 100856–100856. 7 indexed citations
6.
Maserati, Lorenzo, Andrea Ciavatti, Martina Foschi, et al.. (2023). Photoinduced Current Transient Spectroscopy on Metal Halide Perovskites: Electron Trapping and Ion Drift. ACS Energy Letters. 8(10). 4371–4379. 12 indexed citations
7.
Kirkensgaard, Jacob J. K., et al.. (2023). Application of Low-Frequency Raman Spectroscopy to Probe Dynamics of Lipid Mesophase Transformations upon Hydration. The Journal of Physical Chemistry B. 127(14). 3223–3230. 5 indexed citations
8.
Zhang, Min, et al.. (2023). Heterogeneous and Surface-Catalyzed Amyloid Aggregation Monitored by Spatially Resolved Fluorescence and Single Molecule Microscopy. The Journal of Physical Chemistry Letters. 14(4). 912–919. 7 indexed citations
9.
Foderà, Vito, et al.. (2023). Stereochemistry and Intermolecular Interactions Influence Carrier Peptide-Mediated Insulin Delivery. Molecular Pharmaceutics. 20(2). 1202–1212. 5 indexed citations
10.
Vetri, Valeria, et al.. (2023). Carrier peptide interactions with liposome membranes induce reversible clustering by surface adsorption and shape deformation. Journal of Colloid and Interface Science. 650(Pt B). 1821–1832. 5 indexed citations
11.
Stie, Mai Bay, et al.. (2022). Sustainable strategies for waterborne electrospinning of biocompatible nanofibers based on soy protein isolate. Sustainable materials and technologies. 34. e00519–e00519. 22 indexed citations
12.
Sancataldo, Giuseppe, et al.. (2022). α-casein micelles-membranes interaction: Flower-like lipid protein coaggregates formation. Biochimica et Biophysica Acta (BBA) - General Subjects. 1866(10). 130196–130196. 5 indexed citations
13.
Groenning, Minna, et al.. (2022). Reproducible Formation of Insulin Superstructures: Amyloid-Like Fibrils, Spherulites, and Particulates. Methods in molecular biology. 2551. 297–309. 6 indexed citations
14.
Bucciarelli, Saskia, et al.. (2019). Disentangling the role of solvent polarity and protein solvation in folding and self-assembly of α-lactalbumin. Journal of Colloid and Interface Science. 561. 749–761. 14 indexed citations
15.
Brady, Ryan A., Nicholas J. Brooks, Vito Foderà, Pietro Cicuta, & Lorenzo Di Michele. (2018). Amphiphilic-DNA Platform for the Design of Crystalline Frameworks with Programmable Structure and Functionality. Journal of the American Chemical Society. 140(45). 15384–15392. 38 indexed citations
16.
Santangelo, M., Vito Foderà, Valeria Militello, & Valeria Vetri. (2016). Back to the oligomeric state: pH-induced dissolution of concanavalin A amyloid-like fibrils into non-native oligomers. RSC Advances. 6(79). 75082–75091. 10 indexed citations
17.
Minicozzi, Velia, Vito Foderà, Valeria Militello, et al.. (2015). Thioflavin T templates amyloid β(1–40) conformation and aggregation pathway. Biophysical Chemistry. 206. 1–11. 34 indexed citations
18.
Foderà, Vito & Athene M. Donald. (2010). Tracking the heterogeneous distribution of amyloid spherulites and their population balance with free fibrils. The European Physical Journal E. 33(4). 273–282. 22 indexed citations
19.
Foderà, Vito, Minna Groenning, Valeria Vetri, et al.. (2008). Thioflavin T Hydroxylation at Basic pH and Its Effect on Amyloid Fibril Detection. The Journal of Physical Chemistry B. 112(47). 15174–15181. 103 indexed citations
20.
Foderà, Vito, Fabio Librizzi, Minna Groenning, Marco van de Weert, & Maurizio Leone. (2008). Secondary Nucleation and Accessible Surface in Insulin Amyloid Fibril Formation. The Journal of Physical Chemistry B. 112(12). 3853–3858. 140 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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