Kerensa Broersen

4.0k total citations · 3 hit papers
45 papers, 3.1k citations indexed

About

Kerensa Broersen is a scholar working on Molecular Biology, Physiology and Food Science. According to data from OpenAlex, Kerensa Broersen has authored 45 papers receiving a total of 3.1k indexed citations (citations by other indexed papers that have themselves been cited), including 22 papers in Molecular Biology, 22 papers in Physiology and 10 papers in Food Science. Recurrent topics in Kerensa Broersen's work include Alzheimer's disease research and treatments (21 papers), Proteins in Food Systems (9 papers) and Protein Structure and Dynamics (8 papers). Kerensa Broersen is often cited by papers focused on Alzheimer's disease research and treatments (21 papers), Proteins in Food Systems (9 papers) and Protein Structure and Dynamics (8 papers). Kerensa Broersen collaborates with scholars based in Netherlands, Belgium and United Kingdom. Kerensa Broersen's co-authors include Frédéric Rousseau, Joost Schymkowitz, Annelies Vandersteen, Federica Cioffi, Harmen H. J. de Jongh, Kris Pauwels, Wim Jonckheere, Bart De Strooper, Iryna Benilova and R.J. Hamer and has published in prestigious journals such as Journal of Biological Chemistry, The EMBO Journal and PLoS ONE.

In The Last Decade

Kerensa Broersen

45 papers receiving 3.0k citations

Hit Papers

Neurotoxicity of Alzheimer's disease Aβ peptides is induc... 2010 2026 2015 2020 2010 2022 2025 100 200 300 400

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Kerensa Broersen Netherlands 29 1.8k 1.3k 459 372 369 45 3.1k
Anna Pensalfini United States 26 2.4k 1.3× 1.9k 1.4× 358 0.8× 327 0.9× 371 1.0× 31 3.5k
Harry LeVine United States 36 3.3k 1.9× 2.6k 1.9× 776 1.7× 689 1.9× 536 1.5× 72 5.3k
Subashchandrabose Chinnathambi India 33 1.6k 0.9× 1.2k 0.9× 383 0.8× 198 0.5× 450 1.2× 97 2.7k
Rui‐tian Liu China 29 1.1k 0.6× 815 0.6× 416 0.9× 155 0.4× 265 0.7× 67 2.8k
Kazuma Murakami Japan 31 1.9k 1.1× 1.5k 1.1× 808 1.8× 397 1.1× 289 0.8× 80 3.0k
Stephan Schilling Germany 32 2.1k 1.2× 1.7k 1.2× 516 1.1× 533 1.4× 618 1.7× 61 3.7k
Dagmar E. Ehrnhoefer Canada 22 1.8k 1.0× 2.0k 1.5× 372 0.8× 272 0.7× 1.2k 3.3× 34 4.0k
William P. Esler United States 23 2.2k 1.2× 1.8k 1.3× 477 1.0× 445 1.2× 372 1.0× 40 3.4k
Michael R. Sierks United States 36 1.3k 0.7× 2.3k 1.7× 359 0.8× 244 0.7× 534 1.4× 93 4.3k
Annett Boeddrich Germany 10 1.2k 0.7× 1.6k 1.2× 249 0.5× 241 0.6× 842 2.3× 14 2.7k

Countries citing papers authored by Kerensa Broersen

Since Specialization
Citations

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

Fields of papers citing papers by Kerensa Broersen

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Kerensa Broersen

This figure shows the co-authorship network connecting the top 25 collaborators of Kerensa Broersen. A scholar is included among the top collaborators of Kerensa Broersen 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 Kerensa Broersen. Kerensa Broersen 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.
Schalkwijk, Saskia van, Soenita S. Goerdayal, Andrei Prodan, et al.. (2024). Biopurification using non-growing microorganisms to improve plant protein ingredients. npj Science of Food. 8(1). 48–48. 8 indexed citations
2.
Broersen, Kerensa, et al.. (2023). Robust Tissue Fabrication for Long-Term Culture of iPSC-Derived Brain Organoids for Aging Research. Journal of Visualized Experiments. 3 indexed citations
3.
Boerema, Ate S., Jan N. Keijser, Tingting Chen, et al.. (2023). The TNFR1 antagonist Atrosimab reduces neuronal loss, glial activation and memory deficits in an acute mouse model of neurodegeneration. Scientific Reports. 13(1). 10622–10622. 10 indexed citations
4.
Santiago, Grissel Trujillo‐de, et al.. (2022). Use of standard U-bottom and V-bottom well plates to generate neuroepithelial embryoid bodies. PLoS ONE. 17(5). e0262062–e0262062. 12 indexed citations
5.
Broersen, Kerensa, et al.. (2022). Engineering Organoids for in vitro Modeling of Phenylketonuria. Frontiers in Molecular Neuroscience. 14. 787242–787242. 8 indexed citations
6.
Passeri, Elodie, Kamil Elkhoury, Margaretha Morsink, et al.. (2022). Alzheimer’s Disease: Treatment Strategies and Their Limitations. International Journal of Molecular Sciences. 23(22). 13954–13954. 313 indexed citations breakdown →
7.
The, Hai Le, Anne Leferink, Albert van den Berg, et al.. (2021). Transwell‐Integrated 2 µm Thick Transparent Polydimethylsiloxane Membranes with Controlled Pore Sizes and Distribution to Model the Blood‐Brain Barrier. Advanced Materials Technologies. 6(12). 21 indexed citations
8.
Cioffi, Federica, et al.. (2021). A Review of Oxidative Stress Products and Related Genes in Early Alzheimer’s Disease. Journal of Alzheimer s Disease. 83(3). 977–1001. 46 indexed citations
9.
The, Hai Le, Valeria V. Orlova, Albert van den Berg, et al.. (2020). Multiplexed blood–brain barrier organ-on-chip. Lab on a Chip. 20(17). 3132–3143. 57 indexed citations
10.
Teodorowicz, Małgorzata, Olaf Perdijk, Coen Govers, et al.. (2017). Optimized Triton X-114 assisted lipopolysaccharide (LPS) removal method reveals the immunomodulatory effect of food proteins. PLoS ONE. 12(3). e0173778–e0173778. 64 indexed citations
11.
Broersen, Kerensa, et al.. (2017). The influence of N-terminal acetylation on micelle-induced conformational changes and aggregation of α-Synuclein. PLoS ONE. 12(5). e0178576–e0178576. 28 indexed citations
12.
Hubin, Ellen, Stéphanie Deroo, Clemens F. Kaminski, et al.. (2015). Two distinct β-sheet structures in Italian-mutant amyloid-beta fibrils: a potential link to different clinical phenotypes. Cellular and Molecular Life Sciences. 72(24). 4899–4913. 31 indexed citations
13.
Barrera, Exequiel, Sebastián A. Andújar, Ellen Hubin, et al.. (2015). New mimetic peptides inhibitors of Αβ aggregation. Molecular guidance for rational drug design. European Journal of Medicinal Chemistry. 95. 136–152. 19 indexed citations
14.
Hubin, Ellen, Nico A. J. van Nuland, Kerensa Broersen, & Kris Pauwels. (2014). Transient dynamics of Aβ contribute to toxicity in Alzheimer’s disease. Cellular and Molecular Life Sciences. 71(18). 3507–3521. 80 indexed citations
15.
Vandersteen, Annelies, Marcelo F. Masman, Greet De Baets, et al.. (2012). Molecular Plasticity Regulates Oligomerization and Cytotoxicity of the Multipeptide-length Amyloid-β Peptide Pool. Journal of Biological Chemistry. 287(44). 36732–36743. 38 indexed citations
16.
Vandersteen, Annelies, Ellen Hubin, Rabia Sarroukh, et al.. (2012). A comparative analysis of the aggregation behavior of amyloid‐β peptide variants. FEBS Letters. 586(23). 4088–4093. 61 indexed citations
17.
Pauwels, Kris, Thomas L. Williams, Kyle L. Morris, et al.. (2011). Structural Basis for Increased Toxicity of Pathological Aβ42:Aβ40 Ratios in Alzheimer Disease. Journal of Biological Chemistry. 287(8). 5650–5660. 202 indexed citations
18.
Broersen, Kerensa, Frédéric Rousseau, & Joost Schymkowitz. (2010). The culprit behind amyloid beta peptide related neurotoxicity in Alzheimer's disease: oligomer size or conformation?. Alzheimer s Research & Therapy. 2(4). 12–12. 118 indexed citations
19.
Broersen, Kerensa, Alphons G. J. Voragen, R.J. Hamer, & Harmen H. J. de Jongh. (2004). Glycoforms of β‐lactoglobulin with improved thermostability and preserved structural packing. Biotechnology and Bioengineering. 86(1). 78–87. 86 indexed citations
20.
Kosters, Hans A., Kerensa Broersen, J. de Groot, et al.. (2003). Chemical processing as a tool to generate ovalbumin variants with changed stability. Biotechnology and Bioengineering. 84(1). 61–70. 37 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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