Henrik Biverstål

2.0k total citations
35 papers, 1.6k citations indexed

About

Henrik Biverstål is a scholar working on Molecular Biology, Physiology and Cellular and Molecular Neuroscience. According to data from OpenAlex, Henrik Biverstål has authored 35 papers receiving a total of 1.6k indexed citations (citations by other indexed papers that have themselves been cited), including 26 papers in Molecular Biology, 25 papers in Physiology and 5 papers in Cellular and Molecular Neuroscience. Recurrent topics in Henrik Biverstål's work include Alzheimer's disease research and treatments (24 papers), Protein Structure and Dynamics (17 papers) and Prion Diseases and Protein Misfolding (4 papers). Henrik Biverstål is often cited by papers focused on Alzheimer's disease research and treatments (24 papers), Protein Structure and Dynamics (17 papers) and Prion Diseases and Protein Misfolding (4 papers). Henrik Biverstål collaborates with scholars based in Sweden, Latvia and United Kingdom. Henrik Biverstål's co-authors include Jan Johansson, Jenny Presto, Christopher M. Dobson, Tuomas P. J. Knowles, André Fisahn, Birgitta Frohm, Sara Linse, Firoz Roshan Kurudenkandy, Christofer Lendel and Axel Abelein and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

Henrik Biverstål

35 papers receiving 1.6k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Henrik Biverstål Sweden 18 1.1k 1.0k 272 231 191 35 1.6k
Marten Beeg Italy 23 949 0.9× 1.0k 1.0× 188 0.7× 209 0.9× 183 1.0× 47 1.8k
Sean Chia United Kingdom 21 916 0.9× 929 0.9× 221 0.8× 233 1.0× 82 0.4× 46 1.5k
Brian O’Nuallain United States 17 1.2k 1.1× 1.0k 1.0× 217 0.8× 235 1.0× 219 1.1× 22 1.6k
Luke Rajah United Kingdom 9 994 0.9× 962 0.9× 281 1.0× 193 0.8× 83 0.4× 9 1.5k
Audrey A. Darabie Canada 14 1.1k 1.1× 782 0.8× 192 0.7× 261 1.1× 162 0.8× 16 1.5k
Alexander J. Dear United Kingdom 20 806 0.8× 775 0.8× 256 0.9× 164 0.7× 77 0.4× 40 1.3k
Michele Perni United Kingdom 17 923 0.9× 907 0.9× 148 0.5× 207 0.9× 164 0.9× 29 1.6k
Jessica Meinhardt Germany 11 1.1k 1.0× 864 0.8× 284 1.0× 138 0.6× 240 1.3× 14 1.4k
Youcef Fezoui United States 8 1.3k 1.2× 1.1k 1.1× 336 1.2× 280 1.2× 110 0.6× 10 1.7k
Axel Abelein Sweden 19 664 0.6× 654 0.6× 171 0.6× 143 0.6× 78 0.4× 36 1.1k

Countries citing papers authored by Henrik Biverstål

Since Specialization
Citations

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

Fields of papers citing papers by Henrik Biverstål

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Henrik Biverstål

This figure shows the co-authorship network connecting the top 25 collaborators of Henrik Biverstål. A scholar is included among the top collaborators of Henrik Biverstål 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 Henrik Biverstål. Henrik Biverstål 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.
Nordvall, Gunnar, Ping Yan, Lotta Agholme, et al.. (2025). γ-Secretase modulation inhibits amyloid plaque formation and growth and stimulates plaque regression in amyloid precursor protein/presenilin-1 mice. Journal of Pharmacology and Experimental Therapeutics. 392(4). 103400–103400. 1 indexed citations
2.
Kumar, Rakesh, Luis Enrique Arroyo‐García, Azad Farzadfard, et al.. (2024). Specific inhibition of α‐synuclein oligomer generation and toxicity by the chaperone domain Bri2 BRICHOS. Protein Science. 33(8). e5091–e5091. 4 indexed citations
3.
Shimozawa, Makoto, Henrik Biverstål, Ganna Shevchenko, et al.. (2023). Identification of cytoskeletal proteins as binding partners of Bri2 BRICHOS domain. Molecular and Cellular Neuroscience. 125. 103843–103843. 3 indexed citations
4.
Kaya, Ibrahim, Mohammadreza Shariatgorji, Johan Lundkvist, et al.. (2023). Prosaposin maintains lipid homeostasis in dopamine neurons and counteracts experimental parkinsonism in rodents. Nature Communications. 14(1). 5804–5804. 28 indexed citations
5.
Chen, Gefei, Yuniesky Andrade‐Talavera, Xueying Zhong, et al.. (2022). Abilities of the BRICHOS domain to prevent neurotoxicity and fibril formation are dependent on a highly conserved Asp residue. RSC Chemical Biology. 3(11). 1342–1358. 12 indexed citations
6.
Zhong, Xueying, Rakesh Kumar, Yu Wang, et al.. (2022). Amyloid Fibril Formation of Arctic Amyloid-β 1–42 Peptide is Efficiently Inhibited by the BRICHOS Domain. ACS Chemical Biology. 17(8). 2201–2211. 19 indexed citations
7.
Abelein, Axel, Gefei Chen, Médoune Sarr, et al.. (2020). High-yield Production of Amyloid-β Peptide Enabled by a Customized Spider Silk Domain. Scientific Reports. 10(1). 235–235. 52 indexed citations
8.
Biverstål, Henrik, Rakesh Kumar, Médoune Sarr, et al.. (2020). Functionalization of amyloid fibrils via the Bri2 BRICHOS domain. Scientific Reports. 10(1). 21765–21765. 16 indexed citations
9.
Chen, Gefei, Yuniesky Andrade‐Talavera, Simone Tambaro, et al.. (2020). Augmentation of Bri2 molecular chaperone activity against amyloid-β reduces neurotoxicity in mouse hippocampus in vitro. Communications Biology. 3(1). 45 indexed citations
10.
Wallin, Cecilia, Jüri Jarvet, Henrik Biverstål, et al.. (2020). Metal ion coordination delays amyloid-β peptide self-assembly by forming an aggregation–inert complex. Journal of Biological Chemistry. 295(21). 7224–7234. 27 indexed citations
11.
Honcharenko, Dmytro, Jyotirmoy Maity, Henrik Biverstål, et al.. (2019). Amyloid-β Peptide Targeting Peptidomimetics for Prevention of Neurotoxicity. ACS Chemical Neuroscience. 10(3). 1462–1477. 11 indexed citations
12.
Tambaro, Simone, Axel Leppert, Gefei Chen, et al.. (2019). Blood–brain and blood–cerebrospinal fluid passage of BRICHOS domains from two molecular chaperones in mice. Journal of Biological Chemistry. 294(8). 2606–5220. 16 indexed citations
13.
Brüning, Thomas, Petra Sántha, Henrik Biverstål, et al.. (2017). Improved method for cannula fixation for long-term intracerebral brain infusion. Journal of Neuroscience Methods. 290. 145–150. 9 indexed citations
14.
Jaudzems, Kristaps, et al.. (2017). Structural studies of amyloid-β peptides: Unlocking the mechanism of aggregation and the associated toxicity. Biochimie. 140. 176–192. 64 indexed citations
15.
Steffen, Johannes, Markus Krohn, Thomas Brüning, et al.. (2017). Expression of endogenous mouse APP modulates β-amyloid deposition in hAPP-transgenic mice. Acta Neuropathologica Communications. 5(1). 49–49. 22 indexed citations
16.
Haslbeck, Martin, Firoz Roshan Kurudenkandy, Erik Hermansson, et al.. (2016). Dementia-related Bri2 BRICHOS is a versatile molecular chaperone that efficiently inhibits Aβ42 toxicity in Drosophila. Biochemical Journal. 473(20). 3683–3704. 49 indexed citations
17.
Biverstål, Henrik, Erik Hermansson, Axel Leppert, et al.. (2015). Dissociation of a BRICHOS trimer into monomers leads to increased inhibitory effect on Aβ42 fibril formation. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1854(8). 835–843. 22 indexed citations
18.
Cohen, Samuel I. A., Paolo Arosio, Jenny Presto, et al.. (2015). A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers. Nature Structural & Molecular Biology. 22(3). 207–213. 351 indexed citations
19.
Campo, Marta del, Catarina R. Oliveira, Wiep Scheper, et al.. (2014). BRI2 ectodomain affects Aβ42 fibrillation and tau truncation in human neuroblastoma cells. Cellular and Molecular Life Sciences. 72(8). 1599–1611. 11 indexed citations
20.
Kurudenkandy, Firoz Roshan, Misha Zilberter, Henrik Biverstål, et al.. (2014). Amyloid-β-Induced Action Potential Desynchronization and Degradation of Hippocampal Gamma Oscillations Is Prevented by Interference with Peptide Conformation Change and Aggregation. Journal of Neuroscience. 34(34). 11416–11425. 92 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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