Jan Bieschke

7.5k total citations · 3 hit papers
56 papers, 6.0k citations indexed

About

Jan Bieschke is a scholar working on Molecular Biology, Physiology and Neurology. According to data from OpenAlex, Jan Bieschke has authored 56 papers receiving a total of 6.0k indexed citations (citations by other indexed papers that have themselves been cited), including 33 papers in Molecular Biology, 30 papers in Physiology and 13 papers in Neurology. Recurrent topics in Jan Bieschke's work include Alzheimer's disease research and treatments (28 papers), Prion Diseases and Protein Misfolding (21 papers) and Neurological diseases and metabolism (11 papers). Jan Bieschke is often cited by papers focused on Alzheimer's disease research and treatments (28 papers), Prion Diseases and Protein Misfolding (21 papers) and Neurological diseases and metabolism (11 papers). Jan Bieschke collaborates with scholars based in United States, Germany and United Kingdom. Jan Bieschke's co-authors include Erich E. Wanker, Jeffery W. Kelly, Dagmar E. Ehrnhoefer, Heike J. Wobst, Rudi Lurz, Annett Boeddrich, Martin Herbst, Ralf P. Friedrich, Andrew Dillin and Ehud Cohen and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Jan Bieschke

53 papers receiving 5.9k citations

Hit Papers

EGCG redirects amyloidogenic polypeptides into unstructur... 2006 2026 2012 2019 2008 2010 2006 250 500 750 1000

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Jan Bieschke United States 32 3.1k 3.1k 809 613 562 56 6.0k
Cristina Cecchi Italy 36 2.4k 0.8× 2.4k 0.8× 889 1.1× 353 0.6× 505 0.9× 97 4.3k
Dagmar E. Ehrnhoefer Canada 22 1.8k 0.6× 2.0k 0.6× 827 1.0× 372 0.6× 1.2k 2.1× 34 4.0k
Monica Bucciantini Italy 31 2.5k 0.8× 3.7k 1.2× 443 0.5× 292 0.5× 412 0.7× 87 5.6k
Harry LeVine United States 36 3.3k 1.1× 2.6k 0.8× 359 0.4× 776 1.3× 536 1.0× 72 5.3k
Gunnar Brinkmalm Sweden 39 3.2k 1.0× 2.2k 0.7× 576 0.7× 441 0.7× 638 1.1× 134 5.4k
Eduardo M. Castaño Argentina 33 3.8k 1.2× 2.5k 0.8× 468 0.6× 684 1.1× 585 1.0× 73 4.9k
László Ötvös United States 39 3.9k 1.3× 4.1k 1.3× 398 0.5× 802 1.3× 1.1k 1.9× 97 7.9k
Per Hammarström Sweden 45 3.2k 1.0× 4.5k 1.5× 397 0.5× 425 0.7× 381 0.7× 145 7.2k
Miguel Calero Spain 39 3.3k 1.1× 2.9k 1.0× 759 0.9× 581 0.9× 747 1.3× 132 6.5k
Katsuhiko Yanagisawa Japan 51 5.9k 1.9× 4.9k 1.6× 527 0.7× 784 1.3× 1.2k 2.1× 144 9.1k

Countries citing papers authored by Jan Bieschke

Since Specialization
Citations

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

Fields of papers citing papers by Jan Bieschke

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Jan Bieschke

This figure shows the co-authorship network connecting the top 25 collaborators of Jan Bieschke. A scholar is included among the top collaborators of Jan Bieschke 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 Jan Bieschke. Jan Bieschke 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.
Hill, Elizabeth, Mark Batchelor, Juan M. Ribes, et al.. (2024). Syntaxin-6 delays prion protein fibril formation and prolongs the presence of toxic aggregation intermediates. eLife. 13. 2 indexed citations
2.
Hosszu, Laszlo L. P., Mark Batchelor, Emmanuel Risse, et al.. (2023). Loss of Residues 119–136, Including the First β-strand of Human Prion Protein, Generates an Aggregation-competent Partially “Open” Form. Journal of Molecular Biology. 435(15). 168158–168158.
3.
Nahass, George R., Yong Xu, Mark Batchelor, et al.. (2021). Brazilin Removes Toxic Alpha-Synuclein and Seeding Competent Assemblies from Parkinson Brain by Altering Conformational Equilibrium. Journal of Molecular Biology. 433(8). 166878–166878. 8 indexed citations
4.
Hosszu, Laszlo L. P., Rebecca Conners, Mark Batchelor, et al.. (2020). Structural effects of the highly protective V127 polymorphism on human prion protein. Communications Biology. 3(1). 402–402. 7 indexed citations
5.
Bieschke, Jan, et al.. (2016). Unconventional Chaperone Inhibits Amyloid Formation by Promoting off-Pathway Aggregation. Biophysical Journal. 110(3). 551a–552a. 1 indexed citations
6.
Jin, Sha, Niraja Kedia, Eva Illes‐Toth, et al.. (2016). Amyloid-β(1–42) Aggregation Initiates Its Cellular Uptake and Cytotoxicity. Journal of Biological Chemistry. 291(37). 19590–19606. 91 indexed citations
7.
Hegenbart, Ute, Christoph Kimmich, Niraja Kedia, et al.. (2016). Aggregation of Full-length Immunoglobulin Light Chains from Systemic Light Chain Amyloidosis (AL) Patients Is Remodeled by Epigallocatechin-3-gallate. Journal of Biological Chemistry. 292(6). 2328–2344. 36 indexed citations
8.
Bieschke, Jan, et al.. (2015). The Effect of (−)-Epigallo-catechin-(3)-gallate on Amyloidogenic Proteins Suggests a Common Mechanism. Advances in experimental medicine and biology. 863. 139–161. 60 indexed citations
9.
Bieschke, Jan, et al.. (2014). Aggregation in AL Amyloidosis. Biophysical Journal. 106(2). 58a–58a. 1 indexed citations
10.
Wobst, Heike J., Apurwa M Sharma, Marc I. Diamond, Erich E. Wanker, & Jan Bieschke. (2014). The green tea polyphenol (−)‐epigallocatechin gallate prevents the aggregation of tau protein into toxic oligomers at substoichiometric ratios. FEBS Letters. 589(1). 77–83. 164 indexed citations
11.
Bieschke, Jan. (2013). Natural Compounds May Open New Routes to Treatment of Amyloid Diseases. Neurotherapeutics. 10(3). 429–439. 71 indexed citations
12.
Amo, Juan Miguel López del, Uwe Fink, Muralidhar Dasari, et al.. (2012). Structural Properties of EGCG-Induced, Nontoxic Alzheimer's Disease Aβ Oligomers. Journal of Molecular Biology. 421(4-5). 517–524. 138 indexed citations
13.
Sommer, Andrei P., Jan Bieschke, Ralf P. Friedrich, et al.. (2011). 670 nm Laser Light and EGCG Complementarily Reduce Amyloid-β Aggregates in Human Neuroblastoma Cells: Basis for Treatment of Alzheimer's Disease?. Photomedicine and Laser Surgery. 30(1). 54–60. 59 indexed citations
14.
Bieschke, Jan, Martin Herbst, Thomas Wiglenda, et al.. (2011). Small-molecule conversion of toxic oligomers to nontoxic β-sheet–rich amyloid fibrils. Nature Chemical Biology. 8(1). 93–101. 386 indexed citations
15.
Ehrnhoefer, Dagmar E., Jan Bieschke, Annett Boeddrich, et al.. (2008). EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers. Nature Structural & Molecular Biology. 15(6). 558–566. 1191 indexed citations breakdown →
16.
Cohen, Ehud, et al.. (2006). Opposing Activities Protect Against Age-Onset Proteotoxicity. Science. 313(5793). 1604–1610. 687 indexed citations breakdown →
17.
Giese, Armin, Benedikt Bader, Jan Bieschke, et al.. (2005). Single particle detection and characterization of synuclein co-aggregation. Biochemical and Biophysical Research Communications. 333(4). 1202–1210. 39 indexed citations
18.
Sarafoff, Nikolaus, Jan Bieschke, Armin Giese, et al.. (2005). Automated PrPres amplification using indirect sonication. Journal of Biochemical and Biophysical Methods. 63(3). 213–221. 13 indexed citations
19.
Koltermann, Andre, Ulrich Kettling, Jan Bieschke, T. Winkler, & Manfred Eigen. (1998). Rapid assay processing by integration of dual-color fluorescence cross-correlation spectroscopy: High throughput screening for enzyme activity. Proceedings of the National Academy of Sciences. 95(4). 1421–1426. 111 indexed citations
20.
Schwille, Petra, et al.. (1997). Kinetic investigations by fluorescence correlation spectroscopy: The analytical and diagnostic potential of diffusion studies. Biophysical Chemistry. 66(2-3). 211–228. 129 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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