Axel Leppert

625 total citations
31 papers, 424 citations indexed

About

Axel Leppert is a scholar working on Molecular Biology, Materials Chemistry and Biomaterials. According to data from OpenAlex, Axel Leppert has authored 31 papers receiving a total of 424 indexed citations (citations by other indexed papers that have themselves been cited), including 27 papers in Molecular Biology, 10 papers in Materials Chemistry and 9 papers in Biomaterials. Recurrent topics in Axel Leppert's work include Protein Structure and Dynamics (14 papers), Enzyme Structure and Function (10 papers) and Heat shock proteins research (8 papers). Axel Leppert is often cited by papers focused on Protein Structure and Dynamics (14 papers), Enzyme Structure and Function (10 papers) and Heat shock proteins research (8 papers). Axel Leppert collaborates with scholars based in Sweden, Denmark and Estonia. Axel Leppert's co-authors include Michael Landreh, Jan Johansson, Gefei Chen, Henrik Biverstål, Axel Abelein, Hans Hebert, Simone Tambaro, Jenny Presto, Harriet E. Nilsson and Cagla Sahin and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and Nature Communications.

In The Last Decade

Axel Leppert

30 papers receiving 420 citations

Peers

Axel Leppert

PHYSI

BIOMA

Young‐Jun Choe South Korea

Srivastav Ranganathan India

Joseph M. Perchiacca United States

Nina Kristine Reitan Norway

Wencheng Xia China

Melissa Birol United States

Xi-xiu Xie China

Fulvio Grigolato Switzerland

Fude Sun China

Jaime Santos Spain

Young‐Jun Choe South Korea

Axel Leppert

327 ×1.1

105 ×0.8

PHYSI

37 ×0.4

BIOMA

55 ×0.8

58 ×1.3

Citations per year, relative to Axel Leppert Axel Leppert (= 1×) peers Young‐Jun Choe

Countries citing papers authored by Axel Leppert

Since Specialization

Citations

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

Fields of papers citing papers by Axel Leppert

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Axel Leppert

This figure shows the co-authorship network connecting the top 25 collaborators of Axel Leppert. A scholar is included among the top collaborators of Axel Leppert 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 Axel Leppert. Axel Leppert is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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20 of 20 papers shown

Leppert, Axel, Rakesh Kumar, Lotte B. Nielsen, et al.. (2025). Helicobacter pylori CagA protein is a potent and broad-spectrum amyloid inhibitor. Science Advances. 11(24). eads7525–eads7525.

Leppert, Axel, Carmine Pasquale Cerrato, David P. Lane, et al.. (2024). Controlling Drug Partitioning in Individual Protein Condensates through Laser-Induced Microscale Phase Transitions. Journal of the American Chemical Society. 146(28). 19555–19565. 12 indexed citations

Wang, Han, Yu Wang, Axel Leppert, et al.. (2024). Spiders Use Structural Conversion of Globular Amyloidogenic Domains to Make Strong Silk Fibers. Advanced Functional Materials. 34(23). 8 indexed citations

Wang, Han, Yu Wang, Axel Leppert, et al.. (2024). Spiders Use Structural Conversion of Globular Amyloidogenic Domains to Make Strong Silk Fibers (Adv. Funct. Mater. 23/2024). Advanced Functional Materials. 34(23). 3 indexed citations

Landreh, Michael, et al.. (2024). Liquid-liquid crystalline phase separation of spider silk proteins. Communications Chemistry. 7(1). 260–260. 9 indexed citations

Leppert, Axel, et al.. (2023). A new kid in the folding funnel: Molecular chaperone activities of the BRICHOS domain. Protein Science. 32(6). e4645–e4645. 18 indexed citations

Wang, Yu, Hairui Yu, Ruifang Liu, et al.. (2023). Spider Silk Protein Forms Amyloid‐Like Nanofibrils through a Non‐Nucleation‐Dependent Polymerization Mechanism. Small. 19(46). e2304031–e2304031. 13 indexed citations

Chen, Gefei, Axel Leppert, Harriet E. Nilsson, et al.. (2023). Short hydrophobic loop motifs in BRICHOS domains determine chaperone activity against amorphous protein aggregation but not against amyloid formation. Communications Biology. 6(1). 497–497. 6 indexed citations

Omnus, Deike J., et al.. (2023). The heat shock protein LarA activates the Lon protease in response to proteotoxic stress. Nature Communications. 14(1). 7636–7636. 9 indexed citations

10.

Leppert, Axel, Cagla Sahin, Dilraj Lama, et al.. (2023). A “grappling hook” interaction connects self-assembly and chaperone activity of Nucleophosmin 1. PNAS Nexus. 2(2). pgac303–pgac303. 10 indexed citations

11.

Sahin, Cagla, Axel Leppert, & Michael Landreh. (2023). Advances in mass spectrometry to unravel the structure and function of protein condensates. Nature Protocols. 18(12). 3653–3661. 9 indexed citations

12.

Leppert, Axel, Gefei Chen, Dilraj Lama, et al.. (2023). Liquid–Liquid Phase Separation Primes Spider Silk Proteins for Fiber Formation via a Conditional Sticker Domain. Nano Letters. 23(12). 5836–5841. 44 indexed citations

13.

Österlund, Nicklas, Axel Leppert, Astrid Gräslund, et al.. (2022). Mass Spectrometry and Machine Learning Reveal Determinants of Client Recognition by Antiamyloid Chaperones. Molecular & Cellular Proteomics. 21(10). 100413–100413. 8 indexed citations

14.

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

15.

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

16.

Sierra, Carlos, Axel Leppert, Antonios N. Pouliopoulos, et al.. (2020). Recombinant BRICHOS chaperone domains delivered to mouse brain parenchyma by focused ultrasound and microbubbles are internalized by hippocampal and cortical neurons. Molecular and Cellular Neuroscience. 105. 103498–103498. 19 indexed citations

17.

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

18.

Kaldmäe, Margit, Axel Leppert, Gefei Chen, et al.. (2019). High intracellular stability of the spidroin N‐terminal domain in spite of abundant amyloidogenic segments revealed by in‐cell hydrogen/deuterium exchange mass spectrometry. FEBS Journal. 287(13). 2823–2833. 11 indexed citations

19.

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

20.

Göke, Michael, Axel Leppert, P. Flemming, et al.. (2001). Darmtuberkulose: leichter zu übersehen als zu sichern. Zeitschrift für Gastroenterologie. 39(12). 1015–1022. 3 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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