F. Ulrich Hartl

68.5k total citations · 27 hit papers
284 papers, 53.2k citations indexed

About

F. Ulrich Hartl is a scholar working on Molecular Biology, Materials Chemistry and Cell Biology. According to data from OpenAlex, F. Ulrich Hartl has authored 284 papers receiving a total of 53.2k indexed citations (citations by other indexed papers that have themselves been cited), including 267 papers in Molecular Biology, 86 papers in Materials Chemistry and 48 papers in Cell Biology. Recurrent topics in F. Ulrich Hartl's work include Heat shock proteins research (154 papers), Protein Structure and Dynamics (96 papers) and Enzyme Structure and Function (86 papers). F. Ulrich Hartl is often cited by papers focused on Heat shock proteins research (154 papers), Protein Structure and Dynamics (96 papers) and Enzyme Structure and Function (86 papers). F. Ulrich Hartl collaborates with scholars based in Germany, United States and United Kingdom. F. Ulrich Hartl's co-authors include Manajit Hayer‐Hartl, Andreas Bracher, Jörg Martin, Walter Neupert, Mark S. Hipp, Jason C. Young, Joseph P. Hendrick, Thomas Langer, Arthur L. Horwich and Ismail Moarefi and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

F. Ulrich Hartl

283 papers receiving 52.3k citations

Hit Papers

Molecular Chaperones in the Cytosol: from Nascent Chain ... 1989 2026 2001 2013 2002 2011 1993 1997 2013 500 1000 1.5k 2.0k 2.5k

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
F. Ulrich Hartl Germany 122 45.6k 10.0k 8.8k 5.3k 4.0k 284 53.2k
Susan Lindquist United States 125 44.9k 1.0× 8.1k 0.8× 4.1k 0.5× 2.9k 0.6× 7.3k 1.8× 301 56.5k
Robert Huber Germany 135 46.8k 1.0× 6.8k 0.7× 11.3k 1.3× 3.9k 0.7× 1.7k 0.4× 600 66.7k
Axel T. Brünger United States 103 42.9k 0.9× 12.5k 1.3× 12.3k 1.4× 3.0k 0.6× 2.7k 0.7× 298 56.0k
Bernd Bukau Germany 107 30.3k 0.7× 6.6k 0.7× 6.1k 0.7× 4.0k 0.8× 1.5k 0.4× 259 34.5k
Jane S. Richardson United States 57 43.5k 1.0× 4.5k 0.4× 12.8k 1.4× 4.9k 0.9× 1.9k 0.5× 130 59.8k
Ralf W. Grosse‐Kunstleve United States 37 48.2k 1.1× 5.8k 0.6× 14.8k 1.7× 5.3k 1.0× 2.0k 0.5× 65 67.1k
Vladimir N. Uversky United States 132 51.9k 1.1× 7.2k 0.7× 13.9k 1.6× 2.5k 0.5× 10.8k 2.7× 1.1k 73.4k
David Eisenberg United States 120 46.7k 1.0× 3.9k 0.4× 10.0k 1.1× 3.8k 0.7× 12.3k 3.1× 409 62.2k
Randy J. Read United Kingdom 69 62.2k 1.4× 7.9k 0.8× 19.0k 2.2× 7.2k 1.4× 2.8k 0.7× 197 86.9k
Wolfgang Kabsch Germany 47 34.2k 0.8× 5.3k 0.5× 12.7k 1.4× 2.5k 0.5× 1.8k 0.4× 65 47.6k

Countries citing papers authored by F. Ulrich Hartl

Since Specialization
Citations

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

Fields of papers citing papers by F. Ulrich Hartl

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by F. Ulrich Hartl. 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 F. Ulrich Hartl. The network helps show where F. Ulrich Hartl may publish in the future.

Co-authorship network of co-authors of F. Ulrich Hartl

This figure shows the co-authorship network connecting the top 25 collaborators of F. Ulrich Hartl. A scholar is included among the top collaborators of F. Ulrich Hartl 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 F. Ulrich Hartl. F. Ulrich Hartl 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.
Bracher, Andreas, Florian Beck, William Wan, et al.. (2024). Visualizing chaperonin function in situ by cryo-electron tomography. Nature. 633(8029). 459–464. 10 indexed citations
2.
Hipp, Mark S. & F. Ulrich Hartl. (2024). Interplay of Proteostasis Capacity and Protein Aggregation: Implications for Cellular Function and Disease. Journal of Molecular Biology. 436(14). 168615–168615. 22 indexed citations
3.
Wales, Thomas E., Aleksandra Pajak, Steven Howell, et al.. (2024). Resolving chaperone-assisted protein folding on the ribosome at the peptide level. Nature Structural & Molecular Biology. 31(12). 1888–1897. 9 indexed citations
4.
Krainer, Georg, Matthias M. Schneider, Timothy J. Welsh, et al.. (2024). Single-molecule digital sizing of proteins in solution. Nature Communications. 15(1). 7740–7740. 5 indexed citations
5.
Riemenschneider, Henrick, Qiang Guo, Jakob M. Bader, et al.. (2022). Gel‐like inclusions of C‐terminal fragments of TDP‐43 sequester stalled proteasomes in neurons. EMBO Reports. 23(6). e53890–e53890. 39 indexed citations
6.
Yuste‐Checa, Patricia, Victoria A. Trinkaus, Huping Wang, et al.. (2021). The extracellular chaperone Clusterin enhances Tau aggregate seeding in a cellular model. Nature Communications. 12(1). 4863–4863. 52 indexed citations
7.
Blumenstock, Sonja, et al.. (2021). Fluc‐EGFP reporter mice reveal differential alterations of neuronal proteostasis in aging and disease. The EMBO Journal. 40(19). e107260–e107260. 16 indexed citations
8.
Klaips, Courtney L., et al.. (2020). Sis1 potentiates the stress response to protein aggregation and elevated temperature. Nature Communications. 11(1). 6271–6271. 32 indexed citations
9.
Balchin, David, et al.. (2020). Bacterial Hsp70 resolves misfolded states and accelerates productive folding of a multi-domain protein. Nature Communications. 11(1). 365–365. 103 indexed citations
10.
Zinzula, Luca, J. Basquin, Stefan Bohn, et al.. (2020). High-resolution structure and biophysical characterization of the nucleocapsid phosphoprotein dimerization domain from the Covid-19 severe acute respiratory syndrome coronavirus 2. Biochemical and Biophysical Research Communications. 538. 54–62. 86 indexed citations
11.
Hipp, Mark S., Prasad Kasturi, & F. Ulrich Hartl. (2019). The proteostasis network and its decline in ageing. Nature Reviews Molecular Cell Biology. 20(7). 421–435. 961 indexed citations breakdown →
12.
Balchin, David, Manajit Hayer‐Hartl, & F. Ulrich Hartl. (2016). In vivo aspects of protein folding and quality control. Science. 353(6294). aac4354–aac4354. 1045 indexed citations breakdown →
13.
Kirstein, Janine, Daisuke Morito, Taichi Kakihana, et al.. (2015). Proteotoxic stress and ageing triggers the loss of redox homeostasis across cellular compartments. The EMBO Journal. 34(18). 2334–2349. 73 indexed citations
14.
Bracher, Andreas, Thomas R. Hauser, Cuimin Liu, F. Ulrich Hartl, & Manajit Hayer‐Hartl. (2015). Structural Analysis of the Rubisco-Assembly Chaperone RbcX-II from Chlamydomonas reinhardtii. PLoS ONE. 10(8). e0135448–e0135448. 14 indexed citations
15.
Kim, Yujin, Mark S. Hipp, Andreas Bracher, Manajit Hayer‐Hartl, & F. Ulrich Hartl. (2013). Molecular Chaperone Functions in Protein Folding and Proteostasis. Annual Review of Biochemistry. 82(1). 323–355. 1102 indexed citations breakdown →
16.
Herzog, Franz, Abdullah Kahraman, Daniel Boehringer, et al.. (2012). Structural Probing of a Protein Phosphatase 2A Network by Chemical Cross-Linking and Mass Spectrometry. Science. 337(6100). 1348–1352. 326 indexed citations
17.
Broadley, Sarah A. & F. Ulrich Hartl. (2007). Mitochondrial stress signaling: a pathway unfolds. Trends in Cell Biology. 18(1). 1–4. 49 indexed citations
18.
Young, Jason C., Nicholas J. Hoogenraad, & F. Ulrich Hartl. (2003). Molecular Chaperones Hsp90 and Hsp70 Deliver Preproteins to the Mitochondrial Import Receptor Tom70. Cell. 112(1). 41–50. 706 indexed citations breakdown →
19.
Hayer‐Hartl, Manajit, Karla L. Ewalt, & F. Ulrich Hartl. (1999). On the Role of Symmetrical and Asymmetrical Chaperonin Complexes in Assisted Protein Folding. Biological Chemistry. 380(5). 531–40. 16 indexed citations
20.
Martin, Jörg, et al.. (1991). Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate. Nature. 352(6330). 36–42. 748 indexed citations breakdown →

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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