Jörg Tatzelt

6.5k total citations
96 papers, 4.9k citations indexed

About

Jörg Tatzelt is a scholar working on Molecular Biology, Neurology and Nutrition and Dietetics. According to data from OpenAlex, Jörg Tatzelt has authored 96 papers receiving a total of 4.9k indexed citations (citations by other indexed papers that have themselves been cited), including 86 papers in Molecular Biology, 41 papers in Neurology and 26 papers in Nutrition and Dietetics. Recurrent topics in Jörg Tatzelt's work include Prion Diseases and Protein Misfolding (64 papers), Neurological diseases and metabolism (41 papers) and Trace Elements in Health (26 papers). Jörg Tatzelt is often cited by papers focused on Prion Diseases and Protein Misfolding (64 papers), Neurological diseases and metabolism (41 papers) and Trace Elements in Health (26 papers). Jörg Tatzelt collaborates with scholars based in Germany, United States and Canada. Jörg Tatzelt's co-authors include Konstanze F. Winklhofer, Christian Haass, Stanley B. Prusiner, William J. Welch, F. Ulrich Hartl, Angelika S. Rambold, Hermann Schätzl, Margit Miesbauer, Wolfgang Wurst and S. J. DeArmond and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Jörg Tatzelt

91 papers receiving 4.8k citations

Peers

Jörg Tatzelt

NEURO

PHYSI

NEURO

Konstanze F. Winklhofer Germany

Rubén Vidal United States

Vilma R. Martins Brazil

Janetta G. Culvenor Australia

Noriyuki Nishida Japan

Paolo Paganetti Switzerland

Kurt J. De Vos United Kingdom

Anil G. Cashikar United States

Gerold Schmitt‐Ulms Canada

Surachai Supattapone United States

Konstanze F. Winklhofer Germany

Jörg Tatzelt

4.5k ×1.2

1.3k ×1.0

NEURO

1.5k ×1.5

PHYSI

2.4k ×2.7

NEURO

561 ×0.7

Citations per year, relative to Jörg Tatzelt Jörg Tatzelt (= 1×) peers Konstanze F. Winklhofer

Countries citing papers authored by Jörg Tatzelt

Since Specialization

Citations

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

Fields of papers citing papers by Jörg Tatzelt

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Jörg Tatzelt

This figure shows the co-authorship network connecting the top 25 collaborators of Jörg Tatzelt. A scholar is included among the top collaborators of Jörg Tatzelt 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 Jörg Tatzelt. Jörg Tatzelt 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

Mohammadi, Behnam, et al.. (2026). Presymptomatic pharmacological inhibition of mGluR5 improves survival in a mouse model of prion diseases. Acta Neuropathologica Communications.

Ramos, Sashary, et al.. (2023). Hydration makes a difference! How to tune protein complexes between liquid–liquid and liquid–solid phase separation. Physical Chemistry Chemical Physics. 25(41). 28063–28069. 15 indexed citations

Oliva, Rosario, Sadasivam Jeganathan�, Verian Bader, et al.. (2023). Linear ubiquitination induces NEMO phase separation to activate NF-κB signaling. Life Science Alliance. 6(4). e202201607–e202201607. 23 indexed citations

Oliva, Rosario, et al.. (2021). The N-terminal domain of the prion protein is required and sufficient for liquid–liquid phase separation: A crucial role of the Aβ-binding domain. Journal of Biological Chemistry. 297(1). 100860–100860. 26 indexed citations

Bader, Verian, Anna Pilsl, Anita Schlierf, et al.. (2020). The parkin-coregulated gene product PACRG promotes TNF signaling by stabilizing LUBAC. Science Signaling. 13(617). 14 indexed citations

Tatzelt, Jörg, Johanna Dudek, Adrienne W. Paton, et al.. (2019). The signal peptide plus a cluster of positive charges in prion protein dictate chaperone-mediated Sec61 channel gating. Biology Open. 8(3). 26 indexed citations

Eigenbrod, Sabina, Petra Frick, Uwe Bertsch, et al.. (2017). Substitutions of PrP N-terminal histidine residues modulate scrapie disease pathogenesis and incubation time in transgenic mice. PLoS ONE. 12(12). e0188989–e0188989. 11 indexed citations

Tatzelt, Jörg, et al.. (2017). The RAB GTPase RAB18 modulates macroautophagy and proteostasis. Biochemical and Biophysical Research Communications. 486(3). 738–743. 42 indexed citations

Puig, Berta, Hermann C. Altmeppen, Luise Linsenmeier, et al.. (2016). Secretory pathway retention of mutant prion protein induces p38-MAPK activation and lethal disease in mice. Scientific Reports. 6(1). 24970–24970. 21 indexed citations

10.

McCarthy, J. Michael, Markus Franke, Jeremy C. Simpson, et al.. (2013). Anti-Prion Drug mPPIg5 Inhibits PrPC Conversion to PrPSc. PLoS ONE. 8(1). e55282–e55282. 25 indexed citations

11.

Pilsl, Anna, Patrick Beaudette, Kamyar Hadian, et al.. (2013). The E3 Ligase Parkin Maintains Mitochondrial Integrity by Increasing Linear Ubiquitination of NEMO. Molecular Cell. 49(5). 908–921. 166 indexed citations

12.

Kremmer, Elisabeth, et al.. (2010). The Novel Membrane Protein TMEM59 Modulates Complex Glycosylation, Cell Surface Expression, and Secretion of the Amyloid Precursor Protein. Journal of Biological Chemistry. 285(27). 20664–20674. 56 indexed citations

13.

Chu, Nam, Diana Olschewski, R. Seidel, et al.. (2010). Protein immobilization on liposomes and lipid‐coated nanoparticles by protein trans‐splicing. Journal of Peptide Science. 16(10). 582–588. 17 indexed citations

14.

Tatzelt, Jörg & Hermann Schätzl. (2007). Molecular basis of cerebral neurodegeneration in prion diseases. FEBS Journal. 274(3). 606–611. 28 indexed citations

15.

Olschewski, Diana, R. Seidel, Margit Miesbauer, et al.. (2007). Semisynthetic Murine Prion Protein Equipped with a GPI Anchor Mimic Incorporates into Cellular Membranes. Chemistry & Biology. 14(9). 994–1006. 44 indexed citations

16.

Beekes, Michael, et al.. (2005). The polysaccharide scaffold of PrP 27-30 is a common compound of natural prions and consists of α-linked polyglucose. Biological Chemistry. 386(11). 1149–55. 20 indexed citations

17.

Gostner, Johanna M., et al.. (2004). Pathogenic mutations inactivate parkin by distinct mechanisms. Journal of Neurochemistry. 92(1). 114–122. 82 indexed citations

18.

Winklhofer, Konstanze F., et al.. (2003). Determinants of the in Vivo Folding of the Prion Protein. Journal of Biological Chemistry. 278(17). 14961–14970. 57 indexed citations

19.

Winklhofer, Konstanze F., et al.. (2003). Inactivation of Parkin by Oxidative Stress and C-terminal Truncations. Journal of Biological Chemistry. 278(47). 47199–47208. 116 indexed citations

20.

Winklhofer, Konstanze F., et al.. (2003). Inhibition of Complex Glycosylation Increases the Formation of PrP^sc. Traffic. 4(5). 313–322. 55 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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