Dieter Langosch

8.0k total citations
112 papers, 6.4k citations indexed

About

Dieter Langosch is a scholar working on Molecular Biology, Cell Biology and Cellular and Molecular Neuroscience. According to data from OpenAlex, Dieter Langosch has authored 112 papers receiving a total of 6.4k indexed citations (citations by other indexed papers that have themselves been cited), including 103 papers in Molecular Biology, 37 papers in Cell Biology and 27 papers in Cellular and Molecular Neuroscience. Recurrent topics in Dieter Langosch's work include Lipid Membrane Structure and Behavior (51 papers), Cellular transport and secretion (34 papers) and RNA and protein synthesis mechanisms (23 papers). Dieter Langosch is often cited by papers focused on Lipid Membrane Structure and Behavior (51 papers), Cellular transport and secretion (34 papers) and RNA and protein synthesis mechanisms (23 papers). Dieter Langosch collaborates with scholars based in Germany, United States and Netherlands. Dieter Langosch's co-authors include Heinrich Betz, Joachim Kirsch, Joachim Bormann, Rico Laage, L. A. Thomas, Christian Ungermann, Guido R.Y. De Meyer, I. Pribilla, Mark G. Teese and Bertram Schmitt and has published in prestigious journals such as Science, Chemical Reviews and Proceedings of the National Academy of Sciences.

In The Last Decade

Dieter Langosch

110 papers receiving 6.3k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Dieter Langosch Germany 42 5.1k 2.3k 1.5k 787 321 112 6.4k
J. Michael Edwardson United Kingdom 46 4.4k 0.9× 1.4k 0.6× 1.7k 1.1× 714 0.9× 423 1.3× 163 6.2k
Juan Llopis Spain 29 5.3k 1.0× 1.5k 0.6× 1.2k 0.8× 419 0.5× 336 1.0× 69 7.9k
John K. Northup United States 42 5.4k 1.1× 2.0k 0.8× 1.3k 0.9× 618 0.8× 464 1.4× 84 7.1k
Bazbek Davletov United Kingdom 44 4.8k 0.9× 2.1k 0.9× 3.4k 2.2× 1.2k 1.5× 428 1.3× 101 7.3k
William N. Green United States 36 3.5k 0.7× 1.5k 0.6× 960 0.6× 426 0.5× 180 0.6× 59 4.4k
Hiroshi Tokumitsu Japan 40 4.5k 0.9× 1.3k 0.6× 795 0.5× 580 0.7× 273 0.9× 117 6.1k
Kendall Blumer United States 47 6.7k 1.3× 1.3k 0.6× 1.5k 1.0× 545 0.7× 525 1.6× 107 8.1k
Vivian Hook United States 44 3.4k 0.7× 1.9k 0.8× 1.2k 0.8× 1.5k 2.0× 255 0.8× 193 6.1k
Walter Blackstock United Kingdom 28 3.4k 0.7× 1.2k 0.5× 852 0.6× 838 1.1× 290 0.9× 52 5.0k
Jonathan C. Trinidad United States 37 4.0k 0.8× 1.0k 0.4× 825 0.5× 595 0.8× 250 0.8× 85 5.3k

Countries citing papers authored by Dieter Langosch

Since Specialization
Citations

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

Fields of papers citing papers by Dieter Langosch

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Dieter Langosch

This figure shows the co-authorship network connecting the top 25 collaborators of Dieter Langosch. A scholar is included among the top collaborators of Dieter Langosch 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 Dieter Langosch. Dieter Langosch 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.
Kamp, Frits, Gabriele Basset, Claudia Abou‐Ajram, et al.. (2025). Charting γ-secretase substrates by explainable AI. Nature Communications. 16(1). 5428–5428. 2 indexed citations
2.
Spitz, Charlotte, Christine Schlosser, Walter Stelzer, et al.. (2020). Non-canonical Shedding of TNFα by SPPL2a Is Determined by the Conformational Flexibility of Its Transmembrane Helix. iScience. 23(12). 101775–101775. 16 indexed citations
3.
Agam, Ganesh, et al.. (2020). Determining the Stoichiometry of Small Protein Oligomers Using Steady-State Fluorescence Anisotropy. Biophysical Journal. 119(1). 99–114. 13 indexed citations
4.
5.
Götz, Alexander, Maximilian C. C. J. C. Ebert, Walter Stelzer, et al.. (2018). Glycine Perturbs Local and Global Conformational Flexibility of a Transmembrane Helix. Biochemistry. 57(8). 1326–1337. 41 indexed citations
6.
Scharnagl, Christina, et al.. (2014). Side-Chain to Main-Chain Hydrogen Bonding Controls the Intrinsic Backbone Dynamics of the Amyloid Precursor Protein Transmembrane Helix. Biophysical Journal. 106(6). 1318–1326. 28 indexed citations
7.
Stelzer, Walter, et al.. (2014). Signal peptide peptidase functions in ERAD to cleave the unfolded protein response regulator XBP 1u. The EMBO Journal. 33(21). 2492–2506. 90 indexed citations
8.
Munter, Lisa Marie, Peter W. Hildebrand, Muralidhar Dasari, et al.. (2010). Amyloid beta 42 peptide (Aβ42)-lowering compounds directly bind to Aβ and interfere with amyloid precursor protein (APP) transmembrane dimerization. Proceedings of the National Academy of Sciences. 107(33). 14597–14602. 91 indexed citations
9.
Poschner, Bernhard C., et al.. (2009). Structural features of fusogenic model transmembrane domains that differentially regulate inner and outer leaflet mixing in membrane fusion. Molecular Membrane Biology. 27(1). 1–10. 19 indexed citations
10.
Langosch, Dieter & Isaiah T. Arkin. (2009). Interaction and conformational dynamics of membrane‐spanning protein helices. Protein Science. 18(7). 1343–1358. 96 indexed citations
11.
Poschner, Bernhard C., et al.. (2009). Sequence-Specific Conformational Dynamics of Model Transmembrane Domains Determines Their Membrane Fusogenic Function. Journal of Molecular Biology. 386(3). 733–741. 29 indexed citations
12.
Poschner, Bernhard C. & Dieter Langosch. (2009). Stabilization of conformationally dynamic helices by covalently attached acyl chains. Protein Science. 18(8). 1801–1805. 12 indexed citations
13.
Stelzer, Walter, et al.. (2008). Sequence-Specific Conformational Flexibility of SNARE Transmembrane Helices Probed by Hydrogen/Deuterium Exchange. Biophysical Journal. 95(3). 1326–1335. 46 indexed citations
14.
Fuchs, Angelika, et al.. (2008). Complex Patterns of Histidine, Hydroxylated Amino Acids and the GxxxG Motif Mediate High-affinity Transmembrane Domain Interactions. Journal of Molecular Biology. 385(3). 912–923. 26 indexed citations
15.
Munter, Lisa Marie, Philipp Voigt, Anja Harmeier, et al.. (2007). GxxxG motifs within the amyloid precursor protein transmembrane sequence are critical for the etiology of Aβ42. The EMBO Journal. 26(6). 1702–1712. 240 indexed citations
16.
Mascia, Laura & Dieter Langosch. (2006). Evidence that late-endosomal SNARE multimerization complex is promoted by transmembrane segments. Biochimica et Biophysica Acta (BBA) - Biomembranes. 1768(3). 457–466. 8 indexed citations
17.
Sengupta, Durba, Lars Meinhold, Dieter Langosch, G. Matthias Ullmann, & Jeremy C. Smith. (2005). Understanding the energetics of helical peptide orientation in membranes. Proteins Structure Function and Bioinformatics. 58(4). 913–922. 36 indexed citations
18.
Langosch, Dieter, et al.. (2002). In Vitro Selection of Self‐Interacting Transmembrane Segments‐‐Membrane Proteins Approached from a Different Perspective. IUBMB Life. 54(3). 109–113. 14 indexed citations
19.
Betz, Heinrich, et al.. (1995). Baculovirus‐driven expression and purification of glycine receptor α1 homo‐oligomers. FEBS Letters. 368(3). 495–499. 10 indexed citations
20.
Laube, Bodo, Dieter Langosch, Heinrich Betz, & Volker Schmieden. (1995). Hyperekplexia mutations of the glycine receptor unmask the inhibitory subsite for β-amino-acids. Neuroreport. 6(6). 897–900. 33 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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