Lothar Gremer

5.9k total citations · 1 hit paper
83 papers, 4.3k citations indexed

About

Lothar Gremer is a scholar working on Molecular Biology, Physiology and Cell Biology. According to data from OpenAlex, Lothar Gremer has authored 83 papers receiving a total of 4.3k indexed citations (citations by other indexed papers that have themselves been cited), including 58 papers in Molecular Biology, 35 papers in Physiology and 17 papers in Cell Biology. Recurrent topics in Lothar Gremer's work include Alzheimer's disease research and treatments (35 papers), Protein Structure and Dynamics (15 papers) and Protein Kinase Regulation and GTPase Signaling (14 papers). Lothar Gremer is often cited by papers focused on Alzheimer's disease research and treatments (35 papers), Protein Structure and Dynamics (15 papers) and Protein Kinase Regulation and GTPase Signaling (14 papers). Lothar Gremer collaborates with scholars based in Germany, United States and Netherlands. Lothar Gremer's co-authors include Ortwin Meyer, Holger Dobbek, Robert Huber, Dieter Willbold, Wolfgang Hoyer, Henrike Heise, Gunnar F. Schröder, Mohammad Reza Ahmadian, Vitali Svetlitchnyi and Raimond B. G. Ravelli 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

Lothar Gremer

82 papers receiving 4.3k citations

Hit Papers

Fibril structure of amyloid-β(1–42) by cryo–electron micr... 2017 2026 2020 2023 2017 250 500 750

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Lothar Gremer Germany 32 2.6k 1.4k 797 512 511 83 4.3k
Cláudio M. Gomes Portugal 39 2.9k 1.1× 809 0.6× 467 0.6× 494 1.0× 600 1.2× 156 4.9k
S.S. Hasnain United Kingdom 41 2.6k 1.0× 429 0.3× 599 0.8× 1.1k 2.2× 293 0.6× 181 5.6k
S.V. Antonyuk United Kingdom 36 2.0k 0.8× 451 0.3× 431 0.5× 825 1.6× 240 0.5× 106 4.3k
Richard W. Strange United Kingdom 40 2.0k 0.8× 446 0.3× 561 0.7× 1.1k 2.2× 288 0.6× 115 4.6k
Jeffrey N. Agar United States 33 2.3k 0.9× 570 0.4× 1.1k 1.4× 324 0.6× 279 0.5× 73 4.7k
Duilio Cascio United States 21 1.8k 0.7× 828 0.6× 188 0.2× 942 1.8× 307 0.6× 41 3.6k
David N. Silverman United States 50 5.7k 2.2× 487 0.4× 545 0.7× 652 1.3× 640 1.3× 180 7.4k
Lin Jiang United States 30 4.0k 1.6× 1.5k 1.1× 90 0.1× 991 1.9× 278 0.5× 52 5.6k
Raquel L. Lieberman United States 28 1.9k 0.7× 520 0.4× 190 0.2× 545 1.1× 436 0.9× 85 3.2k
Thomas C. Squier United States 39 3.5k 1.4× 565 0.4× 243 0.3× 554 1.1× 774 1.5× 134 5.7k

Countries citing papers authored by Lothar Gremer

Since Specialization
Citations

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

Fields of papers citing papers by Lothar Gremer

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Lothar Gremer

This figure shows the co-authorship network connecting the top 25 collaborators of Lothar Gremer. A scholar is included among the top collaborators of Lothar Gremer 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 Lothar Gremer. Lothar Gremer 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.
Willbold, Dieter, et al.. (2025). Lecanemab Binds to Transgenic Mouse Model‐Derived Amyloid‐β Fibril Structures Resembling Alzheimer's Disease Type I, Type II and Arctic Folds. Neuropathology and Applied Neurobiology. 51(3). e70022–e70022. 2 indexed citations
2.
Woods, Eric, Tim M. Schwarz, Mahander Pratap Singh, et al.. (2025). Mapping the Path to Cryogenic Atom Probe Tomography Analysis of Biomolecules. Microscopy and Microanalysis. 31(4). 1 indexed citations
3.
Stefanski, Anja, Lothar Gremer, Christoph G. W. Gertzen, et al.. (2023). DNA-binding and protein structure of nuclear factors likely acting in genetic information processing in the Paulinella chromatophore. Proceedings of the National Academy of Sciences. 120(27). e2221595120–e2221595120. 1 indexed citations
4.
Becker, Nina I., Benedikt Frieg, Lothar Gremer, et al.. (2023). Atomic Resolution Insights into pH Shift Induced Deprotonation Events in LS-Shaped Aβ(1–42) Amyloid Fibrils. Journal of the American Chemical Society. 145(4). 2161–2169. 10 indexed citations
5.
Gremer, Lothar, Benedikt Frieg, Luisa U. Schäfer, et al.. (2023). Cryo-EM of Aβ fibrils from mouse models find tg-APPArcSwe fibrils resemble those found in patients with sporadic Alzheimer’s disease. Nature Neuroscience. 26(12). 2073–2080. 30 indexed citations
6.
Maity, Debabrata, et al.. (2022). Cucurbit[7]uril Inhibits Islet Amyloid Polypeptide Aggregation by Targeting N Terminus Hot Segments and Attenuates Cytotoxicity. Chemistry - A European Journal. 28(38). e202201698–e202201698. 4 indexed citations
7.
König, Anna, Lothar Gremer, Markus Tusche, et al.. (2021). Structural details of amyloid β oligomers in complex with human prion protein as revealed by solid-state MAS NMR spectroscopy. Journal of Biological Chemistry. 296. 100499–100499. 30 indexed citations
8.
Reiners, Jens, et al.. (2020). TopModel: Template-Based Protein Structure Prediction at Low Sequence Identity Using Top-Down Consensus and Deep Neural Networks. Journal of Chemical Theory and Computation. 16(3). 1953–1967. 36 indexed citations
9.
Maity, Debabrata, Sunil Kumar, Lothar Gremer, et al.. (2020). Sub-stoichiometric inhibition of IAPP aggregation: a peptidomimetic approach to anti-amyloid agents. RSC Chemical Biology. 1(4). 225–232. 20 indexed citations
10.
Gremer, Lothar, et al.. (2020). Clustering of human prion protein and α-synuclein oligomers requires the prion protein N-terminus. Communications Biology. 3(1). 365–365. 22 indexed citations
11.
Gremer, Lothar, Raimond B. G. Ravelli, Dieter Willbold, et al.. (2019). Atomic structure of PI3-kinase SH3 amyloid fibrils by cryo-electron microscopy. Nature Communications. 10(1). 3754–3754. 31 indexed citations
12.
Gremer, Lothar, Elke Reinartz, Anna König, et al.. (2018). A d-enantiomeric peptide interferes with heteroassociation of amyloid-β oligomers and prion protein. Journal of Biological Chemistry. 293(41). 15748–15764. 23 indexed citations
13.
Miti, Tatiana, Carlos J. Pérez-Rivera, Jeremy Barton, et al.. (2018). Origin of metastable oligomers and their effects on amyloid fibril self-assembly. Chemical Science. 9(27). 5937–5948. 80 indexed citations
14.
Gremer, Lothar, C. Schenk, Elke Reinartz, et al.. (2017). Fibril structure of amyloid-β(1–42) by cryo–electron microscopy. Science. 358(6359). 116–119. 802 indexed citations breakdown →
15.
Wördehoff, Michael M., Hamed Shaykhalishahi, Lothar Gremer, et al.. (2017). Opposed Effects of Dityrosine Formation in Soluble and Aggregated α-Synuclein on Fibril Growth. Journal of Molecular Biology. 429(20). 3018–3030. 37 indexed citations
16.
Klein, Antonia, Markus Tusche, Christine Schlosser, et al.. (2016). Competitive Mirror Image Phage Display Derived Peptide Modulates Amyloid Beta Aggregation and Toxicity. PLoS ONE. 11(2). e0147470–e0147470. 13 indexed citations
17.
Stark, Zornitza, Monique M. Ryan, Ion Cristian Cirstea, et al.. (2011). Two novel germline KRAS mutations: expanding the molecular and clinical phenotype. Clinical Genetics. 81(6). 590–594. 23 indexed citations
18.
Gremer, Lothar, Alessandro De Luca, Torsten Merbitz-Zahradnik, et al.. (2009). Duplication of Glu37 in the switch I region of HRAS impairs effector/GAP binding and underlies Costello syndrome by promoting enhanced growth factor-dependent MAPK and AKT activation. Human Molecular Genetics. 19(5). 790–802. 32 indexed citations
19.
Dobbek, Holger, Lothar Gremer, R. Kiefersauer, Robert Huber, & Ortwin Meyer. (2002). Catalysis at a dinuclear [CuSMo(O)OH] cluster in a CO dehydrogenase resolved at 1.1-Å resolution. Proceedings of the National Academy of Sciences. 99(25). 15971–15976. 308 indexed citations
20.
Dobbek, Holger, Vitali Svetlitchnyi, Lothar Gremer, Robert Huber, & Ortwin Meyer. (2001). Crystal Structure of a Carbon Monoxide Dehydrogenase Reveals a [Ni-4Fe-5S] Cluster. Science. 293(5533). 1281–1285. 423 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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