Ariel Lustig

7.6k total citations
110 papers, 6.3k citations indexed

About

Ariel Lustig is a scholar working on Molecular Biology, Cell Biology and Materials Chemistry. According to data from OpenAlex, Ariel Lustig has authored 110 papers receiving a total of 6.3k indexed citations (citations by other indexed papers that have themselves been cited), including 87 papers in Molecular Biology, 23 papers in Cell Biology and 17 papers in Materials Chemistry. Recurrent topics in Ariel Lustig's work include Protein Structure and Dynamics (18 papers), Enzyme Structure and Function (16 papers) and Bacteriophages and microbial interactions (15 papers). Ariel Lustig is often cited by papers focused on Protein Structure and Dynamics (18 papers), Enzyme Structure and Function (16 papers) and Bacteriophages and microbial interactions (15 papers). Ariel Lustig collaborates with scholars based in Switzerland, Germany and United States. Ariel Lustig's co-authors include Jürgen Engel, Richard A. Kammerer, Ueli Aebi, Peter Burkhard, Therese Schulthess, Ruth Landwehr, Andreas Engel, A. Joseph Kalb, Min Li and Andrea Mattevi and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Nucleic Acids Research and Journal of Biological Chemistry.

In The Last Decade

Ariel Lustig

109 papers receiving 6.1k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Ariel Lustig Switzerland 48 4.3k 1.5k 717 620 468 110 6.3k
Richard A. Kammerer Switzerland 43 3.5k 0.8× 1.5k 1.0× 419 0.6× 372 0.6× 308 0.7× 101 5.2k
Leonard H. Rome United States 46 6.2k 1.4× 934 0.6× 393 0.5× 401 0.6× 912 1.9× 133 8.9k
Andrey V. Kajava France 49 4.9k 1.1× 1.1k 0.8× 550 0.8× 817 1.3× 494 1.1× 152 7.4k
Timothy R. Dafforn United Kingdom 50 5.0k 1.2× 1.0k 0.7× 566 0.8× 477 0.8× 379 0.8× 152 7.4k
Michael Overduin United Kingdom 43 5.8k 1.3× 2.1k 1.4× 373 0.5× 717 1.2× 620 1.3× 129 7.6k
Walter F. Stafford United States 40 3.9k 0.9× 1.2k 0.8× 584 0.8× 360 0.6× 374 0.8× 114 5.7k
Atsushi Ikai Japan 39 3.4k 0.8× 1.0k 0.7× 759 1.1× 264 0.4× 436 0.9× 219 6.4k
Teni Boulikas United States 36 4.8k 1.1× 666 0.4× 344 0.5× 870 1.4× 519 1.1× 77 7.7k
Jeremy C. Simpson Ireland 41 3.8k 0.9× 1.9k 1.3× 519 0.7× 529 0.9× 717 1.5× 137 6.5k
Charles M. Deber Canada 55 7.5k 1.7× 633 0.4× 478 0.7× 669 1.1× 608 1.3× 218 9.7k

Countries citing papers authored by Ariel Lustig

Since Specialization
Citations

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

Fields of papers citing papers by Ariel Lustig

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Ariel Lustig

This figure shows the co-authorship network connecting the top 25 collaborators of Ariel Lustig. A scholar is included among the top collaborators of Ariel Lustig 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 Ariel Lustig. Ariel Lustig 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.
Kozono, David, Andreas Engel, Kitaru Suda, et al.. (2005). Co-axial Association of Recombinant Eye Lens Aquaporin-0 Observed in Loosely Packed 3D Crystals. Journal of Molecular Biology. 355(4). 605–611. 31 indexed citations
2.
Aivaliotis, Michalis, et al.. (2004). Isolation and Characterization of an Outer Membrane Protein of Chlorobium tepidum. Photosynthesis Research. 79(2). 161–166. 6 indexed citations
3.
Daniel, Ezra, et al.. (2003). On the molecular mass of Lumbricus erythrocruorin. Micron. 35(1-2). 131–132. 5 indexed citations
4.
Sasaki, Takako, et al.. (2002). Functional Studies on Recombinant Domains of Mac-2-binding Protein. Journal of Biological Chemistry. 277(18). 15690–15696. 46 indexed citations
5.
Özbek, Suat, et al.. (2002). Structure/Function Relationships in the Minicollagen ofHydra Nematocysts. Journal of Biological Chemistry. 277(51). 49200–49204. 35 indexed citations
6.
Shneider, Mikhail M., Sergei P. Boudko, Ariel Lustig, & Vadim V. Mesyanzhinov. (2001). Properties of Bacteriophage T4 Baseplate Protein Encoded by Gene 8. Biochemistry (Moscow). 66(6). 693–697. 8 indexed citations
7.
Strelkov, Sergei V., Harald Herrmann, Norbert Geisler, et al.. (2001). Divide-and-conquer crystallographic approach towards an atomic structure of intermediate filaments. Journal of Molecular Biology. 306(4). 773–781. 103 indexed citations
8.
Pegoraro, Stefano, Christine B. Karim, Ariel Lustig, et al.. (2001). Sarcolipin, the Shorter Homologue of Phospholamban, Forms Oligomeric Structures in Detergent Micelles and in Liposomes. Journal of Biological Chemistry. 276(33). 30845–30852. 57 indexed citations
9.
Rosenbusch, J.P., et al.. (2001). Approaches to determining membrane protein structures to high resolution: do selections of subpopulations occur?. Micron. 32(1). 75–90. 25 indexed citations
10.
Sterner, Reinhard, et al.. (2001). Dissection of a (betaalpha)8-barrel enzyme into two folded halves.. Nature Structural Biology. 8(1). 32–36. 122 indexed citations
11.
Burkhard, Peter, Markus Meier, & Ariel Lustig. (2000). Design of a minimal protein oligomerization domain by a structural approach. Protein Science. 9(12). 2294–2301. 84 indexed citations
12.
Herrmann, Harald, Sergei V. Strelkov, Bernhard Feja, et al.. (1999). The intermediate filament protein consensus motif of helix 2B: Atomic structure and contribution to assembly. Molecular Biology of the Cell. 10. 2 indexed citations
13.
Oberholzer, Thomas, et al.. (1999). Enzymatic reactions in liposomes using the detergent-induced liposome loading method. Biochimica et Biophysica Acta (BBA) - Biomembranes. 1416(1-2). 57–68. 33 indexed citations
14.
Tsiotis, Georgios, et al.. (1999). Investigation of the structure of spinach photosystem II reaction center complex. European Journal of Biochemistry. 259(1-2). 320–324. 9 indexed citations
15.
Dekker, Niek, Jan Tommassen, Ariel Lustig, Jürg P. Rosenbusch, & Hubertus M. Verheij. (1997). Dimerization Regulates the Enzymatic Activity of Escherichia coli Outer Membrane Phospholipase A. Journal of Biological Chemistry. 272(6). 3179–3184. 68 indexed citations
16.
Kellenberger, E., et al.. (1996). Mechanism of the long tail-fiber deployment of bacteriophages T-even and its role in adsorption, infection and sedimentation. Biophysical Chemistry. 59(1-2). 41–59. 15 indexed citations
17.
Herrmann, Harald, Markus Häner, Monika Brettel, et al.. (1996). Structure and Assembly Properties of the Intermediate Filament Protein Vimentin: The Role of its Head, Rod and Tail Domains. Journal of Molecular Biology. 264(5). 933–953. 279 indexed citations
18.
Sterner, Reinhard, Gerd R. Kleemann, Halina Szadkowski, et al.. (1996). Phosphoribosyl anthranilate isomerase from Thermotoga maritima is an extremely stable and active homodimer. Protein Science. 5(10). 2000–2008. 69 indexed citations
19.
Benz, Roland, et al.. (1989). Porin fromThiobacillus versutus. FEMS Microbiology Letters. 65(3). 319–322. 3 indexed citations
20.
Yacobi, Avraham, et al.. (1977). Comparative subcutaneous absorption of local anesthetics: lidocaine, procaine and tetracaine.. Library Stack (Library Stack). 225(2). 330–42. 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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