Lothar Esser

5.6k total citations · 1 hit paper
77 papers, 4.4k citations indexed

About

Lothar Esser is a scholar working on Molecular Biology, Organic Chemistry and Inorganic Chemistry. According to data from OpenAlex, Lothar Esser has authored 77 papers receiving a total of 4.4k indexed citations (citations by other indexed papers that have themselves been cited), including 33 papers in Molecular Biology, 27 papers in Organic Chemistry and 18 papers in Inorganic Chemistry. Recurrent topics in Lothar Esser's work include Photosynthetic Processes and Mechanisms (19 papers), Organometallic Complex Synthesis and Catalysis (12 papers) and Synthesis and characterization of novel inorganic/organometallic compounds (8 papers). Lothar Esser is often cited by papers focused on Photosynthetic Processes and Mechanisms (19 papers), Organometallic Complex Synthesis and Catalysis (12 papers) and Synthesis and characterization of novel inorganic/organometallic compounds (8 papers). Lothar Esser collaborates with scholars based in United States, Germany and China. Lothar Esser's co-authors include Di Xia, Herbert Schumann, Juliane A. Meese‐Marktscheffel, Chang‐An Yu, Linda Yu, J. Deisenhofer, Dick Van der Helm, Barbara Smith, Ranjan Chakraborty and Patrick G. Harran and has published in prestigious journals such as Science, Chemical Reviews and Proceedings of the National Academy of Sciences.

In The Last Decade

Lothar Esser

76 papers receiving 4.3k citations

Hit Papers

Synthesis, Structure, and... 1995 2026 2005 2015 1995 200 400 600

Author Peers

Peers are selected by citation overlap in the author's most active subfields. citations · hero ref

Author Last Decade Papers Cites
Lothar Esser 2.2k 1.4k 805 626 565 77 4.4k
Antonio Romero 3.1k 1.5× 1.2k 0.9× 505 0.6× 338 0.5× 520 0.9× 151 5.8k
Gregory D. Van Duyne 4.6k 2.1× 1.8k 1.3× 486 0.6× 995 1.6× 760 1.3× 95 7.2k
Isabel Usón 2.6k 1.2× 1.8k 1.3× 1.3k 1.6× 408 0.7× 1.6k 2.8× 204 5.7k
J.B. Bonanno 2.5k 1.2× 720 0.5× 573 0.7× 344 0.5× 616 1.1× 81 4.5k
P. John Hart 2.9k 1.4× 636 0.5× 406 0.5× 186 0.3× 473 0.8× 115 6.3k
Michail N. Isupov 3.7k 1.7× 402 0.3× 375 0.5× 466 0.7× 1.3k 2.4× 116 5.2k
Derek T. Logan 3.0k 1.4× 288 0.2× 909 1.1× 315 0.5× 737 1.3× 119 4.8k
Santosh Panjikar 2.8k 1.3× 649 0.5× 296 0.4× 510 0.8× 1.0k 1.8× 151 4.6k
Owen Johnson 1.8k 0.8× 584 0.4× 579 0.7× 307 0.5× 863 1.5× 6 3.3k
Hans E. Parge 2.0k 0.9× 432 0.3× 468 0.6× 265 0.4× 277 0.5× 44 3.7k

Countries citing papers authored by Lothar Esser

Since Specialization
Citations

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

Fields of papers citing papers by Lothar Esser

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Lothar Esser

This figure shows the co-authorship network connecting the top 25 collaborators of Lothar Esser. A scholar is included among the top collaborators of Lothar Esser 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 Esser. Lothar Esser 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.
Xia, Di, Fei Zhou, Lothar Esser, & Zhaohai Qin. (2023). Exploiting structural variations in highly conserved mitochondrial complex III to develop antifungal agents. Biophysical Journal. 122(3). 241a–241a.
2.
Lin, Dong, Nathan Watson, Lothar Esser, et al.. (2023). Structures of Cancer Antigen Mesothelin and Its Complexes with Therapeutic Antibodies. Cancer Research Communications. 3(2). 175–191. 15 indexed citations
3.
Esser, Lothar, Fei Zhou, Yihui Zhou, et al.. (2016). Hydrogen Bonding to the Substrate Is Not Required for Rieske Iron-Sulfur Protein Docking to the Quinol Oxidation Site of Complex III. Journal of Biological Chemistry. 291(48). 25019–25031. 20 indexed citations
4.
Esser, Lothar, Fei Zhou, Kristen M. Pluchino, et al.. (2016). Structures of the Multidrug Transporter P-glycoprotein Reveal Asymmetric ATP Binding and the Mechanism of Polyspecificity. Journal of Biological Chemistry. 292(2). 446–461. 145 indexed citations
5.
Xia, Di, Lothar Esser, Wai‐Kwan Tang, et al.. (2012). Structural analysis of cytochrome bc1 complexes: Implications to the mechanism of function. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1827(11-12). 1278–1294. 139 indexed citations
6.
Xia, Di, Lothar Esser, Wai‐Kwan Tang, et al.. (2012). Redox Coupled Conformational Changes in Cytochrome BC1 Complex: Implication to the Bifurcated Electron Transfer at the Quinol Oxidation Site. Biophysical Journal. 102(3). 3a–3a. 1 indexed citations
7.
Bao, Rui, et al.. (2012). Crystallization and preliminary X-ray diffraction analysis of PsaA, the adhesive pilin subunit that forms the pH 6 antigen on the surface ofYersinia pestis. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 68(10). 1243–1246. 1 indexed citations
8.
Su, Ting, Lothar Esser, Di Xia, Chang‐An Yu, & Linda Yu. (2011). Generation, characterization and crystallization of a cytochrome c1-subunit IV fused cytochrome bc1 complex from Rhodobacter sphaeroides. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1817(2). 298–305. 6 indexed citations
9.
Yu, Chang‐An, et al.. (2008). Domain conformational switch of the iron–sulfur protein in cytochrome bc1 complex is induced by the electron transfer from cytochrome bL to bH. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1777(7-8). 1038–1043. 19 indexed citations
10.
Esser, Lothar, Maria Elberry, Fei Zhou, et al.. (2007). Inhibitor-complexed Structures of the Cytochrome bc1 from the Photosynthetic Bacterium Rhodobacter sphaeroides. Journal of Biological Chemistry. 283(5). 2846–2857. 112 indexed citations
11.
Elberry, Maria, et al.. (2006). Generation, characterization and crystallization of a highly active and stable cytochrome bc1 complex mutant from Rhodobacter sphaeroides. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1757(7). 835–840. 14 indexed citations
12.
Li, Yongfu, Orsolya Polgár, Masaki Okada, et al.. (2006). Towards understanding the mechanism of action of the multidrug resistance-linked half-ABC transporter ABCG2: A molecular modeling study. Journal of Molecular Graphics and Modelling. 25(6). 837–851. 36 indexed citations
13.
Poole, S., et al.. (2006). Crystallization and preliminary X-ray diffraction analysis of CfaE, the adhesive subunit of the CFA/I fimbriae from human enterotoxigenicEscherichia coli. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 62(2). 121–124. 14 indexed citations
14.
Ferguson, Andrew D., Ranjan Chakraborty, Barbara Smith, et al.. (2002). Structural Basis of Gating by the Outer Membrane Transporter FecA. Science. 295(5560). 1715–1719. 287 indexed citations
15.
Guo, Fusheng, Michael R. Maurizi, Lothar Esser, & Di Xia. (2002). Crystal Structure of ClpA, an Hsp100 Chaperone and Regulator of ClpAP Protease. Journal of Biological Chemistry. 277(48). 46743–46752. 171 indexed citations
16.
Li, Jing, et al.. (2001). Total Synthesis of Nominal Diazonamides-Part 1: Convergent Preparation of the Structure Proposed for (−)-Diazonamide A. Angewandte Chemie International Edition. 40(24). 4765–4769. 130 indexed citations
17.
Li, Jing, Anthony W. G. Burgett, Lothar Esser, Carlos Amezcua, & Patrick G. Harran. (2001). Total Synthesis of Nominal Diazonamides-Part 2: On the True Structure and Origin of Natural Isolates. Angewandte Chemie International Edition. 40(24). 4770–4773. 160 indexed citations
18.
Wu, Yusheng, Lothar Esser, & Jef K. De Brabander. (2000). Revision of the Absolute Configuration of Salicylihalamide A through Asymmetric Total Synthesis. Angewandte Chemie International Edition. 39(23). 4308–4310. 61 indexed citations
19.
Deisenhofer, J., Susan K. Buchanan, Barbara Smith, et al.. (1999). Crystal structure of the outer membrane active transporter FepA from Escherichia coli.. Nature Structural Biology. 6(1). 56–63. 473 indexed citations
20.
Wang, Chyung‐Ru, et al.. (1997). Identification, expression, and crystallization of the protease‐resistant conserved domain of synapsin I. Protein Science. 6(10). 2264–2267. 8 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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