Robert Huber

81.9k total citations · 29 hit papers
600 papers, 66.7k citations indexed

About

Robert Huber is a scholar working on Molecular Biology, Materials Chemistry and Oncology. According to data from OpenAlex, Robert Huber has authored 600 papers receiving a total of 66.7k indexed citations (citations by other indexed papers that have themselves been cited), including 473 papers in Molecular Biology, 170 papers in Materials Chemistry and 106 papers in Oncology. Recurrent topics in Robert Huber's work include Enzyme Structure and Function (168 papers), Peptidase Inhibition and Analysis (89 papers) and Protein Structure and Dynamics (75 papers). Robert Huber is often cited by papers focused on Enzyme Structure and Function (168 papers), Peptidase Inhibition and Analysis (89 papers) and Protein Structure and Dynamics (75 papers). Robert Huber collaborates with scholars based in Germany, United States and United Kingdom. Robert Huber's co-authors include Wolfram Bode, Richard A. Engh, J. Deisenhofer, M. Groll, O. Epp, Hartmut Michel, Albrecht Messerschmidt, Kunio Miki, H.D. Bartunik and Matthias Bochtler and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

Robert Huber

598 papers receiving 64.5k citations

Hit Papers

Accurate bond and angle parameters for X-ray protein stru... 1973 2026 1990 2008 1991 1985 1997 1984 1995 500 1000 1.5k 2.0k

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Robert Huber Germany 135 46.8k 11.3k 9.2k 6.8k 6.3k 600 66.7k
Randy J. Read United Kingdom 69 62.2k 1.3× 19.0k 1.7× 6.9k 0.7× 7.9k 1.2× 2.7k 0.4× 197 86.9k
Paul D. Adams United States 78 62.3k 1.3× 17.9k 1.6× 6.2k 0.7× 6.8k 1.0× 1.8k 0.3× 360 86.3k
Ralf W. Grosse‐Kunstleve United States 37 48.2k 1.0× 14.8k 1.3× 5.4k 0.6× 5.8k 0.9× 1.3k 0.2× 65 67.1k
Janet M. Thornton United Kingdom 117 70.9k 1.5× 20.5k 1.8× 4.5k 0.5× 5.2k 0.8× 1.5k 0.2× 488 92.5k
Ruedi Aebersold Switzerland 160 86.7k 1.9× 3.4k 0.3× 9.0k 1.0× 9.8k 1.4× 5.6k 0.9× 783 117.7k
Kevin Cowtan United Kingdom 30 44.2k 0.9× 12.7k 1.1× 5.1k 0.6× 5.3k 0.8× 1.1k 0.2× 63 62.9k
Paul Emsley United Kingdom 23 44.0k 0.9× 12.1k 1.1× 5.5k 0.6× 5.3k 0.8× 1.1k 0.2× 45 61.8k
Airlie J. McCoy United Kingdom 43 43.0k 0.9× 12.2k 1.1× 4.9k 0.5× 6.2k 0.9× 1.2k 0.2× 96 60.1k
Jane S. Richardson United States 57 43.5k 0.9× 12.8k 1.1× 4.4k 0.5× 4.5k 0.7× 840 0.1× 130 59.8k
Kurt Wüthrich Switzerland 130 65.0k 1.4× 16.3k 1.4× 3.7k 0.4× 6.9k 1.0× 962 0.2× 653 83.0k

Countries citing papers authored by Robert Huber

Since Specialization
Citations

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

Fields of papers citing papers by Robert Huber

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Robert Huber

This figure shows the co-authorship network connecting the top 25 collaborators of Robert Huber. A scholar is included among the top collaborators of Robert Huber 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 Robert Huber. Robert Huber 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.
Kari, Vijayalakshmi, Melanie Spitzner, Christof Lenz, et al.. (2022). Dipeptidyl peptidase 9 triggers BRCA2 degradation and promotes DNA damage repair. EMBO Reports. 23(10). e54136–e54136. 20 indexed citations
2.
García‐Pardo, Javier, Peter J. Lyons, Francesc Avilés, et al.. (2018). Crystal structure and mechanism of human carboxypeptidase O: Insights into its specific activity for acidic residues. Proceedings of the National Academy of Sciences. 115(17). E3932–E3939. 16 indexed citations
3.
Gražulis, S., E. Manakova, Manfred Roessle, et al.. (2005). Structure of the metal-independent restriction enzyme BfiI reveals fusion of a specific DNA-binding domain with a nonspecific nuclease. Proceedings of the National Academy of Sciences. 102(44). 15797–15802. 81 indexed citations
4.
Breithaupt, Constanze, Anna Schubart, Hilke Zander, et al.. (2003). Structural insights into the antigenicity of myelin oligodendrocyte glycoprotein. Proceedings of the National Academy of Sciences. 100(16). 9446–9451. 105 indexed citations
5.
Svetlitchnyi, Vitali, Holger Dobbek, Wolfram Meyer‐Klaucke, et al.. (2003). A functional Ni-Ni-[4Fe-4S] cluster in the monomeric acetyl-CoA synthase from Carboxydothermus hydrogenoformans. Proceedings of the National Academy of Sciences. 101(2). 446–451. 203 indexed citations
6.
Fischer, Markus, Kristina Kemter, Richard Feicht, et al.. (2003). Riboflavin synthase of Schizosaccharomyces pombe. Protein dynamics revealed by 19F NMR protein perturbation experiments. BMC Biochemistry. 4(1). 18–18. 16 indexed citations
7.
Macieira, Sofia, Berta M. Martins, & Robert Huber. (2003). Oxygen-dependent coproporphyrinogen-III oxidase fromEscherichia coli: one-step purification and biochemical characterisation. FEMS Microbiology Letters. 226(1). 31–37. 3 indexed citations
8.
Raaijmakers, H.C.A., Sofia Macieira, João M.L. Dias, et al.. (2002). Gene Sequence and the 1.8 Å Crystal Structure of the Tungsten-Containing Formate Dehydrogenase from Desulfovibrio gigas. Structure. 10(9). 1261–1272. 139 indexed citations
9.
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
10.
Gerhardt, S., Ilka Haase, Stefan Steinbacher, et al.. (2002). The Structural Basis of Riboflavin Binding to Schizosaccharomyces pombe 6,7-Dimethyl-8-ribityllumazine Synthase. Journal of Molecular Biology. 318(5). 1317–1329. 61 indexed citations
11.
Cha, Hyunju, Erhard Kopetzki, Robert Huber, Martin Lanzendörfer, & Hans Brandstetter. (2002). Structural Basis of the Adaptive Molecular Recognition by MMP9. Journal of Molecular Biology. 320(5). 1065–1079. 109 indexed citations
12.
Kairies, Norman, Hans‐Georg Beisel, Pablo Fuentes‐Prior, et al.. (2001). The 2.0-Å crystal structure of tachylectin 5A provides evidence for the common origin of the innate immunity and the blood coagulation systems. Proceedings of the National Academy of Sciences. 98(24). 13519–13524. 121 indexed citations
13.
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
14.
Bracher, Andreas, Markus Fischer, Wolfgang Eisenreich, et al.. (1999). Histidine 179 Mutants of GTP Cyclohydrolase I Catalyze the Formation of 2-Amino-5-formylamino-6-ribofuranosylamino-4(3H)-pyrimidinone Triphosphate. Journal of Biological Chemistry. 274(24). 16727–16735. 35 indexed citations
15.
Dick, Tobias P., Alexander K. Nussbaum, Martin Deeg, et al.. (1998). Contribution of Proteasomal β-Subunits to the Cleavage of Peptide Substrates Analyzed with Yeast Mutants. Journal of Biological Chemistry. 273(40). 25637–25646. 209 indexed citations
16.
Laber, Bernd, Tim Clausen, Robert Huber, et al.. (1996). Cloning, purification, and crystallization of Escherichia coli cystathionine β‐lyase. FEBS Letters. 379(1). 94–96. 12 indexed citations
17.
Romero, Antonio, Herbert Nar, Robert Huber, et al.. (1994). Crystal structure analysis and refinement at 2·15Å resolution of amicyanin, a type I blue copper protein, from Thiobacillus versutus. Journal of Molecular Biology. 236(4). 1196–1211. 59 indexed citations
18.
Bürger, Alexander, Dieter Voges, Pascal Demange, et al.. (1994). Structural and Electrophysiological Analysis of Annexin V Mutants. Journal of Molecular Biology. 237(4). 479–499. 46 indexed citations
19.
Voges, Dieter, Robert Berendes, Alexander Bürger, et al.. (1994). Three-dimensional Structure of Membrane-bound Annexin V. Journal of Molecular Biology. 238(2). 199–213. 150 indexed citations
20.
Padmanabhan, K., A. Tulinsky, Chang H. Park, et al.. (1993). Structure of Human Des(1-45) Factor Xa at 2·2 Å Resolution. Journal of Molecular Biology. 232(3). 947–966. 350 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.

You can learn more about the impact of Robert Huber by visiting their Pantheon page.

Explore authors with similar magnitude of impact

Rankless by CCL
2026