Robert B. Russell

17.4k total citations · 4 hit papers
93 papers, 9.8k citations indexed

About

Robert B. Russell is a scholar working on Molecular Biology, Materials Chemistry and Cell Biology. According to data from OpenAlex, Robert B. Russell has authored 93 papers receiving a total of 9.8k indexed citations (citations by other indexed papers that have themselves been cited), including 77 papers in Molecular Biology, 28 papers in Materials Chemistry and 9 papers in Cell Biology. Recurrent topics in Robert B. Russell's work include Protein Structure and Dynamics (41 papers), Enzyme Structure and Function (28 papers) and Machine Learning in Bioinformatics (20 papers). Robert B. Russell is often cited by papers focused on Protein Structure and Dynamics (41 papers), Enzyme Structure and Function (28 papers) and Machine Learning in Bioinformatics (20 papers). Robert B. Russell collaborates with scholars based in Germany, United Kingdom and United States. Robert B. Russell's co-authors include Alexander Stark, Stephen M. Cohen, Julius Brennecke, Patrick Aloy, Geoffrey J. Barton, David R. Hipfner, Evangelia Petsalaki, Victor Neduva, Natascha Bushati and Chris P. Ponting and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

Robert B. Russell

93 papers receiving 9.5k citations

Hit Papers

bantam Encodes a Developmentally Regulated microRNA that ... 1992 2026 2003 2014 2003 2005 2003 1992 500 1000 1.5k

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Robert B. Russell Germany 43 8.1k 2.3k 1.4k 659 658 93 9.8k
Robert B. Russell Germany 37 6.1k 0.8× 1.6k 0.7× 823 0.6× 868 1.3× 361 0.5× 68 7.7k
Michael J. Thompson United States 33 6.8k 0.8× 444 0.2× 627 0.4× 417 0.6× 682 1.0× 82 8.4k
Julian Gough United Kingdom 37 7.3k 0.9× 549 0.2× 945 0.7× 235 0.4× 1.5k 2.3× 73 9.4k
Titia K. Sixma Netherlands 61 13.1k 1.6× 718 0.3× 555 0.4× 258 0.4× 1.4k 2.1× 126 15.0k
M. Madan Babu United Kingdom 57 11.9k 1.5× 379 0.2× 1.2k 0.8× 587 0.9× 1.4k 2.1× 133 14.0k
Philip M. Kim Canada 40 6.3k 0.8× 321 0.1× 687 0.5× 641 1.0× 872 1.3× 94 7.6k
John F. McDonald United States 53 4.9k 0.6× 1.0k 0.5× 424 0.3× 140 0.2× 843 1.3× 190 9.2k
James Cuff United States 9 6.5k 0.8× 484 0.2× 463 0.3× 209 0.3× 1.1k 1.6× 12 7.8k
Ashley M. Buckle Australia 43 4.1k 0.5× 497 0.2× 1.1k 0.8× 160 0.2× 773 1.2× 156 7.2k
Manuela Helmer‐Citterich Italy 34 3.9k 0.5× 691 0.3× 489 0.3× 476 0.7× 382 0.6× 118 4.8k

Countries citing papers authored by Robert B. Russell

Since Specialization
Citations

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

Fields of papers citing papers by Robert B. Russell

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Robert B. Russell

This figure shows the co-authorship network connecting the top 25 collaborators of Robert B. Russell. A scholar is included among the top collaborators of Robert B. Russell 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 B. Russell. Robert B. Russell 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.
Beyer, Tina, Gaurav D. Diwan, Franziska Klose, et al.. (2025). Ciliopathy-Associated Missense Mutations in IFT140 are Tolerated by the Inherent Resilience of the IFT Machinery. Molecular & Cellular Proteomics. 24(3). 100916–100916. 1 indexed citations
2.
Marchi, Fabiola De, Jasna Križ, Jean‐Pierre Julien, et al.. (2023). Emerging Trends in the Field of Inflammation and Proteinopathy in ALS/FTD Spectrum Disorder. Biomedicines. 11(6). 1599–1599. 17 indexed citations
3.
Beyer, Tina, Emma Peskett, Georg Otto, et al.. (2023). De-Suppression of Mesenchymal Cell Identities and Variable Phenotypic Outcomes Associated with Knockout of Bbs1. Cells. 12(22). 2662–2662. 1 indexed citations
4.
Petriman, Narcis-Adrian, Marta Loureiro, Michael Täschner, et al.. (2022). Biochemically validated structural model of the 15‐subunit intraflagellar transport complex IFT‐B. The EMBO Journal. 41(24). e112440–e112440. 32 indexed citations
6.
Kishore, Asha, Ashwin Ashok Kumar Sreelatha, Marc Sturm, et al.. (2018). Understanding the role of genetic variability in LRRK2 in Indian population. Movement Disorders. 34(4). 496–505. 8 indexed citations
7.
Mazin, Pavel, Mikhail S. Gelfand, Andrey A. Mironov, et al.. (2010). An automated stochastic approach to the identification of the protein specificity determinants and functional subfamilies. Algorithms for Molecular Biology. 5(1). 29–29. 49 indexed citations
8.
Kalinina, Olga V., Robert B. Russell, A. B. Rakhmaninova, & Mikhail S. Gelfand. (2007). Computational method for predicting protein functional sites with the use of specificity determinants. Molecular Biology. 41(1). 137–147. 7 indexed citations
9.
Shah, Parantu K., Patrick Aloy, Peer Bork, & Robert B. Russell. (2005). Structural similarity to bridge sequence space: Finding new families on the bridges. Protein Science. 14(5). 1305–1314. 10 indexed citations
10.
Linding, Rune, Alexander Stark, Federico De Masi, et al.. (2005). Systematic Discovery of New Recognition Peptides Mediating Protein Interaction. 13 indexed citations
11.
Copley, Richard R., Patrick Aloy, Robert B. Russell, & Maximilian J. Telford. (2004). Systematic searches for molecular synapomorphies in model metazoan genomes give some support for Ecdysozoa after accounting for the idiosyncrasies of Caenorhabditis elegans. Evolution & Development. 6(3). 164–169. 45 indexed citations
12.
Aloy, Patrick & Robert B. Russell. (2003). Understanding and predicting protein assemblies with 3D structures. Comparative and Functional Genomics. 4(4). 410–415. 7 indexed citations
13.
Aloy, Patrick, Francesca D. Ciccarelli, Christina Leutwein, et al.. (2002). A complex prediction: three‐dimensional model of the yeast exosome. EMBO Reports. 3(7). 628–635. 80 indexed citations
14.
Katso, Roy, Robert B. Russell, & Trivadi S. Ganesan. (1999). Functional Analysis of H-Ryk, an Atypical Member of the Receptor Tyrosine Kinase Family. Molecular and Cellular Biology. 19(9). 6427–6440. 64 indexed citations
15.
Russell, Robert B. & Michael J.E. Sternberg. (1997). Two new examples of protein structural similarities within the structure-function twilight zone. Protein Engineering Design and Selection. 10(4). 333–338. 23 indexed citations
16.
Russell, Robert B., Richard R. Copley, & Geoffrey J. Barton. (1996). Protein Fold Recognition by Mapping Predicted Secondary Structures. Journal of Molecular Biology. 259(3). 349–365. 99 indexed citations
17.
Russell, Robert B. & Michael J.E. Sternberg. (1995). Structure Prediction: How good are we?. Current Biology. 5(5). 488–490. 17 indexed citations
18.
Russell, Robert B.. (1994). Domain insertion. Protein Engineering Design and Selection. 7(12). 1407–1410. 42 indexed citations
19.
Russell, Robert B., J. Breed, & Geoffrey J. Barton. (1992). Conservation analysis and structure prediction of the SH2 family of phosphotyrosine binding domains. FEBS Letters. 304(1). 15–20. 82 indexed citations
20.
Barton, Geoffrey J., et al.. (1992). Generation and interpretation of protein sequence and structural multiple alignments. Journal of Protein Chemistry. 11(4). 389–389. 1 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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