Robert T. Sauer

39.5k total citations · 5 hit papers
366 papers, 31.4k citations indexed

About

Robert T. Sauer is a scholar working on Molecular Biology, Genetics and Materials Chemistry. According to data from OpenAlex, Robert T. Sauer has authored 366 papers receiving a total of 31.4k indexed citations (citations by other indexed papers that have themselves been cited), including 315 papers in Molecular Biology, 139 papers in Genetics and 77 papers in Materials Chemistry. Recurrent topics in Robert T. Sauer's work include Bacterial Genetics and Biotechnology (133 papers), RNA and protein synthesis mechanisms (119 papers) and Protein Structure and Dynamics (96 papers). Robert T. Sauer is often cited by papers focused on Bacterial Genetics and Biotechnology (133 papers), RNA and protein synthesis mechanisms (119 papers) and Protein Structure and Dynamics (96 papers). Robert T. Sauer collaborates with scholars based in United States, Netherlands and Germany. Robert T. Sauer's co-authors include Tania A. Baker, Carl O. Pabo, Wendell A. Lim, Kenneth C. Keiler, P R Waller, James U. Bowie, Eric Roche, Andreas Martin, Igor Levchenko and Dawn A. Parsell and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

Robert T. Sauer

363 papers receiving 30.6k citations

Hit Papers

PROTEIN-DNA RECOGNITION 1984 2026 1998 2012 1984 1992 1996 1998 2011 400 800 1.2k

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Robert T. Sauer United States 97 26.6k 10.3k 5.7k 4.4k 3.4k 366 31.4k
Thomas C. Terwilliger United States 65 39.5k 1.5× 6.9k 0.7× 11.2k 2.0× 3.2k 0.7× 4.4k 1.3× 215 53.2k
Nigel W. Moriarty United States 35 26.8k 1.0× 4.4k 0.4× 7.8k 1.4× 2.0k 0.5× 3.1k 0.9× 77 37.9k
Jeffrey J. Headd United States 17 28.2k 1.1× 4.5k 0.4× 7.4k 1.3× 2.1k 0.5× 3.2k 0.9× 20 39.1k
Gary J. Kapral United States 11 25.5k 1.0× 4.1k 0.4× 6.3k 1.1× 1.9k 0.4× 3.0k 0.9× 12 35.1k
F. William Studier United States 60 26.8k 1.0× 11.7k 1.1× 2.8k 0.5× 8.2k 1.9× 2.1k 0.6× 98 36.5k
Pavel V. Afonine United States 43 24.5k 0.9× 4.0k 0.4× 7.4k 1.3× 2.0k 0.5× 3.0k 0.9× 104 34.0k
Vincent B. Chen United States 16 25.3k 1.0× 4.0k 0.4× 6.3k 1.1× 1.9k 0.4× 3.0k 0.9× 22 35.1k
Thomas A. Steitz United States 109 35.0k 1.3× 9.3k 0.9× 4.0k 0.7× 3.9k 0.9× 1.1k 0.3× 274 40.0k
Li‐Wei Hung United States 30 21.2k 0.8× 3.6k 0.3× 5.5k 1.0× 1.6k 0.4× 2.5k 0.7× 68 29.4k
Zbyszek Otwinowski United States 40 27.2k 1.0× 5.5k 0.5× 10.4k 1.8× 1.5k 0.3× 3.6k 1.0× 109 43.4k

Countries citing papers authored by Robert T. Sauer

Since Specialization
Citations

This map shows the geographic impact of Robert T. Sauer'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 T. Sauer with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Robert T. Sauer more than expected).

Fields of papers citing papers by Robert T. Sauer

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Robert T. Sauer

This figure shows the co-authorship network connecting the top 25 collaborators of Robert T. Sauer. A scholar is included among the top collaborators of Robert T. Sauer 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 T. Sauer. Robert T. Sauer 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.
Shih, T. Shane, Robert T. Sauer, & Tania A. Baker. (2024). How the double-ring ClpAP protease motor grips the substrate to unfold and degrade stable proteins. Journal of Biological Chemistry. 300(11). 107861–107861.
2.
Ghanbarpour, Alireza, Fei X, Tristan A. Bell, et al.. (2023). A closed translocation channel in the substrate-free AAA+ ClpXP protease diminishes rogue degradation. Nature Communications. 14(1). 7281–7281. 11 indexed citations
3.
Ghanbarpour, Alireza, Fei X, Tania A. Baker, Joseph H. Davis, & Robert T. Sauer. (2023). The SspB adaptor drives structural changes in the AAA+ ClpXP protease during ssrA-tagged substrate delivery. Proceedings of the National Academy of Sciences. 120(6). e2219044120–e2219044120. 8 indexed citations
4.
Saunders, Reuben A., Benjamin M. Stinson, Tania A. Baker, & Robert T. Sauer. (2020). Multistep substrate binding and engagement by the AAA+ ClpXP protease. Proceedings of the National Academy of Sciences. 117(45). 28005–28013. 16 indexed citations
5.
Cárcamo‐Oyarce, Gerardo, Robert A. Grant, Jia Jia Zhang, et al.. (2020). ClpP1P2 peptidase activity promotes biofilm formation in Pseudomonas aeruginosa. Molecular Microbiology. 115(6). 1094–1109. 22 indexed citations
6.
Kim, Sora, et al.. (2020). ClpAP proteolysis does not require rotation of the ClpA unfoldase relative to ClpP. eLife. 9. 10 indexed citations
7.
Xue, Fei, et al.. (2020). Structural basis of ClpXP recognition and unfolding of ssrA-tagged substrates. eLife. 9. 51 indexed citations
8.
Kim, Seokhee & Robert T. Sauer. (2014). Distinct regulatory mechanisms balance DegP proteolysis to maintain cellular fitness during heat stress. Genes & Development. 28(8). 902–911. 25 indexed citations
9.
Lima, Santiago, Monica S. Guo, Rachna Chaba, Carol A. Gross, & Robert T. Sauer. (2013). Dual Molecular Signals Mediate the Bacterial Response to Outer-Membrane Stress. Science. 340(6134). 837–841. 139 indexed citations
10.
Schmitz, Karl R., et al.. (2013). Antibacterial Activity of and Resistance to Small Molecule Inhibitors of the ClpP Peptidase. DSpace@MIT (Massachusetts Institute of Technology). 1 indexed citations
11.
Mauldin, Randall V. & Robert T. Sauer. (2012). Allosteric regulation of DegS protease subunits though a shared energy landscape. Europe PMC (PubMed Central). 32 indexed citations
12.
Barthelme, Dominik & Robert T. Sauer. (2012). Identification of the Cdc48•20 S Proteasome as an Ancient AAA+ Proteolytic Machine. Science. 337(6096). 843–846. 94 indexed citations
13.
Chaba, Rachna, Benjamin M. Alba, Monica S. Guo, et al.. (2011). Signal integration by DegS and RseB governs the σ E -mediated envelope stress response in Escherichia coli. Proceedings of the National Academy of Sciences. 108(5). 2106–2111. 54 indexed citations
14.
Cezairliyan, Brent O. & Robert T. Sauer. (2007). Inhibition of regulated proteolysis by RseB. Proceedings of the National Academy of Sciences. 104(10). 3771–3776. 57 indexed citations
15.
Chien, Peter, Robert A. Grant, Robert T. Sauer, & Tania A. Baker. (2007). Structure and Substrate Specificity of an SspB Ortholog: Design Implications for AAA+ Adaptors. Structure. 15(10). 1296–1305. 17 indexed citations
16.
Kenniston, Jon, Tania A. Baker, & Robert T. Sauer. (2005). Partitioning between unfolding and release of native domains during ClpXP degradation determines substrate selectivity and partial processing. Proceedings of the National Academy of Sciences. 102(5). 1390–1395. 89 indexed citations
17.
Bolon, Daniel N., Robert A. Grant, Tania A. Baker, & Robert T. Sauer. (2005). Specificity versus stability in computational protein design. Proceedings of the National Academy of Sciences. 102(36). 12724–12729. 116 indexed citations
18.
Milla, Marcos E. & Robert T. Sauer. (1995). Critical side-chain interactions at a subunit interface in the Arc repressor dimer. Biochemistry. 34(10). 3344–3351. 35 indexed citations
19.
Burgering, Maurits J. M., Rolf Boelens, Dara E. Gilbert, et al.. (1994). Solution Structure of Dimeric Mnt Repressor (1-76). Biochemistry. 33(50). 15036–15045. 54 indexed citations
20.
Gussin, Gary N., Alexander D. Johnson, Carl O. Pabo, & Robert T. Sauer. (1983). Repressor and Cro Protein: Structure, Function, and Role in Lysogenization. Cold Spring Harbor Monograph Archive. 13. 93–121. 73 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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