Susan Marqusee

10.6k total citations · 2 hit papers
128 papers, 8.3k citations indexed

About

Susan Marqusee is a scholar working on Molecular Biology, Materials Chemistry and Atomic and Molecular Physics, and Optics. According to data from OpenAlex, Susan Marqusee has authored 128 papers receiving a total of 8.3k indexed citations (citations by other indexed papers that have themselves been cited), including 118 papers in Molecular Biology, 44 papers in Materials Chemistry and 21 papers in Atomic and Molecular Physics, and Optics. Recurrent topics in Susan Marqusee's work include Protein Structure and Dynamics (74 papers), Enzyme Structure and Function (43 papers) and RNA and protein synthesis mechanisms (40 papers). Susan Marqusee is often cited by papers focused on Protein Structure and Dynamics (74 papers), Enzyme Structure and Function (43 papers) and RNA and protein synthesis mechanisms (40 papers). Susan Marqusee collaborates with scholars based in United States, Russia and Italy. Susan Marqusee's co-authors include Robert L. Baldwin, Carlos Bustamante, Chiwook Park, Elizabeth A. Shank, Ciro Cecconi, Aaron K. Chamberlain, Julie Hollien, Eric R. Goedken, Tracy M. Handel and James L. Keck and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

Susan Marqusee

125 papers receiving 8.2k citations

Hit Papers

2 papers align trajectories

What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

Helix stabilization by Glu-...Lys+ salt bridges in short peptides of de novo design.

1987 816 citations Susan Marqusee et al. Proceedings of the National Academy of Sciences profile →
Unusually stable helix formation in short alanine-based peptides.

1989 667 citations Susan Marqusee et al. Proceedings of the National Academy of Sciences profile →

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Susan Marqusee United States	46	7.0k	2.6k	1.3k	1.0k	636	128	8.3k
Zaida Luthey‐Schulten United States	50	8.1k 1.2×	3.0k 1.2×	1.2k 0.9×	786 0.8×	539 0.8×	133	9.6k
Yaakov Levy Israel	47	6.0k 0.8×	1.9k 0.7×	932 0.7×	653 0.6×	527 0.8×	161	7.4k
Dorothee Kern United States	40	8.7k 1.2×	2.9k 1.1×	925 0.7×	1.6k 1.5×	1.1k 1.7×	75	10.5k
Catherine A. Royer United States	49	6.2k 0.9×	2.2k 0.9×	824 0.6×	710 0.7×	935 1.5×	192	8.2k
José M. Sánchez‐Ruiz Spain	49	6.2k 0.9×	2.8k 1.1×	746 0.6×	575 0.6×	752 1.2×	140	7.5k
Gary J. Pielak United States	58	7.7k 1.1×	3.1k 1.2×	859 0.7×	1.1k 1.1×	1.4k 2.3×	209	9.9k
George I. Makhatadze United States	51	8.3k 1.2×	4.1k 1.6×	1.3k 1.0×	1.2k 1.2×	714 1.1×	143	10.3k
Andrea Amadei Italy	39	5.9k 0.8×	1.8k 0.7×	1.9k 1.5×	930 0.9×	792 1.2×	190	8.2k
Hue Sun Chan Canada	56	10.2k 1.5×	5.3k 2.1×	1.5k 1.2×	1.1k 1.0×	738 1.2×	149	11.7k
Víctor Muñoz United States	50	7.8k 1.1×	4.2k 1.6×	1.2k 0.9×	1.1k 1.1×	759 1.2×	111	8.6k

Countries citing papers authored by Susan Marqusee

Since Specialization

Citations

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

Fields of papers citing papers by Susan Marqusee

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Susan Marqusee

This figure shows the co-authorship network connecting the top 25 collaborators of Susan Marqusee. A scholar is included among the top collaborators of Susan Marqusee 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 Susan Marqusee. Susan Marqusee is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

Sort: Min cites: Since: Top N: Style:

20 of 20 papers shown

Kumar, Kaavya Krishna, Haoqing Wang, Chris Habrian, et al.. (2024). Stepwise activation of a metabotropic glutamate receptor. Nature. 629(8013). 951–956. 19 indexed citations

Gupta, Sayan, et al.. (2024). Enabling simultaneous photoluminescence spectroscopy and X-ray footprinting mass spectrometry to study protein conformation and interactions. Analytical Methods. 17(6). 1214–1225.

Hayes, Ryan L., et al.. (2024). Selection pressures on evolution of ribonuclease H explored with rigorous free–energy–based design. Proceedings of the National Academy of Sciences. 121(3). e2312029121–e2312029121. 5 indexed citations

Lawrence, Rosalie, Sophie R. Shoemaker, Smriti Sangwan, et al.. (2023). A helical fulcrum in eIF2B coordinates allosteric regulation of stress signaling. Nature Chemical Biology. 20(4). 422–431. 1 indexed citations

Glasgow, Anum, et al.. (2023). Ligand-specific changes in conformational flexibility mediate long-range allostery in the lac repressor. Nature Communications. 14(1). 1179–1179. 20 indexed citations

Farquhar, Erik R., Rohit Jain, Michael Sullivan, et al.. (2022). An automated liquid jet for fluorescence dosimetry and microsecond radiolytic labeling of proteins. Communications Biology. 5(1). 866–866. 7 indexed citations

Costello, Shawn M., Sophie R. Shoemaker, Annalee W. Nguyen, et al.. (2022). The SARS-CoV-2 spike reversibly samples an open-trimer conformation exposing novel epitopes. Nature Structural & Molecular Biology. 29(3). 229–238. 74 indexed citations

Latorraca, Naomi R., et al.. (2021). Mechanistic basis for ubiquitin modulation of a protein energy landscape. Proceedings of the National Academy of Sciences. 118(12). 7 indexed citations

Chen, Zhijie, Alan Shaw, Hugh D. Wilson, et al.. (2020). Single-molecule diffusometry reveals no catalysis-induced diffusion enhancement of alkaline phosphatase as proposed by FCS experiments. Proceedings of the National Academy of Sciences. 117(35). 21328–21335. 32 indexed citations

10.

Guinn, Emily J., Pengfei Tian, Mia Shin, Robert B. Best, & Susan Marqusee. (2018). A small single-domain protein folds through the same pathway on and off the ribosome. Proceedings of the National Academy of Sciences. 115(48). 12206–12211. 39 indexed citations

11.

Gabizon, Ronen, Christian A.M. Wilson, Kambiz M. Hamadani, et al.. (2015). The heat released during catalytic turnover enhances the diffusion of an enzyme. RePEc: Research Papers in Economics. 2 indexed citations

12.

Jha, Santosh Kumar & Susan Marqusee. (2014). Kinetic evidence for a two-stage mechanism of protein denaturation by guanidinium chloride. Proceedings of the National Academy of Sciences. 111(13). 4856–4861. 80 indexed citations

13.

Hu, Wenbing, Benjamin T. Walters, Zhong-Yuan Kan, et al.. (2013). Stepwise protein folding at near amino acid resolution by hydrogen exchange and mass spectrometry. Proceedings of the National Academy of Sciences. 110(19). 7684–7689. 146 indexed citations

14.

Chodera, John D., et al.. (2012). The molten globule state is unusually deformable under mechanical force. Proceedings of the National Academy of Sciences. 109(10). 3796–3801. 75 indexed citations

15.

Chodera, John D., et al.. (2012). Limitations of Constant-Force-Feedback Experiments. Biophysical Journal. 103(7). 1490–1499. 36 indexed citations

16.

Miller, Katherine H., et al.. (2010). A Hinge Region cis-Proline in Ribonuclease A Acts as a Conformational Gatekeeper for C-Terminal Domain Swapping. Journal of Molecular Biology. 400(3). 567–578. 24 indexed citations

17.

Freedman, Tanya S., Holger Sondermann, Gregory D. Friedland, et al.. (2006). A Ras-induced conformational switch in the Ras activator Son of sevenless. Proceedings of the National Academy of Sciences. 103(45). 16692–16697. 116 indexed citations

18.

Cecconi, Ciro, Elizabeth A. Shank, Carlos Bustamante, & Susan Marqusee. (2005). Direct Observation of the Three-State Folding of a Single Protein Molecule. Science. 309(5743). 2057–2060. 489 indexed citations

19.

Robic, Srebrenka, et al.. (2003). Role of residual structure in the unfolded state of a thermophilic protein. Proceedings of the National Academy of Sciences. 100(20). 11345–11349. 106 indexed citations

20.

Miller, Erik J., Kael F. Fischer, & Susan Marqusee. (2002). Experimental evaluation of topological parameters determining protein-folding rates. Proceedings of the National Academy of Sciences. 99(16). 10359–10363. 65 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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