Joseph E. Curtis

3.7k total citations
81 papers, 3.0k citations indexed

About

Joseph E. Curtis is a scholar working on Molecular Biology, Materials Chemistry and Atomic and Molecular Physics, and Optics. According to data from OpenAlex, Joseph E. Curtis has authored 81 papers receiving a total of 3.0k indexed citations (citations by other indexed papers that have themselves been cited), including 58 papers in Molecular Biology, 30 papers in Materials Chemistry and 9 papers in Atomic and Molecular Physics, and Optics. Recurrent topics in Joseph E. Curtis's work include Protein Structure and Dynamics (32 papers), Enzyme Structure and Function (23 papers) and Protein purification and stability (17 papers). Joseph E. Curtis is often cited by papers focused on Protein Structure and Dynamics (32 papers), Enzyme Structure and Function (23 papers) and Protein purification and stability (17 papers). Joseph E. Curtis collaborates with scholars based in United States, United Kingdom and France. Joseph E. Curtis's co-authors include Susan Krueger, Alexei P. Sokolov, Douglas J. Tobias, Hirsh Nanda, Pavel Jungwirth, Joon Ho Roh, Z. Chowdhuri, Roger B. Gregory, V. N. Novikov and Maria Monica Castellanos and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Physical Review Letters.

In The Last Decade

Joseph E. Curtis

79 papers receiving 2.9k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Joseph E. Curtis United States 34 1.9k 745 516 339 324 81 3.0k
Jay R. Knutson United States 32 2.5k 1.3× 485 0.7× 607 1.2× 309 0.9× 390 1.2× 123 4.2k
Péter Závodszky Hungary 34 2.4k 1.3× 1.0k 1.4× 519 1.0× 324 1.0× 292 0.9× 183 5.4k
Yoshinori Satow Japan 31 2.6k 1.4× 1.0k 1.4× 290 0.6× 595 1.8× 176 0.5× 89 4.5k
Jim Warwicker United Kingdom 37 4.1k 2.2× 797 1.1× 515 1.0× 587 1.7× 329 1.0× 125 5.2k
Bernhard Rupp United States 37 2.8k 1.5× 1.5k 2.0× 184 0.4× 243 0.7× 201 0.6× 139 4.7k
James D. Lear United States 48 6.1k 3.2× 848 1.1× 329 0.6× 432 1.3× 687 2.1× 87 7.8k
José L. Neira Spain 38 3.5k 1.9× 1.2k 1.6× 338 0.7× 122 0.4× 365 1.1× 195 4.4k
Alfonso Mondragón United States 37 3.4k 1.8× 411 0.6× 331 0.6× 242 0.7× 120 0.4× 92 4.8k
A. Héroux United States 41 3.3k 1.7× 530 0.7× 171 0.3× 113 0.3× 200 0.6× 90 4.6k

Countries citing papers authored by Joseph E. Curtis

Since Specialization
Citations

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

Fields of papers citing papers by Joseph E. Curtis

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Joseph E. Curtis. 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 Joseph E. Curtis. The network helps show where Joseph E. Curtis may publish in the future.

Co-authorship network of co-authors of Joseph E. Curtis

This figure shows the co-authorship network connecting the top 25 collaborators of Joseph E. Curtis. A scholar is included among the top collaborators of Joseph E. Curtis 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 Joseph E. Curtis. Joseph E. Curtis 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.
Hatch, Harold W., Christina Bergonzo, Marco A. Blanco, et al.. (2024). Anisotropic coarse-grain Monte Carlo simulations of lysozyme, lactoferrin, and NISTmAb by precomputing atomistic models. The Journal of Chemical Physics. 161(9). 3 indexed citations
2.
Chakravarthy, Srinivas, Manas Chakraborty, Marco Tonelli, et al.. (2024). SEC‐SAXS/MC Ensemble Structural Studies of the Microtubule Binding Protein Cdt1 Show Monomeric, Folded‐Over Conformations. Cytoskeleton. 82(6). 372–387. 1 indexed citations
3.
Thelen, Jacob L., Volker S. Urban, Hugh O’Neill, et al.. (2024). Morphological Characterization of Self-Amplifying mRNA Lipid Nanoparticles. ACS Nano. 18(2). 1464–1476. 24 indexed citations
4.
Xu, Amy Y., Marco A. Blanco, Maria Monica Castellanos, et al.. (2023). Role of Domain–Domain Interactions on the Self-Association and Physical Stability of Monoclonal Antibodies: Effect of pH and Salt. The Journal of Physical Chemistry B. 127(39). 8344–8357. 8 indexed citations
5.
Xu, Amy Y., Nicholas Clark, Hyojin Kim, et al.. (2022). Effects of Monovalent Salt on Protein-Protein Interactions of Dilute and Concentrated Monoclonal Antibody Formulations. Antibodies. 11(2). 24–24. 11 indexed citations
6.
Jeong, Cheol, et al.. (2022). Styrene–Maleic Acid Copolymer Nanodiscs to Determine the Shape of Membrane Proteins. The Journal of Physical Chemistry B. 126(5). 1034–1044. 3 indexed citations
7.
8.
Bowerman, Samuel, Joseph E. Curtis, Joseph Clayton, Emre Brookes, & Jeff Wereszczynski. (2019). BEES: Bayesian Ensemble Estimation from SAS. Biophysical Journal. 117(3). 399–407. 8 indexed citations
9.
Blanco, Marco A., Harold W. Hatch, Joseph E. Curtis, & Vincent K. Shen. (2018). A methodology to calculate small-angle scattering profiles of macromolecular solutions from molecular simulations in the grand-canonical ensemble. The Journal of Chemical Physics. 149(8). 84203–84203. 3 indexed citations
10.
Castellanos, Maria Monica, et al.. (2018). Characterization of the NISTmAb Reference Material using small-angle scattering and molecular simulation. Analytical and Bioanalytical Chemistry. 410(8). 2141–2159. 27 indexed citations
11.
Nanda, Hirsh, et al.. (2018). Relaxation dynamics of saturated and unsaturated oriented lipid bilayers. Soft Matter. 14(29). 6119–6127. 15 indexed citations
12.
Blanco, Marco A., Harold W. Hatch, Joseph E. Curtis, & Vincent K. Shen. (2018). Evaluating the Effects of Hinge Flexibility on the Solution Structure of Antibodies at Concentrated Conditions. Journal of Pharmaceutical Sciences. 108(5). 1663–1674. 15 indexed citations
13.
Castellanos, Maria Monica, James A. Snyder, Srinivas Chakravarthy, et al.. (2017). Characterization of Monoclonal Antibody–Protein Antigen Complexes Using Small-Angle Scattering and Molecular Modeling. Antibodies. 6(4). 25–25. 9 indexed citations
14.
Castañeda, Carlos A., Olivier Walker, Apurva Chaturvedi, et al.. (2016). Linkage via K27 Bestows Ubiquitin Chains with Unique Properties among Polyubiquitins. Structure. 24(3). 423–436. 51 indexed citations
15.
Perkins, Stephen J., David W. Wright, Hailiang Zhang, et al.. (2016). Atomistic modelling of scattering data in the Collaborative Computational Project for Small Angle Scattering (CCP-SAS). Journal of Applied Crystallography. 49(6). 1861–1875. 60 indexed citations
16.
Brookes, Emre, et al.. (2015). The GenApp framework integrated with Airavata for managed compute resource submissions. Concurrency and Computation Practice and Experience. 27(16). 4292–4303. 9 indexed citations
17.
Zaccai, Nathan R., J. Todd Hoopes, Joseph E. Curtis, et al.. (2015). Deuterium Labeling Together with Contrast Variation Small-Angle Neutron Scattering Suggests How Skp Captures and Releases Unfolded Outer Membrane Proteins. Methods in enzymology on CD-ROM/Methods in enzymology. 159–210. 39 indexed citations
18.
Curtis, Joseph E., Hailiang Zhang, & Hirsh Nanda. (2014). SLDMOL: A tool for the structural characterization of thermally disordered membrane proteins. Computer Physics Communications. 185(11). 3010–3015. 4 indexed citations
19.
Khodadadi, Sheila, Joseph E. Curtis, & Alexei P. Sokolov. (2011). Protein Dynamics at the Picosecond-Nanosecond Time Scale: a Complementary Study by Dielectric Spectroscopy, Neutron Spectroscopy and MD Simulation. Biophysical Journal. 100(3). 18a–18a. 1 indexed citations
20.
Khosla, Chaitan, Joseph E. Curtis, John DeModena, Ursula Rinas, & James E. Bailey. (1990). Expression of Intracellular Hemoglobin Improves Protein Synthesis in Oxygen-Limited Escherichia coli. Nature Biotechnology. 8(9). 849–853. 96 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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