Michael C. Baxa

520 total citations
17 papers, 415 citations indexed

About

Michael C. Baxa is a scholar working on Molecular Biology, Materials Chemistry and Atomic and Molecular Physics, and Optics. According to data from OpenAlex, Michael C. Baxa has authored 17 papers receiving a total of 415 indexed citations (citations by other indexed papers that have themselves been cited), including 17 papers in Molecular Biology, 12 papers in Materials Chemistry and 4 papers in Atomic and Molecular Physics, and Optics. Recurrent topics in Michael C. Baxa's work include Protein Structure and Dynamics (16 papers), Enzyme Structure and Function (12 papers) and Mass Spectrometry Techniques and Applications (3 papers). Michael C. Baxa is often cited by papers focused on Protein Structure and Dynamics (16 papers), Enzyme Structure and Function (12 papers) and Mass Spectrometry Techniques and Applications (3 papers). Michael C. Baxa collaborates with scholars based in United States, South Korea and Poland. Michael C. Baxa's co-authors include Tobin R. Sosnick, Karl F. Freed, Esmael J. Haddadian, John Jumper, Wookyung Yu, Bryan A. Krantz, Robin S. Dothager, John J. Skinner, James R. Hinshaw and Abhishek Jha and has published in prestigious journals such as Chemical Reviews, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Michael C. Baxa

17 papers receiving 411 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Michael C. Baxa United States 11 372 213 83 68 48 17 415
João Henriques Sweden 8 383 1.0× 192 0.9× 72 0.9× 67 1.0× 30 0.6× 10 436
Karin A. Crowhurst United States 9 561 1.5× 319 1.5× 138 1.7× 58 0.9× 64 1.3× 15 616
Santiago Esteban‐Martín Spain 9 379 1.0× 186 0.9× 68 0.8× 43 0.6× 38 0.8× 12 454
Lars Meinhold Germany 10 331 0.9× 197 0.9× 54 0.7× 97 1.4× 27 0.6× 10 394
Adam W. Van Wynsberghe United States 7 366 1.0× 155 0.7× 39 0.5× 76 1.1× 26 0.5× 8 430
Naoto Hori United States 12 516 1.4× 148 0.7× 43 0.5× 55 0.8× 41 0.9× 20 573
Jory Z. Ruscio United States 7 409 1.1× 113 0.5× 67 0.8× 71 1.0× 98 2.0× 9 484
Christopher M. Dobson United Kingdom 8 423 1.1× 231 1.1× 80 1.0× 33 0.5× 55 1.1× 8 475
Anton Abyzov France 8 465 1.3× 162 0.8× 163 2.0× 24 0.4× 40 0.8× 23 533
María M. García‐Mira Spain 11 561 1.5× 374 1.8× 57 0.7× 81 1.2× 80 1.7× 14 598

Countries citing papers authored by Michael C. Baxa

Since Specialization
Citations

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

Fields of papers citing papers by Michael C. Baxa

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Michael C. Baxa. 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 Michael C. Baxa. The network helps show where Michael C. Baxa may publish in the future.

Co-authorship network of co-authors of Michael C. Baxa

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

All Works

17 of 17 papers shown
1.
Baxa, Michael C., Srinivas Chakravarthy, Joseph R. Sachleben, et al.. (2024). How hydrophobicity, side chains, and salt affect the dimensions of disordered proteins. Protein Science. 33(5). e4986–e4986. 4 indexed citations
2.
Zhang, Ning, Damini Sood, Nanhao Chen, et al.. (2024). Temperature-dependent fold-switching mechanism of the circadian clock protein KaiB. Proceedings of the National Academy of Sciences. 121(51). e2412327121–e2412327121. 6 indexed citations
3.
Sosnick, Tobin R. & Michael C. Baxa. (2024). Collapse and Protein Folding: Should We Be Surprised That Biothermodynamics Works So Well?. Annual Review of Biophysics. 54(1). 17–34. 3 indexed citations
4.
Zmyslowski, Adam M., et al.. (2022). HDX-MS performed on BtuB in E. coli outer membranes delineates the luminal domain’s allostery and unfolding upon B12 and TonB binding. Proceedings of the National Academy of Sciences. 119(20). e2119436119–e2119436119. 21 indexed citations
5.
Baxa, Michael C. & Tobin R. Sosnick. (2021). Engineered Metal-Binding Sites to Probe Protein Folding Transition States: Psi Analysis. Methods in molecular biology. 2376. 31–63. 3 indexed citations
6.
Peng, Xiangda, Michael C. Baxa, Joseph R. Sachleben, et al.. (2021). Prediction and Validation of a Protein’s Free Energy Surface Using Hydrogen Exchange and (Importantly) Its Denaturant Dependence. Journal of Chemical Theory and Computation. 18(1). 550–561. 15 indexed citations
7.
Gates, Zachary P., Michael C. Baxa, Wookyung Yu, et al.. (2017). Perplexing cooperative folding and stability of a low-sequence complexity, polyproline 2 protein lacking a hydrophobic core. Proceedings of the National Academy of Sciences. 114(9). 2241–2246. 27 indexed citations
8.
Yu, Wookyung, et al.. (2016). Cooperative folding near the downhill limit determined with amino acid resolution by hydrogen exchange. Proceedings of the National Academy of Sciences. 113(17). 4747–4752. 8 indexed citations
9.
Baxa, Michael C., Wookyung Yu, Aashish N. Adhikari, et al.. (2015). Even with nonnative interactions, the updated folding transition states of the homologs Proteins G & L are extensive and similar. Proceedings of the National Academy of Sciences. 112(27). 8302–8307. 20 indexed citations
10.
Baxa, Michael C., Esmael J. Haddadian, John Jumper, Karl F. Freed, & Tobin R. Sosnick. (2014). Loss of conformational entropy in protein folding calculated using realistic ensembles and its implications for NMR-based calculations. Proceedings of the National Academy of Sciences. 111(43). 15396–15401. 99 indexed citations
11.
Skinner, John J., Wookyung Yu, Michael C. Baxa, et al.. (2014). Benchmarking all-atom simulations using hydrogen exchange. Proceedings of the National Academy of Sciences. 111(45). 15975–15980. 65 indexed citations
12.
Baxa, Michael C., et al.. (2012). A “Link‐Psi” strategy using crosslinking indicates that the folding transition state of ubiquitin is not very malleable. Protein Science. 21(6). 819–827. 8 indexed citations
13.
Baxa, Michael C., Esmael J. Haddadian, Abhishek Jha, Karl F. Freed, & Tobin R. Sosnick. (2012). Context and Force Field Dependence of the Loss of Protein Backbone Entropy upon Folding Using Realistic Denatured and Native State Ensembles. Journal of the American Chemical Society. 134(38). 15929–15936. 30 indexed citations
14.
Baxa, Michael C., Karl F. Freed, & Tobin R. Sosnick. (2009). ψ-Constrained Simulations of Protein Folding Transition States: Implications for Calculating ϕ. Journal of Molecular Biology. 386(4). 920–928. 12 indexed citations
15.
Baxa, Michael C., et al.. (2009). Metal Binding Kinetics of Bi-Histidine Sites Used in ψ Analysis: Evidence of High-Energy Protein Folding Intermediates. Biochemistry. 48(13). 2950–2959. 13 indexed citations
16.
Baxa, Michael C., Karl F. Freed, & Tobin R. Sosnick. (2008). Quantifying the Structural Requirements of the Folding Transition State of Protein A and Other Systems. Journal of Molecular Biology. 381(5). 1362–1381. 28 indexed citations
17.
Sosnick, Tobin R., Bryan A. Krantz, Robin S. Dothager, & Michael C. Baxa. (2006). Characterizing the Protein Folding Transition State Using ψ Analysis. Chemical Reviews. 106(5). 1862–1876. 53 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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