Gary J. Pielak

12.2k total citations
209 papers, 9.9k citations indexed

About

Gary J. Pielak is a scholar working on Molecular Biology, Materials Chemistry and Cell Biology. According to data from OpenAlex, Gary J. Pielak has authored 209 papers receiving a total of 9.9k indexed citations (citations by other indexed papers that have themselves been cited), including 167 papers in Molecular Biology, 76 papers in Materials Chemistry and 32 papers in Cell Biology. Recurrent topics in Gary J. Pielak's work include Protein Structure and Dynamics (123 papers), Enzyme Structure and Function (73 papers) and Photosynthetic Processes and Mechanisms (48 papers). Gary J. Pielak is often cited by papers focused on Protein Structure and Dynamics (123 papers), Enzyme Structure and Function (73 papers) and Photosynthetic Processes and Mechanisms (48 papers). Gary J. Pielak collaborates with scholars based in United States, China and United Kingdom. Gary J. Pielak's co-authors include Conggang Li, Mohona Sarkar, Austin E. Smith, Gregory B. Young, Yaqiang Wang, Rachel D. Cohen, Aleister J. Saunders, Andrew C. Miklos, A. Grant Mauk and Alex J. Guseman and has published in prestigious journals such as Nature, Science and Chemical Reviews.

In The Last Decade

Gary J. Pielak

201 papers receiving 9.8k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Gary J. Pielak United States 58 7.7k 3.1k 1.4k 1.1k 859 209 9.9k
Catherine A. Royer United States 49 6.2k 0.8× 2.2k 0.7× 935 0.6× 710 0.6× 824 1.0× 192 8.2k
Lila M. Gierasch United States 64 10.9k 1.4× 2.8k 0.9× 1.8k 1.3× 1.2k 1.0× 384 0.4× 220 12.9k
Heinrich Röder United States 63 8.0k 1.0× 4.1k 1.3× 1.6k 1.1× 1.9k 1.7× 1.5k 1.8× 204 11.9k
Jeetain Mittal United States 57 10.5k 1.4× 4.0k 1.3× 736 0.5× 846 0.7× 1.3k 1.5× 174 14.1k
Tobin R. Sosnick United States 55 9.9k 1.3× 4.2k 1.3× 1.1k 0.8× 1.5k 1.3× 999 1.2× 169 11.1k
Dagmar Ringe United States 69 10.5k 1.4× 4.7k 1.5× 2.0k 1.4× 965 0.8× 744 0.9× 230 16.2k
D. Wayne Bolen United States 44 7.3k 1.0× 3.5k 1.1× 1.3k 0.9× 911 0.8× 1.1k 1.2× 70 9.3k
Julie D. Forman‐Kay Canada 77 18.7k 2.4× 4.9k 1.6× 2.2k 1.5× 2.8k 2.4× 636 0.7× 218 21.8k
Zbigniew Dauter United States 62 9.9k 1.3× 3.8k 1.2× 897 0.6× 667 0.6× 347 0.4× 352 15.4k
Florante A. Quiocho United States 72 13.6k 1.8× 4.8k 1.5× 2.3k 1.6× 2.1k 1.8× 567 0.7× 205 19.1k

Countries citing papers authored by Gary J. Pielak

Since Specialization
Citations

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

Fields of papers citing papers by Gary J. Pielak

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Gary J. Pielak. 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 Gary J. Pielak. The network helps show where Gary J. Pielak may publish in the future.

Co-authorship network of co-authors of Gary J. Pielak

This figure shows the co-authorship network connecting the top 25 collaborators of Gary J. Pielak. A scholar is included among the top collaborators of Gary J. Pielak 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 Gary J. Pielak. Gary J. Pielak 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.
Parnham, Stuart, et al.. (2025). Crowding beyond excluded volume: A tale of two dimers. Protein Science. 34(4). e70062–e70062. 4 indexed citations
2.
Pielak, Gary J., et al.. (2024). Quantitative entropy–enthalpy compensation in intraprotein interactions from model compound data. Protein Science. 33(6). e5013–e5013. 2 indexed citations
3.
Liu, Xiaoli, Yuwei Ge, Liying Wang, et al.. (2024). Trimethylamine N‐oxide (TMAO) doubly locks the hydrophobic core and surfaces of protein against desiccation stress. Protein Science. 33(8). e5107–e5107. 3 indexed citations
4.
Pielak, Gary J., et al.. (2023). How Sugars Protect Dry Protein Structure. Biochemistry. 62(5). 1044–1052. 48 indexed citations
5.
Speer, Shannon L., Wenwen Zheng, Xin Jiang, et al.. (2021). The intracellular environment affects protein–protein interactions. Proceedings of the National Academy of Sciences. 118(11). 64 indexed citations
6.
Piszkiewicz, Samantha, et al.. (2021). Dried Protein Structure Revealed at the Residue Level by Liquid-Observed Vapor Exchange NMR. Biochemistry. 60(2). 152–159. 16 indexed citations
7.
Atkin, Joanna M., et al.. (2021). Water’s Variable Role in Protein Stability Uncovered by Liquid-Observed Vapor Exchange NMR. Biochemistry. 60(41). 3041–3045. 17 indexed citations
8.
Stadmiller, Samantha S., et al.. (2021). Danio rerio Oocytes for Eukaryotic In-Cell NMR. Biochemistry. 60(6). 451–459. 9 indexed citations
9.
Pielak, Gary J., et al.. (2021). Protection by desiccation‐tolerance proteins probed at the residue level. Protein Science. 31(2). 396–406. 20 indexed citations
10.
Piszkiewicz, Samantha & Gary J. Pielak. (2019). Protecting Enzymes from Stress-Induced Inactivation. Biochemistry. 58(37). 3825–3833. 48 indexed citations
11.
Stadmiller, Samantha S. & Gary J. Pielak. (2018). Enthalpic stabilization of an SH3 domain by D2O. Protein Science. 27(9). 1710–1716. 18 indexed citations
12.
Guseman, Alex J., et al.. (2018). Surface Charge Modulates Protein–Protein Interactions in Physiologically Relevant Environments. Biochemistry. 57(11). 1681–1684. 58 indexed citations
13.
Cohen, Rachel D. & Gary J. Pielak. (2017). Quinary interactions with an unfolded state ensemble. Protein Science. 26(9). 1698–1703. 26 indexed citations
14.
Smith, Austin E., et al.. (2016). In-cell thermodynamics and a new role for protein surfaces. Proceedings of the National Academy of Sciences. 113(7). 1725–1730. 139 indexed citations
15.
Monteith, William & Gary J. Pielak. (2014). Residue level quantification of protein stability in living cells. Proceedings of the National Academy of Sciences. 111(31). 11335–11340. 104 indexed citations
16.
Sarkar, Mohona, Austin E. Smith, & Gary J. Pielak. (2013). Impact of reconstituted cytosol on protein stability. Proceedings of the National Academy of Sciences. 110(48). 19342–19347. 165 indexed citations
17.
Dedmon, Matthew M., Chetan N. Patel, Gregory B. Young, & Gary J. Pielak. (2002). FlgM gains structure in living cells. Proceedings of the National Academy of Sciences. 99(20). 12681–12684. 253 indexed citations
18.
Geren, Lois, James R. Beasley, Aleister J. Saunders, et al.. (1995). Design of a Ruthenium-Cytochrome c Derivative to Measure Electron Transfer to the Initial Acceptor in Cytochrome c Oxidase. Journal of Biological Chemistry. 270(6). 2466–2472. 82 indexed citations
19.
Pielak, Gary J., et al.. (1995). A native tertiary interaction stabilizes the A state of cytochrome c. Biochemistry. 34(10). 3140–3143. 83 indexed citations
20.
Betz, Stephen F. & Gary J. Pielak. (1992). Introduction of a disulfide bond into cytochrome c stabilizes a compact denatured state. Biochemistry. 31(49). 12337–12344. 57 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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