Saul Treviño

2.2k total citations
11 papers, 1.7k citations indexed

About

Saul Treviño is a scholar working on Molecular Biology, Materials Chemistry and Genetics. According to data from OpenAlex, Saul Treviño has authored 11 papers receiving a total of 1.7k indexed citations (citations by other indexed papers that have themselves been cited), including 11 papers in Molecular Biology, 6 papers in Materials Chemistry and 2 papers in Genetics. Recurrent topics in Saul Treviño's work include Protein Structure and Dynamics (9 papers), Enzyme Structure and Function (6 papers) and RNA and protein synthesis mechanisms (3 papers). Saul Treviño is often cited by papers focused on Protein Structure and Dynamics (9 papers), Enzyme Structure and Function (6 papers) and RNA and protein synthesis mechanisms (3 papers). Saul Treviño collaborates with scholars based in United States, Russia and Slovakia. Saul Treviño's co-authors include J. Martin Scholtz, C. Nick Pace, Erode N. Prabhakaran, Gerald R. Grimsley, Bret A. Shirley, K.S. Gajiwala, John D. Landua, Richard L. Thurlkill, Stephanie Schaefer and Satoshi Iimura and has published in prestigious journals such as Journal of Molecular Biology, Philosophical Transactions of the Royal Society B Biological Sciences and Journal of Pharmaceutical Sciences.

In The Last Decade

Saul Treviño

10 papers receiving 1.6k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Saul Treviño United States 10 1.2k 364 143 136 127 11 1.7k
Bret A. Shirley United States 11 1.4k 1.2× 563 1.5× 94 0.7× 153 1.1× 116 0.9× 11 1.9k
Javier Gómez Spain 24 1.6k 1.3× 622 1.7× 80 0.6× 174 1.3× 60 0.5× 52 2.3k
Harumi Fukada Japan 22 1.3k 1.2× 246 0.7× 68 0.5× 103 0.8× 285 2.2× 65 1.8k
Carlos H.I. Ramos Brazil 32 2.6k 2.2× 397 1.1× 74 0.5× 100 0.7× 140 1.1× 145 3.5k
K.A. Majorek United States 17 975 0.8× 281 0.8× 64 0.4× 95 0.7× 79 0.6× 35 1.8k
Н. А. Родионова Russia 10 1.1k 1.0× 430 1.2× 194 1.4× 67 0.5× 182 1.4× 45 1.6k
Przemyslaw Porebski United States 18 1.1k 1.0× 480 1.3× 54 0.4× 116 0.9× 57 0.4× 38 1.9k
Pedro L. Mateo Spain 26 2.1k 1.8× 792 2.2× 121 0.8× 168 1.2× 79 0.6× 65 2.5k
Francesc Rabanal Spain 33 1.9k 1.6× 348 1.0× 119 0.8× 172 1.3× 68 0.5× 74 2.9k
Svend Ludvigsen Denmark 25 1.4k 1.2× 315 0.9× 99 0.7× 188 1.4× 116 0.9× 33 2.0k

Countries citing papers authored by Saul Treviño

Since Specialization
Citations

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

Fields of papers citing papers by Saul Treviño

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Saul Treviño

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

All Works

11 of 11 papers shown
1.
Thurlkill, Richard L., Saul Treviño, J. Martin Scholtz, & Gerald R. Grimsley. (2023). Determining the Conformational Stability of a Protein from Urea and Thermal Unfolding Curves. Current Protocols. 3(3). e723–e723.
2.
Pace, C. Nick, John D. Landua, Saul Treviño, et al.. (2014). Contribution of hydrogen bonds to protein stability. Protein Science. 23(5). 652–661. 397 indexed citations
3.
Grimsley, Gerald R., Saul Treviño, Richard L. Thurlkill, & J. Martin Scholtz. (2013). Determining the Conformational Stability of a Protein from Urea and Thermal Unfolding Curves. Current Protocols in Protein Science. 71(1). Unit28.4–Unit28.4. 15 indexed citations
4.
Pace, C. Nick, John D. Landua, Saul Treviño, et al.. (2011). Contribution of Hydrophobic Interactions to Protein Stability. Journal of Molecular Biology. 408(3). 514–528. 336 indexed citations
5.
Treviño, Saul, J. Martin Scholtz, & C. Nick Pace. (2008). Measuring and Increasing Protein Solubility. Journal of Pharmaceutical Sciences. 97(10). 4155–4166. 121 indexed citations
6.
Treviño, Saul, Stephanie Schaefer, J. Martin Scholtz, & C. Nick Pace. (2007). Increasing Protein Conformational Stability by Optimizing β-Turn Sequence. Journal of Molecular Biology. 373(1). 211–218. 140 indexed citations
7.
Treviño, Saul, J. Martin Scholtz, & C. Nick Pace. (2006). Amino Acid Contribution to Protein Solubility: Asp, Glu, and Ser Contribute more Favorably than the other Hydrophilic Amino Acids in RNase Sa. Journal of Molecular Biology. 366(2). 449–460. 209 indexed citations
8.
Treviño, Saul, Kuppan Gokulan, Richard L. Thurlkill, et al.. (2005). Asp79 Makes a Large, Unfavorable Contribution to the Stability of RNase Sa. Journal of Molecular Biology. 354(4). 967–978. 27 indexed citations
9.
Pace, C. Nick, Saul Treviño, Erode N. Prabhakaran, & J. Martin Scholtz. (2004). Protein structure, stability and solubility in water and other solvents. Philosophical Transactions of the Royal Society B Biological Sciences. 359(1448). 1225–1235. 303 indexed citations
10.
Laurents, Douglas V., Beatrice M.P. Huyghues‐Despointes, Marta Bruix, et al.. (2003). Charge–Charge Interactions are Key Determinants of the pK Values of Ionizable Groups in Ribonuclease Sa (pI=3.5) and a Basic Variant (pI=10.2). Journal of Molecular Biology. 325(5). 1077–1092. 91 indexed citations
11.
Yakovlev, Gennady I., Vladimir A. Mitkevich, Kevin L. Shaw, et al.. (2003). Contribution of active site residues to the activity and thermal stability of ribonuclease Sa. Protein Science. 12(10). 2367–2373. 23 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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