José M. Sánchez‐Ruiz

9.2k total citations
140 papers, 7.5k citations indexed

About

José M. Sánchez‐Ruiz is a scholar working on Molecular Biology, Materials Chemistry and Physical and Theoretical Chemistry. According to data from OpenAlex, José M. Sánchez‐Ruiz has authored 140 papers receiving a total of 7.5k indexed citations (citations by other indexed papers that have themselves been cited), including 124 papers in Molecular Biology, 59 papers in Materials Chemistry and 16 papers in Physical and Theoretical Chemistry. Recurrent topics in José M. Sánchez‐Ruiz's work include Protein Structure and Dynamics (91 papers), Enzyme Structure and Function (58 papers) and Photosynthetic Processes and Mechanisms (15 papers). José M. Sánchez‐Ruiz is often cited by papers focused on Protein Structure and Dynamics (91 papers), Enzyme Structure and Function (58 papers) and Photosynthetic Processes and Mechanisms (15 papers). José M. Sánchez‐Ruiz collaborates with scholars based in Spain, United States and Sweden. José M. Sánchez‐Ruiz's co-authors include Beatriz Ibarra‐Molero, Valeria A. Risso, Víctor Muñoz, George I. Makhatadze, Raúl Pérez‐Jiménez, Pedro L. Mateo, Manuel Cortijo, María M. García‐Mira, Raquel Godoy‐Ruiz and José Luis López‐Lacomba and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

José M. Sánchez‐Ruiz

138 papers receiving 7.4k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
José M. Sánchez‐Ruiz Spain 49 6.2k 2.8k 752 746 575 140 7.5k
D. Wayne Bolen United States 44 7.3k 1.2× 3.5k 1.2× 1.3k 1.7× 1.1k 1.4× 911 1.6× 70 9.3k
J. Martin Scholtz United States 45 8.5k 1.4× 3.0k 1.1× 748 1.0× 682 0.9× 1.2k 2.1× 91 10.9k
George I. Makhatadze United States 51 8.3k 1.4× 4.1k 1.5× 714 0.9× 1.3k 1.7× 1.2k 2.1× 143 10.3k
Gerald R. Grimsley United States 24 5.5k 0.9× 1.6k 0.6× 592 0.8× 289 0.4× 550 1.0× 31 7.3k
Kunihiro Kuwajima Japan 43 6.8k 1.1× 4.1k 1.5× 729 1.0× 324 0.4× 629 1.1× 141 8.2k
Pinak Chakrabarti India 51 5.9k 1.0× 3.0k 1.1× 400 0.5× 334 0.4× 764 1.3× 161 9.2k
Maurice R. Eftink United States 33 5.3k 0.9× 1.6k 0.6× 851 1.1× 610 0.8× 1.0k 1.8× 99 7.5k
Duilio Cascio United States 55 8.0k 1.3× 2.0k 0.7× 705 0.9× 239 0.3× 591 1.0× 156 10.8k
Vincent J. Hilser United States 38 5.0k 0.8× 2.0k 0.7× 477 0.6× 453 0.6× 785 1.4× 97 5.7k
Yves Engelborghs Belgium 51 5.0k 0.8× 1.0k 0.4× 928 1.2× 538 0.7× 334 0.6× 202 8.3k

Countries citing papers authored by José M. Sánchez‐Ruiz

Since Specialization
Citations

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

Fields of papers citing papers by José M. Sánchez‐Ruiz

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by José M. Sánchez‐Ruiz. 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 José M. Sánchez‐Ruiz. The network helps show where José M. Sánchez‐Ruiz may publish in the future.

Co-authorship network of co-authors of José M. Sánchez‐Ruiz

This figure shows the co-authorship network connecting the top 25 collaborators of José M. Sánchez‐Ruiz. A scholar is included among the top collaborators of José M. Sánchez‐Ruiz 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 José M. Sánchez‐Ruiz. José M. Sánchez‐Ruiz 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.
Medina‐Carmona, Encarnación, Andrej Berg, Gaspar Pinto, et al.. (2025). Redefining the Limits of Functional Continuity in the Early Evolution of P-Loop NTPases. Molecular Biology and Evolution. 42(4).
2.
Pantoja‐Uceda, David, Mariano Ortega‐Muñoz, Valeria A. Risso, et al.. (2025). Enzyme Enhancement Through Computational Stability Design Targeting NMR-Determined Catalytic Hotspots. Journal of the American Chemical Society. 147(18). 14978–14996. 5 indexed citations
3.
Mateljak, Ivan, Roman Kittl, Roland Ludwig, et al.. (2024). Stable and Promiscuous Galactose Oxidases Engineered by Directed Evolution, Atomistic Design, and Ancestral Sequence Reconstruction. ACS Synthetic Biology. 14(1). 239–246. 1 indexed citations
4.
Moreno‐Paz, Mercedes, Fernando Puente‐Sánchez, Laura Sánchez‐García, et al.. (2023). Immunoanalytical Approach for Detecting and Identifying Ancestral Peptide Biomarkers in Early Earth Analogue Environments. Analytical Chemistry. 95(12). 5323–5330. 1 indexed citations
5.
Medina‐Carmona, Encarnación, Antonio J. Mota, Juan M. Cuerva, et al.. (2023). Cell Survival Enabled by Leakage of a Labile Metabolic Intermediate. Molecular Biology and Evolution. 40(3). 3 indexed citations
6.
Risso, Valeria A., Beatriz Ibarra‐Molero, Yosuke Hoshino, et al.. (2021). Heme-binding enables allosteric modulation in an ancient TIM-barrel glycosidase. Nature Communications. 12(1). 380–380. 23 indexed citations
7.
Risso, Valeria A., Adrian Romero‐Rivera, Mariano Ortega‐Muñoz, et al.. (2020). Enhancing a de novo enzyme activity by computationally-focused ultra-low-throughput screening. Chemical Science. 11(24). 6134–6148. 36 indexed citations
8.
Garcia‐Ruiz, Eva, Patricia Gómez de Santos, Paloma Santos‐Moriano, et al.. (2018). Directed -in vitro- evolution of Precambrian and extant Rubiscos. Scientific Reports. 8(1). 5532–5532. 22 indexed citations
9.
Ibarra‐Molero, Beatriz, Athi N. Naganathan, José M. Sánchez‐Ruiz, & Víctor Muñoz. (2015). Modern Analysis of Protein Folding by Differential Scanning Calorimetry. Methods in enzymology on CD-ROM/Methods in enzymology. 567. 281–318. 54 indexed citations
10.
Godoy‐Ruiz, Raquel, Eric R. Henry, Jan Kubelka, et al.. (2008). Estimating Free-Energy Barrier Heights for an Ultrafast Folding Protein from Calorimetric and Kinetic Data. The Journal of Physical Chemistry B. 112(19). 5938–5949. 74 indexed citations
11.
Pérez‐Jiménez, Raúl, Raquel Godoy‐Ruiz, Beatriz Ibarra‐Molero, & José M. Sánchez‐Ruiz. (2004). The effect of charge-introduction mutations on E. coli thioredoxin stability. Biophysical Chemistry. 115(2-3). 105–107. 11 indexed citations
12.
Thórólfsson, Matthı́as, et al.. (2004). Structural and stability effects of phosphorylation: Localized structural changes in phenylalanine hydroxylase. Protein Science. 13(5). 1219–1226. 23 indexed citations
13.
Campos, Luis A., María M. García‐Mira, Raquel Godoy‐Ruiz, José M. Sánchez‐Ruiz, & Javier Sancho. (2004). Do Proteins Always Benefit from a Stability Increase? Relevant and Residual Stabilisation in a Three-state Protein by Charge Optimisation. Journal of Molecular Biology. 344(1). 223–237. 39 indexed citations
14.
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
15.
Parody‐Morreale, Antonio, et al.. (2003). Energetic Evidence for Formation of a pH-dependent Hydrophobic Cluster in the Denatured State of Thermus thermophilus Ribonuclease H. Journal of Molecular Biology. 329(4). 731–743. 76 indexed citations
16.
Sánchez‐Ruiz, José M.. (1995). Differential Scanning Calorimetry of Proteins. Sub-cellular biochemistry. 24. 133–176. 72 indexed citations
17.
Sánchez‐Ruiz, José M.. (1992). Theoretical analysis of Lumry-Eyring models in differential scanning calorimetry. Biophysical Journal. 61(4). 921–935. 436 indexed citations
18.
Conejero‐Lara, Francisco, Pedro L. Mateo, Francesc Avilés, & José M. Sánchez‐Ruiz. (1991). Effect of zinc(2+) on the thermal denaturation of carboxypeptidase B. Biochemistry. 30(8). 2067–2072. 44 indexed citations
19.
Galisteo, María L., Pedro L. Mateo, & José M. Sánchez‐Ruiz. (1991). Kinetic study on the irreversible thermal denaturation of yeast phosphoglycerate kinase. Biochemistry. 30(8). 2061–2066. 103 indexed citations
20.
Sánchez‐Ruiz, José M., José Luis López‐Lacomba, Manuel Cortijo, & Pedro L. Mateo. (1988). Differential scanning calorimetry of the irreversible thermal denaturation of thermolysin. Biochemistry. 27(5). 1648–1652. 396 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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