Jorge Babul

1.7k total citations · 1 hit paper
58 papers, 1.5k citations indexed

About

Jorge Babul is a scholar working on Molecular Biology, Materials Chemistry and Cancer Research. According to data from OpenAlex, Jorge Babul has authored 58 papers receiving a total of 1.5k indexed citations (citations by other indexed papers that have themselves been cited), including 48 papers in Molecular Biology, 23 papers in Materials Chemistry and 18 papers in Cancer Research. Recurrent topics in Jorge Babul's work include Enzyme Structure and Function (23 papers), Cancer, Hypoxia, and Metabolism (18 papers) and Pancreatic function and diabetes (16 papers). Jorge Babul is often cited by papers focused on Enzyme Structure and Function (23 papers), Cancer, Hypoxia, and Metabolism (18 papers) and Pancreatic function and diabetes (16 papers). Jorge Babul collaborates with scholars based in Chile, United States and Brazil. Jorge Babul's co-authors include Earle Stellwagen, Victoria Guixé, Ricardo Cabrera, D G Fraenkel, Mauricio Báez, Tito Ureta, Richard Charles Garratt, César A. Ramírez‐Sarmiento, Eliana Rabajille and Hermann M. Niemeyer and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Journal of Molecular Biology.

In The Last Decade

Jorge Babul

58 papers receiving 1.3k citations

Hit Papers

align trajectories

What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

Measurement of protein concentration with interferences optics

1969 380 citations Jorge Babul et al. Analytical Biochemistry profile →

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Jorge Babul Chile	18	1.2k	463	242	197	173	58	1.5k
Gregory D. Reinhart United States	25	1.6k 1.4×	463 1.0×	320 1.3×	254 1.3×	268 1.5×	75	2.0k
Ian P. Trayer United Kingdom	28	1.4k 1.2×	123 0.3×	352 1.5×	212 1.1×	105 0.6×	84	2.1k
Charles A. Collyer Australia	24	915 0.8×	338 0.7×	140 0.6×	176 0.9×	42 0.2×	57	1.8k
Zaiguo Li United States	20	1.1k 0.9×	184 0.4×	258 1.1×	177 0.9×	46 0.3×	37	1.6k
Vladimir N. Kasho United States	26	2.1k 1.8×	596 1.3×	201 0.8×	211 1.1×	34 0.2×	58	3.0k
Richard L. Cross United States	35	3.8k 3.2×	264 0.6×	149 0.6×	94 0.5×	126 0.7×	55	4.1k
Michael G. Gore United Kingdom	23	1.2k 1.0×	209 0.5×	173 0.7×	53 0.3×	62 0.4×	102	1.9k
G. Jogl United States	28	1.6k 1.4×	343 0.7×	127 0.5×	64 0.3×	114 0.7×	55	2.2k
A.P. Turnbull United Kingdom	19	822 0.7×	278 0.6×	233 1.0×	46 0.2×	47 0.3×	51	1.2k
Hyung‐Ho Ha South Korea	26	848 0.7×	301 0.7×	107 0.4×	79 0.4×	115 0.7×	63	1.8k

Countries citing papers authored by Jorge Babul

Since Specialization

Citations

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

Fields of papers citing papers by Jorge Babul

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Jorge Babul

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

All Works

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20 of 20 papers shown

Peulen, Thomas-Otavio, et al.. (2024). DNA controls the dimerization of the human FoxP1 forkhead domain. Cell Reports Physical Science. 5(3). 101854–101854. 3 indexed citations

Galaz‐Davison, Pablo, et al.. (2023). DNA facilitates heterodimerization between human transcription factors FoxP1 and FoxP2 by increasing their conformational flexibility. iScience. 26(7). 107228–107228. 1 indexed citations

Ramírez‐Sarmiento, César A., et al.. (2021). Human FoxP Transcription Factors as Tractable Models of the Evolution and Functional Outcomes of Three-Dimensional Domain Swapping. International Journal of Molecular Sciences. 22(19). 10296–10296. 1 indexed citations

Babul, Jorge, et al.. (2021). Single-molecule optical tweezers reveals folding steps of the domain swapping mechanism of a protein. Biophysical Journal. 120(21). 4809–4818. 2 indexed citations

Alzate‐Morales, Jans, et al.. (2020). Characterization of hydroxymethylpyrimidine phosphate kinase from mesophilic and thermophilic bacteria and structural insights into their differential thermal stability. Archives of Biochemistry and Biophysics. 688. 108389–108389. 9 indexed citations

Komives, Elizabeth A., et al.. (2020). Intrinsically Disordered Regions of the DNA-Binding Domain of Human FoxP1 Facilitate Domain Swapping. Journal of Molecular Biology. 432(19). 5411–5429. 11 indexed citations

Ramírez‐Sarmiento, César A., et al.. (2019). The protonation state of an evolutionarily conserved histidine modulates domain swapping stability of FoxP1. Scientific Reports. 9(1). 5441–5441. 15 indexed citations

Komives, Elizabeth A., et al.. (2017). Unusual dimerization of a BcCsp mutant leads to reduced conformational dynamics. FEBS Journal. 284(12). 1882–1896. 3 indexed citations

Báez, Mauricio, et al.. (2016). Regulatory network of the allosteric ATP inhibition of E. coli phosphofructokinase-2 studied by hybrid dimers. Biochimie. 128-129. 209–216. 3 indexed citations

10.

Barriga, Andrés, et al.. (2016). New visible and selective DNA staining method in gels with tetrazolium salts. Analytical Biochemistry. 517. 31–35. 4 indexed citations

11.

Komives, Elizabeth A., et al.. (2016). Three-Dimensional Domain Swapping Changes the Folding Mechanism of the Forkhead Domain of FoxP1. Biophysical Journal. 110(11). 2349–2360. 22 indexed citations

12.

Báez, Mauricio, Christian A.M. Wilson, César A. Ramírez‐Sarmiento, Victoria Guixé, & Jorge Babul. (2012). Expanded Monomeric Intermediate upon Cold and Heat Unfolding of Phosphofructokinase-2 from Escherichia coli. Biophysical Journal. 103(10). 2187–2194. 9 indexed citations

13.

Cabrera, Ricardo, Jorge Babul, & Victoria Guixé. (2010). Ribokinase family evolution and the role of conserved residues at the active site of the PfkB subfamily representative, Pfk-2 from Escherichia coli. Archives of Biochemistry and Biophysics. 502(1). 23–30. 29 indexed citations

14.

Cabrera, Ricardo, et al.. (2010). The Crystal Complex of Phosphofructokinase-2 of Escherichia coli with Fructose-6-phosphate. Journal of Biological Chemistry. 286(7). 5774–5783. 26 indexed citations

15.

Rivas‐Pardo, Jaime Andrés, et al.. (2010). Divalent metal cation requirements of phosphofructokinase-2 from E. coli. Evidence for a high affinity binding site for Mn2+. Archives of Biochemistry and Biophysics. 505(1). 60–66. 9 indexed citations

16.

Cabrera, Ricardo, A.L.B. Ambrosio, Richard Charles Garratt, Victoria Guixé, & Jorge Babul. (2008). Crystallographic Structure of Phosphofructokinase-2 from Escherichia coli in Complex with Two ATP Molecules. Implications for Substrate Inhibition. Journal of Molecular Biology. 383(3). 588–602. 26 indexed citations

17.

Báez, Mauricio, et al.. (2008). Uncoupling the MgATP‐induced inhibition and aggregation of Escherichia coli phosphofructokinase‐2 by C‐terminal mutations. FEBS Letters. 582(13). 1907–1912. 8 indexed citations

18.

Cabrera, Ricardo, et al.. (2006). Crystallization and preliminary crystallographic analysis of the tetrameric form of phosphofructokinase-2 fromEscherichia coli, a member of the ribokinase family. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 62(9). 935–937. 3 indexed citations

19.

Cabrera, Ricardo, et al.. (2005). Role of Cys‐295 on subunit interactions and allosteric regulation of phosphofructokinase‐2 from Escherichia coli. FEBS Letters. 579(11). 2313–2318. 10 indexed citations

20.

Torres, Juan Carlos, Victoria Guixé, & Jorge Babul. (1995). A New Method of Assessing Rates of the Futile Cycle during Glycolytic and Gluconeogenic Metabolism. Archives of Biochemistry and Biophysics. 321(2). 517–525. 5 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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