Begoña Heras

3.3k total citations
90 papers, 2.5k citations indexed

About

Begoña Heras is a scholar working on Molecular Biology, Genetics and Endocrinology. According to data from OpenAlex, Begoña Heras has authored 90 papers receiving a total of 2.5k indexed citations (citations by other indexed papers that have themselves been cited), including 49 papers in Molecular Biology, 29 papers in Genetics and 23 papers in Endocrinology. Recurrent topics in Begoña Heras's work include Bacterial Genetics and Biotechnology (28 papers), Antibiotic Resistance in Bacteria (19 papers) and Enzyme Structure and Function (18 papers). Begoña Heras is often cited by papers focused on Bacterial Genetics and Biotechnology (28 papers), Antibiotic Resistance in Bacteria (19 papers) and Enzyme Structure and Function (18 papers). Begoña Heras collaborates with scholars based in Australia, United States and Spain. Begoña Heras's co-authors include Jennifer L. Martin, M.J. Scanlon, Jason J. Paxman, Mark A. Schembri, Makrina Totsika, Stephen R. Shouldice, Maša Čemažar, David J. Craik, Christian W. Gruber and Russell Jarrott and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Angewandte Chemie International Edition.

In The Last Decade

Begoña Heras

84 papers receiving 2.4k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Begoña Heras Australia 28 1.5k 491 487 399 314 90 2.5k
Zhao‐Xun Liang Singapore 34 2.1k 1.4× 637 1.3× 261 0.5× 306 0.8× 337 1.1× 88 3.2k
Frédéric Kerff Belgium 24 1.5k 1.0× 535 1.1× 413 0.8× 191 0.5× 203 0.6× 67 3.0k
Ann H. West United States 25 1.9k 1.3× 748 1.5× 288 0.6× 406 1.0× 150 0.5× 67 3.0k
Joshua J. Woodward United States 35 2.5k 1.7× 505 1.0× 187 0.4× 159 0.4× 193 0.6× 57 4.9k
Mark Paetzel Canada 32 2.2k 1.5× 960 2.0× 175 0.4× 445 1.1× 162 0.5× 59 3.3k
Zengyi Chang China 31 2.1k 1.4× 576 1.2× 264 0.5× 777 1.9× 166 0.5× 82 2.7k
Vincent Villeret France 31 1.9k 1.3× 597 1.2× 100 0.2× 498 1.2× 238 0.8× 85 2.9k
Daniel Wall United States 39 3.2k 2.2× 1.2k 2.4× 322 0.7× 275 0.7× 569 1.8× 85 4.6k
J.D. Pédelacq France 19 2.3k 1.5× 537 1.1× 261 0.5× 271 0.7× 95 0.3× 35 3.0k
Gunnar F. Kaufmann United States 30 2.2k 1.5× 406 0.8× 190 0.4× 93 0.2× 239 0.8× 69 3.2k

Countries citing papers authored by Begoña Heras

Since Specialization
Citations

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

Fields of papers citing papers by Begoña Heras

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Begoña Heras

This figure shows the co-authorship network connecting the top 25 collaborators of Begoña Heras. A scholar is included among the top collaborators of Begoña Heras 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 Begoña Heras. Begoña Heras 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.
Lam, Ling Ning, Artur Matysik, Thomas D. Watts, et al.. (2025). Role of sortase-assembled Ebp pili in Enterococcus faecalis adhesion to iron oxides and its impact on extracellular electron transfer. Microbiology Spectrum. 13(3). e0233724–e0233724. 2 indexed citations
2.
Akhtar, Naureen, Begoña Heras, James B. Murray, et al.. (2025). Identification of an Allene Warhead That Selectively Targets a Histidine Residue in the Escherichia coli Oxidoreductase Enzyme DsbA. ACS Medicinal Chemistry Letters. 16(4). 625–630. 1 indexed citations
3.
Mohanty, Biswaranjan, Wesam S. Alwan, Menachem J. Gunzburg, et al.. (2025). Discovery of a Cryptic Pocket in Ec DsbA Opens New Opportunities for Antibacterial Discovery. Angewandte Chemie International Edition. 64(49). e202515306–e202515306.
4.
Owyong, Tze Cin, Oana Sanislav, Lukas Englmaier, et al.. (2024). Global analysis of endogenous protein disorder in cells. Nature Methods. 22(1). 124–134. 3 indexed citations
5.
Doak, B.C., Kieran Rimmer, M.L. Williams, et al.. (2024). Fluoromethylketone‐Fragment Conjugates Designed as Covalent Modifiers of Ec DsbA are Atypical Substrates. ChemMedChem. 19(16). e202300684–e202300684. 3 indexed citations
6.
Wawrzyniak, Ivan, Philippe Ruiz, Jason J. Paxman, et al.. (2023). Genome-Wide Analysis of Antigen 43 (Ag43) Variants: New Insights in Their Diversity, Distribution and Prevalence in Bacteria. International Journal of Molecular Sciences. 24(6). 5500–5500. 7 indexed citations
7.
Qin, Jilong, Katie A. Wilson, Sohinee Sarkar, et al.. (2022). Conserved FimH mutations in the global Escherichia coli ST131 multi-drug resistant lineage weaken interdomain interactions and alter adhesin function. Computational and Structural Biotechnology Journal. 20. 4532–4541. 6 indexed citations
8.
Liu, Mengjie, Bicheng Yao, Hamid Soleimaninejad, et al.. (2021). Construction of a Highly Sensitive Thiol‐Reactive AIEgen‐Peptide Conjugate for Monitoring Protein Unfolding and Aggregation in Cells. Advanced Healthcare Materials. 10(24). e2101300–e2101300. 27 indexed citations
9.
Wang, Geqing, M.L. Williams, Wesam S. Alwan, et al.. (2020). Rapid Elaboration of Fragments into Leads by X-ray Crystallographic Screening of Parallel Chemical Libraries (REFiLX). Journal of Medicinal Chemistry. 63(13). 6863–6875. 21 indexed citations
10.
Wang, Geqing, et al.. (2019). The Fragment-Based Development of a Benzofuran Hit as a New Class of Escherichia coli DsbA Inhibitors. Molecules. 24(20). 3756–3756. 19 indexed citations
11.
Paxman, Jason J., et al.. (2019). Molecular and structural insights into an asymmetric proteolytic complex (ClpP1P2) from Mycobacterium smegmatis. Scientific Reports. 9(1). 18019–18019. 17 indexed citations
12.
Premkumar, Lakshmanane, Fabian Kurth, Gordon J. King, et al.. (2014). Structure of the Acinetobacter baumannii Dithiol Oxidase DsbA Bound to Elongation Factor EF-Tu Reveals a Novel Protein Interaction Site. Journal of Biological Chemistry. 289(29). 19869–19880. 13 indexed citations
13.
Bes, M. Teresa, et al.. (2013). Unraveling the Redox Properties of the Global Regulator FurA from Anabaena sp. PCC 7120: Disulfide Reductase Activity Based on Its CXXC Motifs. Antioxidants and Redox Signaling. 20(9). 1396–1406. 14 indexed citations
14.
Shouldice, Stephen R., Begoña Heras, Patricia Walden, et al.. (2011). Structure and Function of DsbA, a Key Bacterial Oxidative Folding Catalyst. Antioxidants and Redox Signaling. 14(9). 1729–1760. 86 indexed citations
15.
Heras, Begoña, Makrina Totsika, Russell Jarrott, et al.. (2010). Structural and Functional Characterization of Three DsbA Paralogues from Salmonella enterica Serovar Typhimurium. Journal of Biological Chemistry. 285(24). 18423–18432. 43 indexed citations
16.
Vivian, J.P., Kieran Rimmer, Simon R. Bushell, et al.. (2009). Structure and Function of the Oxidoreductase DsbA1 from Neisseria meningitidis. Journal of Molecular Biology. 394(5). 931–943. 32 indexed citations
17.
Shouldice, Stephen R., Begoña Heras, Russell Jarrott, et al.. (2009). Characterization of the DsbA Oxidative Folding Catalyst from Pseudomonas aeruginosa Reveals a Highly Oxidizing Protein that Binds Small Molecules. Antioxidants and Redox Signaling. 12(8). 921–931. 25 indexed citations
18.
Hiniker, Annie, Guoping Ren, Begoña Heras, et al.. (2007). Laboratory evolution of one disulfide isomerase to resemble another. Proceedings of the National Academy of Sciences. 104(28). 11670–11675. 27 indexed citations
19.
Heras, Begoña, Mareike Kurz, Stephen R. Shouldice, & Jennifer L. Martin. (2007). The name's bond……disulfide bond. Current Opinion in Structural Biology. 17(6). 691–698. 49 indexed citations
20.
Heras, Begoña, Mareike Kurz, Russell Jarrott, et al.. (2007). Staphylococcus aureus DsbA Does Not Have a Destabilizing Disulfide. Journal of Biological Chemistry. 283(7). 4261–4271. 55 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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