Maureen Higgins

4.1k total citations
50 papers, 1.6k citations indexed

About

Maureen Higgins is a scholar working on Molecular Biology, Oncology and Organic Chemistry. According to data from OpenAlex, Maureen Higgins has authored 50 papers receiving a total of 1.6k indexed citations (citations by other indexed papers that have themselves been cited), including 37 papers in Molecular Biology, 14 papers in Oncology and 13 papers in Organic Chemistry. Recurrent topics in Maureen Higgins's work include Genomics, phytochemicals, and oxidative stress (24 papers), Cancer-related Molecular Pathways (10 papers) and Bioactive Compounds and Antitumor Agents (7 papers). Maureen Higgins is often cited by papers focused on Genomics, phytochemicals, and oxidative stress (24 papers), Cancer-related Molecular Pathways (10 papers) and Bioactive Compounds and Antitumor Agents (7 papers). Maureen Higgins collaborates with scholars based in United Kingdom, United States and Sweden. Maureen Higgins's co-authors include Sonia Laı́n, Johanna Campbell, Albena T. Dinkova‐Kostova, David P. Lane, Anna R. McCarthy, Nicholas J. Westwood, Alastair M. Thompson, Oliver Staples, Jonathan J. Hollick and Virginia Appleyard and has published in prestigious journals such as Journal of Biological Chemistry, Brain and Cancer Cell.

In The Last Decade

Maureen Higgins

49 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
Maureen Higgins United Kingdom 21 1.0k 445 348 298 214 50 1.6k
Kheem S. Bisht United States 23 1.4k 1.4× 264 0.6× 594 1.7× 375 1.3× 64 0.3× 33 2.4k
Michelle Barbi de Moura United States 16 1.2k 1.2× 281 0.6× 84 0.2× 228 0.8× 83 0.4× 17 2.0k
Birgit Heltweg Germany 10 716 0.7× 252 0.6× 840 2.4× 390 1.3× 88 0.4× 11 1.4k
M. Gertz Germany 16 974 1.0× 219 0.5× 1.1k 3.1× 617 2.1× 127 0.6× 19 2.0k
Barry D. Gehm United States 17 937 0.9× 260 0.6× 521 1.5× 75 0.3× 54 0.3× 20 1.8k
Jintang Du China 18 1.3k 1.3× 445 1.0× 1.3k 3.9× 758 2.5× 166 0.8× 24 2.8k
Chuan‐Ming Xie China 18 738 0.7× 187 0.4× 44 0.1× 228 0.8× 81 0.4× 42 1.3k
Paola Perucca Italy 12 542 0.5× 196 0.4× 290 0.8× 49 0.2× 105 0.5× 20 904
Ekaterina Bobrovnikova-Marjon United States 16 1.5k 1.4× 214 0.5× 91 0.3× 822 2.8× 52 0.2× 18 2.6k

Countries citing papers authored by Maureen Higgins

Since Specialization
Citations

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

Fields of papers citing papers by Maureen Higgins

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Maureen Higgins

This figure shows the co-authorship network connecting the top 25 collaborators of Maureen Higgins. A scholar is included among the top collaborators of Maureen Higgins 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 Maureen Higgins. Maureen Higgins 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.
Walker, David, Maureen Higgins, Tomasz Wenta, et al.. (2025). Identification of a BACH1 lung cancer signature: A novel tool for understanding BACH1 biology and identifying new inhibitors. Redox Biology. 85. 103789–103789. 1 indexed citations
2.
Naidu, Sharadha Dayalan, Abel D. Ang, Carole Yee, et al.. (2025). CD5L is a target of transcription factor Nrf2. PubMed. 776. 152225–152225.
3.
Soliman, Aiten M., Mostafa M. Ghorab, Maureen Higgins, et al.. (2025). NQO1 induction and radiation-based biodistribution study of a new quinoline derivative identified in a screen of 6,8-diiodoquinazolinone sulfonamide conjugates. European Journal of Medicinal Chemistry. 296. 117855–117855. 1 indexed citations
4.
Georgakopoulos, Nikolaos, Sandeep K. Talapatra, Dina Dikovskaya, et al.. (2022). Phenyl Bis-Sulfonamide Keap1-Nrf2 Protein–Protein Interaction Inhibitors with an Alternative Binding Mode. Journal of Medicinal Chemistry. 65(10). 7380–7398. 19 indexed citations
5.
Roth, Kevin A., Elena V. Knatko, Maureen Higgins, et al.. (2021). Clinically relevant aberrant Filip1l DNA methylation detected in a murine model of cutaneous squamous cell carcinoma. EBioMedicine. 67. 103383–103383. 6 indexed citations
6.
Naidu, Sharadha Dayalan, Takafumi Suzuki, Dina Dikovskaya, et al.. (2021). The isoquinoline PRL-295 increases the thermostability of Keap1 and disrupts its interaction with Nrf2. iScience. 25(1). 103703–103703. 20 indexed citations
7.
Soliman, Aiten M., et al.. (2020). Radiomodulatory effect of a non-electrophilic NQO1 inducer identified in a screen of new 6, 8-diiodoquinazolin-4(3H)-ones carrying a sulfonamide moiety. European Journal of Medicinal Chemistry. 200. 112467–112467. 20 indexed citations
8.
Caldwell, Stuart T., Maureen Higgins, Takafumi Suzuki, et al.. (2020). Nrf2 is activated by disruption of mitochondrial thiol homeostasis but not by enhanced mitochondrial superoxide production. Journal of Biological Chemistry. 296. 100169–100169. 33 indexed citations
9.
Arafa, Reem K., et al.. (2016). NAD(P)H:quinone oxidoreductase 1 inducer activity of some novel anilinoquinazoline derivatives. Drug Design Development and Therapy. Volume 10. 2515–2524. 5 indexed citations
10.
Ghorab, Mostafa M., Mansour S. Alsaid, Marwa G. El‐Gazzar, et al.. (2016). NAD(P)H: quinone oxidoreductase 1 inducer activity of novel 4-aminoquinazoline derivatives. Journal of Enzyme Inhibition and Medicinal Chemistry. 31(6). 1369–1374. 3 indexed citations
11.
Hamed, Ahmed R., Tarik A. Mohamed, Emad M. Hassan, et al.. (2016). Bioactive polymethoxylated flavonoids from Chiliadenus montanus. Journal of chemical and pharmaceutical research. 8(3). 788–793. 7 indexed citations
12.
Knatko, Elena V., Sally H. Ibbotson, Ying Zhang, et al.. (2015). Nrf2 Activation Protects against Solar-Simulated Ultraviolet Radiation in Mice and Humans. Cancer Prevention Research. 8(6). 475–486. 95 indexed citations
13.
Alsaid, Mansour S., Mostafa M. Ghorab, Maureen Higgins, Albena T. Dinkova‐Kostova, & Abdelaaty A. Shahat. (2015). NAD(P)H: Quinone Oxidoreductase 1 inducer activity of some enaminone derivatives.. Discovery Research Portal (University of Dundee). 26(1). 7–12. 5 indexed citations
14.
Ghorab, Mostafa M., Maureen Higgins, Mansour S. Alsaid, et al.. (2014). Synthesis, molecular modeling and NAD(P)H:quinone oxidoreductase 1 inducer activity of novel cyanoenone and enone benzenesulfonamides. Journal of Enzyme Inhibition and Medicinal Chemistry. 29(6). 840–845. 7 indexed citations
15.
McCarthy, Anna R., Maureen Higgins, Johanna Campbell, et al.. (2013). Tenovin-D3, a Novel Small-Molecule Inhibitor of Sirtuin SirT2, Increases p21 ( CDKN1A ) Expression in a p53-Independent Manner. Molecular Cancer Therapeutics. 12(4). 352–360. 36 indexed citations
16.
Leeuwen, Ingeborg M.M. van, et al.. (2013). Modulation of p53 C-Terminal Acetylation by mdm2, p14ARF, and Cytoplasmic SirT2. Molecular Cancer Therapeutics. 12(4). 471–480. 30 indexed citations
17.
Drummond, Catherine J., et al.. (2013). Incompatible effects of p53 and HDAC inhibition on p21 expression and cell cycle progression. Cell Death and Disease. 4(3). e533–e533. 33 indexed citations
18.
Staples, Oliver, Jonathan J. Hollick, Johanna Campbell, et al.. (2008). Characterization, chemical optimization and anti-tumor activity of a tubulin poison identified by a p53-based phenotypic screen. Cell Cycle. 7(21). 3417–3427. 12 indexed citations
19.
Laı́n, Sonia, Jonathan J. Hollick, Johanna Campbell, et al.. (2007). Discovery, in vivo activity, and mechanism of action of a small-molecule p53 activator. Molecular Cancer Therapeutics. 6(12). 3 indexed citations
20.
Ménendez, Sergio, et al.. (2003). Nuclear export inhibitor leptomycin B induces the appearance of novel forms of human Mdm2 protein. British Journal of Cancer. 88(4). 636–643. 11 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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