Rachel N. Austin

3.1k total citations
71 papers, 2.5k citations indexed

About

Rachel N. Austin is a scholar working on Inorganic Chemistry, Materials Chemistry and Molecular Biology. According to data from OpenAlex, Rachel N. Austin has authored 71 papers receiving a total of 2.5k indexed citations (citations by other indexed papers that have themselves been cited), including 30 papers in Inorganic Chemistry, 29 papers in Materials Chemistry and 27 papers in Molecular Biology. Recurrent topics in Rachel N. Austin's work include Metal-Catalyzed Oxygenation Mechanisms (30 papers), Porphyrin and Phthalocyanine Chemistry (12 papers) and Catalytic Processes in Materials Science (12 papers). Rachel N. Austin is often cited by papers focused on Metal-Catalyzed Oxygenation Mechanisms (30 papers), Porphyrin and Phthalocyanine Chemistry (12 papers) and Catalytic Processes in Materials Science (12 papers). Rachel N. Austin collaborates with scholars based in United States, France and Germany. Rachel N. Austin's co-authors include John T. Groves, B.G. Frederick, M. Clayton Wheeler, Dominique Mandon, Avram Gold, Lars C. Grabow, Gerben J. Zylstra, Dayi Deng, John D. Lipscomb and James Terner and has published in prestigious journals such as Journal of the American Chemical Society, Angewandte Chemie International Edition and Nature Communications.

In The Last Decade

Rachel N. Austin

69 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
Rachel N. Austin United States 30 1.0k 805 631 465 451 71 2.5k
Giorgio Gatti Italy 29 1.2k 1.2× 823 1.0× 268 0.4× 412 0.9× 244 0.5× 114 2.7k
Mei Wang China 31 1.1k 1.1× 608 0.8× 298 0.5× 142 0.3× 322 0.7× 205 3.5k
Evert C. Duin United States 32 797 0.8× 679 0.8× 1.1k 1.8× 203 0.4× 262 0.6× 74 3.0k
Shi‐Lu Chen China 33 968 0.9× 633 0.8× 814 1.3× 121 0.3× 334 0.7× 135 3.2k
Ying Yang China 26 628 0.6× 648 0.8× 177 0.3× 120 0.3× 230 0.5× 145 2.3k
Christopher Richardson Australia 27 935 0.9× 1.2k 1.5× 400 0.6× 240 0.5× 229 0.5× 107 3.4k
Sumit Bhaduri India 28 1.0k 1.0× 1.3k 1.7× 361 0.6× 91 0.2× 291 0.6× 128 3.4k
Tatsuya Oshima Japan 28 429 0.4× 383 0.5× 489 0.8× 635 1.4× 363 0.8× 171 2.6k
Henri Patin France 25 1.3k 1.3× 1000 1.2× 357 0.6× 215 0.5× 613 1.4× 110 3.8k
Danni Jiang China 26 2.2k 2.1× 1.3k 1.6× 228 0.4× 304 0.7× 744 1.6× 66 4.0k

Countries citing papers authored by Rachel N. Austin

Since Specialization
Citations

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

Fields of papers citing papers by Rachel N. Austin

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Rachel N. Austin. 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 Rachel N. Austin. The network helps show where Rachel N. Austin may publish in the future.

Co-authorship network of co-authors of Rachel N. Austin

This figure shows the co-authorship network connecting the top 25 collaborators of Rachel N. Austin. A scholar is included among the top collaborators of Rachel N. Austin 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 Rachel N. Austin. Rachel N. Austin 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.
Kulik, Heather J., et al.. (2025). Fontimonas thermophila Alkane Monooxygenase (FtAlkB) Is an Alkyl Fluoride Dehalogenase. Journal of the American Chemical Society. 147(11). 9085–9090. 2 indexed citations
2.
Samuel, Laura, Martha Abshire Saylor, Boeun Kim, et al.. (2025). Financial Strain and Child Health: Measures and Evidence From a Systematic Literature Review. AJPM Focus. 4(4). 100337–100337.
3.
Kulik, Heather J., et al.. (2025). No Bridge between Us: EXAFS and Computations Confirm Two Distant Iron Ions Comprise the Active Site of Alkane Monooxygenase (AlkB). Journal of the American Chemical Society. 147(3). 2432–2443. 2 indexed citations
4.
Börgel, Jonas, Ran Gao, David Tai Leong, et al.. (2025). Benchmarking the Reactivity of Caged Iron(IV)-Oxo Sites within Metal–Organic Frameworks. Journal of the American Chemical Society. 147(25). 21325–21330.
5.
Wilcox, Dean E., et al.. (2023). Metallothionein-3 attenuates the effect of Cu2+ ions on actin filaments. Journal of Inorganic Biochemistry. 242. 112157–112157. 6 indexed citations
6.
Shen, Yating, Jingyu Liu, Rachel N. Austin, et al.. (2023). Zinc localization and speciation in rice grain under variable soil zinc deficiency. Plant and Soil. 491(1-2). 605–626. 2 indexed citations
7.
Austin, Rachel N., et al.. (2022). An Overview of the Electron-Transfer Proteins That Activate Alkane Monooxygenase (AlkB). Frontiers in Microbiology. 13. 845551–845551. 23 indexed citations
8.
LeSauter, Joseph, et al.. (2019). Elevated zinc transporter ZnT3 in the dentate gyrus of mast cell‐deficient mice. European Journal of Neuroscience. 51(6). 1504–1513. 3 indexed citations
9.
Mahdavi‐Shakib, Akbar, Juan Manuel Arce‐Ramos, Rachel N. Austin, et al.. (2019). Frequencies and Thermal Stability of Isolated Surface Hydroxyls on Pyrogenic TiO2 Nanoparticles. The Journal of Physical Chemistry C. 123(40). 24533–24548. 43 indexed citations
10.
Banerjee, Soham, Amirali Zangiabadi, Akbar Mahdavi‐Shakib, et al.. (2019). Quantitative Structural Characterization of Catalytically Active TiO2 Nanoparticles. ACS Applied Nano Materials. 2(10). 6268–6276. 14 indexed citations
11.
Leiva‐Presa, Àngels, et al.. (2018). Pb(ii) binding to the brain specific mammalian metallothionein isoform MT3 and its isolated αMT3 and βMT3 domains. Metallomics. 11(2). 349–361. 13 indexed citations
12.
Hsieh, Chun H., et al.. (2017). The Enigmatic P450 Decarboxylase OleT Is Capable of, but Evolved To Frustrate, Oxygen Rebound Chemistry. Biochemistry. 56(26). 3347–3357. 62 indexed citations
13.
Nelson, Ryan C., Byeongjin Baek, Pamela Ruíz, et al.. (2015). Experimental and Theoretical Insights into the Hydrogen-Efficient Direct Hydrodeoxygenation Mechanism of Phenol over Ru/TiO2. ACS Catalysis. 5(11). 6509–6523. 248 indexed citations
14.
Zhou, Xiaobo, I. Tyrone Ghampson, Rachel A. Pollock, et al.. (2014). Effects of support identity and metal dispersion in supported ruthenium hydrodeoxygenation catalysts. Applied Catalysis A General. 477. 64–74. 161 indexed citations
15.
Austin, Rachel N. & John T. Groves. (2011). Alkane-oxidizing metalloenzymes in the carbon cycle. Metallomics. 3(8). 775–775. 59 indexed citations
16.
Austin, Rachel N., Dayi Deng, Yongying Jiang, et al.. (2006). The Diagnostic Substrate Bicyclohexane Reveals a Radical Mechanism for Bacterial Cytochrome P450 in Whole Cells. Angewandte Chemie International Edition. 45(48). 8192–8194. 29 indexed citations
17.
Bertrand, Étienne, R.R. Sakai, Luke A. Moe, et al.. (2005). Reaction mechanisms of non-heme diiron hydroxylases characterized in whole cells. Journal of Inorganic Biochemistry. 99(10). 1998–2006. 34 indexed citations
18.
Ramachandran, Prashanth, et al.. (1996). Role of O-acetyltransferase in activation of oxidised metabolites of the genotoxic environmental pollutant 1-nitropyrene. Mutation Research/Genetic Toxicology. 369(3-4). 209–220. 10 indexed citations
19.
Ochsenbein, Philippe, Dominique Mandon, Jean Fischer, et al.. (1993). Das Oxoferryl‐π‐Radikalkation von meso‐Tetramesitylporphyrin mit achtfach in β‐Stellung chlorierten Pyrroleinheiten: elektronische und strukturelle Eigenschaften. Angewandte Chemie. 105(10). 1504–1505. 3 indexed citations
20.
Steward, W.P., et al.. (1988). Phase I study of recombinant DNA granulocyte macrophage colony stimulating factor.. PubMed. 324–6. 6 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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