Robert J. Falconer

3.4k total citations · 1 hit paper
75 papers, 2.6k citations indexed

About

Robert J. Falconer is a scholar working on Molecular Biology, Food Science and Atomic and Molecular Physics, and Optics. According to data from OpenAlex, Robert J. Falconer has authored 75 papers receiving a total of 2.6k indexed citations (citations by other indexed papers that have themselves been cited), including 35 papers in Molecular Biology, 13 papers in Food Science and 10 papers in Atomic and Molecular Physics, and Optics. Recurrent topics in Robert J. Falconer's work include Protein purification and stability (13 papers), Protein Structure and Dynamics (10 papers) and Spectroscopy and Quantum Chemical Studies (10 papers). Robert J. Falconer is often cited by papers focused on Protein purification and stability (13 papers), Protein Structure and Dynamics (10 papers) and Spectroscopy and Quantum Chemical Studies (10 papers). Robert J. Falconer collaborates with scholars based in Australia, United Kingdom and United States. Robert J. Falconer's co-authors include Jordan W. Bye, Brett M. Collins, Anton P. J. Middelberg, Andrea Markelz, Jacqui M. McRae, Xing Wang, Yun Liu, Guangze Yang, Chun‐Xia Zhao and Letao Xu and has published in prestigious journals such as Journal of Biological Chemistry, SHILAP Revista de lepidopterología and Analytical Chemistry.

In The Last Decade

Robert J. Falconer

72 papers receiving 2.6k 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.

Lipid Nanoparticles for Drug Delivery

2021 346 citations Robert J. Falconer et al. profile →

Peers

Robert J. Falconer

BIOMA

EEE

Yuriy F. Zuev Russia

Aichun Dong United States

Kentaro Shiraki Japan

Roberto D. Lins Brazil

Anna K. H. Hirsch Germany

Rajiv Bhat India

José Luis R. Arrondo Spain

Mariusz Gagoś Poland

Álvaro Ortega Spain

Maarten R. Egmond Netherlands

Yuriy F. Zuev Russia

Robert J. Falconer

920 ×0.8

569 ×1.0

272 ×0.8

443 ×1.4

BIOMA

146 ×0.5

EEE

Citations per year, relative to Robert J. Falconer Robert J. Falconer (= 1×) peers Yuriy F. Zuev

Countries citing papers authored by Robert J. Falconer

Since Specialization

Citations

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

Fields of papers citing papers by Robert J. Falconer

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Robert J. Falconer. 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 Robert J. Falconer. The network helps show where Robert J. Falconer may publish in the future.

Co-authorship network of co-authors of Robert J. Falconer

This figure shows the co-authorship network connecting the top 25 collaborators of Robert J. Falconer. A scholar is included among the top collaborators of Robert J. Falconer 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 Robert J. Falconer. Robert J. Falconer 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

Falconer, Robert J., et al.. (2025). The effect of gelatinisation and enzymatic hydrolysis methods on the starch, sugar and physicochemical profiles of faba bean milk. International Journal of Biological Macromolecules. 304(Pt 2). 140898–140898. 1 indexed citations

Besford, Quinn A., et al.. (2024). Interactions between small organic molecules and water measured using pressure perturbation calorimetry. Journal of Thermal Analysis and Calorimetry. 149(17). 9223–9231. 1 indexed citations

Evans, Jack D., Francesco Carraro, Heinz Amenitsch, et al.. (2023). Protein-induced modifications in crystal morphology of a hydrogen-bonded organic framework. Journal of Materials Chemistry A. 11(42). 23026–23033. 6 indexed citations

Mousavi, Ehsan, et al.. (2021). Design and in-vitro testing of a portable patient isolation chamber for bedside aerosol containment and filtration. Building and Environment. 207. 108467–108467. 3 indexed citations

Falconer, Robert J.. (2019). Advances in liquid formulations of parenteral therapeutic proteins. Biotechnology Advances. 37(7). 107412–107412. 57 indexed citations

Watrelot, Aude A., Martin Day, Alex Schulkin, et al.. (2019). Oxygen exposure during red wine fermentation modifies tannin reactivity with poly-l-proline. Food Chemistry. 297. 124923–124923. 12 indexed citations

Falconer, Robert J., et al.. (2016). Control of Globular Protein Thermal Stability in Aqueous Formulations by the Positively Charged Amino Acid Excipients. Journal of Pharmaceutical Sciences. 105(12). 3532–3536. 13 indexed citations

Bye, Jordan W., et al.. (2016). Analysis of Mesoscopic Structured 2-Propanol/Water Mixtures Using Pressure Perturbation Calorimetry and Molecular Dynamic Simulation. Journal of Solution Chemistry. 46(1). 175–189. 8 indexed citations

Falconer, Robert J., et al.. (2015). Controlling protein stability: Mechanisms revealed using formulations of arginine, glycine and guanidinium HCl with three globular proteins. International Journal of Pharmaceutics. 486(1-2). 131–135. 54 indexed citations

10.

Downey, Mark O., et al.. (2015). The complexity of condensed tannin binding to bovine serum albumin – An isothermal titration calorimetry study. Food Chemistry. 190. 173–178. 47 indexed citations

11.

Wallace, Vincent P., Denis Férachou, Shahid Uddin, et al.. (2015). Modulation of the Hydration Water Around Monoclonal Antibodies on Addition of Excipients Detected by Terahertz Time-Domain Spectroscopy. Journal of Pharmaceutical Sciences. 104(12). 4025–4033. 14 indexed citations

12.

Bye, Jordan W., et al.. (2014). Biopharmaceutical liquid formulation: a review of the science of protein stability and solubility in aqueous environments. Biotechnology Letters. 36(5). 869–875. 51 indexed citations

13.

Ding, Tao, Ruoyu Li, J. Axel Zeitler, et al.. (2010). Terahertz and far infrared Spectroscopy of alanine-rich peptides having variable ellipticity. Optics Express. 18(26). 27431–27431. 49 indexed citations

14.

Falconer, Robert J. & Brett M. Collins. (2010). Survey of the year 2009: applications of isothermal titration calorimetry. Journal of Molecular Recognition. 24(1). 1–16. 50 indexed citations

15.

Falconer, Robert J., Anita Penkova, Ilian Jelesarov, & Brett M. Collins. (2010). Survey of the year 2008: applications of isothermal titration calorimetry. Journal of Molecular Recognition. 23(5). 395–413. 51 indexed citations

16.

Kaar, Waltraud, Yu Fan, Bijun Zeng, et al.. (2008). Microbial bio‐production of a recombinant stimuli‐responsive biosurfactant. Biotechnology and Bioengineering. 102(1). 176–187. 15 indexed citations

17.

Kaar, Waltraud, et al.. (2008). Expression and purification of a nanostructure-forming peptide. Journal of Biotechnology. 135(1). 85–91. 14 indexed citations

18.

Zaccai, Nathan R., et al.. (2006). Assembly of Human Papillomavirus Type-16 Virus-Like Particles: Multifactorial Study of Assembly and Competing Aggregation. Biotechnology Progress. 22(2). 554–560. 29 indexed citations

19.

Falconer, Robert J., Brian K. O’Neill, & Anton P. J. Middelberg. (1999). Chemical treatment ofEscherichia coli: 3. Selective extraction of a recombinant protein from cytoplasmic inclusion bodies in intact cells. Biotechnology and Bioengineering. 62(4). 455–460. 35 indexed citations

20.

Falconer, Robert J.. (1988). Radiographic Evaluation of Ankle Trauma. Clinics in Podiatric Medicine and Surgery. 5(4). 877–891. 3 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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