Agata Rekas

1.6k total citations
30 papers, 1.3k citations indexed

About

Agata Rekas is a scholar working on Molecular Biology, Physiology and Materials Chemistry. According to data from OpenAlex, Agata Rekas has authored 30 papers receiving a total of 1.3k indexed citations (citations by other indexed papers that have themselves been cited), including 14 papers in Molecular Biology, 8 papers in Physiology and 8 papers in Materials Chemistry. Recurrent topics in Agata Rekas's work include Heat shock proteins research (8 papers), Enzyme Structure and Function (8 papers) and Alzheimer's disease research and treatments (7 papers). Agata Rekas is often cited by papers focused on Heat shock proteins research (8 papers), Enzyme Structure and Function (8 papers) and Alzheimer's disease research and treatments (7 papers). Agata Rekas collaborates with scholars based in Australia, United States and United Kingdom. Agata Rekas's co-authors include John A. Carver, David C. Thorn, Mark R. Wilson, Roberto Cappai, Margaret Sunde, Jean‐René Alattia, Atsushi Miyawaki, Mitsuhiko Ikura, Takeharu Nagai and Kevin J. Barnham and has published in prestigious journals such as Journal of Biological Chemistry, Journal of Molecular Biology and Biochemistry.

In The Last Decade

Agata Rekas

29 papers receiving 1.3k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Agata Rekas Australia	16	871	312	220	195	184	30	1.3k
Erica Frare Italy	18	1.2k 1.4×	588 1.9×	206 0.9×	168 0.9×	182 1.0×	23	1.7k
Keith A. Oberg United States	13	960 1.1×	458 1.5×	99 0.5×	122 0.6×	97 0.5×	20	1.5k
Irantzu Pallarès Spain	19	972 1.1×	357 1.1×	160 0.7×	122 0.6×	109 0.6×	44	1.4k
Douglas M. Fowler United States	7	1.6k 1.8×	1.0k 3.3×	112 0.5×	520 2.7×	178 1.0×	10	2.3k
Amol Pawar United Kingdom	7	1.2k 1.3×	798 2.6×	98 0.4×	156 0.8×	143 0.8×	9	1.5k
Chi L.L. Pham Australia	25	926 1.1×	844 2.7×	73 0.3×	131 0.7×	483 2.6×	48	1.8k
Jesper Søndergaard Pedersen Denmark	15	830 1.0×	467 1.5×	84 0.4×	120 0.6×	63 0.3×	17	1.3k
Rita P.‐Y. Chen Taiwan	21	797 0.9×	299 1.0×	49 0.2×	67 0.3×	106 0.6×	55	1.2k
John Goers United States	17	674 0.8×	449 1.4×	114 0.5×	141 0.7×	418 2.3×	24	1.6k
Rajaraman Krishnan United States	13	1.5k 1.7×	582 1.9×	47 0.2×	152 0.8×	120 0.7×	17	1.7k

Countries citing papers authored by Agata Rekas

Since Specialization

Citations

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

Fields of papers citing papers by Agata Rekas

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Agata Rekas

This figure shows the co-authorship network connecting the top 25 collaborators of Agata Rekas. A scholar is included among the top collaborators of Agata Rekas 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 Agata Rekas. Agata Rekas 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

Melton, Laurence D., Shinji Kihara, Amy Y. Xu, et al.. (2025). Measured effect of encapsulation and freeze-drying on the structural organisation of β-Lactoglobulin–pectin complex coacervates with curcumin and folic acid. Food Chemistry. 491. 145208–145208. 1 indexed citations

Balu, Rajkamal, et al.. (2024). A controlled co-assembly approach to tune temperature responsiveness of biomimetic proteins. Journal of Materials Chemistry B. 13(4). 1302–1315.

Balu, Rajkamal, Jitendra Mata, Agata Rekas, et al.. (2022). Crowder-directed interactions and conformational dynamics in multistimuli-responsive intrinsically disordered protein. Science Advances. 8(51). eabq2202–eabq2202. 9 indexed citations

Duff, Anthony P., Tamim A. Darwish, Anwen M. Krause‐Heuer, et al.. (2022). Deuteration for biological SANS: Case studies, success and challenges in chemistry and biology. Methods in enzymology on CD-ROM/Methods in enzymology. 677. 85–126. 4 indexed citations

Rekas, Agata, et al.. (2020). The Aggregation of αB-Crystallin under Crowding Conditions Is Prevented by αA-Crystallin: Implications for α-Crystallin Stability and Lens Transparency. Journal of Molecular Biology. 432(20). 5593–5613. 11 indexed citations

Xu, Amy Y., Laurence D. Melton, Timothy J. Ryan, et al.. (2017). Sugar-coated proteins: the importance of degree of polymerisation of oligo-galacturonic acid on protein binding and aggregation. Soft Matter. 13(14). 2698–2707. 10 indexed citations

Duff, Anthony P., et al.. (2015). Robust High-Yield Methodologies for 2H and 2H/15N/13C Labeling of Proteins for Structural Investigations Using Neutron Scattering and NMR. Methods in enzymology on CD-ROM/Methods in enzymology. 565. 3–25. 41 indexed citations

Curtain, Cyril C., Nigel Kirby, Haydyn D. T. Mertens, et al.. (2014). Alpha-synuclein oligomers and fibrils originate in two distinct conformer pools: a small angle X-ray scattering and ensemble optimisation modelling study. Molecular BioSystems. 11(1). 190–196. 21 indexed citations

Esposito, Gennaro, Megan Garvey, Alessandra Corazza, et al.. (2013). Monitoring the Interaction between beta(2)-Microglobulin and the Molecular Chaperone alpha B-crystallin by NMR and Mass Spectrometry alpha B-CRYSTALLIN DISSOCIATES beta(2)-MICROGLOBULIN OLIGOMERS. UCL Discovery (University College London). 2 indexed citations

10.

Esposito, Gennaro, Megan Garvey, Vera Alverdi, et al.. (2013). Monitoring the Interaction between β2-Microglobulin and the Molecular Chaperone αB-crystallin by NMR and Mass Spectrometry. Journal of Biological Chemistry. 288(24). 17844–17858. 30 indexed citations

11.

Rekas, Agata, Keun Jae Ahn, Jongsun Kim, & John A. Carver. (2012). The chaperone activity of α‐synuclein: Utilizing deletion mutants to map its interaction with target proteins. Proteins Structure Function and Bioinformatics. 80(5). 1316–1325. 24 indexed citations

12.

Benesch, Justin L. P., J. Andrew Aquilina, Andrew J. Baldwin, et al.. (2010). The Quaternary Organization and Dynamics of the Molecular Chaperone HSP26 Are Thermally Regulated. Chemistry & Biology. 17(9). 1008–1017. 35 indexed citations

13.

Rekas, Agata, Robert Knott, Anna Sokolova, et al.. (2010). The structure of dopamine induced α-synuclein oligomers. European Biophysics Journal. 39(10). 1407–1419. 80 indexed citations

14.

Treweek, Teresa M., Agata Rekas, Mark J. Walker, & John A. Carver. (2010). A quantitative NMR spectroscopic examination of the flexibility of the C-terminal extensions of the molecular chaperones, αA- and αB-crystallin. Experimental Eye Research. 91(5). 691–699. 49 indexed citations

15.

Rekas, Agata, Victor Lo, Geoffrey Michael Gadd, Roberto Cappai, & Seok Il Yun. (2008). PAMAM Dendrimers as Potential Agents against Fibrillation ofα‐Synuclein, a Parkinson's Disease‐Related Protein. Macromolecular Bioscience. 9(3). 230–238. 58 indexed citations

16.

Rekas, Agata, Lucy Jankova, David C. Thorn, Roberto Cappai, & John A. Carver. (2007). Monitoring the prevention of amyloid fibril formation by α‐crystallin. FEBS Journal. 274(24). 6290–6304. 64 indexed citations

17.

Ghahghaei, Arezou, Agata Rekas, William E. Price, & John A. Carver. (2006). The effect of dextran on subunit exchange of the molecular chaperone αA-crystallin. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1774(1). 102–111. 23 indexed citations

18.

Treweek, Teresa M., Agata Rekas, Robyn A. Lindner, et al.. (2005). R120G αB‐crystallin promotes the unfolding of reduced α‐lactalbumin and is inherently unstable. FEBS Journal. 272(3). 711–724. 71 indexed citations

19.

Rekas, Agata, Christopher G. Adda, J. Andrew Aquilina, et al.. (2004). Interaction of the Molecular Chaperone αB-Crystallin with α-Synuclein: Effects on Amyloid Fibril Formation and Chaperone Activity. Journal of Molecular Biology. 340(5). 1167–1183. 191 indexed citations

20.

Carver, John A., Agata Rekas, David C. Thorn, & Mark R. Wilson. (2003). Small Heat‐shock Proteins and Clusterin: Intra‐ and Extracellular Molecular Chaperones with a Common Mechanism of Action and Function?. IUBMB Life. 55(12). 661–668. 163 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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