Mary Christie

811 total citations
21 papers, 583 citations indexed

About

Mary Christie is a scholar working on Molecular Biology, Radiology, Nuclear Medicine and Imaging and Infectious Diseases. According to data from OpenAlex, Mary Christie has authored 21 papers receiving a total of 583 indexed citations (citations by other indexed papers that have themselves been cited), including 16 papers in Molecular Biology, 4 papers in Radiology, Nuclear Medicine and Imaging and 3 papers in Infectious Diseases. Recurrent topics in Mary Christie's work include RNA Research and Splicing (7 papers), RNA and protein synthesis mechanisms (5 papers) and Glycosylation and Glycoproteins Research (4 papers). Mary Christie is often cited by papers focused on RNA Research and Splicing (7 papers), RNA and protein synthesis mechanisms (5 papers) and Glycosylation and Glycoproteins Research (4 papers). Mary Christie collaborates with scholars based in Australia, Germany and United Kingdom. Mary Christie's co-authors include Alastair G. Stewart, Boštjan Kobe, Jade K. Forwood, Elisa Izaurralde, Eric Huntzinger, Oliver Weichenrieder, Gergely Róna, Beáta G. Vértessy, Chiung-Wen Chang and Andreas Boland and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Molecular Cell.

In The Last Decade

Mary Christie

21 papers receiving 576 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Mary Christie Australia 10 504 73 64 57 45 21 583
Sarah L. Irons United Kingdom 11 539 1.1× 96 1.3× 115 1.8× 73 1.3× 31 0.7× 19 710
Christophe Caillat France 18 442 0.9× 68 0.9× 23 0.4× 131 2.3× 79 1.8× 20 601
Wen Deng China 13 534 1.1× 67 0.9× 37 0.6× 103 1.8× 144 3.2× 28 777
Thomas Zögg Belgium 9 374 0.7× 106 1.5× 15 0.2× 29 0.5× 26 0.6× 16 560
Jonathan J. Ellis Australia 10 678 1.3× 36 0.5× 24 0.4× 40 0.7× 44 1.0× 14 801
Cristina Puchades United States 8 614 1.2× 65 0.9× 21 0.3× 118 2.1× 47 1.0× 8 748
Nikolay Dobrev Germany 6 382 0.8× 66 0.9× 37 0.6× 14 0.2× 75 1.7× 8 471
Jeffrey G. Marblestone 8 515 1.0× 76 1.0× 21 0.3× 47 0.8× 20 0.4× 11 607
Madalena Renouard France 12 583 1.2× 28 0.4× 97 1.5× 29 0.5× 31 0.7× 15 679
Pawel Listwan Australia 12 459 0.9× 82 1.1× 15 0.2× 63 1.1× 18 0.4× 17 553

Countries citing papers authored by Mary Christie

Since Specialization
Citations

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

Fields of papers citing papers by Mary Christie

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Mary Christie

This figure shows the co-authorship network connecting the top 25 collaborators of Mary Christie. A scholar is included among the top collaborators of Mary Christie 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 Mary Christie. Mary Christie 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.
Zekri, Latifa, Ilona Hagelstein, Melanie Märklin, et al.. (2024). Immunocytokines with target cell–restricted IL-15 activity for treatment of B cell malignancies. Science Translational Medicine. 16(737). eadh1988–eadh1988. 6 indexed citations
2.
Sobti, Meghna, et al.. (2023). Molecular basis for GIGYF–TNRC6 complex assembly. RNA. 29(6). 724–734. 5 indexed citations
3.
Franck, Charlotte, Karishma Patel, Louise J. Walport, et al.. (2023). Discovery and characterization of cyclic peptides selective for the C-terminal bromodomains of BET family proteins. Structure. 31(8). 912–923.e4. 5 indexed citations
4.
Franck, Charlotte, Anupriya Aggarwal, Karishma Patel, et al.. (2023). Discovery of High Affinity Cyclic Peptide Ligands for Human ACE2 with SARS-CoV-2 Entry Inhibitory Activity. ACS Chemical Biology. 19(1). 141–152. 6 indexed citations
5.
Zekri, Latifa, Natalia Ruétalo, Mary Christie, et al.. (2023). Novel ACE2 fusion protein with adapting activity against SARS-CoV-2 variants in vitro. Frontiers in Immunology. 14. 1112505–1112505. 4 indexed citations
6.
Holtkamp, Hannah U., Satya Amirapu, Irene Low, et al.. (2022). Real-time optical diagnosis of prostate cancer: a clinical study on fresh biopsy cores. 18–18. 1 indexed citations
7.
Christie, Mary & Cátia Igreja. (2021). eIF4E‐homologous protein (4EHP): a multifarious cap‐binding protein. FEBS Journal. 290(2). 266–285. 20 indexed citations
8.
Norman, Alexander, Charlotte Franck, Mary Christie, et al.. (2021). Discovery of Cyclic Peptide Ligands to the SARS-CoV-2 Spike Protein Using mRNA Display. ACS Central Science. 7(6). 1001–1008. 49 indexed citations
9.
Sobti, Meghna, Robert Ishmukhametov, James C. Bouwer, et al.. (2019). Cryo-EM reveals distinct conformations of E. coli ATP synthase on exposure to ATP. eLife. 8. 43 indexed citations
10.
Langley, D.B., Peter Schofield, Jennifer Jackson, et al.. (2019). Human Antibody Bispecifics through Phage Display Selection. Biochemistry. 58(13). 1701–1704. 6 indexed citations
11.
Langley, David B., Ben Crossett, Peter Schofield, et al.. (2017). Structural basis of antigen recognition: crystal structure of duck egg lysozyme. Acta Crystallographica Section D Structural Biology. 73(11). 910–920. 7 indexed citations
12.
Stewart, Alastair G., et al.. (2017). Structural characterisation of TNRC6A nuclear localisation signal in complex with importin-alpha. PLoS ONE. 12(8). e0183587–e0183587. 8 indexed citations
13.
Rouet, Romain, David B. Langley, Peter Schofield, et al.. (2017). Structural reconstruction of protein ancestry. Proceedings of the National Academy of Sciences. 114(15). 3897–3902. 9 indexed citations
14.
Allen, Mark D., Mary Christie, Peter M. Jones, et al.. (2015). Solution structure of a soluble fragment derived from a membrane protein by shotgun proteolysis. Protein Engineering Design and Selection. 28(10). 445–450. 6 indexed citations
15.
Rouet, Romain, Kip Dudgeon, Mary Christie, David B. Langley, & Daniel Christ. (2015). Fully Human VH Single Domains That Rival the Stability and Cleft Recognition of Camelid Antibodies. Journal of Biological Chemistry. 290(19). 11905–11917. 48 indexed citations
16.
Christie, Mary, Chiung-Wen Chang, Gergely Róna, et al.. (2015). Structural Biology and Regulation of Protein Import into the Nucleus. Journal of Molecular Biology. 428(10). 2060–2090. 187 indexed citations
17.
Jonas, Stefanie, Mary Christie, Daniel Peter, et al.. (2014). An asymmetric PAN3 dimer recruits a single PAN2 exonuclease to mediate mRNA deadenylation and decay. Nature Structural & Molecular Biology. 21(7). 599–608. 38 indexed citations
18.
Róna, Gergely, Máté Borsos, Jonathan J. Ellis, et al.. (2014). Dynamics of re-constitution of the human nuclear proteome after cell division is regulated by NLS-adjacent phosphorylation. Cell Cycle. 13(22). 3551–3564. 18 indexed citations
19.
Christie, Mary, Andreas Boland, Eric Huntzinger, Oliver Weichenrieder, & Elisa Izaurralde. (2013). Structure of the PAN3 Pseudokinase Reveals the Basis for Interactions with the PAN2 Deadenylase and the GW182 Proteins. Molecular Cell. 51(3). 360–373. 83 indexed citations
20.
Christie, Mary, et al.. (2013). Structural Characterisation of the Nuclear Import Receptor Importin Alpha in Complex with the Bipartite NLS of Prp20. PLoS ONE. 8(12). e82038–e82038. 28 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.

Explore authors with similar magnitude of impact

Rankless by CCL
2026