Melissa Call

1.7k total citations
37 papers, 984 citations indexed

About

Melissa Call is a scholar working on Molecular Biology, Immunology and Oncology. According to data from OpenAlex, Melissa Call has authored 37 papers receiving a total of 984 indexed citations (citations by other indexed papers that have themselves been cited), including 19 papers in Molecular Biology, 18 papers in Immunology and 7 papers in Oncology. Recurrent topics in Melissa Call's work include T-cell and B-cell Immunology (14 papers), Immune Cell Function and Interaction (13 papers) and Lipid Membrane Structure and Behavior (7 papers). Melissa Call is often cited by papers focused on T-cell and B-cell Immunology (14 papers), Immune Cell Function and Interaction (13 papers) and Lipid Membrane Structure and Behavior (7 papers). Melissa Call collaborates with scholars based in Australia, United States and United Kingdom. Melissa Call's co-authors include Matthew E. Call, Kai W. Wucherpfennig, Monika‐Sarah E. D. Schulze, Raphael Trenker, Étienne Gagnon, Eric S. Huseby, Dhruv K. Sethi, Jason W. Pyrdol, Wouter Pos and Lu Deng and has published in prestigious journals such as Cell, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Melissa Call

34 papers receiving 972 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Melissa Call Australia 17 556 389 188 124 65 37 984
Gundo Diedrich United States 15 525 0.9× 530 1.4× 305 1.6× 102 0.8× 67 1.0× 28 1.1k
Janet A. Fennelly United Kingdom 12 646 1.2× 439 1.1× 380 2.0× 172 1.4× 72 1.1× 13 1.3k
Natalia Sigal United States 12 759 1.4× 526 1.4× 170 0.9× 38 0.3× 64 1.0× 22 1.2k
Shinji Ikemizu United Kingdom 10 822 1.5× 353 0.9× 389 2.1× 160 1.3× 75 1.2× 11 1.4k
Jeanmarie Guenot United States 13 370 0.7× 363 0.9× 179 1.0× 213 1.7× 61 0.9× 19 824
Gordon Powers United States 14 526 0.9× 423 1.1× 223 1.2× 275 2.2× 48 0.7× 25 1.1k
Gabriele Matschiner Germany 14 383 0.7× 517 1.3× 123 0.7× 200 1.6× 58 0.9× 25 950
Jean‐Baptiste Reiser France 12 770 1.4× 272 0.7× 144 0.8× 178 1.4× 31 0.5× 29 1.0k
Sara Venturini United States 9 279 0.5× 458 1.2× 94 0.5× 169 1.4× 43 0.7× 11 865
Sri H. Ramarathinam Australia 19 631 1.1× 741 1.9× 308 1.6× 241 1.9× 68 1.0× 42 1.1k

Countries citing papers authored by Melissa Call

Since Specialization
Citations

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

Fields of papers citing papers by Melissa Call

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Melissa Call

This figure shows the co-authorship network connecting the top 25 collaborators of Melissa Call. A scholar is included among the top collaborators of Melissa Call 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 Melissa Call. Melissa Call 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.
Ramsey, Jolene, J. C. K. Tovey, Daniel Cameron, et al.. (2025). Resolution of a T1-Like Bacteriophage Outbreak by Receptor Engineering. Molecular Biotechnology.
2.
Kuchel, Nathan W., Bernadine G.C. Lu, Kym N. Lowes, et al.. (2024). Mutational profiling of SARS-CoV-2 papain-like protease reveals requirements for function, structure, and drug escape. Nature Communications. 15(1). 6219–6219. 5 indexed citations
3.
Call, Matthew E., et al.. (2024). Deep mutational scanning reveals transmembrane features governing surface expression of the B cell antigen receptor. Frontiers in Immunology. 15. 1426795–1426795.
4.
Watson, Katherine A., et al.. (2023). Human EGFRvIII chimeric antigen receptor T cells demonstrate favorable safety profile and curative responses in orthotopic glioblastoma. Clinical & Translational Immunology. 12(3). e1440–e1440. 10 indexed citations
5.
Elazar, Assaf, Jonathan J. Weinstein, Raphael Trenker, et al.. (2022). De novo-designed transmembrane domains tune engineered receptor functions. eLife. 11. 34 indexed citations
6.
Trenker, Raphael, et al.. (2021). Human and viral membrane–associated E3 ubiquitin ligases MARCH1 and MIR2 recognize different features of CD86 to downregulate surface expression. Journal of Biological Chemistry. 297(1). 100900–100900. 9 indexed citations
7.
Call, Melissa, et al.. (2020). T Cell Activation Machinery: Form and Function in Natural and Engineered Immune Receptors. International Journal of Molecular Sciences. 21(19). 7424–7424. 10 indexed citations
8.
Park, Soohyung, et al.. (2020). Experimentally Guided Computational Methods Yield Highly Accurate Insights into Transmembrane Interactions within the T Cell Receptor Complex. The Journal of Physical Chemistry B. 124(46). 10303–10310. 1 indexed citations
9.
Bridgford, Jessica L., Su Min Lee, Paola Guglielmelli, et al.. (2019). Novel drivers and modifiers of MPL-dependent oncogenic transformation identified by deep mutational scanning. Blood. 135(4). 287–292. 34 indexed citations
10.
Byrne, Eamon F.X., et al.. (2018). A serine in the first transmembrane domain of the human E3 ubiquitin ligase MARCH9 is critical for down-regulation of its protein substrates. Journal of Biological Chemistry. 294(7). 2470–2485. 8 indexed citations
11.
Brouwer, Jason M., Ping Lan, Angus D. Cowan, et al.. (2017). Conversion of Bim-BH3 from Activator to Inhibitor of Bak through Structure-Based Design. Molecular Cell. 68(4). 659–672.e9. 52 indexed citations
12.
Trenker, Raphael, Melissa Call, & Matthew E. Call. (2016). Progress and prospects for structural studies of transmembrane interactions in single-spanning receptors. Current Opinion in Structural Biology. 39. 115–123. 15 indexed citations
13.
Knoblich, Konstantin, Soohyung Park, Leonie van ‘t Hag, et al.. (2015). Transmembrane Complexes of DAP12 Crystallized in Lipid Membranes Provide Insights into Control of Oligomerization in Immunoreceptor Assembly. Cell Reports. 11(8). 1184–1192. 22 indexed citations
14.
Berry, Richard, Stephen J. Headey, Melissa Call, et al.. (2014). Structure of the Chicken CD3ϵδ/γ Heterodimer and Its Assembly with the αβT Cell Receptor. Journal of Biological Chemistry. 289(12). 8240–8251. 13 indexed citations
15.
Berry, Richard, Philippa M. Saunders, J.P. Vivian, et al.. (2013). Targeting of a natural killer cell receptor family by a viral immunoevasin. Nature Immunology. 14(7). 699–705. 37 indexed citations
17.
Pos, Wouter, Dhruv K. Sethi, Melissa Call, et al.. (2012). Crystal Structure of the HLA-DM–HLA-DR1 Complex Defines Mechanisms for Rapid Peptide Selection. Cell. 151(7). 1557–1568. 125 indexed citations
18.
Wucherpfennig, Kai W., Étienne Gagnon, Melissa Call, Eric S. Huseby, & Matthew E. Call. (2010). Structural Biology of the T-cell Receptor: Insights into Receptor Assembly, Ligand Recognition, and Initiation of Signaling. Cold Spring Harbor Perspectives in Biology. 2(4). a005140–a005140. 117 indexed citations
19.
Call, Melissa, Monika‐Sarah E. D. Schulze, Kevin Fowler, et al.. (2010). HLA-DM captures partially empty HLA-DR molecules for catalyzed removal of peptide. Nature Immunology. 12(1). 54–61. 80 indexed citations
20.
Call, Melissa, Xuechao Xing, Gregory D. Cuny, et al.. (2009). In Vivo Enhancement of Peptide Display by MHC Class II Molecules with Small Molecule Catalysts of Peptide Exchange. The Journal of Immunology. 182(10). 6342–6352. 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.

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