Ester Fraga

585 total citations
24 papers, 519 citations indexed

About

Ester Fraga is a scholar working on Molecular Biology, Immunology and Radiology, Nuclear Medicine and Imaging. According to data from OpenAlex, Ester Fraga has authored 24 papers receiving a total of 519 indexed citations (citations by other indexed papers that have themselves been cited), including 15 papers in Molecular Biology, 13 papers in Immunology and 9 papers in Radiology, Nuclear Medicine and Imaging. Recurrent topics in Ester Fraga's work include Immunotherapy and Immune Responses (12 papers), Monoclonal and Polyclonal Antibodies Research (9 papers) and T-cell and B-cell Immunology (8 papers). Ester Fraga is often cited by papers focused on Immunotherapy and Immune Responses (12 papers), Monoclonal and Polyclonal Antibodies Research (9 papers) and T-cell and B-cell Immunology (8 papers). Ester Fraga collaborates with scholars based in Canada and United States. Ester Fraga's co-authors include Bhagirath Singh, Glen R. Loppnow, Michelle Webb, R H Schwartz, Barbara S. Fox, Chengrong Chen, Arun Fotedar, Michael Boyer, Moira A. Barton and Babita Agrawal and has published in prestigious journals such as Journal of the American Chemical Society, The Journal of Immunology and The Journal of Physical Chemistry B.

In The Last Decade

Ester Fraga

23 papers receiving 507 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Ester Fraga Canada 11 259 239 117 73 70 24 519
Chikako Torigoe United States 12 252 1.0× 365 1.5× 147 1.3× 17 0.2× 32 0.5× 21 647
Diether Recktenwald United States 12 144 0.6× 422 1.8× 28 0.2× 77 1.1× 20 0.3× 21 712
Jens Hennecke Belgium 9 281 1.1× 507 2.1× 106 0.9× 20 0.3× 15 0.2× 11 797
K. Hartmann Germany 9 247 1.0× 138 0.6× 79 0.7× 30 0.4× 14 0.2× 16 573
Jeanmarie Guenot United States 13 370 1.4× 363 1.5× 213 1.8× 55 0.8× 17 0.2× 19 824
Thomas Weidemann Germany 18 97 0.4× 644 2.7× 123 1.1× 52 0.7× 14 0.2× 30 907
Denise Porter United States 9 55 0.2× 386 1.6× 27 0.2× 34 0.5× 61 0.9× 10 553
Boris P. Atanasov Bulgaria 14 176 0.7× 345 1.4× 38 0.3× 35 0.5× 20 0.3× 37 575
Kathryn M. Armstrong United States 11 276 1.1× 165 0.7× 143 1.2× 13 0.2× 24 0.3× 11 429
MM Frank United States 8 119 0.5× 303 1.3× 50 0.4× 45 0.6× 35 0.5× 11 536

Countries citing papers authored by Ester Fraga

Since Specialization
Citations

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

Fields of papers citing papers by Ester Fraga

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Ester Fraga

This figure shows the co-authorship network connecting the top 25 collaborators of Ester Fraga. A scholar is included among the top collaborators of Ester Fraga 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 Ester Fraga. Ester Fraga 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.
Fraga, Ester & Glen R. Loppnow. (2002). The Role of Specific Amino Acid Residues in The Vibrational Properties of Plastocyanin. The Journal of Physical Chemistry B. 106(40). 10474–10481. 4 indexed citations
2.
Fraga, Ester & Glen R. Loppnow. (1998). Proteins as Solvents:  Blue Copper Proteins as a Molecular Ruler for Solvent Effects on Resonance Raman Intensities. The Journal of Physical Chemistry B. 102(39). 7659–7665. 28 indexed citations
3.
Loppnow, Glen R. & Ester Fraga. (1997). Proteins as Solvents:  The Role of Amino Acid Composition in the Excited-State Charge Transfer Dynamics of Plastocyanins. Journal of the American Chemical Society. 119(5). 896–905. 41 indexed citations
4.
Fraga, Ester, et al.. (1996). Immune responses to self peptides naturally presented by murine class II Major Histocompatibility Complex molecules. Molecular Immunology. 33(7-8). 625–633. 18 indexed citations
5.
Fraga, Ester, Michelle Webb, & Glen R. Loppnow. (1996). Charge-Transfer Dynamics in Plastocyanin, a Blue Copper Protein, from Resonance Raman Intensities. The Journal of Physical Chemistry. 100(8). 3278–3287. 81 indexed citations
6.
Agrawal, Babita, Ester Fraga, Kevin P. Kane, & Bhagirath Singh. (1994). Up-regulation of the MHC class II molecules on B cells by peptide ligands.. The Journal of Immunology. 152(3). 965–975. 7 indexed citations
7.
Fraga, Ester, et al.. (1993). Characterization of murine T cell responses to peptides of the variable region of self T cell receptor beta -chains.. The Journal of Immunology. 151(8). 4045–4054. 6 indexed citations
8.
Fraga, Ester, et al.. (1992). Inhibition of superantigen recognition by peptides of the variable region of the T cell receptor β chain. European Journal of Immunology. 22(4). 937–941. 5 indexed citations
9.
Boyer, Michael, et al.. (1992). Unusually diverse T cell response to a repeating tripeptide epitope. Cellular Immunology. 140(1). 206–218. 6 indexed citations
10.
11.
Agrawal, Babita, et al.. (1991). T cells that recognize peptide sequences of self MHC class II molecules exist in syngeneic mice. The Journal of Immunology. 147(2). 383–390. 38 indexed citations
12.
Boyer, Michael, Ester Fraga, Kim Oikawa, et al.. (1990). Functional degeneracy of residues in a T cell peptide epitope contributes to its recognition by different T cell hybridomas. International Immunology. 2(12). 1221–1233. 9 indexed citations
13.
Boyer, Michael, et al.. (1990). Critical role of an amino acid residue in a T cell determinant is due to its interaction with a neighboring non‐critical residue. European Journal of Immunology. 20(9). 2145–2148. 12 indexed citations
14.
Singh, Bhagirath, et al.. (1990). Role of the first external domain of I-Aβ chain in immune responses and diabetes in non-obese diabetic (NOD) mice. Journal of Autoimmunity. 3(5). 507–521. 4 indexed citations
15.
Fotedar, Arun, Michael Boyer, Ester Fraga, et al.. (1990). Characterization of agretopes and epitopes involved in the presentation of beef insulin to T cells. Molecular Immunology. 27(7). 603–611. 3 indexed citations
16.
17.
Kilgannon, Patrick, Ester Fraga, & Bhagirath Singh. (1986). Fine-specificity analysis of antibodies directed to the C-terminal peptides of cytochrome c recognized by T-lymphocytes. Molecular Immunology. 23(3). 311–318. 4 indexed citations
18.
Schwartz, R H, Barbara S. Fox, Ester Fraga, Chengrong Chen, & Bhagirath Singh. (1985). The T lymphocyte response to cytochrome c. V. Determination of the minimal peptide size required for stimulation of T cell clones and assessment of the contribution of each residue beyond this size to antigenic potency.. The Journal of Immunology. 135(4). 2598–2608. 92 indexed citations
19.
20.
Singh, Bhagirath, Ester Fraga, & Moira A. Barton. (1978). Characterization and Genetic Control of the Immune Response to Synthetic Polypeptide Antigens of Defined Geometry. The Journal of Immunology. 121(2). 784–789. 8 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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