Rachel B. Kapust

3.5k total citations · 2 hit papers
12 papers, 2.8k citations indexed

About

Rachel B. Kapust is a scholar working on Molecular Biology, Ecology and Radiology, Nuclear Medicine and Imaging. According to data from OpenAlex, Rachel B. Kapust has authored 12 papers receiving a total of 2.8k indexed citations (citations by other indexed papers that have themselves been cited), including 7 papers in Molecular Biology, 5 papers in Ecology and 5 papers in Radiology, Nuclear Medicine and Imaging. Recurrent topics in Rachel B. Kapust's work include Bacteriophages and microbial interactions (5 papers), Monoclonal and Polyclonal Antibodies Research (5 papers) and Virus-based gene therapy research (3 papers). Rachel B. Kapust is often cited by papers focused on Bacteriophages and microbial interactions (5 papers), Monoclonal and Polyclonal Antibodies Research (5 papers) and Virus-based gene therapy research (3 papers). Rachel B. Kapust collaborates with scholars based in United States and Hungary. Rachel B. Kapust's co-authors include David S. Waugh, Terry D. Copeland, József Tőzsér, Jeffrey D. Fox, Scott Cherry, David E. Anderson, Joseph E. Tropea, Emanuela Felley‐Bosco, Shawn E. Lupold and Stefan Ambs and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Biochemical and Biophysical Research Communications.

In The Last Decade

Rachel B. Kapust

12 papers receiving 2.8k citations

Hit Papers

Escherichia coli maltose‐binding protein is uncommonly ef... 1999 2026 2008 2017 1999 2001 250 500 750
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.

  1. Escherichia coli maltose‐binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused
    1999 770 citations Rachel B. Kapust, David S. Waugh Protein Science profile →
  2. Tobacco etch virus protease: mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency
    2001 715 citations Rachel B. Kapust, József Tőzsér et al. Protein Engineering Design and Selection profile →

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Rachel B. Kapust United States 11 2.1k 513 486 307 275 12 2.8k
Savvas C. Makrides United States 22 2.1k 1.0× 370 0.7× 598 1.2× 165 0.5× 236 0.9× 27 3.1k
Luciana Dente Italy 30 2.5k 1.2× 331 0.6× 643 1.3× 267 0.9× 205 0.7× 57 3.5k
Pradman K. Qasba United States 33 3.0k 1.4× 568 1.1× 673 1.4× 422 1.4× 135 0.5× 107 4.0k
Erik Holmgren Sweden 22 1.3k 0.6× 577 1.1× 357 0.7× 201 0.7× 178 0.6× 44 2.2k
Sui‐Lam Wong Canada 25 2.5k 1.2× 237 0.5× 478 1.0× 260 0.8× 276 1.0× 54 3.1k
Jack S. Benner United States 35 4.1k 1.9× 583 1.1× 808 1.7× 344 1.1× 502 1.8× 56 4.7k
Scott Cherry United States 21 1.8k 0.9× 213 0.4× 573 1.2× 263 0.9× 176 0.6× 39 2.5k
Séverine Frutiger Switzerland 29 2.2k 1.1× 236 0.5× 335 0.7× 402 1.3× 126 0.5× 49 3.5k
Roberto Fattorusso Italy 29 1.9k 0.9× 215 0.4× 317 0.7× 255 0.8× 180 0.7× 129 2.7k
Saran A. Narang Canada 38 3.2k 1.5× 777 1.5× 576 1.2× 153 0.5× 388 1.4× 114 3.8k

Countries citing papers authored by Rachel B. Kapust

Since Specialization
Citations

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

Fields of papers citing papers by Rachel B. Kapust

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Rachel B. Kapust. 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 Rachel B. Kapust. The network helps show where Rachel B. Kapust may publish in the future.

Co-authorship network of co-authors of Rachel B. Kapust

This figure shows the co-authorship network connecting the top 25 collaborators of Rachel B. Kapust. A scholar is included among the top collaborators of Rachel B. Kapust 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 Rachel B. Kapust. Rachel B. Kapust is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

12 of 12 papers shown
1.
Nallamsetty, Sreedevi, Rachel B. Kapust, József Tőzsér, et al.. (2004). Efficient site-specific processing of fusion proteins by tobacco vein mottling virus protease in vivo and in vitro. Protein Expression and Purification. 38(1). 108–115. 117 indexed citations
2.
Zdanov, Alexander, et al.. (2003). Tobacco Etch Virus Protease: Crystal Structure of the Active Enzyme and Its Inactive Mutant. Russian Journal of Bioorganic Chemistry. 29(5). 415–418. 4 indexed citations
3.
Kapust, Rachel B., Karen M. Routzahn, & David S. Waugh. (2002). Processive Degradation of Nascent Polypeptides, Triggered by Tandem AGA Codons, Limits the Accumulation of Recombinant Tobacco Etch Virus Protease in Escherichia coli BL21(DE3). Protein Expression and Purification. 24(1). 61–70. 29 indexed citations
4.
Kapust, Rachel B., József Tőzsér, Terry D. Copeland, & David S. Waugh. (2002). The P1′ specificity of tobacco etch virus protease. Biochemical and Biophysical Research Communications. 294(5). 949–955. 309 indexed citations
5.
Phan, Jason, Alexander Zdanov, A.G. Evdokimov, et al.. (2002). Structural Basis for the Substrate Specificity of Tobacco Etch Virus Protease. Journal of Biological Chemistry. 277(52). 50564–50572. 200 indexed citations
6.
7.
Kapust, Rachel B., József Tőzsér, Jeffrey D. Fox, et al.. (2001). Tobacco etch virus protease: mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency. Protein Engineering Design and Selection. 14(12). 993–1000. 715 indexed citations breakdown →
8.
Kapust, Rachel B., et al.. (2000). Controlled Intracellular Processing of Fusion Proteins by TEV Protease. Protein Expression and Purification. 19(2). 312–318. 171 indexed citations
9.
Eisenmesser, Elan, Rachel B. Kapust, Joseph P. Nawrocki, et al.. (2000). Expression, Purification, Refolding, and Characterization of Recombinant Human Interleukin-13: Utilization of Intracellular Processing. Protein Expression and Purification. 20(2). 186–195. 25 indexed citations
10.
Kapust, Rachel B. & David S. Waugh. (1999). Escherichia coli maltose‐binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused. Protein Science. 8(8). 1668–1674. 770 indexed citations breakdown →
11.
Sarma, Siddhartha P., et al.. (1998). The Amino-terminal Domain of Human STAT4. Journal of Biological Chemistry. 273(27). 17109–17114. 13 indexed citations
12.
Forrester, Kathleen, Stefan Ambs, Shawn E. Lupold, et al.. (1996). Nitric oxide-induced p53 accumulation and regulation of inducible nitric oxide synthase expression by wild-type p53.. Proceedings of the National Academy of Sciences. 93(6). 2442–2447. 378 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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