Karen N. Allen

7.7k total citations · 1 hit paper
137 papers, 5.8k citations indexed

About

Karen N. Allen is a scholar working on Molecular Biology, Materials Chemistry and Biochemistry. According to data from OpenAlex, Karen N. Allen has authored 137 papers receiving a total of 5.8k indexed citations (citations by other indexed papers that have themselves been cited), including 89 papers in Molecular Biology, 66 papers in Materials Chemistry and 29 papers in Biochemistry. Recurrent topics in Karen N. Allen's work include Enzyme Structure and Function (60 papers), Biochemical and Molecular Research (29 papers) and Protein Structure and Dynamics (23 papers). Karen N. Allen is often cited by papers focused on Enzyme Structure and Function (60 papers), Biochemical and Molecular Research (29 papers) and Protein Structure and Dynamics (23 papers). Karen N. Allen collaborates with scholars based in United States, Germany and Canada. Karen N. Allen's co-authors include Debra Dunaway‐Mariano, Sushmita D. Lahiri, Barbara Imperiali, Guofeng Zhang, L. Aravind, A. Maxwell Burroughs, Dagmar Ringe, N.R. Silvaggi, Jeremiah D. Farelli and Ezra Peisach and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

Karen N. Allen

136 papers receiving 5.8k citations

Hit Papers

Construction and Analysis of Two Genome-Scale Deletion Li... 2017 2026 2020 2023 2017 100 200 300 400

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Karen N. Allen United States 43 4.0k 1.9k 687 613 473 137 5.8k
James B. Thoden United States 45 4.7k 1.2× 2.4k 1.3× 884 1.3× 744 1.2× 392 0.8× 153 6.6k
Sherry L. Mowbray Sweden 42 3.8k 1.0× 1.1k 0.6× 521 0.8× 545 0.9× 816 1.7× 111 5.3k
Rudolf Ladenstein Sweden 47 5.8k 1.5× 2.7k 1.4× 516 0.8× 389 0.6× 583 1.2× 131 7.8k
Debra Dunaway‐Mariano United States 46 5.0k 1.3× 2.3k 1.2× 1.1k 1.5× 906 1.5× 413 0.9× 203 7.2k
Rik K. Wierenga Finland 48 6.7k 1.7× 2.8k 1.5× 927 1.3× 331 0.5× 526 1.1× 158 8.8k
Michail N. Isupov United Kingdom 34 3.7k 0.9× 1.3k 0.7× 445 0.6× 402 0.7× 466 1.0× 116 5.2k
Marcia E. Newcomer United States 41 3.4k 0.9× 576 0.3× 552 0.8× 663 1.1× 482 1.0× 102 5.7k
Joseph D. Schrag Canada 40 5.8k 1.5× 760 0.4× 616 0.9× 600 1.0× 417 0.9× 71 7.4k
S.E. Ealick United States 52 6.7k 1.7× 2.0k 1.1× 867 1.3× 707 1.2× 562 1.2× 246 9.3k
Urszula Derewenda United States 42 4.9k 1.2× 917 0.5× 356 0.5× 463 0.8× 374 0.8× 81 6.5k

Countries citing papers authored by Karen N. Allen

Since Specialization
Citations

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

Fields of papers citing papers by Karen N. Allen

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Karen N. Allen. 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 Karen N. Allen. The network helps show where Karen N. Allen may publish in the future.

Co-authorship network of co-authors of Karen N. Allen

This figure shows the co-authorship network connecting the top 25 collaborators of Karen N. Allen. A scholar is included among the top collaborators of Karen N. Allen 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 Karen N. Allen. Karen N. Allen 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.
Imperiali, Barbara, et al.. (2025). Selection of nanobodies against liponanoparticle‐embedded membrane proteins by yeast‐surface display. Protein Science. 34(10). e70293–e70293. 1 indexed citations
2.
Ghosh, Soumi, et al.. (2024). Proteome-wide bioinformatic annotation and functional validation of the monotopic phosphoglycosyl transferase superfamily. Proceedings of the National Academy of Sciences. 121(49). e2417572121–e2417572121.
3.
Allen, Karen N., et al.. (2024). Dual Glycosyltransferases from Campylobacter concisus Diverge from the Canonical Campylobacter N-Linked Glycan Assembly Pathway. Biochemistry. 63(18). 2369–2379. 1 indexed citations
4.
Allen, Karen N., et al.. (2023). Synergistic computational and experimental studies of a phosphoglycosyl transferase membrane/ligand ensemble. Journal of Biological Chemistry. 299(10). 105194–105194. 8 indexed citations
6.
Allen, Karen N., et al.. (2023). Co‐conserved sequence motifs are predictive of substrate specificity in a family of monotopic phosphoglycosyl transferases. Protein Science. 32(6). e4646–e4646. 5 indexed citations
8.
Beglov, Dmitri, David Hall, Amanda Wakefield, et al.. (2018). Exploring the structural origins of cryptic sites on proteins. Proceedings of the National Academy of Sciences. 115(15). E3416–E3425. 93 indexed citations
9.
Allen, Karen N., et al.. (2018). Monotopic Membrane Proteins Join the Fold. Trends in Biochemical Sciences. 44(1). 7–20. 50 indexed citations
10.
Koo, Byoung‐Mo, George Kritikos, Jeremiah D. Farelli, et al.. (2017). Construction and Analysis of Two Genome-Scale Deletion Libraries for Bacillus subtilis. Cell Systems. 4(3). 291–305.e7. 414 indexed citations breakdown →
11.
Kozakov, Dima, David R. Hall, Stefan Jehle, et al.. (2015). Ligand deconstruction: Why some fragment binding positions are conserved and others are not. Proceedings of the National Academy of Sciences. 112(20). E2585–94. 56 indexed citations
12.
Rago, Florencia, Daniel J. Saltzberg, Karen N. Allen, & Dean R. Tolan. (2015). Enzyme Substrate Specificity Conferred by Distinct Conformational Pathways. Journal of the American Chemical Society. 137(43). 13876–13886. 12 indexed citations
13.
Gerlt, J.A., Karen N. Allen, Steven C. Almo, et al.. (2011). The Enzyme Function Initiative. Biochemistry. 50(46). 9950–9962. 141 indexed citations
14.
Lu, Zhibing, Debra Dunaway‐Mariano, & Karen N. Allen. (2011). The X‐ray crystallographic structure and specificity profile of HAD superfamily phosphohydrolase BT1666: Comparison of paralogous functions in B. thetaiotaomicron. Proteins Structure Function and Bioinformatics. 79(11). 3099–3107. 14 indexed citations
15.
Huang, Hua, Y. Patskovsky, R. Toro, et al.. (2011). Divergence of Structure and Function in the Haloacid Dehalogenase Enzyme Superfamily: Bacteroides thetaiotaomicron BT2127 Is an Inorganic Pyrophosphatase. Biochemistry. 50(41). 8937–8949. 37 indexed citations
16.
Allen, Karen N. & Debra Dunaway‐Mariano. (2009). Markers of fitness in a successful enzyme superfamily. Current Opinion in Structural Biology. 19(6). 658–665. 86 indexed citations
17.
Silvaggi, N.R., Grant E. Boldt, Mark S. Hixon, et al.. (2007). Structures of Clostridium botulinum Neurotoxin Serotype A Light Chain Complexed with Small-Molecule Inhibitors Highlight Active-Site Flexibility. Chemistry & Biology. 14(5). 533–542. 102 indexed citations
18.
Ali, Mayssam H., Christina Taylor, Gevorg Grigoryan, et al.. (2005). Design of a Heterospecific, Tetrameric, 21-Residue Miniprotein with Mixed α/β Structure. Structure. 13(2). 225–234. 28 indexed citations
19.
Choi, Kyung H., Jun Shi, Christopher E. Hopkins, Dean R. Tolan, & Karen N. Allen. (2001). Snapshots of Catalysis:  the Structure of Fructose-1,6-(bis)phosphate Aldolase Covalently Bound to the Substrate Dihydroxyacetone Phosphate,. Biochemistry. 40(46). 13868–13875. 66 indexed citations
20.
Allen, Karen N., Arnon Lavie, Arthur Glasfeld, et al.. (1994). Role of the Divalent Metal Ion in Sugar Binding, Ring Opening, and Isomerization by D-Xylose Isomerase: Replacement of a Catalytic Metal by an Amino Acid. Biochemistry. 33(6). 1488–1494. 64 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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