Dorothy Beckett

3.8k total citations · 1 hit paper
80 papers, 3.1k citations indexed

About

Dorothy Beckett is a scholar working on Molecular Biology, Cell Biology and Organic Chemistry. According to data from OpenAlex, Dorothy Beckett has authored 80 papers receiving a total of 3.1k indexed citations (citations by other indexed papers that have themselves been cited), including 53 papers in Molecular Biology, 52 papers in Cell Biology and 18 papers in Organic Chemistry. Recurrent topics in Dorothy Beckett's work include Biotin and Related Studies (50 papers), RNA and protein synthesis mechanisms (25 papers) and Cellular transport and secretion (21 papers). Dorothy Beckett is often cited by papers focused on Biotin and Related Studies (50 papers), RNA and protein synthesis mechanisms (25 papers) and Cellular transport and secretion (21 papers). Dorothy Beckett collaborates with scholars based in United States, Germany and Sweden. Dorothy Beckett's co-authors include Elena G. Kovaleva, Peter J. Schatz, Emily D. Streaker, Keehwan Kwon, Olke C. Uhlenbeck, Yan Xu, Elizabeth Nenortas, Michael F. Summers, Brian W. Matthews and L.H. Weaver and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Nature Communications.

In The Last Decade

Dorothy Beckett

80 papers receiving 3.1k citations

Hit Papers

A minimal peptide substrate in biotin holoenzyme syntheta... 1999 2026 2008 2017 1999 100 200 300 400 500

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Dorothy Beckett United States 31 1.9k 1.4k 675 455 393 80 3.1k
Bart Hazes Canada 27 2.1k 1.1× 531 0.4× 261 0.4× 142 0.3× 394 1.0× 53 3.6k
Youwei Yan United States 22 1.1k 0.6× 294 0.2× 366 0.5× 275 0.6× 156 0.4× 34 2.4k
Dustin J. Maly United States 39 2.3k 1.2× 676 0.5× 727 1.1× 345 0.8× 192 0.5× 118 4.3k
Paul R. Caron United States 26 4.0k 2.1× 349 0.3× 265 0.4× 256 0.6× 391 1.0× 40 5.2k
V.N. Malashkevich United States 34 2.4k 1.2× 301 0.2× 273 0.4× 293 0.6× 230 0.6× 65 4.1k
Douglas K. Struck United States 30 2.8k 1.5× 403 0.3× 253 0.4× 211 0.5× 691 1.8× 46 4.0k
Matthew J. Bottomley Italy 24 2.3k 1.2× 370 0.3× 157 0.2× 367 0.8× 231 0.6× 53 3.8k
Michael S. Kay United States 24 1.5k 0.8× 248 0.2× 346 0.5× 312 0.7× 97 0.2× 49 2.4k
Hannah Alexander United States 30 2.6k 1.4× 596 0.4× 81 0.1× 906 2.0× 343 0.9× 69 4.4k
W.P. Burmeister France 32 1.9k 1.0× 134 0.1× 310 0.5× 560 1.2× 438 1.1× 63 3.5k

Countries citing papers authored by Dorothy Beckett

Since Specialization
Citations

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

Fields of papers citing papers by Dorothy Beckett

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Dorothy Beckett

This figure shows the co-authorship network connecting the top 25 collaborators of Dorothy Beckett. A scholar is included among the top collaborators of Dorothy Beckett 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 Dorothy Beckett. Dorothy Beckett 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.
Klontz, Erik H., Chao Li, James K. Fields, et al.. (2020). Structure and dynamics of an α-fucosidase reveal a mechanism for highly efficient IgG transfucosylation. Nature Communications. 11(1). 6204–6204. 30 indexed citations
2.
Bonsor, Daniel A., Evelyn Weiss, Jingheng Wang, et al.. (2018). The Helicobacter pylori adhesin protein HopQ exploits the dimer interface of human CEACAMs to facilitate translocation of the oncoprotein CagA. The EMBO Journal. 37(13). 47 indexed citations
3.
Wang, Jingheng, et al.. (2017). Long Distance Modulation of Disorder-to-Order Transitions in Protein Allostery. Biochemistry. 56(34). 4478–4488. 12 indexed citations
4.
Bonsor, Daniel A., Kay Diederichs, Rainer Haas, et al.. (2015). Integrin Engagement by the Helical RGD Motif of the Helicobacter pylori CagL Protein Is Regulated by pH-induced Displacement of a Neighboring Helix. Journal of Biological Chemistry. 290(20). 12929–12940. 25 indexed citations
5.
Ingaramo, Maria & Dorothy Beckett. (2011). Biotinylation, a Post-translational Modification Controlled by the Rate of Protein-Protein Association. Journal of Biological Chemistry. 286(15). 13071–13078. 10 indexed citations
6.
Tungtur, Sudheer, et al.. (2011). In vivo tests of thermodynamic models of transcription repressor function. Biophysical Chemistry. 159(1). 142–151. 19 indexed citations
7.
Beckett, Dorothy. (2010). Measurement and Analysis of Equilibrium Binding Titrations. Methods in enzymology on CD-ROM/Methods in enzymology. 488. 1–16. 57 indexed citations
8.
Ingaramo, Maria & Dorothy Beckett. (2009). Distinct Amino Termini of Two Human HCS Isoforms Influence Biotin Acceptor Substrate Recognition. Journal of Biological Chemistry. 284(45). 30862–30870. 21 indexed citations
9.
Zhao, Huaying, et al.. (2009). Thermodynamic and Structural Investigation of Bispecificity in Protein–Protein Interactions. Journal of Molecular Biology. 389(2). 336–348. 16 indexed citations
10.
Beckett, Dorothy. (2008). Biotin Sensing at the Molecular Level. Journal of Nutrition. 139(1). 167–170. 34 indexed citations
11.
Beckett, Dorothy. (2006). Obsessive Genius: The Inner World of Marie Curie. Physics Today. 59(1). 61–62. 1 indexed citations
12.
Tang, Chun, Erin Loeliger, Paz J. Luncsford, et al.. (2003). Entropic switch regulates myristate exposure in the HIV-1 matrix protein. Proceedings of the National Academy of Sciences. 101(2). 517–522. 258 indexed citations
13.
Kwon, Keehwan, Emily D. Streaker, & Dorothy Beckett. (2002). Binding specificity and the ligand dissociation process in the E. coli biotin holoenzyme synthetase. Protein Science. 11(3). 558–570. 26 indexed citations
14.
Beckett, Dorothy. (2001). Regulated assembly of transcription factors and control of transcription initiation 1 1Edited by D. E. Draper. Journal of Molecular Biology. 314(3). 335–352. 41 indexed citations
16.
Beckett, Dorothy. (1998). [21] Energetic methods to study bifunctional biotin operon repressor. Methods in enzymology on CD-ROM/Methods in enzymology. 295. 424–450. 3 indexed citations
17.
Nenortas, Elizabeth & Dorothy Beckett. (1996). Purification and Characterization of Intact and Truncated Forms of the Escherichia coli Biotin Carboxyl Carrier Subunit of Acetyl-CoA Carboxylase. Journal of Biological Chemistry. 271(13). 7559–7567. 65 indexed citations
18.
Burz, David S., Dorothy Beckett, Nicholas R. Benson, & Gary K. Ackers. (1994). Self-Assembly of Bacteriophage .lambda. cI Repressor: Effects of Single-Site Mutations on the Monomer-Dimer Equilibrium. Biochemistry. 33(28). 8399–8405. 41 indexed citations
19.
Beckett, Dorothy & Olke C. Uhlenbeck. (1988). Ribonucleoprotein complexes of R17 coat protein and a translational operator analog. Journal of Molecular Biology. 204(4). 927–938. 83 indexed citations
20.
Uhlenbeck, Olke C., Jannette Carey, Paul J. Romaniuk, Peggy T. Lowary, & Dorothy Beckett. (1983). Interaction of R17 Coat Protein With Its RNA Binding Site For Translational Repression. Journal of Biomolecular Structure and Dynamics. 1(2). 539–552. 59 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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