Elisabeth Daub

932 total citations
20 papers, 801 citations indexed

About

Elisabeth Daub is a scholar working on Molecular Biology, Materials Chemistry and Clinical Biochemistry. According to data from OpenAlex, Elisabeth Daub has authored 20 papers receiving a total of 801 indexed citations (citations by other indexed papers that have themselves been cited), including 9 papers in Molecular Biology, 9 papers in Materials Chemistry and 5 papers in Clinical Biochemistry. Recurrent topics in Elisabeth Daub's work include Enzyme Structure and Function (7 papers), Amino Acid Enzymes and Metabolism (4 papers) and Bacteriophages and microbial interactions (4 papers). Elisabeth Daub is often cited by papers focused on Enzyme Structure and Function (7 papers), Amino Acid Enzymes and Metabolism (4 papers) and Bacteriophages and microbial interactions (4 papers). Elisabeth Daub collaborates with scholars based in Canada and United States. Elisabeth Daub's co-authors include John F. Honek, David Botstein, Susan L. Clugston, Henry S. Duewel, Valerie J. Robinson, Christopher T. Walsh, Linda D. Kosturko, John F. Barnard, Robert Kinach and Steven A. Wasserman and has published in prestigious journals such as Nucleic Acids Research, The Journal of Physical Chemistry B and Biochemistry.

In The Last Decade

Elisabeth Daub

20 papers receiving 777 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Elisabeth Daub Canada 15 489 197 138 131 122 20 801
James A. Endrizzi United States 20 1.2k 2.4× 305 1.5× 140 1.0× 68 0.5× 81 0.7× 23 1.6k
Yoshiaki Nishiya Japan 16 589 1.2× 159 0.8× 92 0.7× 137 1.0× 71 0.6× 65 816
Walter B. Dempsey United States 20 727 1.5× 406 2.1× 333 2.4× 232 1.8× 135 1.1× 50 1.1k
Tomoharu Gomi Japan 21 801 1.6× 145 0.7× 59 0.4× 175 1.3× 36 0.3× 40 1.1k
Dirk Iwata‐Reuyl United States 25 1.6k 3.2× 223 1.1× 181 1.3× 53 0.4× 99 0.8× 44 1.8k
Agnete Munch‐Petersen Denmark 24 1.4k 2.9× 235 1.2× 338 2.4× 205 1.6× 143 1.2× 35 1.8k
Y. Yasutake Japan 18 549 1.1× 234 1.2× 80 0.6× 76 0.6× 51 0.4× 51 885
Junichi Komoto United States 16 573 1.2× 115 0.6× 59 0.4× 138 1.1× 32 0.3× 21 850
K. Ishikawa Japan 18 655 1.3× 202 1.0× 73 0.5× 51 0.4× 38 0.3× 41 1.2k
Gea K. Schuurman‐Wolters Netherlands 20 772 1.6× 204 1.0× 301 2.2× 99 0.8× 58 0.5× 38 1.2k

Countries citing papers authored by Elisabeth Daub

Since Specialization
Citations

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

Fields of papers citing papers by Elisabeth Daub

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Elisabeth Daub

This figure shows the co-authorship network connecting the top 25 collaborators of Elisabeth Daub. A scholar is included among the top collaborators of Elisabeth Daub 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 Elisabeth Daub. Elisabeth Daub 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.
Suttisansanee, Uthaiwan, Muhammad Syarhabil Ahmad, Zhengding Su, et al.. (2023). Molecular Engineering of E. coli Bacterioferritin: A Versatile Nanodimensional Protein Cage. Molecules. 28(12). 4663–4663. 2 indexed citations
2.
Vaughan, Mark D., Zhengding Su, Elisabeth Daub, & John F. Honek. (2016). Intriguing cellular processing of a fluorinated amino acid during protein biosynthesis in Escherichia coli. Organic & Biomolecular Chemistry. 14(38). 8942–8946. 7 indexed citations
3.
Daub, Elisabeth, et al.. (2016). Bioorthogonal Modification of the Major Sheath Protein of Bacteriophage M13: Extending the Versatility of Bionanomaterial Scaffolds. Bioconjugate Chemistry. 27(10). 2276–2280. 12 indexed citations
4.
Su, Zhengding, et al.. (2009). Interactions of peptides with single-walled carbon nanotubes. Advances in experimental medicine and biology. 611. 235–236. 1 indexed citations
5.
Su, Zhengding, et al.. (2007). Single-Walled Carbon Nanotube Binding Peptides:  Probing Tryptophan's Importance by Unnatural Amino Acid Substitution. The Journal of Physical Chemistry B. 111(51). 14411–14417. 45 indexed citations
6.
Vaughan, Martha, Peter B. Sampson, Elisabeth Daub, & John F. Honek. (2005). Investigation of Bioisosteric Effects on the Interaction of Substrates/ Inhibitors with the Methionyl-tRNA Synthetase from Escherichia coli. Medicinal Chemistry. 1(3). 227–237. 9 indexed citations
7.
Clugston, Susan L., et al.. (2004). Distinct classes of glyoxalase I: metal specificity of the Yersinia pestis, Pseudomonas aeruginosa and Neisseria meningitidis enzymes. Biochemical Journal. 384(1). 111–117. 60 indexed citations
8.
Duewel, Henry S., Elisabeth Daub, Valerie J. Robinson, & John F. Honek. (2001). Elucidation of Solvent Exposure, Side-Chain Reactivity, and Steric Demands of the Trifluoromethionine Residue in a Recombinant Protein. Biochemistry. 40(44). 13167–13176. 42 indexed citations
9.
Clugston, Susan L., Elisabeth Daub, & John F. Honek. (1998). Identification of Glyoxalase I Sequences in Brassica oleracea and Sporobolus stapfianus: Evidence for Gene Duplication Events. Journal of Molecular Evolution. 47(2). 230–234. 18 indexed citations
10.
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12.
Duewel, Henry S., Elisabeth Daub, Valerie J. Robinson, & John F. Honek. (1997). Incorporation of Trifluoromethionine into a Phage Lysozyme:  Implications and a New Marker for Use in Protein 19F NMR. Biochemistry. 36(11). 3404–3416. 77 indexed citations
13.
Duewel, Henry S., Elisabeth Daub, & John F. Honek. (1995). Investigations of the interactions of saccharides with the lysozyme from bacteriophage lambda. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1247(1). 149–158. 17 indexed citations
14.
Kosturko, Linda D., et al.. (1989). The interaction ofE.coliintegration host factor and λcosDNA: multiple complex formation and protein-induced bending. Nucleic Acids Research. 17(1). 317–334. 76 indexed citations
15.
Daub, Elisabeth, Laura E. Zawadzke, David Botstein, & C T Walsh. (1988). Isolation, cloning, and sequencing of the Salmonella typhimurium ddlA gene with purification and characterization of its product, D-alanine:D-alanine ligase (ADP forming). Biochemistry. 27(10). 3701–3708. 54 indexed citations
16.
Chow, Sue, Elisabeth Daub, & Helios Murialdo. (1987). The overproduction of DNA terminase of coliphage lambda. Gene. 60(2-3). 277–289. 41 indexed citations
17.
Galakatos, Nicholas G., Elisabeth Daub, David Botstein, & Christopher T. Walsh. (1986). Biosynthetic alr alanine racemase from Salmonella typhimurium: DNA and protein sequence determination. Biochemistry. 25(11). 3255–3260. 47 indexed citations
18.
Wasserman, Steven A., Elisabeth Daub, Paula Grisafi, David Botstein, & Christopher T. Walsh. (1984). Catabolic alanine racemase from Salmonella typhimurium: DNA sequence, enzyme purification, and characterization. Biochemistry. 23(22). 5182–5187. 83 indexed citations
19.
Cohen, Carolyn, John W. Weisel, G.N. Phillips, et al.. (1983). THE STRUCTURE OF FIBRINOGEN AND FIBRIN: I. ELECTRON MICROSCOPY AND X‐RAY CRYSTALLOGRAPHY OF FIBRINOGEN*. Annals of the New York Academy of Sciences. 408(1). 194–213. 27 indexed citations
20.
Jagt, David L. Vander, et al.. (1975). Effect of pH and thiols on the kinetics of yeast glyoxalase I. Evaluation of the random pathway mechanism. Biochemistry. 14(16). 3669–3675. 61 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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