Emily T. Beebe

773 total citations
17 papers, 283 citations indexed

About

Emily T. Beebe is a scholar working on Molecular Biology, Biotechnology and Biomedical Engineering. According to data from OpenAlex, Emily T. Beebe has authored 17 papers receiving a total of 283 indexed citations (citations by other indexed papers that have themselves been cited), including 15 papers in Molecular Biology, 7 papers in Biotechnology and 5 papers in Biomedical Engineering. Recurrent topics in Emily T. Beebe's work include Biofuel production and bioconversion (4 papers), Photoreceptor and optogenetics research (3 papers) and Transgenic Plants and Applications (3 papers). Emily T. Beebe is often cited by papers focused on Biofuel production and bioconversion (4 papers), Photoreceptor and optogenetics research (3 papers) and Transgenic Plants and Applications (3 papers). Emily T. Beebe collaborates with scholars based in United States, Japan and Switzerland. Emily T. Beebe's co-authors include Brian G. Fox, Shin‐ichi Makino, Steven D. Karlen, Kirk A. Vander Meulen, C.A. Bingman, John L. Markley, Michael A. Goren, John Ralph, Timothy J. Donohue and Akira Nozawa and has published in prestigious journals such as Journal of Biological Chemistry, Molecular Cell and Applied and Environmental Microbiology.

In The Last Decade

Emily T. Beebe

17 papers receiving 275 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Emily T. Beebe United States 11 209 70 60 56 27 17 283
Hans Jasper Genee Denmark 10 290 1.4× 37 0.5× 27 0.5× 27 0.5× 22 0.8× 13 369
Shweta Singh India 12 286 1.4× 39 0.6× 61 1.0× 33 0.6× 10 0.4× 31 377
Dennis Binder Germany 10 290 1.4× 95 1.4× 41 0.7× 51 0.9× 6 0.2× 13 415
Hendrik Waegeman Belgium 9 297 1.4× 62 0.9× 40 0.7× 54 1.0× 8 0.3× 10 368
Ryo Nasuno Japan 14 220 1.1× 34 0.5× 67 1.1× 22 0.4× 41 1.5× 27 346
Simo Abdessamad Baallal Jacobsen Denmark 6 279 1.3× 41 0.6× 32 0.5× 36 0.6× 12 0.4× 7 329
Shun-ichi Akiyama Japan 12 247 1.2× 61 0.9× 34 0.6× 63 1.1× 18 0.7× 45 340
Maybelle Kho Go Singapore 14 361 1.7× 14 0.2× 48 0.8× 31 0.6× 35 1.3× 26 493
Meiying Zheng United States 14 359 1.7× 46 0.7× 163 2.7× 93 1.7× 7 0.3× 21 512
Hyeon-Su Ro South Korea 11 213 1.0× 30 0.4× 99 1.6× 13 0.2× 10 0.4× 34 323

Countries citing papers authored by Emily T. Beebe

Since Specialization
Citations

This map shows the geographic impact of Emily T. Beebe'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 Emily T. Beebe with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Emily T. Beebe more than expected).

Fields of papers citing papers by Emily T. Beebe

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Emily T. Beebe. 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 Emily T. Beebe. The network helps show where Emily T. Beebe may publish in the future.

Co-authorship network of co-authors of Emily T. Beebe

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

All Works

17 of 17 papers shown
1.
Takasuka, Taichi E., Hoon Kim, Kai Deng, et al.. (2023). Quantitative Analysis of The High‐Yield Hydrolysis of Kelp by Laminarinase and Alginate Lyase. ChemBioChem. 24(20). e202300357–e202300357. 4 indexed citations
2.
Smith, Rebecca A., Emily T. Beebe, C.A. Bingman, et al.. (2022). Identification and characterization of a set of monocot BAHD monolignol transferases. PLANT PHYSIOLOGY. 189(1). 37–48. 13 indexed citations
3.
Vries, Lisanne de, Rebecca A. Smith, Yaseen Mottiar, et al.. (2021). pHBMT1, a BAHD-family monolignol acyltransferase, mediates lignin acylation in poplar. PLANT PHYSIOLOGY. 188(2). 1014–1027. 29 indexed citations
4.
Matsumoto, Kazunori, et al.. (2021). Mannose- and Mannobiose-Specific Responses of the Insect-Associated Cellulolytic Bacterium Streptomyces sp. Strain SirexAA-E. Applied and Environmental Microbiology. 87(14). e0271920–e0271920. 9 indexed citations
5.
Karlen, Steven D., Alan Higbee, Emily T. Beebe, et al.. (2020). A bacterial biosynthetic pathway for methylated furan fatty acids. Journal of Biological Chemistry. 295(29). 9786–9801. 19 indexed citations
6.
Aydın, Deniz, Robert Smith, Vanessa Linke, et al.. (2019). An Isoprene Lipid-Binding Protein Promotes Eukaryotic Coenzyme Q Biosynthesis. Molecular Cell. 73(4). 763–774.e10. 31 indexed citations
7.
Kontur, Wayne S., Emily T. Beebe, Kirk A. Vander Meulen, et al.. (2018). A heterodimeric glutathione S-transferase that stereospecifically breaks lignin's β(R)-aryl ether bond reveals the diversity of bacterial β-etherases. Journal of Biological Chemistry. 294(6). 1877–1890. 38 indexed citations
8.
Minkoff, Benjamin B., Shin‐ichi Makino, Miyoshi Haruta, et al.. (2017). A cell-free method for expressing and reconstituting membrane proteins enables functional characterization of the plant receptor-like protein kinase FERONIA. Journal of Biological Chemistry. 292(14). 5932–5942. 18 indexed citations
9.
Pattathil, Sivakumar, Emily T. Beebe, Kai Deng, et al.. (2017). Determination of glycoside hydrolase specificities during hydrolysis of plant cell walls using glycome profiling. Biotechnology for Biofuels. 10(1). 31–31. 16 indexed citations
10.
Ли, Бо, Emily T. Beebe, Daisuke Urano, et al.. (2016). Cell-free translation and purification of Arabidopsis thaliana regulator of G signaling 1 protein. Protein Expression and Purification. 126. 33–41. 8 indexed citations
11.
Beebe, Emily T., Shin‐ichi Makino, John L. Markley, & Brian G. Fox. (2014). Automated Cell-Free Protein Production Methods for Structural Studies. Methods in molecular biology. 1140. 117–135. 4 indexed citations
12.
Jarecki, Brian W., Shin‐ichi Makino, Emily T. Beebe, Brian G. Fox, & Baron Chanda. (2013). Function of Shaker Potassium Channels Produced by Cell-Free Translation Upon Injection into Xenopus Oocytes. Biophysical Journal. 104(2). 197a–197a. 1 indexed citations
13.
Jarecki, Brian W., et al.. (2013). Function of Shaker potassium channels produced by cell-free translation upon injection into Xenopus oocytes. Scientific Reports. 3(1). 1040–1040. 19 indexed citations
14.
Singh, Shanteri, Aram Chang, K.E. Helmich, et al.. (2013). Structural and Functional Characterization of CalS11, a TDP-Rhamnose 3′-O-Methyltransferase Involved in Calicheamicin Biosynthesis. ACS Chemical Biology. 8(7). 1632–1639. 9 indexed citations
15.
Makino, Shin‐ichi, Emily T. Beebe, John L. Markley, & Brian G. Fox. (2013). Cell-Free Protein Synthesis for Functional and Structural Studies. Methods in molecular biology. 161–178. 18 indexed citations
16.
Aly, Khaled A., Emily T. Beebe, Chi Ho Chan, et al.. (2012). Cell‐free production of integral membrane aspartic acid proteases reveals zinc‐dependent methyltransferase activity of the Pseudomonas aeruginosa prepilin peptidase PilD. MicrobiologyOpen. 2(1). 94–104. 19 indexed citations
17.
Beebe, Emily T., Shin‐ichi Makino, Akira Nozawa, et al.. (2010). Robotic large-scale application of wheat cell-free translation to structural studies including membrane proteins. New Biotechnology. 28(3). 239–249. 28 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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