Beth Pietrak

3.1k total citations · 1 hit paper
22 papers, 1.1k citations indexed

About

Beth Pietrak is a scholar working on Molecular Biology, Physiology and Computational Theory and Mathematics. According to data from OpenAlex, Beth Pietrak has authored 22 papers receiving a total of 1.1k indexed citations (citations by other indexed papers that have themselves been cited), including 15 papers in Molecular Biology, 8 papers in Physiology and 7 papers in Computational Theory and Mathematics. Recurrent topics in Beth Pietrak's work include Alzheimer's disease research and treatments (8 papers), Computational Drug Discovery Methods (7 papers) and Protein Structure and Dynamics (6 papers). Beth Pietrak is often cited by papers focused on Alzheimer's disease research and treatments (8 papers), Computational Drug Discovery Methods (7 papers) and Protein Structure and Dynamics (6 papers). Beth Pietrak collaborates with scholars based in United States, United Kingdom and Belgium. Beth Pietrak's co-authors include Nicholas D. Adams, Ralph J. DeBerardinis, Chendong Yang, Pamela Swain, Lei Jiang, Seth J. Parker, Lance S. Terada, Alexander A. Shestov, Benjamin Schwartz and Christian M. Metallo and has published in prestigious journals such as Nature, Nature Communications and Biochemistry.

In The Last Decade

Beth Pietrak

22 papers receiving 1.0k citations

Hit Papers

Reductive carboxylation supports redox homeostasis during... 2016 2026 2019 2022 2016 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
Beth Pietrak United States 15 660 364 261 244 170 22 1.1k
Zhili Xin United States 22 1.0k 1.6× 177 0.5× 183 0.7× 106 0.4× 93 0.5× 44 1.5k
Xiaoshan Min United States 22 1.3k 2.0× 83 0.2× 79 0.3× 252 1.0× 118 0.7× 34 2.0k
Jay S. Tung United States 16 981 1.5× 123 0.3× 125 0.5× 129 0.5× 94 0.6× 18 1.3k
Peppi Prasit United States 21 592 0.9× 150 0.4× 45 0.2× 234 1.0× 189 1.1× 44 1.2k
Sukjoon Yoon South Korea 21 702 1.1× 219 0.6× 123 0.5× 111 0.5× 53 0.3× 54 974
Lemma Kifle United States 7 884 1.3× 85 0.2× 193 0.7× 158 0.6× 68 0.4× 9 1.1k
Agnés C. L. Martin United Kingdom 7 523 0.8× 316 0.9× 74 0.3× 190 0.8× 87 0.5× 7 784
Zhiqiang Cheng China 16 509 0.8× 270 0.7× 52 0.2× 116 0.5× 94 0.6× 50 1.0k
Andrew S. Tasker United States 20 681 1.0× 114 0.3× 84 0.3× 185 0.8× 49 0.3× 45 1.4k
Giovanni Di Maira Italy 19 1.0k 1.6× 119 0.3× 74 0.3× 87 0.4× 46 0.3× 41 1.6k

Countries citing papers authored by Beth Pietrak

Since Specialization
Citations

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

Fields of papers citing papers by Beth Pietrak

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Beth Pietrak

This figure shows the co-authorship network connecting the top 25 collaborators of Beth Pietrak. A scholar is included among the top collaborators of Beth Pietrak 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 Beth Pietrak. Beth Pietrak 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.
Yu, Xiaodi, Rosalie Matico, Dhruv Chauhan, et al.. (2024). Structural basis for the oligomerization-facilitated NLRP3 activation. Nature Communications. 15(1). 1164–1164. 25 indexed citations
2.
Romanov‐Michailidis, Fedor, Chien‐Chi Hsiao, Bradley S. Miller, et al.. (2023). Discovery of an Oral, Beyond-Rule-of-Five Mcl-1 Protein–Protein Interaction Modulator with the Potential of Treating Hematological Malignancies. Journal of Medicinal Chemistry. 66(9). 6122–6148. 16 indexed citations
3.
Matico, Rosalie, Lawrence M. Szewczuk, Beth Pietrak, et al.. (2019). Modular Protein Ligation: A New Paradigm as a Reagent Platform for Pre-Clinical Drug Discovery. Scientific Reports. 9(1). 13078–13078. 2 indexed citations
4.
Jiang, Lei, Alexander A. Shestov, Pamela Swain, et al.. (2016). Reductive carboxylation supports redox homeostasis during anchorage-independent growth. Nature. 532(7598). 255–258. 432 indexed citations breakdown →
5.
Zhao, Huizhen, Yong Jiang, Sharon Sweitzer, et al.. (2014). Crystallographic Structure of a Small Molecule SIRT1 Activator/Enzyme Complex. Biophysical Journal. 106(2). 646a–646a. 6 indexed citations
6.
Rendina, Alan R., Beth Pietrak, Angela Smallwood, et al.. (2013). Mutant IDH1 Enhances the Production of 2-Hydroxyglutarate Due to Its Kinetic Mechanism. Biochemistry. 52(26). 4563–4577. 64 indexed citations
7.
Zhu, Hong, Mary Beth Young, Philippe G. Nantermet, et al.. (2010). Rapid P1 SAR of brain penetrant tertiary carbinamine derived BACE inhibitors. Bioorganic & Medicinal Chemistry Letters. 20(5). 1779–1782. 14 indexed citations
8.
Hills, Ivory D., M. Katharine Holloway, Hong Zhu, et al.. (2009). A conformational constraint improves a β-secretase inhibitor but for an unexpected reason. Bioorganic & Medicinal Chemistry Letters. 19(17). 4993–4995. 11 indexed citations
9.
Stachel, Shawn J., Craig A. Coburn, Kristen L. Jones, et al.. (2009). Discovery of aminoheterocycles as a novel β-secretase inhibitor class: pH dependence on binding activity part 1. Bioorganic & Medicinal Chemistry Letters. 19(11). 2977–2980. 49 indexed citations
10.
Holloway, M. Katharine, Georgia B. McGaughey, Craig A. Coburn, et al.. (2006). Evaluating scoring functions for docking and designing β-secretase inhibitors. Bioorganic & Medicinal Chemistry Letters. 17(3). 823–827. 17 indexed citations
11.
McGaughey, Georgia B., Dennis Colussi, Samuel Graham, et al.. (2006). β-Secretase (BACE-1) inhibitors: Accounting for 10s loop flexibility using rigid active sites. Bioorganic & Medicinal Chemistry Letters. 17(4). 1117–1121. 35 indexed citations
12.
Coburn, Craig A., Shawn J. Stachel, Thomas G. Steele, et al.. (2006). BACE-1 inhibition by a series of ψ[CH2NH] reduced amide isosteres. Bioorganic & Medicinal Chemistry Letters. 16(14). 3635–3638. 45 indexed citations
13.
Stauffer, Shaun R., Matthew G. Stanton, Alison R. Gregro, et al.. (2006). Discovery and SAR of isonicotinamide BACE-1 inhibitors that bind β-secretase in a N-terminal 10s-loop down conformation. Bioorganic & Medicinal Chemistry Letters. 17(6). 1788–1792. 37 indexed citations
15.
Stachel, Shawn J., Craig A. Coburn, Sethu Sankaranarayanan, et al.. (2006). Macrocyclic Inhibitors of β-Secretase:  Functional Activity in an Animal Model.. Journal of Medicinal Chemistry. 49(24). 7252–7252. 1 indexed citations
16.
Stachel, Shawn J., Craig A. Coburn, Sethu Sankaranarayanan, et al.. (2006). Macrocyclic Inhibitors of β-Secretase:  Functional Activity in an Animal Model. Journal of Medicinal Chemistry. 49(21). 6147–6150. 67 indexed citations
17.
Stachel, Shawn J., Craig A. Coburn, Thomas G. Steele, et al.. (2005). Conformationally biased P3 amide replacements of β-secretase inhibitors. Bioorganic & Medicinal Chemistry Letters. 16(3). 641–644. 55 indexed citations
18.
Pietrak, Beth, Ming‐Chih Crouthamel, Katherine Tugusheva, et al.. (2005). Biochemical and cell-based assays for characterization of BACE-1 inhibitors. Analytical Biochemistry. 342(1). 144–151. 37 indexed citations
19.
Lai, Ming‐Tain, Ming‐Chih Crouthamel, Jillian DiMuzio, et al.. (2005). A presenilin‐independent aspartyl protease prefers the γ‐42 site cleavage. Journal of Neurochemistry. 96(1). 118–125. 23 indexed citations
20.
Cao, Hong, Beth Pietrak, & Charles Grubmeyer. (2002). Quinolinate Phosphoribosyltransferase:  Kinetic Mechanism for a Type II PRTase. Biochemistry. 41(10). 3520–3528. 24 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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