Frank Shewmaker

4.9k total citations · 1 hit paper
60 papers, 3.8k citations indexed

About

Frank Shewmaker is a scholar working on Molecular Biology, Neurology and Physiology. According to data from OpenAlex, Frank Shewmaker has authored 60 papers receiving a total of 3.8k indexed citations (citations by other indexed papers that have themselves been cited), including 57 papers in Molecular Biology, 20 papers in Neurology and 16 papers in Physiology. Recurrent topics in Frank Shewmaker's work include Prion Diseases and Protein Misfolding (33 papers), Neurological diseases and metabolism (20 papers) and Alzheimer's disease research and treatments (16 papers). Frank Shewmaker is often cited by papers focused on Prion Diseases and Protein Misfolding (33 papers), Neurological diseases and metabolism (20 papers) and Alzheimer's disease research and treatments (16 papers). Frank Shewmaker collaborates with scholars based in United States, Russia and Germany. Frank Shewmaker's co-authors include Reed B. Wickner, Dmitry Kryndushkin, Robert Tycko, Herman K. Edskes, Ryan P. McGlinchey, Zachary Monahan, Shannon N. Rhoads, Nicolas L. Fawzi, Toru Nakayashiki and Veronica H. Ryan and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and The EMBO Journal.

In The Last Decade

Frank Shewmaker

60 papers receiving 3.8k citations

Hit Papers

Phosphorylation of the FUS low‐complexity domain disrupts... 2017 2026 2020 2023 2017 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
Frank Shewmaker United States 33 3.3k 841 680 666 462 60 3.8k
Jörg Tatzelt Germany 37 3.9k 1.2× 981 1.2× 900 1.3× 1.4k 2.0× 838 1.8× 96 4.9k
Randal Halfmann United States 20 2.8k 0.8× 457 0.5× 204 0.3× 516 0.8× 224 0.5× 38 3.1k
Brandon H. Toyama United States 11 2.0k 0.6× 788 0.9× 144 0.2× 378 0.6× 286 0.6× 12 2.4k
David W. Colby United States 21 2.2k 0.7× 672 0.8× 237 0.3× 636 1.0× 392 0.8× 23 2.6k
Anil G. Cashikar United States 20 2.5k 0.8× 1.1k 1.3× 886 1.3× 377 0.6× 137 0.3× 32 3.8k
Sarah Meehan United Kingdom 23 2.6k 0.8× 1.6k 1.9× 269 0.4× 162 0.2× 155 0.3× 31 3.7k
Lin Guo United States 24 2.5k 0.8× 247 0.3× 852 1.3× 102 0.2× 30 0.1× 71 3.5k
Dorothee Dormann Germany 29 3.8k 1.1× 392 0.5× 2.2k 3.2× 321 0.5× 26 0.1× 50 5.2k
Lukasz Goldschmidt United States 12 1.8k 0.5× 919 1.1× 165 0.2× 104 0.2× 86 0.2× 15 2.4k
Amandine Molliex United States 8 3.0k 0.9× 369 0.4× 736 1.1× 121 0.2× 20 0.0× 10 3.5k

Countries citing papers authored by Frank Shewmaker

Since Specialization
Citations

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

Fields of papers citing papers by Frank Shewmaker

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Frank Shewmaker

This figure shows the co-authorship network connecting the top 25 collaborators of Frank Shewmaker. A scholar is included among the top collaborators of Frank Shewmaker 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 Frank Shewmaker. Frank Shewmaker 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.
Perdikari, Theodora Myrto, Victoria Johnson, Jeremy T. Smyth, et al.. (2021). The oncogenic transcription factor FUS-CHOP can undergo nuclear liquid–liquid phase separation. Journal of Cell Science. 134(17). 37 indexed citations
2.
Rhoads, Shannon N., et al.. (2020). The prion-like domain of Fused in Sarcoma is phosphorylated by multiple kinases affecting liquid- and solid-phase transitions. Molecular Biology of the Cell. 31(23). 2522–2536. 16 indexed citations
3.
Rhoads, Shannon N., Zachary Monahan, Andrew Y. T. Leung, et al.. (2018). The prionlike domain of FUS is multiphosphorylated following DNA damage without altering nuclear localization. Molecular Biology of the Cell. 29(15). 1786–1797. 42 indexed citations
4.
Wickner, Reed B., Dmitry Kryndushkin, Frank Shewmaker, Ryan P. McGlinchey, & Herman K. Edskes. (2018). Study of Amyloids Using Yeast. Methods in molecular biology. 313–339. 6 indexed citations
5.
Daigle, J. Gavin, Karthik Krishnamurthy, Nandini Ramesh, et al.. (2016). Pur-alpha regulates cytoplasmic stress granule dynamics and ameliorates FUS toxicity. Acta Neuropathologica. 131(4). 605–620. 48 indexed citations
6.
Monahan, Zachary, Frank Shewmaker, & Udai Bhan Pandey. (2016). Stress granules at the intersection of autophagy and ALS. Brain Research. 1649(Pt B). 189–200. 84 indexed citations
7.
Villapol, Sonia, Dmitry Kryndushkin, Ashley Campbell, et al.. (2015). Hepatic Expression of Serum Amyloid A1 Is Induced by Traumatic Brain Injury and Modulated by Telmisartan. American Journal Of Pathology. 185(10). 2641–2652. 34 indexed citations
8.
Kryndushkin, Dmitry, Natalia Pripuzova, Barrington G. Burnett, & Frank Shewmaker. (2013). Non-targeted Identification of Prions and Amyloid-forming Proteins from Yeast and Mammalian Cells. Journal of Biological Chemistry. 288(38). 27100–27111. 55 indexed citations
9.
Kryndushkin, Dmitry, Reed B. Wickner, & Frank Shewmaker. (2011). FUS/TLS forms cytoplasmic aggregates, inhibits cell growth and interacts with TDP-43 in a yeast model of amyotrophic lateral sclerosis. Protein & Cell. 2(3). 223–236. 76 indexed citations
10.
Kryndushkin, Dmitry & Frank Shewmaker. (2011). Modeling ALS and FTLD proteinopathies in yeast: An efficient approach for studying protein aggregation and toxicity. Prion. 5(4). 250–257. 18 indexed citations
11.
Wickner, Reed B., Herman K. Edskes, Frank Shewmaker, et al.. (2010). The relationship of prions and translation. Wiley Interdisciplinary Reviews - RNA. 1(1). 81–89. 10 indexed citations
12.
Wickner, Reed B., Frank Shewmaker, Herman K. Edskes, et al.. (2010). Prion amyloid structure explains templating: how proteins can be genes. FEMS Yeast Research. 10(8). 980–991. 55 indexed citations
13.
Shewmaker, Frank, Ryan P. McGlinchey, Kent R. Thurber, et al.. (2009). The Functional Curli Amyloid Is Not Based on In-register Parallel β-Sheet Structure. Journal of Biological Chemistry. 284(37). 25065–25076. 109 indexed citations
14.
Wickner, Reed B., Herman K. Edskes, Frank Shewmaker, Dmitry Kryndushkin, & Julie Nemecek. (2009). Prion variants, species barriers, generation and propagation. Journal of Biology. 8(5). 47–47. 19 indexed citations
15.
Zhou, Zheng, Jun-Bao Fan, Haili Zhu, et al.. (2009). Crowded Cell-like Environment Accelerates the Nucleation Step of Amyloidogenic Protein Misfolding. Journal of Biological Chemistry. 284(44). 30148–30158. 86 indexed citations
16.
Shewmaker, Frank & Reed B. Wickner. (2006). Ageing in yeast does not enhance prion generation. Yeast. 23(16). 1123–1128. 6 indexed citations
17.
Wickner, Reed B., Herman K. Edskes, & Frank Shewmaker. (2006). How to find a prion: [URE3], [PSI+] and [β]. Methods. 39(1). 3–8. 39 indexed citations
18.
Shewmaker, Frank, Michael J. Kerner, Manajit Hayer‐Hartl, et al.. (2004). A mobile loop order–disorder transition modulates the speed of chaperonin cycling. Protein Science. 13(8). 2139–2148. 16 indexed citations
19.
Guidry, Jessie J., Frank Shewmaker, Karol Maskos, Samuel J. Landry, & Pernilla Wittung‐Stafshede. (2003). Probing the interface in a human co-chaperonin heptamer: residues disrupting oligomeric unfolded state identified. BMC Biochemistry. 4(1). 14–14. 16 indexed citations
20.
Shewmaker, Frank, Karol Maskos, Carlos Simmerling, & Samuel J. Landry. (2001). The Disordered Mobile Loop of GroES Folds into a Defined β-Hairpin upon Binding GroEL. Journal of Biological Chemistry. 276(33). 31257–31264. 31 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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