John Shanks

1.7k total citations
24 papers, 1.3k citations indexed

About

John Shanks is a scholar working on Molecular Biology, Cell Biology and Oncology. According to data from OpenAlex, John Shanks has authored 24 papers receiving a total of 1.3k indexed citations (citations by other indexed papers that have themselves been cited), including 20 papers in Molecular Biology, 17 papers in Cell Biology and 4 papers in Oncology. Recurrent topics in John Shanks's work include Microtubule and mitosis dynamics (12 papers), Photosynthetic Processes and Mechanisms (8 papers) and Ubiquitin and proteasome pathways (5 papers). John Shanks is often cited by papers focused on Microtubule and mitosis dynamics (12 papers), Photosynthetic Processes and Mechanisms (8 papers) and Ubiquitin and proteasome pathways (5 papers). John Shanks collaborates with scholars based in United States, Russia and Canada. John Shanks's co-authors include Michael Caplow, Keith D. Wilkinson, Francisca E. Reyes‐Turcu, Harish C. Joshi, Keqiang Ye, Rajeshwar R. Tekmal, Nagalakshmi Keshava, Judith A. Kapp, John A. Petros and Yong Ke and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Molecular Cell.

In The Last Decade

John Shanks

23 papers receiving 1.3k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
John Shanks United States 16 1.0k 442 244 124 101 24 1.3k
Seema Dalal United States 20 900 0.9× 286 0.6× 287 1.2× 233 1.9× 126 1.2× 41 1.5k
Daniel Chelsky United States 20 1.1k 1.1× 205 0.5× 102 0.4× 84 0.7× 87 0.9× 36 1.5k
Francis Tsai United States 21 2.1k 2.0× 473 1.1× 68 0.3× 65 0.5× 58 0.6× 44 2.4k
He‐Hsuan Hsiao Germany 24 1.3k 1.2× 158 0.4× 130 0.5× 121 1.0× 35 0.3× 39 1.8k
Emily Jackson-Machelski United States 15 928 0.9× 373 0.8× 151 0.6× 177 1.4× 103 1.0× 19 1.2k
Joël Poncet France 24 741 0.7× 149 0.3× 85 0.3× 250 2.0× 349 3.5× 35 1.7k
Kyou‐Hoon Han South Korea 21 1.3k 1.3× 148 0.3× 269 1.1× 77 0.6× 98 1.0× 66 1.6k
Eva Kutějová Slovakia 24 1.4k 1.3× 236 0.5× 70 0.3× 78 0.6× 51 0.5× 57 1.6k
Elżbieta Jankowska Poland 21 894 0.9× 135 0.3× 180 0.7× 71 0.6× 66 0.7× 60 1.4k

Countries citing papers authored by John Shanks

Since Specialization
Citations

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

Fields of papers citing papers by John Shanks

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of John Shanks

This figure shows the co-authorship network connecting the top 25 collaborators of John Shanks. A scholar is included among the top collaborators of John Shanks 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 John Shanks. John Shanks 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.
Chernova, Tatiana A., Denis A. Kiktev, Andrey Romanyuk, et al.. (2017). Yeast Short-Lived Actin-Associated Protein Forms a Metastable Prion in Response to Thermal Stress. Cell Reports. 18(3). 751–761. 41 indexed citations
2.
Horton, J.R., Amanda Engstrom, Xu Liu, et al.. (2015). Characterization of a Linked Jumonji Domain of the KDM5/JARID1 Family of Histone H3 Lysine 4 Demethylases. Journal of Biological Chemistry. 291(6). 2631–2646. 92 indexed citations
3.
Ali, Moiez, Tatiana A. Chernova, Gary P. Newnam, et al.. (2014). Stress-dependent Proteolytic Processing of the Actin Assembly Protein Lsb1 Modulates a Yeast Prion. Journal of Biological Chemistry. 289(40). 27625–27639. 25 indexed citations
4.
Chernova, Tatiana A., Andrey Romanyuk, Tatiana Karpova, et al.. (2011). Prion Induction by the Short-Lived, Stress-Induced Protein Lsb2 Is Regulated by Ubiquitination and Association with the Actin Cytoskeleton. Molecular Cell. 43(2). 242–252. 71 indexed citations
5.
Shanks, John, et al.. (2011). Pieces of Me.
6.
Shanks, John, Mary N. Burtnick, Paul J. Brett, et al.. (2009). Burkholderia mallei tssM Encodes a Putative Deubiquitinase That Is Secreted and Expressed inside Infected RAW 264.7 Murine Macrophages. Infection and Immunity. 77(4). 1636–1648. 46 indexed citations
7.
Nicholson, Benjamin, Craig A. Leach, Seth J. Goldenberg, et al.. (2008). Characterization of ubiquitin and ubiquitin‐like‐protein isopeptidase activities. Protein Science. 17(6). 1035–1043. 115 indexed citations
8.
Messick, Troy E., Ayaka J. Iwata, Kathryn L. Sarachan, et al.. (2008). Structural Basis for Ubiquitin Recognition by the Otu1 Ovarian Tumor Domain Protein. Journal of Biological Chemistry. 283(16). 11038–11049. 91 indexed citations
9.
Reyes‐Turcu, Francisca E., John Shanks, David Komander, & Keith D. Wilkinson. (2008). Recognition of Polyubiquitin Isoforms by the Multiple Ubiquitin Binding Modules of Isopeptidase T. Journal of Biological Chemistry. 283(28). 19581–19592. 117 indexed citations
10.
Chernova, Tatiana A., et al.. (2003). Pleiotropic Effects of Ubp6 Loss on Drug Sensitivities and Yeast Prion Are Due to Depletion of the Free Ubiquitin Pool. Journal of Biological Chemistry. 278(52). 52102–52115. 96 indexed citations
11.
Caplow, Michael & John Shanks. (1998). Microtubule Dynamic Instability Does Not Result from Stabilization of Microtubules by Tubulin-GDP-Pi Subunits. Biochemistry. 37(37). 12994–13002. 7 indexed citations
12.
Ye, Keqiang, Yong Ke, Nagalakshmi Keshava, et al.. (1998). Opium alkaloid noscapine is an antitumor agent that arrests metaphase and induces apoptosis in dividing cells. Proceedings of the National Academy of Sciences. 95(4). 1601–1606. 296 indexed citations
13.
Reid, W. Darlene, et al.. (1997). Regional and Fiber-Type Percentages and Sizes in the Hamster Diaphragm After Swim Training. Physical Therapy. 77(2). 178–186. 4 indexed citations
14.
Caplow, Michael & John Shanks. (1996). Evidence that a single monolayer tubulin-GTP cap is both necessary and sufficient to stabilize microtubules.. Molecular Biology of the Cell. 7(4). 663–675. 117 indexed citations
15.
Caplow, Michael & John Shanks. (1995). Induction of microtubule catastrophe by formation of tubulin-GDP and apotubulin subunits at microtubule ends. Biochemistry. 34(48). 15732–15741. 22 indexed citations
16.
Caplow, Michael & John Shanks. (1990). Mechanism for oscillatory assembly of microtubules.. Journal of Biological Chemistry. 265(3). 1414–1418. 8 indexed citations
17.
Caplow, Michael, et al.. (1989). Stabilization of microtubules by tubulin-GDP-inorganic phosphate subunits. Biochemistry. 28(20). 8136–8141. 34 indexed citations
18.
Caplow, Michael, et al.. (1988). Kinetics and mechanism of microtubule length changes by dynamic instability.. Journal of Biological Chemistry. 263(22). 10943–10951. 7 indexed citations
19.
Caplow, Michael, John Shanks, & Bruna P. Brylawski. (1986). Differentiation between dynamic instability and end-to-end annealing models for length changes of steady-state microtubules.. Journal of Biological Chemistry. 261(34). 16233–16240. 26 indexed citations
20.
Caplow, Michael, John Shanks, & Bruna P. Brylawski. (1985). Concerning the anomalous kinetic behavior of microtubules.. Journal of Biological Chemistry. 260(23). 12675–12679. 13 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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