Thomas S. Hays

7.4k total citations
66 papers, 3.9k citations indexed

About

Thomas S. Hays is a scholar working on Molecular Biology, Cell Biology and Cellular and Molecular Neuroscience. According to data from OpenAlex, Thomas S. Hays has authored 66 papers receiving a total of 3.9k indexed citations (citations by other indexed papers that have themselves been cited), including 45 papers in Molecular Biology, 42 papers in Cell Biology and 9 papers in Cellular and Molecular Neuroscience. Recurrent topics in Thomas S. Hays's work include Microtubule and mitosis dynamics (38 papers), Cellular transport and secretion (17 papers) and Photosynthetic Processes and Mechanisms (16 papers). Thomas S. Hays is often cited by papers focused on Microtubule and mitosis dynamics (38 papers), Cellular transport and secretion (17 papers) and Photosynthetic Processes and Mechanisms (16 papers). Thomas S. Hays collaborates with scholars based in United States, France and Austria. Thomas S. Hays's co-authors include Maura McGrail, Edward Wojcik, Sarah Mische, Madeline Serr, Mary E. Porter, J. Richard McIntosh, Paula M. Grissom, Curt M. Pfarr, Martine Coué and Stanley Iyadurai and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Thomas S. Hays

64 papers receiving 3.8k citations

Peers

Thomas S. Hays
Jay R. Unruh United States
Kevin T. Vaughan United States
Stephen L. Rogers United States
Antonina Roll‐Mecak United States
Simon L. Bullock United Kingdom
Jeremy S. Hyams United Kingdom
K. Kevin Pfister United States
Tama Hasson United States
Jay R. Unruh United States
Thomas S. Hays
Citations per year, relative to Thomas S. Hays Thomas S. Hays (= 1×) peers Jay R. Unruh

Countries citing papers authored by Thomas S. Hays

Since Specialization
Citations

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

Fields of papers citing papers by Thomas S. Hays

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Thomas S. Hays. 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 Thomas S. Hays. The network helps show where Thomas S. Hays may publish in the future.

Co-authorship network of co-authors of Thomas S. Hays

This figure shows the co-authorship network connecting the top 25 collaborators of Thomas S. Hays. A scholar is included among the top collaborators of Thomas S. Hays 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 Thomas S. Hays. Thomas S. Hays 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.
Neisch, Amanda L., et al.. (2025). Dynein-driven regulation of postsynaptic membrane architecture and synaptic function. Journal of Cell Science. 138(5).
2.
Guo, Zongqi, Nikolas Zuchowicz, Jessica Bouwmeester, et al.. (2023). Conduction‐Dominated Cryomesh for Organism Vitrification. Advanced Science. 11(3). e2303317–e2303317. 11 indexed citations
3.
Zhan, Li, Min-gang Li, Thomas S. Hays, & John C. Bischof. (2021). Cryopreservation method for Drosophila melanogaster embryos. Nature Communications. 12(1). 2412–2412. 31 indexed citations
4.
Rebbeck, Robyn T., et al.. (2020). Novel drug discovery platform for spinocerebellar ataxia, using fluorescence technology targeting β-III-spectrin. Journal of Biological Chemistry. 296. 100215–100215. 6 indexed citations
5.
Thomas, David D., et al.. (2017). β-III-spectrin spinocerebellar ataxia type 5 mutation reveals a dominant cytoskeletal mechanism that underlies dendritic arborization. Proceedings of the National Academy of Sciences. 114(44). E9376–E9385. 26 indexed citations
6.
Fealey, Michael E., Fengbin Wang, Albina Orlova, et al.. (2017). Structural basis for high-affinity actin binding revealed by a β-III-spectrin SCA5 missense mutation. Nature Communications. 8(1). 1350–1350. 37 indexed citations
8.
Materassi, Donatello, et al.. (2013). An exact approach for studying cargo transport by an ensemble of molecular motors. PubMed. 6(1). 14–14. 5 indexed citations
9.
Reis, Gerald F., Ge Yang, Lukasz Szpankowski, et al.. (2012). Molecular motor function in axonal transport in vivo probed by genetic and computational analysis inDrosophila. Molecular Biology of the Cell. 23(9). 1700–1714. 67 indexed citations
10.
Mische, Sarah, Yungui He, LingZhi Ma, et al.. (2008). Dynein Light Intermediate Chain: An Essential Subunit That Contributes to Spindle Checkpoint Inactivation. Molecular Biology of the Cell. 19(11). 4918–4929. 57 indexed citations
11.
Iyadurai, Stanley, John T. Robinson, LingZhi Ma, et al.. (2008). Dynein and Star interact in EGFR signaling and ligand trafficking. Journal of Cell Science. 121(16). 2643–2651. 12 indexed citations
12.
Mische, Sarah, Mingang Li, Madeline Serr, & Thomas S. Hays. (2007). Direct Observation of Regulated Ribonucleoprotein Transport Across the Nurse Cell/Oocyte Boundary. Molecular Biology of the Cell. 18(6). 2254–2263. 49 indexed citations
13.
Song, Yujuan, Gregory Benison, Afua Nyarko, Thomas S. Hays, & Elisar Barbar. (2007). Potential Role for Phosphorylation in Differential Regulation of the Assembly of Dynein Light Chains. Journal of Biological Chemistry. 282(23). 17272–17279. 34 indexed citations
14.
Li, Min-gang, Madeline Serr, Eric A. Newman, & Thomas S. Hays. (2004). TheDrosophilatctex-1 Light Chain Is Dispensable for Essential Cytoplasmic Dynein Functions but Is Required during Spermatid Differentiation. Molecular Biology of the Cell. 15(7). 3005–3014. 53 indexed citations
15.
Basto, Renata, Frédéric Scaërou, Sarah Mische, et al.. (2004). In Vivo Dynamics of the Rough Deal Checkpoint Protein during Drosophila Mitosis. Current Biology. 14(1). 56–61. 86 indexed citations
16.
Silvanovich, Andre, Min-gang Li, Madeline Serr, Sarah Mische, & Thomas S. Hays. (2003). The Third P-loop Domain in Cytoplasmic Dynein Heavy Chain Is Essential for Dynein Motor Function and ATP-sensitive Microtubule Binding. Molecular Biology of the Cell. 14(4). 1355–1365. 77 indexed citations
17.
Iyadurai, Stanley, Mingang Li, Susan P. Gilbert, & Thomas S. Hays. (1999). Evidence for cooperative interactions between the two motor domains of cytoplasmic dynein. Current Biology. 9(14). 771–774. 19 indexed citations
18.
Gepner, J. I., Min-gang Li, Susan A. Ludmann, et al.. (1996). Cytoplasmic Dynein Function Is Essential in Drosophila melanogaster. Genetics. 142(3). 865–878. 111 indexed citations
19.
Hays, Thomas S., Renate Deuring, Barbara Robertson, Mary Prout, & Margaret T. Fuller. (1989). Interacting Proteins Identified by Genetic Interactions: a Missense Mutation in α-Tubulin Fails to Complement Alleles of the Testis-Specific β-Tubulin Gene of Drosophila melanogaster. Molecular and Cellular Biology. 9(3). 875–884. 13 indexed citations
20.
Hays, Thomas S. & Edward D. Salmon. (1982). The action of colchicine on microtubules on isolated mitotic spindles. The Journal of Cell Biology. 95. 2 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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