Matthew J. Tyska

6.8k total citations · 1 hit paper
90 papers, 4.8k citations indexed

About

Matthew J. Tyska is a scholar working on Molecular Biology, Cell Biology and Cardiology and Cardiovascular Medicine. According to data from OpenAlex, Matthew J. Tyska has authored 90 papers receiving a total of 4.8k indexed citations (citations by other indexed papers that have themselves been cited), including 49 papers in Molecular Biology, 39 papers in Cell Biology and 22 papers in Cardiology and Cardiovascular Medicine. Recurrent topics in Matthew J. Tyska's work include Cellular Mechanics and Interactions (26 papers), Cardiomyopathy and Myosin Studies (22 papers) and Muscle Physiology and Disorders (20 papers). Matthew J. Tyska is often cited by papers focused on Cellular Mechanics and Interactions (26 papers), Cardiomyopathy and Myosin Studies (22 papers) and Muscle Physiology and Disorders (20 papers). Matthew J. Tyska collaborates with scholars based in United States, France and South Korea. Matthew J. Tyska's co-authors include Russell E. McConnell, Mark S. Mooseker, Nathan E. Grega‐Larson, David M. Warshaw, Scott W. Crawley, Rajalakshmi Nambiar, Robert J. Coffey, David A. Shifrin, Daisuke Hoshino and Seema Sinha and has published in prestigious journals such as Cell, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Matthew J. Tyska

82 papers receiving 4.8k citations

Hit Papers

Blebbisomes are large, or... 2025 2026 2025 5 10 15 20

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Matthew J. Tyska United States 38 2.9k 1.3k 914 711 444 90 4.8k
Xuefei Ma United States 28 2.1k 0.7× 1.8k 1.4× 714 0.8× 183 0.3× 269 0.6× 55 4.2k
Elisabeth Ehler United Kingdom 52 4.9k 1.7× 1.4k 1.1× 3.2k 3.5× 355 0.5× 283 0.6× 137 7.7k
Ruowen Ge Singapore 35 2.1k 0.7× 554 0.4× 263 0.3× 560 0.8× 656 1.5× 95 3.8k
Fons J. Verbeek Netherlands 32 2.2k 0.7× 609 0.5× 265 0.3× 294 0.4× 455 1.0× 153 4.6k
François Aguet United States 30 3.1k 1.0× 862 0.7× 266 0.3× 775 1.1× 516 1.2× 70 5.2k
Simon Morley United Kingdom 45 4.0k 1.4× 503 0.4× 741 0.8× 242 0.3× 388 0.9× 138 5.3k
Michael D. Henry United States 41 5.5k 1.9× 1.5k 1.2× 225 0.2× 1.2k 1.7× 550 1.2× 105 8.4k
Alistair N. Hume United Kingdom 27 3.9k 1.3× 2.4k 1.8× 185 0.2× 1.2k 1.7× 915 2.1× 50 5.7k
Nan Hu China 40 2.8k 0.9× 237 0.2× 1.1k 1.2× 825 1.2× 617 1.4× 199 6.1k

Countries citing papers authored by Matthew J. Tyska

Since Specialization
Citations

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

Fields of papers citing papers by Matthew J. Tyska

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Matthew J. Tyska. 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 Matthew J. Tyska. The network helps show where Matthew J. Tyska may publish in the future.

Co-authorship network of co-authors of Matthew J. Tyska

This figure shows the co-authorship network connecting the top 25 collaborators of Matthew J. Tyska. A scholar is included among the top collaborators of Matthew J. Tyska 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 Matthew J. Tyska. Matthew J. Tyska 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.
Arora, Karan, Taylor L. Sheehy, C. Patrick McAtee, et al.. (2025). Macromolecular Diamidobenzimidazole Conjugates Can Activate Stimulator of Interferon Genes. Journal of the American Chemical Society. 147(38). 35149–35163.
2.
Choudhary, Dharmendra, Abigail C. Neininger, Alaina H. Willet, et al.. (2025). Nonmuscle α-Actinin-4 Couples Sarcomere Function to Cardiac Remodeling. Circulation Research. 138(1). e326412–e326412.
3.
Jeppesen, Dennis K., Jérôme Ambroise, Evan Krystofiak, et al.. (2025). Blebbisomes are large, organelle-rich extracellular vesicles with cell-like properties. Nature Cell Biology. 27(3). 438–448. 20 indexed citations breakdown →
4.
Meenderink, Leslie M., et al.. (2025). Microvillus inclusion disease-causing MYO5B point mutations exert differential effects on motor function. Journal of Biological Chemistry. 301(4). 108328–108328. 1 indexed citations
5.
Fitz, Gillian N., et al.. (2024). Mitotic spindle positioning protein (MISP) preferentially binds to aged F-actin. Journal of Biological Chemistry. 300(5). 107279–107279.
6.
Gaeta, Isabella & Matthew J. Tyska. (2023). BioID2 screening identifies KIAA1671 as an EPS8 proximal factor that marks sites of microvillus growth. Molecular Biology of the Cell. 34(4). ar31–ar31.
7.
Giogha, Cristina, Clare V. Oates, Paul J. McMillan, et al.. (2022). Targeting of microvillus protein Eps8 by the NleH effector kinases from enteropathogenic E. coli. Proceedings of the National Academy of Sciences. 119(34). e2204332119–e2204332119. 7 indexed citations
8.
Gaeta, Isabella, Mengyang Zhao, Ruining Deng, et al.. (2021). ASIST: Annotation-free synthetic instance segmentation and tracking by adversarial simulations. Computers in Biology and Medicine. 134. 104501–104501. 11 indexed citations
9.
Seervai, Riyad N. H., Rahul Jangid, Menuka Karki, et al.. (2020). The Huntingtin-interacting protein SETD2/HYPB is an actin lysine methyltransferase. Science Advances. 6(40). 32 indexed citations
10.
Tyska, Matthew J., et al.. (2020). The small EF-hand protein CALML4 functions as a critical myosin light chain within the intermicrovillar adhesion complex. Journal of Biological Chemistry. 295(28). 9281–9296. 20 indexed citations
11.
Smith, Cody J., et al.. (2019). Actin assembly and non-muscle myosin activity drive dendrite retraction in an UNC-6/Netrin dependent self-avoidance response. PLoS Genetics. 15(6). e1008228–e1008228. 19 indexed citations
12.
Meenderink, Leslie M., et al.. (2019). Actin Dynamics Drive Microvillar Motility and Clustering during Brush Border Assembly. Developmental Cell. 50(5). 545–556.e4. 46 indexed citations
13.
Li, Jianchao, et al.. (2017). Structure of Myo7b/USH1C complex suggests a general PDZ domain binding mode by MyTH4-FERM myosins. Proceedings of the National Academy of Sciences. 114(19). E3776–E3785. 33 indexed citations
14.
Kraft, Lewis J., et al.. (2014). Motor and Tail Homology 1 (TH1) Domains Antagonistically Control Myosin-1 Dynamics. Biophysical Journal. 106(3). 649–658. 10 indexed citations
15.
McConnell, Russell E., et al.. (2011). Proteomic analysis of the enterocyte brush border. American Journal of Physiology-Gastrointestinal and Liver Physiology. 300(5). G914–G926. 83 indexed citations
16.
McConnell, Russell E. & Matthew J. Tyska. (2007). Myosin-1a powers the sliding of apical membrane along microvillar actin bundles. The Journal of Cell Biology. 177(4). 671–681. 77 indexed citations
17.
O’Connell, Christopher B., Matthew J. Tyska, & Mark S. Mooseker. (2006). Myosin at work: Motor adaptations for a variety of cellular functions. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1773(5). 615–630. 75 indexed citations
18.
Post, Penny, et al.. (2002). Myosin-IXb Is a Single-headed and Processive Motor. Journal of Biological Chemistry. 277(14). 11679–11683. 65 indexed citations
19.
Palmiter, Kimberly A., et al.. (1999). Kinetic differences at the single molecule level account for the functional diversity of rabbit cardiac myosin isoforms. The Journal of Physiology. 519(3). 669–678. 101 indexed citations
20.
Lauzon, Anne‐Marie, Matthew J. Tyska, Arthur S. Rovner, et al.. (1998). A 7-amino-acid insert in the heavy chain nucleotide binding loop alters the kinetics of smooth muscle myosin in the laser trap.. Journal of Muscle Research and Cell Motility. 19(8). 825–837. 119 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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