Nathan T. Wright

3.4k total citations
82 papers, 2.5k citations indexed

About

Nathan T. Wright is a scholar working on Molecular Biology, Cardiology and Cardiovascular Medicine and Biomedical Engineering. According to data from OpenAlex, Nathan T. Wright has authored 82 papers receiving a total of 2.5k indexed citations (citations by other indexed papers that have themselves been cited), including 36 papers in Molecular Biology, 14 papers in Cardiology and Cardiovascular Medicine and 14 papers in Biomedical Engineering. Recurrent topics in Nathan T. Wright's work include Cardiomyopathy and Myosin Studies (11 papers), S100 Proteins and Annexins (9 papers) and Cellular Mechanics and Interactions (6 papers). Nathan T. Wright is often cited by papers focused on Cardiomyopathy and Myosin Studies (11 papers), S100 Proteins and Annexins (9 papers) and Cellular Mechanics and Interactions (6 papers). Nathan T. Wright collaborates with scholars based in United States, Australia and United Kingdom. Nathan T. Wright's co-authors include J. D. Humphrey, Jay D. Humphrey, David J. Weber, H. Deramond, Stephen M. Belkoff, Danna B. Zimmer, Kristen M. Varney, Ronald N. Harty, Jillian M. Licata and Ziying Han and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and PLoS ONE.

In The Last Decade

Nathan T. Wright

76 papers receiving 2.4k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Nathan T. Wright United States 26 754 442 297 269 246 82 2.5k
Hiroyuki Saito Japan 26 285 0.4× 178 0.4× 224 0.8× 242 0.9× 235 1.0× 137 2.3k
Kim S. Midwood United Kingdom 44 2.1k 2.7× 853 1.9× 490 1.6× 299 1.1× 156 0.6× 86 7.3k
Wilhelm K. Aicher Germany 42 1.6k 2.1× 1.2k 2.7× 493 1.7× 114 0.4× 156 0.6× 156 5.3k
Eric Song United States 32 1.1k 1.4× 246 0.6× 298 1.0× 126 0.5× 74 0.3× 83 3.4k
Akihiro Saito Japan 32 1.1k 1.5× 579 1.3× 541 1.8× 329 1.2× 172 0.7× 170 3.3k
Young Hwan Park South Korea 33 777 1.0× 665 1.5× 829 2.8× 270 1.0× 145 0.6× 203 4.1k
Xiao Zhang China 35 2.1k 2.8× 298 0.7× 552 1.9× 79 0.3× 157 0.6× 183 4.0k
John L. Robertson United States 37 894 1.2× 546 1.2× 1.2k 4.1× 70 0.3× 211 0.9× 167 4.6k
Zhihong Wu China 34 902 1.2× 665 1.5× 817 2.8× 80 0.3× 242 1.0× 162 3.6k
Qing Xie China 38 1.6k 2.1× 270 0.6× 194 0.7× 103 0.4× 112 0.5× 168 4.1k

Countries citing papers authored by Nathan T. Wright

Since Specialization
Citations

This map shows the geographic impact of Nathan T. Wright'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 Nathan T. Wright with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Nathan T. Wright more than expected).

Fields of papers citing papers by Nathan T. Wright

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Nathan T. Wright. 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 Nathan T. Wright. The network helps show where Nathan T. Wright may publish in the future.

Co-authorship network of co-authors of Nathan T. Wright

This figure shows the co-authorship network connecting the top 25 collaborators of Nathan T. Wright. A scholar is included among the top collaborators of Nathan T. Wright 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 Nathan T. Wright. Nathan T. Wright 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.
2.
Li, Yi, Nathan T. Wright, & Robert J. Bloch. (2025). The juxtamembrane sequence of small ankyrin 1 mediates the binding of its cytoplasmic domain to SERCA1 and is required for inhibitory activity. Journal of Biological Chemistry. 301(3). 108216–108216. 1 indexed citations
3.
Mariano, Jennifer, et al.. (2024). Compound heterozygous variants in MYBPC1 lead to severe distal arthrogryposis type-1 manifestations. Gene. 910. 148339–148339. 3 indexed citations
4.
Wright, Nathan T., et al.. (2023). Calpain Regulation and Dysregulation—Its Effects on the Intercalated Disk. International Journal of Molecular Sciences. 24(14). 11726–11726. 4 indexed citations
5.
Mičule, Ieva, Nathan T. Wright, Volker Straub, et al.. (2020). Collagen VI-related limb-girdle syndrome caused by frequent mutation in COL6A3 gene with conflicting reports of pathogenicity. Neuromuscular Disorders. 30(6). 483–491. 4 indexed citations
6.
Ackermann, Maegen A., Nicole A. P. Lieberman, Christopher Berndsen, et al.. (2017). Novel obscurins mediate cardiomyocyte adhesion and size via the PI3K/AKT/mTOR signaling pathway. Journal of Molecular and Cellular Cardiology. 111. 27–39. 29 indexed citations
7.
Rossi, Daniela, Johanna Palmio, Anni Evilä, et al.. (2017). A novel FLNC frameshift and an OBSCN variant in a family with distal muscular dystrophy. PLoS ONE. 12(10). e0186642–e0186642. 29 indexed citations
8.
Wright, Nathan T., et al.. (2015). Chemical shift assignments for the Ig2 domain of human obscurin A. Biomolecular NMR Assignments. 10(1). 63–65. 4 indexed citations
9.
Clark, Nicholas, et al.. (2014). Structures of TraI in solution. Journal of Molecular Modeling. 20(6). 2308–2308. 5 indexed citations
10.
Muster, Tim H., et al.. (2013). Towards effective phosphorus recycling from wastewater: Quantity and quality. Chemosphere. 91(5). 676–684. 76 indexed citations
11.
Wright, Nathan T., et al.. (2013). Structure of giant muscle proteins. Frontiers in Physiology. 4. 368–368. 42 indexed citations
12.
Buller, Andrew R., Jason W. Labonte, Michael F. Freeman, et al.. (2012). Autoproteolytic Activation of ThnT Results in Structural Reorganization Necessary for Substrate Binding and Catalysis. Journal of Molecular Biology. 422(4). 508–518. 10 indexed citations
13.
Wright, Nathan T., Brian R. Cannon, Danna B. Zimmer, & David J. Weber. (2009). S100A1: Structure, Function, and Therapeutic Potential. Current Chemical Biology. 3(2). 138–145. 67 indexed citations
14.
Wright, Nathan T., Brian R. Cannon, Paul T. Wilder, et al.. (2009). Solution Structure of S100A1 Bound to the CapZ Peptide (TRTK12). Journal of Molecular Biology. 386(5). 1265–1277. 42 indexed citations
15.
Wright, Nathan T., Benjamin L. Prosser, Kristen M. Varney, et al.. (2008). S100A1 and Calmodulin Compete for the Same Binding Site on Ryanodine Receptor. Journal of Biological Chemistry. 283(39). 26676–26683. 99 indexed citations
16.
Wright, Nathan T., et al.. (2008). Refinement of the solution structure and dynamic properties of Ca2+-bound rat S100B. Journal of Biomolecular NMR. 42(4). 279–286. 18 indexed citations
17.
Prosser, Benjamin L., Nathan T. Wright, Erick O. Hernández‐Ochoa, et al.. (2007). S100A1 Binds to the Calmodulin-binding Site of Ryanodine Receptor and Modulates Skeletal Muscle Excitation-Contraction Coupling. Journal of Biological Chemistry. 283(8). 5046–5057. 89 indexed citations
18.
Rifat, Dalin, Nathan T. Wright, Kristen M. Varney, David J. Weber, & Lindsay W. Black. (2007). Restriction Endonuclease Inhibitor IPI* of Bacteriophage T4: A Novel Structure for a Dedicated Target. Journal of Molecular Biology. 375(3). 720–734. 55 indexed citations
19.
Wright, Nathan T., Kristen M. Varney, Joseph Markowitz, et al.. (2005). The Three-dimensional Solution Structure of Ca2+-bound S100A1 as Determined by NMR Spectroscopy. Journal of Molecular Biology. 353(2). 410–426. 83 indexed citations
20.
Deramond, H., Nathan T. Wright, & Stephen M. Belkoff. (1999). Temperature elevation caused by bone cement polymerization during vertebroplasty. Bone. 25(2). 17S–21S. 273 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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