Thomas C. Squier

6.8k total citations · 1 hit paper
134 papers, 5.7k citations indexed

About

Thomas C. Squier is a scholar working on Molecular Biology, Cell Biology and Materials Chemistry. According to data from OpenAlex, Thomas C. Squier has authored 134 papers receiving a total of 5.7k indexed citations (citations by other indexed papers that have themselves been cited), including 103 papers in Molecular Biology, 24 papers in Cell Biology and 18 papers in Materials Chemistry. Recurrent topics in Thomas C. Squier's work include Ion channel regulation and function (27 papers), Protein Structure and Dynamics (18 papers) and Endoplasmic Reticulum Stress and Disease (16 papers). Thomas C. Squier is often cited by papers focused on Ion channel regulation and function (27 papers), Protein Structure and Dynamics (18 papers) and Endoplasmic Reticulum Stress and Disease (16 papers). Thomas C. Squier collaborates with scholars based in United States, Italy and Canada. Thomas C. Squier's co-authors include Diana J. Bigelow, Liang Shi, James K. Fredrickson, David D. Thomas, John M. Zachara, Yijia Xiong, M. Uljana Mayer, Todd D. Williams, Baowei Chen and Hongye Sun and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and SHILAP Revista de lepidopterología.

In The Last Decade

Thomas C. Squier

133 papers receiving 5.6k citations

Hit Papers

Respiration of metal (hydr)oxides by Shewanella and Geoba... 2007 2026 2013 2019 2007 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
Thomas C. Squier United States 39 3.5k 822 774 565 554 134 5.7k
Tomo̧ko Ohnishi United States 50 5.8k 1.6× 205 0.2× 481 0.6× 732 1.3× 493 0.9× 188 8.2k
Judy Hirst United Kingdom 57 8.3k 2.4× 360 0.4× 444 0.6× 801 1.4× 635 1.1× 133 12.1k
Hiroyuki Arai Japan 51 4.3k 1.2× 339 0.4× 886 1.1× 696 1.2× 454 0.8× 188 7.9k
Dennis R. Winge United States 80 8.3k 2.3× 151 0.2× 722 0.9× 885 1.6× 1.7k 3.1× 227 17.3k
Fei Mao China 40 2.5k 0.7× 305 0.4× 674 0.9× 431 0.8× 377 0.7× 170 7.1k
Robert C. Bray United Kingdom 53 3.1k 0.9× 145 0.2× 521 0.7× 838 1.5× 463 0.8× 228 9.0k
Yoshitsugu Shiro Japan 51 4.6k 1.3× 253 0.3× 2.3k 3.0× 950 1.7× 1.2k 2.2× 232 8.4k
Gary Cecchini United States 41 3.9k 1.1× 181 0.2× 437 0.6× 284 0.5× 595 1.1× 112 5.6k
Leonid A. Sazanov United Kingdom 43 6.4k 1.8× 165 0.2× 303 0.4× 409 0.7× 467 0.8× 72 7.8k
Paolo Sarti Italy 40 3.0k 0.9× 157 0.2× 1.1k 1.4× 1.2k 2.1× 166 0.3× 158 5.1k

Countries citing papers authored by Thomas C. Squier

Since Specialization
Citations

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

Fields of papers citing papers by Thomas C. Squier

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Thomas C. Squier

This figure shows the co-authorship network connecting the top 25 collaborators of Thomas C. Squier. A scholar is included among the top collaborators of Thomas C. Squier 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 C. Squier. Thomas C. Squier 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.
Baird, Cheryl L., et al.. (2013). Identification of Noninterfacial Amino Acids Important for Molecular Recognition in Calmodulin. Biophysical Journal. 104(2). 18a–18a. 1 indexed citations
2.
Bigelow, Diana J. & Thomas C. Squier. (2011). Thioredoxin-dependent redox regulation of cellular signaling and stress response through reversible oxidation of methionines. Molecular BioSystems. 7(7). 2101–2109. 34 indexed citations
4.
Chen, Baowei, James E. Mahaney, M. Uljana Mayer, Diana J. Bigelow, & Thomas C. Squier. (2009). Concerted but Noncooperative Activation of Nucleotide and Actuator Domains of the Ca-ATPase Upon Calcium Binding. Biophysical Journal. 96(3). 143a–143a. 6 indexed citations
5.
Yan, Ping, Ting Wang, Tatyana V. Knyushko, et al.. (2009). A Targeted Releasable Affinity Probe (TRAP) for In Vivo Photocrosslinking. ChemBioChem. 10(9). 1507–1518. 17 indexed citations
6.
Shi, Liang, Thomas C. Squier, John M. Zachara, & James K. Fredrickson. (2007). Respiration of metal (hydr)oxides by Shewanella and Geobacter: a key role for multihaem c‐type cytochromes. Molecular Microbiology. 65(1). 12–20. 540 indexed citations breakdown →
7.
Shi, Liang, Joshua Adkins, James R. Coleman, et al.. (2006). Proteomic Analysis of Salmonella enterica Serovar Typhimurium Isolated from RAW 264.7 Macrophages. Journal of Biological Chemistry. 281(39). 29131–29140. 123 indexed citations
8.
Sacksteder, Colette A., Yijia Xiong, Jinhui Li, et al.. (2006). Tertiary Structural Rearrangements upon Oxidation of Methionine145 in Calmodulin Promotes Targeted Proteasomal Degradation. Biophysical Journal. 91(4). 1480–1493. 29 indexed citations
10.
Mayer, M. Uljana, Liang Shi, & Thomas C. Squier. (2005). One-step, non-denaturing isolation of an RNA polymerase enzyme complex using an improved multi-use affinity probe resin. Molecular BioSystems. 1(1). 53–56. 19 indexed citations
11.
Xiong, Yijia, et al.. (2004). Hsp90 Enhances Degradation of Oxidized Calmodulin by the 20 S Proteasome. Journal of Biological Chemistry. 279(44). 46135–46142. 83 indexed citations
12.
Negash, Sewite, Qing Yao, Hongye Sun, et al.. (2000). Phospholamban remains associated with the Ca2+- and Mg2+-dependent ATPase following phosphorylation by cAMP-dependent protein kinase. Biochemical Journal. 351(1). 195–195. 46 indexed citations
13.
Sharov, Victor S., Deborah A. Ferrington, Thomas C. Squier, & Christian Schöneich. (1999). Diastereoselective reduction of protein‐bound methionine sulfoxide by methionine sulfoxide reductase. FEBS Letters. 455(3). 247–250. 171 indexed citations
14.
Chen, Linda, et al.. (1998). Changes in Spatial Arrangement between Individual Ca‐ATPase Polypeptide Chains in Response to Phospholamban Phosphorylation. Annals of the New York Academy of Sciences. 853(1). 264–266. 3 indexed citations
15.
Ferrington, Deborah A., et al.. (1997). Decreased conformational stability of the sarcoplasmic reticulum Ca-ATPase in aged skeletal muscle. Biochimica et Biophysica Acta (BBA) - Biomembranes. 1330(2). 233–247. 22 indexed citations
16.
Michaelis, Mary L., Diana J. Bigelow, Christian Schöneich, et al.. (1996). Decreased plasma membrane calcium transport activity in aging brain. Life Sciences. 59(5-6). 405–412. 108 indexed citations
17.
Mills, Denise A., Steve Seibold, Thomas C. Squier, & Mark L. Richter. (1995). ADP binding induces long-distance structural changes in the .beta. polypeptide of the chloroplast ATP synthase. Biochemistry. 34(18). 6100–6108. 9 indexed citations
19.
Gryczyński, Ignacy, Wiesław Wiczk, Giuseppe Inesi, Thomas C. Squier, & Joseph R. Lakowicz. (1989). Characterization of the tryptophan fluorescence from sarcoplasmic reticulum adenosine triphosphatase by frequency-domain fluorescence spectroscopy. Biochemistry. 28(8). 3490–3498. 37 indexed citations
20.
Bishop, James E., Thomas C. Squier, Diana J. Bigelow, & Giuseppe Inesi. (1988). (Iodoacetamido)fluorescein labels a pair of proximal cysteines on the calcium ATPase of sarcoplasmic reticulum. Biochemistry. 27(14). 5233–5240. 49 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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