Douglas Tsao

787 total citations
8 papers, 615 citations indexed

About

Douglas Tsao is a scholar working on Molecular Biology, Materials Chemistry and Pharmacology. According to data from OpenAlex, Douglas Tsao has authored 8 papers receiving a total of 615 indexed citations (citations by other indexed papers that have themselves been cited), including 7 papers in Molecular Biology, 4 papers in Materials Chemistry and 1 paper in Pharmacology. Recurrent topics in Douglas Tsao's work include Protein Structure and Dynamics (5 papers), Enzyme Structure and Function (4 papers) and RNA and protein synthesis mechanisms (3 papers). Douglas Tsao is often cited by papers focused on Protein Structure and Dynamics (5 papers), Enzyme Structure and Function (4 papers) and RNA and protein synthesis mechanisms (3 papers). Douglas Tsao collaborates with scholars based in United States, India and Canada. Douglas Tsao's co-authors include Nikolay V. Dokholyan, Feng Ding, Huifen Nie, David Shirvanyants, Srinivas Ramachandran, Luda Diatchenko, Svetlana A. Shabalina, Josée Gauthier, Shubin Liu and Allen P. Minton and has published in prestigious journals such as Nucleic Acids Research, PLoS ONE and The Journal of Physical Chemistry B.

In The Last Decade

Douglas Tsao

8 papers receiving 613 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Douglas Tsao United States 8 434 136 131 61 55 8 615
Sangita Seshadri United States 8 496 1.1× 137 1.0× 144 1.1× 37 0.6× 73 1.3× 10 824
Giorgio Favrin United Kingdom 11 504 1.2× 309 2.3× 132 1.0× 77 1.3× 53 1.0× 15 683
Dirk Matthes Germany 10 324 0.7× 197 1.4× 79 0.6× 83 1.4× 26 0.5× 14 459
Pia D. Vogel United States 18 659 1.5× 102 0.8× 64 0.5× 31 0.5× 56 1.0× 55 1.1k
Olga Szczepankiewicz Sweden 8 277 0.6× 170 1.3× 99 0.8× 20 0.3× 32 0.6× 8 457
Zhenming Du United States 13 481 1.1× 266 2.0× 66 0.5× 30 0.5× 55 1.0× 20 765
Eric M. Jones United States 13 682 1.6× 223 1.6× 68 0.5× 26 0.4× 65 1.2× 24 823
Yanxian Lin United States 9 652 1.5× 219 1.6× 61 0.5× 40 0.7× 71 1.3× 12 873
Tomas Šneideris United Kingdom 17 451 1.0× 324 2.4× 58 0.4× 48 0.8× 37 0.7× 35 773
Mantas Mališauskas Sweden 13 392 0.9× 347 2.6× 64 0.5× 64 1.0× 32 0.6× 21 643

Countries citing papers authored by Douglas Tsao

Since Specialization
Citations

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

Fields of papers citing papers by Douglas Tsao

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Douglas Tsao

This figure shows the co-authorship network connecting the top 25 collaborators of Douglas Tsao. A scholar is included among the top collaborators of Douglas Tsao 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 Douglas Tsao. Douglas Tsao is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

8 of 8 papers shown
1.
Tsao, Douglas, Jeffrey S. Wieskopf, Naim U. Rashid, et al.. (2012). Serotonin-Induced Hypersensitivity via Inhibition of Catechol O-Methyltransferase Activity. Molecular Pain. 8. 25–25. 15 indexed citations
2.
Shirvanyants, David, Feng Ding, Douglas Tsao, Srinivas Ramachandran, & Nikolay V. Dokholyan. (2012). Discrete Molecular Dynamics: An Efficient And Versatile Simulation Method For Fine Protein Characterization. The Journal of Physical Chemistry B. 116(29). 8375–8382. 180 indexed citations
3.
Tsao, Douglas, Svetlana A. Shabalina, Josée Gauthier, Nikolay V. Dokholyan, & Luda Diatchenko. (2011). Disruptive mRNA folding increases translational efficiency of catechol-O-methyltransferase variant. Nucleic Acids Research. 39(14). 6201–6212. 41 indexed citations
4.
Tsao, Douglas, Shubin Liu, & Nikolay V. Dokholyan. (2011). Regioselectivity of catechol O-methyltransferase confers enhancement of catalytic activity. Chemical Physics Letters. 506(4-6). 135–138. 18 indexed citations
5.
Tsao, Douglas, Luda Diatchenko, & Nikolay V. Dokholyan. (2011). Structural Mechanism of S-Adenosyl Methionine Binding to Catechol O-Methyltransferase. PLoS ONE. 6(8). e24287–e24287. 30 indexed citations
6.
Tsao, Douglas & Nikolay V. Dokholyan. (2010). Macromolecular crowding induces polypeptide compaction and decreases folding cooperativity. Physical Chemistry Chemical Physics. 12(14). 3491–3491. 35 indexed citations
7.
Tsao, Douglas, Allen P. Minton, & Nikolay V. Dokholyan. (2010). A Didactic Model of Macromolecular Crowding Effects on Protein Folding. PLoS ONE. 5(8). e11936–e11936. 18 indexed citations
8.
Ding, Feng, Douglas Tsao, Huifen Nie, & Nikolay V. Dokholyan. (2008). Ab Initio Folding of Proteins with All-Atom Discrete Molecular Dynamics. Structure. 16(7). 1010–1018. 278 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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