Yi Dou

1.3k total citations
21 papers, 1.1k citations indexed

About

Yi Dou is a scholar working on Cell Biology, Molecular Biology and Physiology. According to data from OpenAlex, Yi Dou has authored 21 papers receiving a total of 1.1k indexed citations (citations by other indexed papers that have themselves been cited), including 20 papers in Cell Biology, 16 papers in Molecular Biology and 9 papers in Physiology. Recurrent topics in Yi Dou's work include Hemoglobin structure and function (20 papers), Heme Oxygenase-1 and Carbon Monoxide (8 papers) and Erythrocyte Function and Pathophysiology (6 papers). Yi Dou is often cited by papers focused on Hemoglobin structure and function (20 papers), Heme Oxygenase-1 and Carbon Monoxide (8 papers) and Erythrocyte Function and Pathophysiology (6 papers). Yi Dou collaborates with scholars based in United States, Japan and United Kingdom. Yi Dou's co-authors include John S. Olson, Masao Ikeda‐Saito, Anthony J. Wilkinson, Raymund F. Eich, G.N. Phillips, Mark S. Hargrove, Szymon Krzywda, Tiansheng Li, E.C. Liong and Emily E. Scott and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and Biochemistry.

In The Last Decade

Yi Dou

21 papers receiving 1.0k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Yi Dou United States 18 810 710 282 195 96 21 1.1k
Yannick Ouellet Canada 16 1.0k 1.3× 895 1.3× 318 1.1× 321 1.6× 70 0.7× 16 1.3k
Antonio Tsuneshige United States 16 564 0.7× 411 0.6× 332 1.2× 129 0.7× 52 0.5× 35 799
Hiroshi Mizukami United States 17 534 0.7× 384 0.5× 367 1.3× 126 0.6× 69 0.7× 46 922
Eileen W. Singleton United States 10 842 1.0× 696 1.0× 303 1.1× 269 1.4× 32 0.3× 14 1.1k
Ariki Matsuoka Japan 20 642 0.8× 526 0.7× 255 0.9× 172 0.9× 33 0.3× 34 870
Gary Silkstone United Kingdom 19 431 0.5× 667 0.9× 170 0.6× 115 0.6× 58 0.6× 29 958
Marc V. Thorsteinsson United States 18 558 0.7× 691 1.0× 82 0.3× 97 0.5× 70 0.7× 22 932
Masako Nagai Japan 17 477 0.6× 449 0.6× 180 0.6× 147 0.8× 70 0.7× 45 794
Yoshimasa Yoneyama Japan 22 598 0.7× 631 0.9× 261 0.9× 400 2.1× 92 1.0× 66 1.2k
David L. Budd United States 12 628 0.8× 506 0.7× 166 0.6× 191 1.0× 166 1.7× 16 864

Countries citing papers authored by Yi Dou

Since Specialization
Citations

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

Fields of papers citing papers by Yi Dou

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Yi Dou

This figure shows the co-authorship network connecting the top 25 collaborators of Yi Dou. A scholar is included among the top collaborators of Yi Dou 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 Yi Dou. Yi Dou 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.
Vogel, Kathleen M., Thomas S. Rush, Pawel M. Kozlowski, et al.. (2003). FeNO Structure in Distal Pocket Mutants of Myoglobin Based on Resonance Raman Spectroscopy. Biochemistry. 42(17). 4896–4903. 60 indexed citations
2.
Dou, Yi, et al.. (2002). Myoglobin as a model system for designing heme protein based blood substitutes. Biophysical Chemistry. 98(1-2). 127–148. 90 indexed citations
3.
Liong, E.C., Yi Dou, Emily E. Scott, John S. Olson, & G.N. Phillips. (2001). Waterproofing the Heme Pocket. Journal of Biological Chemistry. 276(12). 9093–9100. 83 indexed citations
4.
Gardner, Paul R., Anne M. Gardner, Lori A. Martin, et al.. (2000). Nitric-oxide Dioxygenase Activity and Function of Flavohemoglobins. Journal of Biological Chemistry. 275(41). 31581–31587. 130 indexed citations
5.
Hori, Hiroshi, et al.. (2000). EPR studies on the photoinduced intermediates of NO complexes in recombinant ferric-Mb trapped at low temperatures. Journal of Inorganic Biochemistry. 82(1-4). 181–187. 6 indexed citations
6.
Thorsteinsson, Marc V., David R. Bevan, Malcolm Potts, et al.. (1999). A Cyanobacterial Hemoglobin with Unusual Ligand Binding Kinetics and Stability Properties. Biochemistry. 38(7). 2117–2126. 49 indexed citations
7.
Roach, Mark P., Masanori Sono, Ann H. Rux, et al.. (1999). Assignment of the Heme Axial Ligand(s) for the Ferric Myoglobin (H93G) and Heme Oxygenase (H25A) Cavity Mutants as Oxygen Donors Using Magnetic Circular Dichroism. Biochemistry. 38(23). 7601–7608. 44 indexed citations
8.
Gooding, Edward A., et al.. (1999). Heme Protein Dynamics Revealed by Geminate Nitric Oxide Recombination in Mutants of Iron and Cobalt Myoglobin. Biochemistry. 38(18). 5918–5924. 49 indexed citations
9.
Unno, Masashi, et al.. (1998). Myoglobin Mutants Giving the Largest Geminate Yield in CO Rebinding in the Nanosecond Time Domain. Biophysical Journal. 75(5). 2188–2194. 22 indexed citations
10.
Bougault, Catherine, Yi Dou, Masao Ikeda‐Saito, et al.. (1998). Solution 1H NMR Study of the Electronic Structure and Magnetic Properties of High-Spin Ferrous or Deoxy Myoglobins. Journal of the American Chemical Society. 120(9). 2113–2123. 25 indexed citations
11.
Brucker, E.A., John S. Olson, G.N. Phillips, Yi Dou, & Masao Ikeda‐Saito. (1996). High Resolution Crystal Structures of the Deoxy, Oxy, and Aquomet Forms of Cobalt Myoglobin. Journal of Biological Chemistry. 271(41). 25419–25422. 55 indexed citations
12.
Dou, Yi, et al.. (1996). Mechanism of Hydrogen Cyanide Binding to Myoglobin. Biochemistry. 35(22). 7107–7113. 54 indexed citations
13.
Dou, Yi, Suzanne J. Admiraal, Masao Ikeda‐Saito, et al.. (1995). Alteration of Axial Coordination by Protein Engineering in Myoglobin. Journal of Biological Chemistry. 270(27). 15993–16001. 57 indexed citations
14.
Hargrove, Mark S., Szymon Krzywda, Anthony J. Wilkinson, et al.. (1994). Stability of Myoglobin: A Model for the Folding of Heme Proteins. Biochemistry. 33(39). 11767–11775. 115 indexed citations
15.
Peisach, J., et al.. (1994). Electron-Nuclear Coupling to the Proximal Histidine in Oxycobalt-Substituted Distal Histidine Mutants of Human Myoglobin. Biochemistry. 33(24). 7609–7618. 11 indexed citations
16.
Qin, Jun, G. N. LA MAR, Yi Dou, Suzanne J. Admiraal, & Masao Ikeda‐Saito. (1994). 1H NMR study of the solution molecular and electronic structure of engineered distal myoglobin His64(E7) Val/Val68(E11) His double mutant. Coordination of His64(E11) at the sixth position in both low-spin and high-spin states.. Journal of Biological Chemistry. 269(2). 1083–1090. 20 indexed citations
17.
Brancaccio, Andrea, Francesca Cutruzzolà, Maurizio Brunori, et al.. (1994). Structural factors governing azide and cyanide binding to mammalian metmyoglobins.. Journal of Biological Chemistry. 269(19). 13843–13853. 104 indexed citations
18.
MAR, G. N. LA, Xuefeng Zhao, Yi Dou, et al.. (1994). 1H NMR investigation of distal mutant deoxy myoglobins. Interpretation of proximal His contact shifts in terms of a localized distal water molecule.. Journal of Biological Chemistry. 269(47). 29629–29635. 20 indexed citations
19.
Ikeda‐Saito, Masao, et al.. (1993). Ligand diffusion in the distal heme pocket of myoglobin. A primary determinant of geminate rebinding.. Journal of Biological Chemistry. 268(10). 6855–6857. 49 indexed citations
20.

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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