Douglas D. Root

940 total citations
37 papers, 746 citations indexed

About

Douglas D. Root is a scholar working on Molecular Biology, Cardiology and Cardiovascular Medicine and Atomic and Molecular Physics, and Optics. According to data from OpenAlex, Douglas D. Root has authored 37 papers receiving a total of 746 indexed citations (citations by other indexed papers that have themselves been cited), including 25 papers in Molecular Biology, 22 papers in Cardiology and Cardiovascular Medicine and 7 papers in Atomic and Molecular Physics, and Optics. Recurrent topics in Douglas D. Root's work include Cardiomyopathy and Myosin Studies (22 papers), Muscle Physiology and Disorders (12 papers) and Cardiovascular Effects of Exercise (11 papers). Douglas D. Root is often cited by papers focused on Cardiomyopathy and Myosin Studies (22 papers), Muscle Physiology and Disorders (12 papers) and Cardiovascular Effects of Exercise (11 papers). Douglas D. Root collaborates with scholars based in United States, Russia and Switzerland. Douglas D. Root's co-authors include Emil Reisler, Kuan Wang, Jin Xu, Kuan Wang, Jian‐Ping Jin, R.K. Cook, Peter A. Rubenstein, Vamsi K. Yadavalli, P. Apel and V. Vutsadakis and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Biochemistry.

In The Last Decade

Douglas D. Root

36 papers receiving 736 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 D. Root United States 16 394 370 175 108 107 37 746
Arthur Elliott United Kingdom 10 393 1.0× 389 1.1× 121 0.7× 71 0.7× 140 1.3× 13 717
Reiji Takashi United States 15 464 1.2× 519 1.4× 232 1.3× 41 0.4× 105 1.0× 17 751
Volker Walhorn Germany 15 221 0.6× 238 0.6× 136 0.8× 73 0.7× 99 0.9× 39 608
Andrew Quigley United Kingdom 14 495 1.3× 76 0.2× 81 0.5× 94 0.9× 182 1.7× 24 912
Kathleen Ue United States 12 455 1.2× 439 1.2× 335 1.9× 25 0.2× 102 1.0× 17 769
Jaime Andrés Rivas‐Pardo United States 16 561 1.4× 249 0.7× 274 1.6× 126 1.2× 465 4.3× 33 1.0k
Kien Xuan Ngo Japan 11 290 0.7× 74 0.2× 204 1.2× 52 0.5× 116 1.1× 27 552
Vladimir A. Lizunov United States 14 664 1.7× 42 0.1× 256 1.5× 76 0.7× 61 0.6× 19 910
Fumimasa Nomura Japan 15 551 1.4× 131 0.4× 75 0.4× 248 2.3× 104 1.0× 42 812
Phedra Marius United Kingdom 13 589 1.5× 48 0.1× 75 0.4× 114 1.1× 41 0.4× 18 689

Countries citing papers authored by Douglas D. Root

Since Specialization
Citations

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

Fields of papers citing papers by Douglas D. Root

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Douglas D. Root

This figure shows the co-authorship network connecting the top 25 collaborators of Douglas D. Root. A scholar is included among the top collaborators of Douglas D. Root 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 D. Root. Douglas D. Root 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.
Tanner, Bertrand C.W., et al.. (2023). Cooperative & competitive binding of anti-myosin tail antibodies revealed by super-resolution microscopy. Archives of Biochemistry and Biophysics. 747. 109753–109753.
2.
Mondal, Hossain Ali, Joe Louis, Vamsi J. Nalam, et al.. (2018). Arabidopsis Actin-depolymerizing Factor3 Is Required for Controlling Aphid Feeding from the Phloem. PMC. 5 indexed citations
3.
Root, Douglas D., et al.. (2018). Cooperative Activation of Striated Muscle Thick Filaments by S2 Binding. Biophysical Journal. 114(3). 646a–646a. 1 indexed citations
4.
Root, Douglas D., et al.. (2018). Data on whole length myosin binding protein C stabilizes myosin S2 as measured by gravitational force spectroscopy. Data in Brief. 18. 1099–1106. 2 indexed citations
5.
Root, Douglas D., et al.. (2013). Asymmetric myosin binding to the thin filament as revealed by a fluorescent nanocircuit. Archives of Biochemistry and Biophysics. 535(1). 14–21. 4 indexed citations
6.
Root, Douglas D., et al.. (2011). Demonstrating the Uses of the Novel Gravitational Force Spectrometer to Stretch and Measure Fibrous Proteins. Journal of Visualized Experiments. 1 indexed citations
7.
Hong, Feng & Douglas D. Root. (2006). Downscaling functional bioassays by single-molecule techniques. Drug Discovery Today. 11(13-14). 640–645. 8 indexed citations
8.
Root, Douglas D., Vamsi K. Yadavalli, Jeffrey G. Forbes, & Kuan Wang. (2006). Coiled-Coil Nanomechanics and Uncoiling and Unfolding of the Superhelix and α-Helices of Myosin. Biophysical Journal. 90(8). 2852–2866. 61 indexed citations
9.
Xu, Jin, et al.. (2004). High flexibility of the actomyosin crossbridge resides in skeletal muscle myosin subfragment-2 as demonstrated by a new single molecule assay. Journal of Structural Biology. 149(2). 117–126. 18 indexed citations
10.
Apel, P., I.V. Blonskaya, O. L. Orelovitch, et al.. (2003). Effect of nanosized surfactant molecules on the etching of ion tracks: New degrees of freedom in design of pore shape. Nuclear Instruments and Methods in Physics Research Section B Beam Interactions with Materials and Atoms. 209. 329–334. 40 indexed citations
11.
Root, Douglas D.. (2002). A Computational Comparison of the Atomic Models of the Actomyosin Interface. Cell Biochemistry and Biophysics. 37(2). 97–110. 8 indexed citations
12.
Hu, Zhibing, et al.. (2000). Native Purification of Biomolecules with Temperature-Mediated Hydrophobic Modulation Liquid Chromatography. Analytical Biochemistry. 283(2). 159–165. 15 indexed citations
13.
Xu, Jin & Douglas D. Root. (2000). Conformational Selection During Weak Binding at the Actin and Myosin Interface. Biophysical Journal. 79(3). 1498–1510. 23 indexed citations
14.
Root, Douglas D., et al.. (1999). Determination of Fluorescent Probe Orientations on Biomolecules by Conformational Searching: Algorithm Testing and Applications to the Atomic Model of Myosin. Journal of Structural Biology. 127(1). 22–34. 16 indexed citations
15.
Xu, Jin & Douglas D. Root. (1998). Domain Motion between the Regulatory Light Chain and the Nucleotide Site in Skeletal Myosin. Journal of Structural Biology. 123(2). 150–161. 11 indexed citations
16.
Root, Douglas D. & Kuan Wang. (1994). Calmodulin-Sensitive Interaction of Human Nebulin Fragments with Actin and Myosin. Biochemistry. 33(42). 12581–12591. 71 indexed citations
17.
Root, Douglas D. & Ke Wang. (1993). Kinetic Silver Staining and Quantification of Proteins Adsorbed to Microtiter Plates. Analytical Biochemistry. 209(2). 354–359. 6 indexed citations
18.
Root, Douglas D. & Emil Reisler. (1992). Cooperativity of thiol-modified myosin filaments. ATPase and motility assays of myosin function. Biophysical Journal. 63(3). 730–740. 30 indexed citations
19.
Root, Douglas D., Pearl Cheung, & Emil Reisler. (1991). Catalytic cooperativity induced by sulfhydryl1-labeling of myosin filaments. Biochemistry. 30(1). 286–294. 17 indexed citations
20.
Root, Douglas D., et al.. (1989). Copper iodide staining of protein blots on nitrocellulose membranes. Analytical Biochemistry. 181(2). 250–253. 14 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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