S. Daopin
Impact in
-
- Protein Structure and Dynamics
- RNA and protein synthesis mechanisms
- Glycosylation and Glycoproteins Research
-
- Enzyme Structure and Function
Papers in
-
- Protein Structure and Dynamics 7
- Glycosylation and Glycoproteins Research 2
- TGF-β signaling in diseases 1
- RNA and protein synthesis mechanisms 1
- S100 Proteins and Annexins 1
-
- Enzyme Structure and Function 6
- Co-authors
- Brian W. Matthews (7 shared papers)W.A. Baase (4 shared papers)David E. Anderson (2 shared papers)Frederick W. Dahlquist (1 shared paper)H. Nicholson (2 shared papers)Joan A. Wozniak (4 shared papers)Tom Alber (1 shared paper)Masaru Matsumura (1 shared paper)
- Journals
- Biochemistry (2 papers)Novartis Foundation symposium (1 paper)Methods (1 paper)Journal of Biological Chemistry (1 paper)Proteins Structure Function and Bioinformatics (1 paper)
- Partner nations
- United States
In The Last Decade
S. Daopin
8 papers receiving 621 citations
Peers
Comparison fields: 5 of 65
- Molecular Biology 556
- Materials Chemistry 331
- Spectroscopy 72
- Cell Biology 65
- Biophysics 22
Countries citing papers authored by S. Daopin
This map shows the geographic impact of S. Daopin'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 S. Daopin with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites S. Daopin more than expected).
Fields of papers citing papers by S. Daopin
This network shows the impact of papers produced by S. Daopin. 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 S. Daopin. The network helps show where S. Daopin may publish in the future.
Co-authors
The 13 scholars most cited alongside S. Daopin, linked wherever they have co-authored with each other. Click a name or a connecting line to browse the papers they share.
All Works
| # | Work | ||
|---|---|---|---|
| 1 | 1991 | 243 | |
| 2 | 1991 | 145 | |
| 3 | 1990 | 81 | |
| 4 | 1991 | 72 | |
| 5 | 1989 | 56 | |
| 6 | 1994 | 25 | |
| 7 | 1990 | 11 | |
| 8 | 2007 | 1 |
About S. Daopin
S. Daopin is a scholar working on Molecular Biology, Materials Chemistry, Ecology, Cell Biology and Infectious Diseases, having authored 8 papers that have together received 634 indexed citations. Recurring topics across this work include Protein Structure and Dynamics (7 papers), Enzyme Structure and Function (6 papers), Bacteriophages and microbial interactions (3 papers), Hemoglobin structure and function (2 papers), Glycosylation and Glycoproteins Research (2 papers), TGF-β signaling in diseases (1 paper), RNA and protein synthesis mechanisms (1 paper) and S100 Proteins and Annexins (1 paper). The work is most often cited by research in Molecular Biology (556 citations), Materials Chemistry (331 citations), Spectroscopy (72 citations), Cell Biology (65 citations) and Biophysics (22 citations). S. Daopin has collaborated with scholars based in United States. Frequent co-authors include Brian W. Matthews, W.A. Baase, David E. Anderson, Frederick W. Dahlquist, H. Nicholson, Joan A. Wozniak, Tom Alber, Masaru Matsumura, D. R. Davies and Markus G. Grütter. Their work appears in journals such as Biochemistry, Novartis Foundation symposium, Methods, Journal of Biological Chemistry and Proteins Structure Function and Bioinformatics.
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.