S. Daopin

727 total citations
8 papers, 634 citations indexed

About

S. Daopin is a scholar working on Molecular Biology, Materials Chemistry and Ecology. According to data from OpenAlex, S. Daopin has authored 8 papers receiving a total of 634 indexed citations (citations by other indexed papers that have themselves been cited), including 8 papers in Molecular Biology, 6 papers in Materials Chemistry and 3 papers in Ecology. Recurrent topics in S. Daopin's work include Protein Structure and Dynamics (7 papers), Enzyme Structure and Function (6 papers) and Bacteriophages and microbial interactions (3 papers). S. Daopin is often cited by papers focused on Protein Structure and Dynamics (7 papers), Enzyme Structure and Function (6 papers) and Bacteriophages and microbial interactions (3 papers). S. Daopin collaborates with scholars based in United States. S. Daopin's co-authors include Brian W. Matthews, W.A. Baase, David E. Anderson, Frederick W. Dahlquist, H. Nicholson, Joan A. Wozniak, Tom Alber, Masaru Matsumura, Michael P. Schlunegger and D. R. Davies and has published in prestigious journals such as Journal of Biological Chemistry, Journal of Molecular Biology and Biochemistry.

In The Last Decade

S. Daopin

8 papers receiving 621 citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
S. Daopin United States	7	556	331	72	65	54	8	634
Y. Mauguen France	10	489 0.9×	295 0.9×	74 1.0×	115 1.8×	79 1.5×	17	652
Elke Duchardt Germany	12	762 1.4×	323 1.0×	142 2.0×	82 1.3×	38 0.7×	14	886
Kerstin Nyberg United Kingdom	7	711 1.3×	394 1.2×	80 1.1×	87 1.3×	90 1.7×	10	847
Hilde Damaschun Germany	17	688 1.2×	315 1.0×	79 1.1×	127 2.0×	28 0.5×	31	848
Marc A. Ceruso Italy	12	590 1.1×	190 0.6×	56 0.8×	75 1.2×	57 1.1×	13	706
Annett Bachmann Switzerland	12	661 1.2×	378 1.1×	99 1.4×	76 1.2×	32 0.6×	12	763
Tzvia Selzer Israel	11	733 1.3×	244 0.7×	46 0.6×	117 1.8×	75 1.4×	15	948
Michael S. Ackerman United States	8	594 1.1×	319 1.0×	137 1.9×	61 0.9×	36 0.7×	9	738
Yvonne Guillou France	12	477 0.9×	233 0.7×	44 0.6×	67 1.0×	77 1.4×	24	585
Bryan E. Finn Sweden	13	631 1.1×	290 0.9×	98 1.4×	67 1.0×	48 0.9×	14	720

Countries citing papers authored by S. Daopin

Since Specialization

Citations

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

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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-authorship network of co-authors of S. Daopin

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

All Works

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8 of 8 papers shown

1.

Daopin, S., et al.. (2007). Structural and Genetic Analysis of Electrostatic and Other Interactions in Bacteriophage T4 Lysozyme. Novartis Foundation symposium. 161. 52–62. 1 indexed citations

2.

Daopin, S., D. R. Davies, Michael P. Schlunegger, & Markus G. Grütter. (1994). Comparison of two crystal structures of TGF-β2: the accuracy of refined protein structures. Acta Crystallographica Section D Biological Crystallography. 50(1). 85–92. 25 indexed citations

3.

Daopin, S., Tom Alber, W.A. Baase, Joan A. Wozniak, & Brian W. Matthews. (1991). Structural and thermodynamic analysis of the packing of two α-helices in bacteriophage T4 lysozyme. Journal of Molecular Biology. 221(2). 647–667. 72 indexed citations

4.

Daopin, S., David E. Anderson, W.A. Baase, Frederick W. Dahlquist, & Brian W. Matthews. (1991). Structural and thermodynamic consequences of burying a charged residue within the hydrophobic core of T4 lysozyme. Biochemistry. 30(49). 11521–11529. 243 indexed citations

5.

Nicholson, H., David E. Anderson, S. Daopin, & Brian W. Matthews. (1991). Analysis of the interaction between charged side chains and the .alpha.-helix dipole using designed thermostable mutants of phage T4 lysozyme. Biochemistry. 30(41). 9816–9828. 145 indexed citations

6.

Daopin, S., W.A. Baase, & Brian W. Matthews. (1990). A mutant T4 lysozyme (Val 131 → Ala) designed to increase thermostability by the reduction of strain within an α‐helix. Proteins Structure Function and Bioinformatics. 7(2). 198–204. 81 indexed citations

7.

Wozniak, Joan A., H.R. Faber, S. Daopin, Xingju Zhang, & Brian W. Matthews. (1990). Crystallization of designed protein variants. Methods. 1(1). 100–104. 11 indexed citations

8.

Matsumura, Masaru, Joan A. Wozniak, S. Daopin, & Brian W. Matthews. (1989). Structural Studies of Mutants of T4 Lysozyme That Alter Hydrophobic Stabilization. Journal of Biological Chemistry. 264(27). 16059–16066. 56 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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