F.J. Stevens

621 total citations
9 papers, 517 citations indexed

About

F.J. Stevens is a scholar working on Molecular Biology, Radiology, Nuclear Medicine and Imaging and Materials Chemistry. According to data from OpenAlex, F.J. Stevens has authored 9 papers receiving a total of 517 indexed citations (citations by other indexed papers that have themselves been cited), including 8 papers in Molecular Biology, 3 papers in Radiology, Nuclear Medicine and Imaging and 3 papers in Materials Chemistry. Recurrent topics in F.J. Stevens's work include Glycosylation and Glycoproteins Research (5 papers), Protein Structure and Dynamics (4 papers) and Monoclonal and Polyclonal Antibodies Research (3 papers). F.J. Stevens is often cited by papers focused on Glycosylation and Glycoproteins Research (5 papers), Protein Structure and Dynamics (4 papers) and Monoclonal and Polyclonal Antibodies Research (3 papers). F.J. Stevens collaborates with scholars based in United States and France. F.J. Stevens's co-authors include M. Schiffer, Rosemarie Raffen, Pièrre Aucouturier, J L Preud'homme, Jacques Chomilier, Sophie Déret, Priscilla Wilkins Stevens, Xiaoyin Cai, P. Raj Pokkuluri and GJ Johnson and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Protein Science and Structure.

In The Last Decade

F.J. Stevens

9 papers receiving 512 citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
F.J. Stevens United States	7	448	80	52	48	47	9	517
E. Minasian Australia	12	330 0.7×	29 0.4×	43 0.8×	69 1.4×	39 0.8×	19	470
Jonas Hanske Germany	15	538 1.2×	38 0.5×	56 1.1×	46 1.0×	19 0.4×	17	692
Jean‐René Alattia Canada	13	504 1.1×	59 0.7×	37 0.7×	25 0.5×	142 3.0×	18	694
Emma E. Watson Australia	12	538 1.2×	43 0.5×	48 0.9×	53 1.1×	29 0.6×	27	682
F.G. Prendergast United States	10	388 0.9×	33 0.4×	65 1.3×	9 0.2×	54 1.1×	12	566
Marco Ceruso United States	7	575 1.3×	16 0.2×	86 1.7×	43 0.9×	30 0.6×	7	697
Chi‐Deu Chang United States	11	796 1.8×	53 0.7×	31 0.6×	121 2.5×	24 0.5×	15	1.0k
OO Blumenfeld United States	12	382 0.9×	33 0.4×	44 0.8×	51 1.1×	225 4.8×	22	671
Matthew D. Sekedat United States	13	660 1.5×	26 0.3×	39 0.8×	27 0.6×	19 0.4×	15	773
Vishnu Priyanka Reddy Chichili Singapore	8	384 0.9×	20 0.3×	46 0.9×	48 1.0×	20 0.4×	10	475

Countries citing papers authored by F.J. Stevens

Since Specialization

Citations

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

Fields of papers citing papers by F.J. Stevens

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by F.J. Stevens. 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 F.J. Stevens. The network helps show where F.J. Stevens may publish in the future.

Co-authorship network of co-authors of F.J. Stevens

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

All Works

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9 of 9 papers shown

1.

Yu, Chunmei, et al.. (2005). Classifying noisy protein sequence data: a case study of immunoglobulin light chains. Computer applications in the biosciences. 21(Suppl 1). i495–i501. 3 indexed citations

2.

Pokkuluri, P. Raj, et al.. (2002). Factors contributing to decreased protein stability when aspartic acid residues are in β‐sheet regions. Protein Science. 11(7). 1687–1694. 18 indexed citations

3.

Stevens, F.J.. (2000). Four structural risk factors identify most fibril-forming kappa light chains. Amyloid. 7(3). 200–211. 76 indexed citations

4.

Raffen, Rosemarie, et al.. (1998). Reengineering immunoglobulin domain interactions by introduction of charged residues. Protein Engineering Design and Selection. 11(4). 303–309. 18 indexed citations

5.

Raffen, Rosemarie, Xiaoyin Cai, GJ Johnson, et al.. (1998). A domain flip as a result of a single amino-acid substitution. Structure. 6(8). 1067–1073. 16 indexed citations

6.

Déret, Sophie, et al.. (1997). Molecular modeling of immunoglobulin light chains implicates hydrophobic residues in non-amyloid light chain deposition disease. Protein Engineering Design and Selection. 10(10). 1191–1197. 40 indexed citations

7.

Stevens, F.J., et al.. (1996). Three quaternary structures for a single protein.. Proceedings of the National Academy of Sciences. 93(14). 7017–7021. 34 indexed citations

8.

Schiffer, M., et al.. (1992). The function of tryptophan residues in membrane proteins. Protein Engineering Design and Selection. 5(3). 213–214. 311 indexed citations

9.

Ferguson, W. G., et al.. (1990). The Effects of an Anaerobic Environment on Corrosion Fatigue. 286. 1 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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