Steven Rosenberg

4.9k total citations · 2 hit papers
49 papers, 4.1k citations indexed

About

Steven Rosenberg is a scholar working on Molecular Biology, Cancer Research and Organic Chemistry. According to data from OpenAlex, Steven Rosenberg has authored 49 papers receiving a total of 4.1k indexed citations (citations by other indexed papers that have themselves been cited), including 17 papers in Molecular Biology, 16 papers in Cancer Research and 9 papers in Organic Chemistry. Recurrent topics in Steven Rosenberg's work include Protease and Inhibitor Mechanisms (16 papers), Cell Adhesion Molecules Research (9 papers) and Peptidase Inhibition and Analysis (7 papers). Steven Rosenberg is often cited by papers focused on Protease and Inhibitor Mechanisms (16 papers), Cell Adhesion Molecules Research (9 papers) and Peptidase Inhibition and Analysis (7 papers). Steven Rosenberg collaborates with scholars based in United States, Russia and United Kingdom. Steven Rosenberg's co-authors include Harold A. Chapman, Ying Wei, Michael Doyle, Daniel I. Simon, David Waltz, Matvey Lukashev, Sarah Bodary, Robert J. Drummond, Navin Rao and Jack F. Kirsch and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

Steven Rosenberg

49 papers receiving 3.9k citations

Hit Papers

Regulation of Integrin Fu... 1994 2026 2004 2015 1996 1994 200 400 600

Author Peers

Peers are selected by citation overlap in the author's most active subfields. citations · hero ref

Author Last Decade Papers Cites
Steven Rosenberg 1.9k 1.8k 1.0k 1.0k 636 49 4.1k
Jack Henkin 2.1k 1.1× 2.5k 1.4× 881 0.8× 485 0.5× 1.3k 2.0× 111 4.8k
Joseph G. Bieth 1.9k 1.0× 2.2k 1.2× 781 0.8× 444 0.4× 947 1.5× 148 5.2k
Maria Vittoria Cubellis 1.6k 0.9× 2.1k 1.2× 932 0.9× 465 0.5× 643 1.0× 91 4.0k
Brunhilde Felding‐Habermann 1.1k 0.6× 2.4k 1.3× 787 0.8× 1.0k 1.0× 2.0k 3.1× 43 5.4k
Staffan Magnusson 640 0.3× 1.7k 0.9× 816 0.8× 482 0.5× 378 0.6× 62 3.8k
Gabor Markus 1.7k 0.9× 1.3k 0.7× 709 0.7× 320 0.3× 751 1.2× 74 3.2k
Gunilla Høyer‐Hansen 3.5k 1.9× 2.2k 1.2× 1.6k 1.6× 1.2k 1.1× 2.1k 3.4× 149 6.3k
Achim Krüger 2.2k 1.2× 2.6k 1.4× 486 0.5× 631 0.6× 2.1k 3.4× 111 5.8k
Peter A. Andreasen 4.5k 2.4× 2.9k 1.6× 2.4k 2.3× 1.5k 1.4× 1.5k 2.4× 158 7.2k
Henrik Gårdsvoll 1.2k 0.7× 891 0.5× 431 0.4× 471 0.5× 631 1.0× 53 2.4k

Countries citing papers authored by Steven Rosenberg

Since Specialization
Citations

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

Fields of papers citing papers by Steven Rosenberg

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Steven Rosenberg

This figure shows the co-authorship network connecting the top 25 collaborators of Steven Rosenberg. A scholar is included among the top collaborators of Steven Rosenberg 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 Steven Rosenberg. Steven Rosenberg 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.
Bu, Xingyao, Vazgen Khankaldyyan, Ignacio Gonzales-Gomez, et al.. (2004). Species-specific urokinase receptor ligands reduce glioma growth and increase survival primarily by an antiangiogenesis mechanism. Laboratory Investigation. 84(6). 667–678. 26 indexed citations
3.
Fong, Susan, Michael Doyle, Robert J. Goodson, et al.. (2002). Random Peptide Bacteriophage Display as a Probe for Urokinase Receptor Ligands. Biological Chemistry. 383(1). 149–58. 6 indexed citations
4.
Rosenberg, Steven. (2001). Recent advances in the molecular biology of hepatitis C virus. Journal of Molecular Biology. 313(3). 451–464. 153 indexed citations
5.
Rosenberg, Steven. (2001). New developments in the urokinase-type plasminogen activator system. Expert Opinion on Therapeutic Targets. 5(6). 711–722. 14 indexed citations
6.
Simon, Daniel I., Ying Wei, Li Zhang, et al.. (2000). Identification of a Urokinase Receptor-Integrin Interaction Site. Journal of Biological Chemistry. 275(14). 10228–10234. 175 indexed citations
7.
Waltz, David, Lisa Natkin, Shaoqiu Zhuo, et al.. (2000). Nonproteolytic Role for the Urokinase Receptor in Cellular Migration In Vivo. American Journal of Respiratory Cell and Molecular Biology. 22(3). 316–322. 75 indexed citations
8.
Ballinger, Marcus, Venkatakrishna Shyamala, Laura V. Doyle, et al.. (1999). Semirational design of a potent, artificial agonist of fibroblast growth factor receptors. Nature Biotechnology. 17(12). 1199–1204. 56 indexed citations
9.
Yebra, Mayra, Graham C. Parry, Staffan Strömblad, et al.. (1996). Requirement of Receptor-bound Urokinase-type Plasminogen Activator for Integrin αvβ5-directed Cell Migration. Journal of Biological Chemistry. 271(46). 29393–29399. 217 indexed citations
10.
Curriden, Scott A., et al.. (1996). Is plasminogen activator inhibitor-1 the molecular switch that governs urokinase receptor-mediated cell adhesion and release?. The Journal of Cell Biology. 134(6). 1563–1571. 404 indexed citations
11.
Stratton-Thomas, Jennifer R., et al.. (1995). Yeast expression and phagemid display of the human urokinase plasminogen activator epidermal growth factor-like domain. Protein Engineering Design and Selection. 8(5). 463–470. 19 indexed citations
12.
Malcolm, Bruce A., Sherman M. Chin, David A. Jewell, et al.. (1992). Expression and characterization of recombinant hepatitis A virus 3C proteinase. Biochemistry. 31(13). 3358–3363. 50 indexed citations
13.
Rosenberg, Steven, et al.. (1992). Application of tritium high resolution NMR spectroscopy to analysis of tritium-labelled amino acids and peptides. Amino Acids. 3(1). 95–104. 11 indexed citations
14.
Clerck, Laura De, et al.. (1991). Fermentation of a Yeast Producing A. Niger Glucose Oxidase: Scale-Up, Purification and Characterization of the Recombinant Enzyme. Nature Biotechnology. 9(6). 559–561. 33 indexed citations
15.
Rosenberg, Steven, Doris Coit, & Patricia Tekamp-Olson. (1990). [28] Glyceraldehyde-3-phosphate dehydrogenase-derived expression cassettes for constitutive synthesis of heterologous proteins. Methods in enzymology on CD-ROM/Methods in enzymology. 185. 341–351. 26 indexed citations
16.
Tekamp-Olson, Patricia, et al.. (1989). Galactose-regulated expression of hepatitis B surface antigen by a recombinant yeast. Biotechnology Letters. 11(5). 301–306. 5 indexed citations
17.
Pemberton, Philip A., et al.. (1989). Characterization of antithrombins produced by active site mutagenesis of human alpha 1-antitrypsin expressed in yeast. Blood. 73(2). 490–496. 12 indexed citations
18.
Hallewell, Robert A., Robert H. Mills, Patricia Tekamp-Olson, et al.. (1987). Amino Terminal Acetylation of Authentic Human Cu,Zn Superoxide Dismutase Produced in Yeast. Nature Biotechnology. 5(4). 363–366. 82 indexed citations
19.
Geoffroy, Gregory L., Steven Rosenberg, Albert W. Herlinger, & Arnold L. Rheingold. (1986). Synthesis and molecular structure of hexacarbonyl-.mu.-iodo(.mu.-diphenylphosphido)diosmium. High-yield syntheses of hexacarbonyldi-.mu.-iododiosmium and octacarbonyldiiododiosmium. Inorganic Chemistry. 25(16). 2916–2919. 5 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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