Stephen P. Chambers

3.1k total citations · 2 hit papers
26 papers, 2.5k citations indexed

About

Stephen P. Chambers is a scholar working on Molecular Biology, Radiology, Nuclear Medicine and Imaging and Epidemiology. According to data from OpenAlex, Stephen P. Chambers has authored 26 papers receiving a total of 2.5k indexed citations (citations by other indexed papers that have themselves been cited), including 23 papers in Molecular Biology, 4 papers in Radiology, Nuclear Medicine and Imaging and 3 papers in Epidemiology. Recurrent topics in Stephen P. Chambers's work include Viral Infectious Diseases and Gene Expression in Insects (8 papers), Biochemical and Molecular Research (4 papers) and Protein purification and stability (4 papers). Stephen P. Chambers is often cited by papers focused on Viral Infectious Diseases and Gene Expression in Insects (8 papers), Biochemical and Molecular Research (4 papers) and Protein purification and stability (4 papers). Stephen P. Chambers collaborates with scholars based in United States, United Kingdom and New Zealand. Stephen P. Chambers's co-authors include Mark A. Murcko, Keith P. Wilson, John A. Thomson, Scott A. Raybuck, Paul R. Caron, James P. Griffith, David J. Livingston, Manuel A. Navia, Robert A. Aldape and Eunice E. Kim and has published in prestigious journals such as Nature, Cell and Proceedings of the National Academy of Sciences.

In The Last Decade

Stephen P. Chambers

26 papers receiving 2.4k citations

Hit Papers

Structure and mechanism of interleukin-lβ converting enzyme 1994 2026 2004 2015 1994 1996 200 400 600

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Stephen P. Chambers United States 18 1.7k 598 465 325 294 26 2.5k
Ted Fox United States 18 1.3k 0.7× 435 0.7× 449 1.0× 141 0.4× 198 0.7× 24 2.0k
Stefania Di Marco Italy 22 1.8k 1.1× 330 0.6× 275 0.6× 252 0.8× 249 0.8× 32 2.6k
Noriyuki Habuka Japan 20 1.3k 0.7× 384 0.6× 615 1.3× 412 1.3× 296 1.0× 36 2.5k
Magali Mathieu France 23 1.5k 0.9× 546 0.9× 318 0.7× 128 0.4× 606 2.1× 37 3.0k
Elisabetta Bianchi Italy 33 1.9k 1.1× 621 1.0× 818 1.8× 426 1.3× 632 2.1× 83 3.8k
Ellen W. Moomaw United States 13 1.1k 0.7× 268 0.4× 344 0.7× 116 0.4× 256 0.9× 19 1.8k
L. Fiume Italy 33 1.7k 1.0× 558 0.9× 536 1.2× 288 0.9× 130 0.4× 120 3.4k
D W McCourt United States 28 1.2k 0.7× 894 1.5× 1.1k 2.3× 583 1.8× 537 1.8× 41 3.4k
Robert A. Love United States 19 1.3k 0.8× 501 0.8× 701 1.5× 91 0.3× 538 1.8× 24 2.3k
Paul R. Caron United States 26 4.0k 2.3× 727 1.2× 725 1.6× 273 0.8× 431 1.5× 40 5.2k

Countries citing papers authored by Stephen P. Chambers

Since Specialization
Citations

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

Fields of papers citing papers by Stephen P. Chambers

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Stephen P. Chambers. 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 Stephen P. Chambers. The network helps show where Stephen P. Chambers may publish in the future.

Co-authorship network of co-authors of Stephen P. Chambers

This figure shows the co-authorship network connecting the top 25 collaborators of Stephen P. Chambers. A scholar is included among the top collaborators of Stephen P. Chambers 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 Stephen P. Chambers. Stephen P. Chambers 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.
Sawyer, Chelsea, et al.. (2019). Miniaturisation of high-throughput plasmid DNA library preparation for next-generation sequencing using multifactorial optimisation. Synthetic and Systems Biotechnology. 4(1). 57–66. 18 indexed citations
2.
Chambers, Stephen P., John R. Fulghum, Douglas A. Austen, Fan Lu, & Susanne E. Swalley. (2008). E. coli and Insect Cell Expression, Automated Purification and Quantitative Analysis. Methods in molecular biology. 498. 143–156. 5 indexed citations
3.
Chambers, Stephen P. & Susanne E. Swalley. (2008). Designing Experiments for High-Throughput Protein Expression. Methods in molecular biology. 498. 19–29. 19 indexed citations
4.
Fox, Ted, Debra Brennan, Douglas A. Austen, et al.. (2007). Development of a Protease Production Platform for Structure-Based Drug Design. Current Protein and Peptide Science. 8(5). 439–445. 1 indexed citations
5.
Dodd, Andrew, David Greenwood, Andrew L. Miller, et al.. (2006). Zebrafish: At the Nexus of Functional and Chemical Genomics. Biotechnology and Genetic Engineering Reviews. 22(1). 77–100. 2 indexed citations
6.
Swalley, Susanne E., John R. Fulghum, & Stephen P. Chambers. (2005). Screening factors effecting a response in soluble protein expression: Formalized approach using design of experiments. Analytical Biochemistry. 351(1). 122–127. 52 indexed citations
7.
Chambers, Stephen P., et al.. (2004). High-throughput screening for soluble recombinant expressed kinases in Escherichia coli and insect cells. Protein Expression and Purification. 36(1). 40–47. 59 indexed citations
8.
Dodd, Andrew, Stephen P. Chambers, Peter E. Nielsen, & Donald R. Love. (2004). Modeling Human Disease by Gene Targeting. Methods in cell biology. 76. 593–612. 5 indexed citations
9.
Dodd, Andrew, Stephen P. Chambers, & Donald R. Love. (2004). Short interfering RNA‐mediated gene targeting in the zebrafish. FEBS Letters. 561(1-3). 89–93. 69 indexed citations
10.
Chambers, Stephen P., et al.. (2003). Sarcoglycans of the zebrafish: orthology and localization to the sarcolemma and myosepta of muscle. Biochemical and Biophysical Research Communications. 303(2). 488–495. 18 indexed citations
11.
Chambers, Stephen P.. (2002). High-throughput protein expression for the post-genomic era. Drug Discovery Today. 7(14). 759–765. 28 indexed citations
12.
Chambers, Stephen P., Andrew Dodd, Rupert W. Overall, et al.. (2001). Dystrophin in Adult Zebrafish Muscle. Biochemical and Biophysical Research Communications. 286(3). 478–483. 36 indexed citations
13.
Nimmesgern, Elmar, Olga Futer, John R. Fulghum, et al.. (1999). Biochemical Analysis of the Modular Enzyme Inosine 5′-Monophosphate Dehydrogenase. Protein Expression and Purification. 17(2). 282–289. 51 indexed citations
14.
Markland, William, Margaret Fitzgibbon, Ted Fox, et al.. (1997). Purification and characterization of the NS3 serine protease domain of hepatitis C virus expressed in Saccharomyces cerevisiae.. Journal of General Virology. 78(1). 39–43. 22 indexed citations
15.
Chen, Wenyong, et al.. (1997). Expression and Purification of Human Interleukin-1β Converting Enzyme fromTrichoplusia niInsect Cells Using a Baculovirus Expression System. Protein Expression and Purification. 9(1). 69–75. 3 indexed citations
16.
Sintchak, Michael D., Mark Fleming, Olga Futer, et al.. (1996). Structure and Mechanism of Inosine Monophosphate Dehydrogenase in Complex with the Immunosuppressant Mycophenolic Acid. Cell. 85(6). 921–930. 347 indexed citations
17.
Morgenstern, Kurt, Chao Lin, Ted Fox, et al.. (1996). Crystal Structure of the Hepatitis C Virus NS3 Protease Domain Complexed with a Synthetic NS4A Cofactor Peptide. Cell. 87(2). 343–355. 554 indexed citations breakdown →
18.
Wilson, Keith P., Matthew J. Fitzgibbon, Paul R. Caron, et al.. (1996). Crystal Structure of p38 Mitogen-activated Protein Kinase. Journal of Biological Chemistry. 271(44). 27696–27700. 202 indexed citations
19.
Wilson, Keith P., John A. Thomson, Eunice E. Kim, et al.. (1994). Structure and mechanism of interleukin-lβ converting enzyme. Nature. 370(6487). 270–275. 705 indexed citations breakdown →
20.
Lepre, Christopher A., et al.. (1993). Nitrogen-15 NMR relaxation studies of the FK506 binding protein: Backbone dynamics of the uncomplexed receptor. Biochemistry. 32(35). 9000–9010. 48 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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