C. Robert Matthews

7.2k total citations
148 papers, 6.1k citations indexed

About

C. Robert Matthews is a scholar working on Molecular Biology, Materials Chemistry and Genetics. According to data from OpenAlex, C. Robert Matthews has authored 148 papers receiving a total of 6.1k indexed citations (citations by other indexed papers that have themselves been cited), including 126 papers in Molecular Biology, 85 papers in Materials Chemistry and 16 papers in Genetics. Recurrent topics in C. Robert Matthews's work include Protein Structure and Dynamics (103 papers), Enzyme Structure and Function (85 papers) and RNA and protein synthesis mechanisms (29 papers). C. Robert Matthews is often cited by papers focused on Protein Structure and Dynamics (103 papers), Enzyme Structure and Function (85 papers) and RNA and protein synthesis mechanisms (29 papers). C. Robert Matthews collaborates with scholars based in United States, Japan and Germany. C. Robert Matthews's co-authors include Jill A. Zitzewitz, Osman Bilsel, Bryan E. Jones, Craig J. Mann, Can Kayatekin, Ying Wu, Louise Wallace, Roxana Ionescu, Edward P. Garvey and Mark R. Hurle and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

C. Robert Matthews

147 papers receiving 5.9k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
C. Robert Matthews United States 46 5.1k 3.0k 613 547 422 148 6.1k
Pau Bernadó France 44 5.2k 1.0× 2.2k 0.7× 462 0.8× 1.1k 2.0× 360 0.9× 131 6.4k
Mónika Fuxreiter Hungary 45 8.8k 1.7× 2.0k 0.7× 1.0k 1.7× 572 1.0× 654 1.5× 110 10.2k
Sophie Jackson United Kingdom 46 6.2k 1.2× 2.7k 0.9× 761 1.2× 542 1.0× 295 0.7× 111 7.1k
Flemming M. Poulsen Denmark 45 5.0k 1.0× 1.7k 0.6× 733 1.2× 1.3k 2.4× 238 0.6× 122 6.5k
Birthe B. Kragelund Denmark 49 5.2k 1.0× 1.4k 0.5× 671 1.1× 696 1.3× 373 0.9× 179 6.9k
Andreas Matouschek United States 46 7.4k 1.4× 2.5k 0.8× 1.8k 2.9× 450 0.8× 636 1.5× 82 8.3k
Frans A. A. Mulder Denmark 38 4.1k 0.8× 1.4k 0.5× 434 0.7× 1.5k 2.8× 281 0.7× 109 5.4k
Michael H. Hecht United States 44 5.3k 1.0× 1.6k 0.5× 571 0.9× 291 0.5× 500 1.2× 104 6.5k
Mikael Akke Sweden 44 5.8k 1.1× 1.9k 0.6× 581 0.9× 2.0k 3.6× 313 0.7× 120 7.0k
D. Wayne Bolen United States 44 7.3k 1.4× 3.5k 1.2× 1.3k 2.0× 911 1.7× 658 1.6× 70 9.3k

Countries citing papers authored by C. Robert Matthews

Since Specialization
Citations

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

Fields of papers citing papers by C. Robert Matthews

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by C. Robert Matthews. 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 C. Robert Matthews. The network helps show where C. Robert Matthews may publish in the future.

Co-authorship network of co-authors of C. Robert Matthews

This figure shows the co-authorship network connecting the top 25 collaborators of C. Robert Matthews. A scholar is included among the top collaborators of C. Robert Matthews 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 C. Robert Matthews. C. Robert Matthews 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.
Newton, Christina C., et al.. (2026). Leisure-Time Physical Activity and Cancer Mortality Among Cancer Survivors. JAMA Network Open. 9(2). e2556971–e2556971.
2.
Zitzewitz, Jill A., et al.. (2019). Nonnative structure in a peptide model of the unfolded state of superoxide dismutase 1 (SOD1): Implications for ALS-linked aggregation. Journal of Biological Chemistry. 294(37). 13708–13717. 7 indexed citations
3.
Nobrega, R. Paul, Christian R. Schwantes, Sagar V. Kathuria, et al.. (2017). Atomistic structural ensemble refinement reveals non-native structure stabilizes a sub-millisecond folding intermediate of CheY. Scientific Reports. 7(1). 44116–44116. 9 indexed citations
4.
Kathuria, Sagar V., Osman Bilsel, Srinivas Chakravarthy, & C. Robert Matthews. (2017). Microfluidic Turbulent Mixers, Time Resolved SAXS and Folding Intermediates of CheY. Biophysical Journal. 112(3). 61a–61a. 1 indexed citations
5.
Matthews, C. Robert, et al.. (2014). Folding of the RNA Recognition Motif (RRM) Domains of the Amyotrophic Lateral Sclerosis (ALS)-linked Protein TDP-43 Reveals an Intermediate State. Journal of Biological Chemistry. 289(12). 8264–8276. 40 indexed citations
6.
Rosen, Laura E., Sagar V. Kathuria, C. Robert Matthews, Osman Bilsel, & Susan Marqusee. (2014). Non-Native Structure Appears in Microseconds during the Folding of E. coli RNase H. Journal of Molecular Biology. 427(2). 443–453. 12 indexed citations
7.
Matthews, C. Robert. (2008). Linking the supply chain to TQM. Quality Engineering. 53(1). 45–46. 13 indexed citations
8.
Kayatekin, Can, Jill A. Zitzewitz, & C. Robert Matthews. (2008). Zinc Binding Modulates the Entire Folding Free Energy Surface of Human Cu,Zn Superoxide Dismutase. Journal of Molecular Biology. 384(2). 540–555. 70 indexed citations
9.
Vadrevu, Ramakrishna, Ying Wu, & C. Robert Matthews. (2007). NMR Analysis of Partially Folded States and Persistent Structure in the Alpha Subunit of Tryptophan Synthase: Implications for the Equilibrium Folding Mechanism of a 29-kDa TIM Barrel Protein. Journal of Molecular Biology. 377(1). 294–306. 18 indexed citations
10.
Levy, Yaakov, et al.. (2006). The Folding Energy Landscape of the Dimerization Domain of Escherichia coli Trp Repressor: A Joint Experimental and Theoretical Investigation. Journal of Molecular Biology. 363(1). 262–278. 13 indexed citations
11.
Wintrode, Patrick L., et al.. (2005). An Obligatory Intermediate Controls the Folding of the α-Subunit of Tryptophan Synthase, a TIM Barrel Protein. Journal of Molecular Biology. 347(5). 911–919. 26 indexed citations
12.
Ibarra‐Molero, Beatriz, Jill A. Zitzewitz, & C. Robert Matthews. (2004). Salt-bridges can Stabilize but do not Accelerate the Folding of the Homodimeric Coiled-coil Peptide GCN4-p1. Journal of Molecular Biology. 336(5). 989–996. 49 indexed citations
13.
Arai, Munehito, Mikio Kataoka, Kunihiro Kuwajima, C. Robert Matthews, & Masahiro Iwakura. (2003). Effects of the Difference in the Unfolded-state Ensemble on the Folding of Escherichia coli Dihydrofolate Reductase. Journal of Molecular Biology. 329(4). 779–791. 25 indexed citations
14.
Wallace, Louise & C. Robert Matthews. (2002). Highly divergent dihydrofolate reductases conserve complex folding mechanisms 1 1Edited by P. E. Wright. Journal of Molecular Biology. 315(2). 193–211. 40 indexed citations
15.
Steinbach, Peter, Roxana Ionescu, & C. Robert Matthews. (2002). Analysis of Kinetics Using a Hybrid Maximum-Entropy/Nonlinear-Least-Squares Method: Application to Protein Folding. Biophysical Journal. 82(4). 2244–2255. 165 indexed citations
16.
17.
Gloss, Lisa M., et al.. (2001). Rough energy landscapes in protein folding: dimeric E. coliTrp repressor folds through three parallel channels11Edited by P. E. Wright. Journal of Molecular Biology. 312(5). 1121–1134. 31 indexed citations
18.
Iwakura, Masahiro, et al.. (1995). Detection of a Stable Intermediate in the Thermal Unfolding of a Cysteine-Free Form of Dihydrofolate Reductase from Escherichia Coli. Biochemistry. 34(33). 10669–10675. 20 indexed citations
19.
Matthews, C. Robert. (1993). PATHWAYS OF PROTEIN FOLDING. Annual Review of Biochemistry. 62(1). 653–683. 368 indexed citations
20.
Iwakura, Masahiro & C. Robert Matthews. (1992). Construction and characterization of a single polypeptide chain containing two enzymatically active dihydrofolate reductase domains. Protein Engineering Design and Selection. 5(8). 791–796. 7 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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