Doug Barrick

5.2k total citations
89 papers, 4.2k citations indexed

About

Doug Barrick is a scholar working on Molecular Biology, Cell Biology and Materials Chemistry. According to data from OpenAlex, Doug Barrick has authored 89 papers receiving a total of 4.2k indexed citations (citations by other indexed papers that have themselves been cited), including 82 papers in Molecular Biology, 35 papers in Cell Biology and 33 papers in Materials Chemistry. Recurrent topics in Doug Barrick's work include Protein Structure and Dynamics (53 papers), Enzyme Structure and Function (32 papers) and Hemoglobin structure and function (21 papers). Doug Barrick is often cited by papers focused on Protein Structure and Dynamics (53 papers), Enzyme Structure and Function (32 papers) and Hemoglobin structure and function (21 papers). Doug Barrick collaborates with scholars based in United States, Germany and France. Doug Barrick's co-authors include Robert L. Baldwin, Cecilia C. Mello, Katherine W. Tripp, Mark E. Zweifel, Christina Marchetti Bradley, Naomi Courtemanche, Tural Aksel, Mark S. Hargrove, John S. Olson and Tobin R. Sosnick and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Nucleic Acids Research.

In The Last Decade

Doug Barrick

88 papers receiving 4.1k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Doug Barrick United States 38 3.6k 1.3k 1.1k 392 337 89 4.2k
Robert M. Sweet United States 23 3.0k 0.8× 1.0k 0.8× 1.1k 1.0× 277 0.7× 262 0.8× 40 4.4k
Eaton E. Lattman United States 32 3.1k 0.9× 1.2k 0.9× 625 0.6× 384 1.0× 310 0.9× 81 3.9k
Elan Eisenmesser United States 30 3.3k 0.9× 813 0.6× 393 0.4× 198 0.5× 265 0.8× 76 4.5k
Jill Trewhella United States 44 4.4k 1.2× 1.9k 1.5× 554 0.5× 316 0.8× 326 1.0× 158 5.7k
Patrick J. Fleming United States 33 2.7k 0.7× 826 0.7× 326 0.3× 369 0.9× 204 0.6× 60 3.4k
Stefano Gianni Italy 39 3.8k 1.1× 1.7k 1.3× 812 0.8× 216 0.6× 205 0.6× 172 4.5k
Neil A. Farrow United States 30 3.8k 1.0× 1.1k 0.9× 463 0.4× 383 1.0× 179 0.5× 51 5.6k
Robert Fairman United States 38 3.5k 1.0× 976 0.8× 497 0.5× 208 0.5× 184 0.5× 102 4.4k
Yoshifumi Nishimura Japan 44 5.0k 1.4× 604 0.5× 379 0.4× 469 1.2× 330 1.0× 198 6.2k
Ingrid R. Vetter Germany 48 6.4k 1.7× 909 0.7× 2.2k 2.0× 747 1.9× 238 0.7× 102 7.9k

Countries citing papers authored by Doug Barrick

Since Specialization
Citations

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

Fields of papers citing papers by Doug Barrick

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Doug Barrick

This figure shows the co-authorship network connecting the top 25 collaborators of Doug Barrick. A scholar is included among the top collaborators of Doug Barrick 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 Doug Barrick. Doug Barrick 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.
Barrick, Doug, et al.. (2025). Bivalent interaction through an intrinsically disordered linker promotes transcription activation complex assembly in Notch signaling. Proceedings of the National Academy of Sciences. 122(30). e2501607122–e2501607122. 1 indexed citations
2.
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Sternke, Matt, Katherine W. Tripp, & Doug Barrick. (2021). Surface residues and nonadditive interactions stabilize a consensus homeodomain protein. Biophysical Journal. 120(23). 5267–5278. 2 indexed citations
5.
Sternke, Matt, Katherine W. Tripp, & Doug Barrick. (2020). The use of consensus sequence information to engineer stability and activity in proteins. Methods in enzymology on CD-ROM/Methods in enzymology. 643. 149–179. 30 indexed citations
6.
Sternke, Matt, Katherine W. Tripp, & Doug Barrick. (2019). Consensus sequence design as a general strategy to create hyperstable, biologically active proteins. Proceedings of the National Academy of Sciences. 116(23). 11275–11284. 126 indexed citations
7.
Fossat, Martin J., Siwen Zhang, D.K. Rai, et al.. (2018). The consequences of cavity creation on the folding landscape of a repeat protein depend upon context. Proceedings of the National Academy of Sciences. 115(35). 18 indexed citations
8.
Das, Rahul K., et al.. (2017). Control of transcriptional activity by design of charge patterning in the intrinsically disordered RAM region of the Notch receptor. Proceedings of the National Academy of Sciences. 114(44). E9243–E9252. 93 indexed citations
9.
Barrick, Doug, et al.. (2011). Deletion of internal structured repeats increases the stability of a leucine-rich repeat protein, YopM. Biophysical Chemistry. 159(1). 152–161. 13 indexed citations
10.
Johnson, Scott E., Ma. Xenia G. Ilagan, Raphael Kopan, & Doug Barrick. (2009). Thermodynamic Analysis of the CSL·Notch Interaction. Journal of Biological Chemistry. 285(9). 6681–6692. 34 indexed citations
11.
Aksel, Tural & Doug Barrick. (2009). Chapter 4 Analysis of Repeat‐Protein Folding Using Nearest‐Neighbor Statistical Mechanical Models. Methods in enzymology on CD-ROM/Methods in enzymology. 455. 95–125. 32 indexed citations
12.
Street, Timothy O., Naomi Courtemanche, & Doug Barrick. (2007). Protein Folding and Stability Using Denaturants. Methods in cell biology. 84. 295–325. 57 indexed citations
13.
Courtemanche, Naomi & Doug Barrick. (2007). Folding thermodynamics and kinetics of the leucine‐rich repeat domain of the virulence factor Internalin B. Protein Science. 17(1). 43–53. 24 indexed citations
14.
Bradley, Christina Marchetti & Doug Barrick. (2006). The Notch Ankyrin Domain Folds via a Discrete, Centralized Pathway. Structure. 14(8). 1303–1312. 43 indexed citations
15.
Mello, Cecilia C. & Doug Barrick. (2004). An experimentally determined protein folding energy landscape. Proceedings of the National Academy of Sciences. 101(39). 14102–14107. 131 indexed citations
16.
Mello, Cecilia C. & Doug Barrick. (2003). Measuring the stability of partly folded proteins using TMAO. Protein Science. 12(7). 1522–1529. 136 indexed citations
17.
Zweifel, Mark E. & Doug Barrick. (2002). Relationships between the temperature dependence of solvent denaturation and the denaturant dependence of protein stability curves. Biophysical Chemistry. 101-102. 221–237. 36 indexed citations
18.
Bormett, Richard W., G. David Smith, Sanford A. Asher, Doug Barrick, & Donald M. Kurtz. (1994). Vibrational circular dichroism measurements of ligand vibrations in haem and non-haem metalloenzymes. Faraday Discussions. 99(99). 327–327. 13 indexed citations
19.
Barrick, Doug & Robert L. Baldwin. (1993). The molten globule intermediate of apomyoglobin and the process of protein folding. Protein Science. 2(6). 869–876. 160 indexed citations
20.
Barrick, Doug, et al.. (1991). Probing the stability of a partly folded apomyoglobin intermediate by site-directed mutagenesis. Biochemistry. 30(17). 4113–4118. 160 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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