Christopher M. Dobson

1.8k total citations
12 papers, 1.4k citations indexed

About

Christopher M. Dobson is a scholar working on Molecular Biology, Materials Chemistry and Cell Biology. According to data from OpenAlex, Christopher M. Dobson has authored 12 papers receiving a total of 1.4k indexed citations (citations by other indexed papers that have themselves been cited), including 11 papers in Molecular Biology, 6 papers in Materials Chemistry and 5 papers in Cell Biology. Recurrent topics in Christopher M. Dobson's work include Protein Structure and Dynamics (7 papers), Enzyme Structure and Function (6 papers) and Hemoglobin structure and function (3 papers). Christopher M. Dobson is often cited by papers focused on Protein Structure and Dynamics (7 papers), Enzyme Structure and Function (6 papers) and Hemoglobin structure and function (3 papers). Christopher M. Dobson collaborates with scholars based in United Kingdom, United States and Belgium. Christopher M. Dobson's co-authors include Michele Vendruscolo, Sheena E. Radford, Martin Karplus, Dmitry M. Korzhnev, Xavier Salvatella, Ariel A. Di Nardo, Alan R. Davidson, Lewis E. Kay, Andrew D. Miranker and Gian Gaetano Tartaglia and has published in prestigious journals such as Nature, Nature Biotechnology and PLoS ONE.

In The Last Decade

Christopher M. Dobson

12 papers receiving 1.4k citations

Peers

Christopher M. Dobson
John W. Shriver United States
Julia Wirmer Germany
Zachary S. Hendsch United States
Christopher M. Dobson United Kingdom
Martin J. Parker United Kingdom
Zach Serber United States
John W. Shriver United States
Christopher M. Dobson
Citations per year, relative to Christopher M. Dobson Christopher M. Dobson (= 1×) peers John W. Shriver

Countries citing papers authored by Christopher M. Dobson

Since Specialization
Citations

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

Fields of papers citing papers by Christopher M. Dobson

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Christopher M. Dobson. 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 Christopher M. Dobson. The network helps show where Christopher M. Dobson may publish in the future.

Co-authorship network of co-authors of Christopher M. Dobson

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

All Works

12 of 12 papers shown
1.
Wyatt, Amy R., Janet R. Kumita, Natalie E. Farrawell, Christopher M. Dobson, & Mark R. Wilson. (2015). Alpha-2-Macroglobulin Is Acutely Sensitive to Freezing and Lyophilization: Implications for Structural and Functional Studies. PLoS ONE. 10(6). e0130036–e0130036. 13 indexed citations
2.
Ciryam, Prajwal, Gian Gaetano Tartaglia, Richard I. Morimoto, Christopher M. Dobson, & Michele Vendruscolo. (2013). Widespread Aggregation and Neurodegenerative Diseases Are Associated with Supersaturated Proteins. Cell Reports. 5(3). 781–790. 224 indexed citations
3.
Korzhnev, Dmitry M., Xavier Salvatella, Michele Vendruscolo, et al.. (2004). Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR. Nature. 430(6999). 586–590. 410 indexed citations
4.
Conejero‐Lara, Francisco, et al.. (1998). Analysis of the interactions between streptokinase domains and human plasminogen. Protein Science. 7(10). 2190–2199. 34 indexed citations
5.
Li, Xiang, et al.. (1994). Solution Structure of the Kringle Domain from Urokinase-type Plasminogen Activator. Journal of Molecular Biology. 235(5). 1548–1559. 26 indexed citations
6.
Taddei, Niccolò, Matthias Buck, R. William Broadhurst, et al.. (1994). Equilibrium Unfolding Studies of Horse Muscle Acylphosphatase. European Journal of Biochemistry. 225(3). 811–817. 20 indexed citations
7.
Dael, H. Van, et al.. (1993). Partially folded states of equine lysozyme. Structural characterization and significance for protein folding. Biochemistry. 32(44). 11886–11894. 70 indexed citations
8.
Dobson, Christopher M., et al.. (1993). Structure and stability of the molten globule state of guinea pig .alpha.-lactalbumin: A hydrogen exchange study. Biochemistry. 32(21). 5681–5691. 158 indexed citations
9.
Cooper, Alan, Stephen J. Eyles, Sheena E. Radford, & Christopher M. Dobson. (1992). Thermodynamic consequences of the removal of a disulphide bridge from hen lysozyme. Journal of Molecular Biology. 225(4). 939–943. 81 indexed citations
10.
Miranker, Andrew D., Sheena E. Radford, Martin Karplus, & Christopher M. Dobson. (1991). Demonstration by NMR of folding domains in lysozyme. Nature. 349(6310). 633–636. 214 indexed citations
11.
Jeenes, David J., Donald MacKenzie, Gale Brightwell, et al.. (1990). Hen Egg White Lysozyme Expressed in and Secreted from, Aspergillus niger is Correctly Processed and Folded. Nature Biotechnology. 8(8). 741–745. 99 indexed citations
12.
States, David J., Thomas E. Creighton, Christopher M. Dobson, & Martin Karplus. (1987). Conformations of intermediates in the folding of the pancreatic trypsin inhibitor. Journal of Molecular Biology. 195(3). 731–739. 85 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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