A.C. Robinson

412 total citations
14 papers, 277 citations indexed

About

A.C. Robinson is a scholar working on Molecular Biology, Atomic and Molecular Physics, and Optics and Genetics. According to data from OpenAlex, A.C. Robinson has authored 14 papers receiving a total of 277 indexed citations (citations by other indexed papers that have themselves been cited), including 13 papers in Molecular Biology, 4 papers in Atomic and Molecular Physics, and Optics and 2 papers in Genetics. Recurrent topics in A.C. Robinson's work include Protein Structure and Dynamics (8 papers), DNA and Nucleic Acid Chemistry (7 papers) and Photosynthetic Processes and Mechanisms (5 papers). A.C. Robinson is often cited by papers focused on Protein Structure and Dynamics (8 papers), DNA and Nucleic Acid Chemistry (7 papers) and Photosynthetic Processes and Mechanisms (5 papers). A.C. Robinson collaborates with scholars based in United States and Spain. A.C. Robinson's co-authors include Bertrand García‐Moreno E., Carlos A. Castañeda, J.L. Schlessman, Brian R. Cannon, Daniel G. Isom, Ananya Majumdar, Bertrand García‐Moreno, Michael S. Chimenti, A. Héroux and V.S. Khangulov and has published in prestigious journals such as Proceedings of the National Academy of Sciences, The Journal of Physical Chemistry B and Biochemistry.

In The Last Decade

A.C. Robinson

12 papers receiving 276 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
A.C. Robinson United States 9 238 57 46 44 28 14 277
Ellinor Haglund United States 11 346 1.5× 150 2.6× 48 1.0× 26 0.6× 42 1.5× 23 440
Xiangda Peng China 10 229 1.0× 55 1.0× 32 0.7× 54 1.2× 11 0.4× 24 273
Rohaine V. Hsu United States 6 295 1.2× 38 0.7× 37 0.8× 17 0.4× 22 0.8× 8 346
Mustafa Tekpinar United States 10 281 1.2× 110 1.9× 28 0.6× 19 0.4× 16 0.6× 21 329
P.S. Horanyi United States 10 226 0.9× 64 1.1× 34 0.7× 11 0.3× 20 0.7× 17 389
José Ramón Peregrina Spain 12 303 1.3× 66 1.2× 15 0.3× 38 0.9× 11 0.4× 13 342
Tuping Zhou Sweden 5 298 1.3× 101 1.8× 32 0.7× 22 0.5× 15 0.5× 6 360
Swarnendu Tripathi United States 11 230 1.0× 87 1.5× 36 0.8× 43 1.0× 28 1.0× 22 292
Soundhararajan Gopi India 11 267 1.1× 86 1.5× 35 0.8× 17 0.4× 27 1.0× 22 293
Tomas Ohlson Sweden 4 317 1.3× 121 2.1× 38 0.8× 22 0.5× 11 0.4× 6 360

Countries citing papers authored by A.C. Robinson

Since Specialization
Citations

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

Fields of papers citing papers by A.C. Robinson

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of A.C. Robinson

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

All Works

14 of 14 papers shown
1.
Jeliazkov, Jeliazko R., A.C. Robinson, Bertrand García‐Moreno E., James M. Berger, & Jeffrey J. Gray. (2019). Toward the computational design of protein crystals with improved resolution. Acta Crystallographica Section D Structural Biology. 75(11). 1015–1027. 5 indexed citations
2.
Robinson, A.C., J.L. Schlessman, & Bertrand García‐Moreno E.. (2018). Dielectric Properties of a Protein Probed by Reversal of a Buried Ion Pair. The Journal of Physical Chemistry B. 122(9). 2516–2524. 9 indexed citations
3.
Robinson, A.C., et al.. (2017). Anomalous Properties of Lys Residues Buried in the Hydrophobic Interior of a Protein Revealed with 15N-Detect NMR Spectroscopy. The Journal of Physical Chemistry Letters. 9(2). 383–387. 16 indexed citations
4.
Ortega, Gabriel, et al.. (2017). Local Backbone Flexibility as a Determinant of the Apparent pKa Values of Buried Ionizable Groups in Proteins. Biochemistry. 56(40). 5338–5346. 9 indexed citations
5.
Robinson, A.C., Ananya Majumdar, J.L. Schlessman, & Bertrand García‐Moreno E.. (2016). Charges in Hydrophobic Environments: A Strategy for Identifying Alternative States in Proteins. Biochemistry. 56(1). 212–218. 16 indexed citations
6.
Robinson, A.C., et al.. (2015). Interactions between Pairs of Charges Buried in the Hydrophobic Interior of a Protein are Unexpectedly Weak. Biophysical Journal. 108(2). 517a–517a. 1 indexed citations
7.
Robinson, A.C., Carlos A. Castañeda, J.L. Schlessman, & Bertrand García‐Moreno E.. (2014). Structural and thermodynamic consequences of burial of an artificial ion pair in the hydrophobic interior of a protein. Proceedings of the National Academy of Sciences. 111(32). 11685–11690. 36 indexed citations
8.
Chimenti, Michael S., V.S. Khangulov, A.C. Robinson, et al.. (2012). Structural Reorganization Triggered by Charging of Lys Residues in the Hydrophobic Interior of a Protein. Structure. 20(6). 1071–1085. 40 indexed citations
9.
Robinson, A.C., Carlos A. Castañeda, J.L. Schlessman, & Bertrand García‐Moreno. (2011). Ion Pairs in the Hydrophobic Interior of a Protein: How Do Proteins Dissolve Salt in Oil?. Biophysical Journal. 100(3). 213a–213a.
10.
Robinson, A.C., et al.. (2011). Thermodynamic principles for the engineering of pH-driven conformational switches and acid insensitive proteins. Biophysical Chemistry. 159(1). 217–226. 12 indexed citations
11.
Shah, Anuj, Jennifer Newman, Matthew Monroe, et al.. (2010). An efficient data format for mass spectrometry-based proteomics. Journal of the American Society for Mass Spectrometry. 21(10). 1784–1788. 13 indexed citations
12.
Chimenti, Michael S., V.S. Khangulov, A.C. Robinson, et al.. (2009). Structural Consequences of the Ionization of Internal Lys Residues in a Protein. Biophysical Journal. 96(3). 587a–587a. 1 indexed citations
13.
Isom, Daniel G., Brian R. Cannon, Carlos A. Castañeda, A.C. Robinson, & Bertrand García‐Moreno E.. (2008). High tolerance for ionizable residues in the hydrophobic interior of proteins. Proceedings of the National Academy of Sciences. 105(46). 17784–17788. 119 indexed citations
14.
Robinson, A.C., et al.. (2004). Synthesis of Pu 1-x Am x O 2-y mixed oxides.

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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