Robert M. Culik

761 total citations
15 papers, 675 citations indexed

About

Robert M. Culik is a scholar working on Molecular Biology, Materials Chemistry and Spectroscopy. According to data from OpenAlex, Robert M. Culik has authored 15 papers receiving a total of 675 indexed citations (citations by other indexed papers that have themselves been cited), including 14 papers in Molecular Biology, 11 papers in Materials Chemistry and 3 papers in Spectroscopy. Recurrent topics in Robert M. Culik's work include Protein Structure and Dynamics (11 papers), Enzyme Structure and Function (9 papers) and Chemical Synthesis and Analysis (3 papers). Robert M. Culik is often cited by papers focused on Protein Structure and Dynamics (11 papers), Enzyme Structure and Function (9 papers) and Chemical Synthesis and Analysis (3 papers). Robert M. Culik collaborates with scholars based in United States, Canada and China. Robert M. Culik's co-authors include Feng Gai, Matthias M. Waegele, Ileana M. Pazos, Wenkai Zhang, Jianqiang Ma, Hyunil Jo, William F. DeGrado, Michelle R. Bunagan, Arnaldo L. Serrano and Ivan V. Korendovych and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Angewandte Chemie International Edition.

In The Last Decade

Robert M. Culik

15 papers receiving 672 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Robert M. Culik United States 12 416 253 182 151 125 15 675
Joshua K. Carr United States 7 262 0.6× 232 0.9× 169 0.9× 58 0.4× 101 0.8× 7 469
Lauren E. Buchanan United States 12 594 1.4× 239 0.9× 170 0.9× 114 0.8× 100 0.8× 23 916
Ann Marie Woys United States 13 583 1.4× 411 1.6× 281 1.5× 108 0.7× 138 1.1× 16 940
Thomas J. Measey United States 17 586 1.4× 207 0.8× 328 1.8× 156 1.0× 75 0.6× 26 769
Göran Carlström Sweden 14 432 1.0× 100 0.4× 122 0.7× 114 0.8× 29 0.2× 31 662
Jakob J. Lopez Germany 15 323 0.8× 73 0.3× 335 1.8× 174 1.2× 78 0.6× 26 699
Rajdeep Chowdhury India 15 290 0.7× 98 0.4× 84 0.5× 97 0.6× 37 0.3× 28 526
Hugo Sanabria United States 19 613 1.5× 104 0.4× 105 0.6× 230 1.5× 156 1.2× 52 1.0k
Kunihiko Ishii Japan 13 302 0.7× 234 0.9× 83 0.5× 218 1.4× 84 0.7× 37 786
Chewook Lee South Korea 14 567 1.4× 467 1.8× 454 2.5× 215 1.4× 131 1.0× 20 1.0k

Countries citing papers authored by Robert M. Culik

Since Specialization
Citations

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

Fields of papers citing papers by Robert M. Culik

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Robert M. Culik

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

All Works

15 of 15 papers shown
1.
Culik, Robert M., Ashok Sekhar, Jayashree Nagesh, et al.. (2018). Effects of maturation on the conformational free-energy landscape of SOD1. Proceedings of the National Academy of Sciences. 115(11). E2546–E2555. 51 indexed citations
2.
Culik, Robert M., et al.. (2015). Tuning the Attempt Frequency of Protein Folding Dynamics via Transition-State Rigidification: Application to Trp-Cage. The Journal of Physical Chemistry Letters. 6(3). 521–526. 11 indexed citations
3.
Ma, Jianqiang, Ileana M. Pazos, Wenkai Zhang, Robert M. Culik, & Feng Gai. (2015). Site-Specific Infrared Probes of Proteins. Annual Review of Physical Chemistry. 66(1). 357–377. 159 indexed citations
4.
5.
Culik, Robert M., et al.. (2014). Experimental Validation of the Role of Trifluoroethanol as a Nanocrowder. The Journal of Physical Chemistry B. 118(39). 11455–11461. 55 indexed citations
6.
Yang, Lijiang, et al.. (2014). How Quickly Can a β-Hairpin Fold from Its Transition State?. The Journal of Physical Chemistry B. 118(12). 3317–3325. 14 indexed citations
7.
Culik, Robert M., et al.. (2013). Using D-amino acids to delineate the mechanism of protein folding: Application to Trp-cage. Chemical Physics. 422. 131–134. 13 indexed citations
8.
Jo, Hyunil, et al.. (2013). Assessment of Local Friction in Protein Folding Dynamics Using a Helix Cross-Linker. The Journal of Physical Chemistry B. 117(47). 14688–14696. 10 indexed citations
9.
Lin, Chun‐Wei, Robert M. Culik, & Feng Gai. (2013). Using VIPT-Jump to Distinguish Between Different Folding Mechanisms: Application to BBL and a Trpzip. Journal of the American Chemical Society. 135(20). 7668–7673. 18 indexed citations
10.
Culik, Robert M., Hyunil Jo, William F. DeGrado, & Feng Gai. (2012). Using Thioamides To Site-Specifically Interrogate the Dynamics of Hydrogen Bond Formation in β-Sheet Folding. Journal of the American Chemical Society. 134(19). 8026–8029. 65 indexed citations
11.
Waegele, Matthias M., Robert M. Culik, & Feng Gai. (2011). Site-Specific Spectroscopic Reporters of the Local Electric Field, Hydration, Structure, and Dynamics of Biomolecules. The Journal of Physical Chemistry Letters. 2(20). 2598–2609. 147 indexed citations
12.
Culik, Robert M., Arnaldo L. Serrano, Michelle R. Bunagan, & Feng Gai. (2011). Achieving Secondary Structural Resolution in Kinetic Measurements of Protein Folding: A Case Study of the Folding Mechanism of Trp‐cage. Angewandte Chemie International Edition. 50(46). 10884–10887. 61 indexed citations
13.
Culik, Robert M., Arnaldo L. Serrano, Michelle R. Bunagan, & Feng Gai. (2011). Achieving Secondary Structural Resolution in Kinetic Measurements of Protein Folding: A Case Study of the Folding Mechanism of Trp‐cage. Angewandte Chemie. 123(46). 11076–11079. 16 indexed citations
14.
Culik, Robert M., Arnaldo L. Serrano, Michelle R. Bunagan, & Feng Gai. (2011). Titelbild: Achieving Secondary Structural Resolution in Kinetic Measurements of Protein Folding: A Case Study of the Folding Mechanism of Trp‐cage (Angew. Chem. 46/2011). Angewandte Chemie. 123(46). 10923–10923. 1 indexed citations
15.
Jo, Hyunil, Robert M. Culik, Ivan V. Korendovych, William F. DeGrado, & Feng Gai. (2010). Selective Incorporation of Nitrile-Based Infrared Probes into Proteins via Cysteine Alkylation. Biochemistry. 49(49). 10354–10356. 47 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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