John L. Markley

39.0k total citations · 9 hit papers
507 papers, 27.9k citations indexed

About

John L. Markley is a scholar working on Molecular Biology, Spectroscopy and Materials Chemistry. According to data from OpenAlex, John L. Markley has authored 507 papers receiving a total of 27.9k indexed citations (citations by other indexed papers that have themselves been cited), including 362 papers in Molecular Biology, 142 papers in Spectroscopy and 99 papers in Materials Chemistry. Recurrent topics in John L. Markley's work include Protein Structure and Dynamics (145 papers), Enzyme Structure and Function (94 papers) and Metabolomics and Mass Spectrometry Studies (64 papers). John L. Markley is often cited by papers focused on Protein Structure and Dynamics (145 papers), Enzyme Structure and Function (94 papers) and Metabolomics and Mass Spectrometry Studies (64 papers). John L. Markley collaborates with scholars based in United States, Japan and United Kingdom. John L. Markley's co-authors include William M. Westler, Marco Tonelli, Eldon L. Ulrich, Woonghee Lee, Helen M. Berman, Frits Abildgaard, David S. Wishart, Brian D. Sykes, Wim Vranken and Hamid R. Eghbalnia and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

John L. Markley

504 papers receiving 27.2k citations

Hit Papers

The CCPN data model for NMR spectroscopy: Development of ... 1995 2026 2005 2015 2005 1995 2014 2007 2006 500 1000 1.5k 2.0k 2.5k

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
John L. Markley United States 72 20.1k 5.2k 4.9k 1.9k 1.8k 507 27.9k
William F. DeGrado United States 111 32.1k 1.6× 6.7k 1.3× 4.5k 0.9× 2.7k 1.4× 1.2k 0.6× 538 43.5k
Wolfram Saenger Germany 85 23.5k 1.2× 8.8k 1.7× 5.4k 1.1× 1.1k 0.6× 2.5k 1.4× 607 39.6k
Jayaraman Chandrasekhar India 44 21.9k 1.1× 9.2k 1.8× 5.6k 1.1× 1.6k 0.8× 764 0.4× 181 47.2k
Kenneth M. Merz United States 73 23.0k 1.1× 8.7k 1.7× 4.7k 1.0× 1.2k 0.6× 706 0.4× 374 41.5k
Lee G. Pedersen United States 43 29.2k 1.5× 8.7k 1.7× 4.1k 0.8× 2.2k 1.2× 487 0.3× 222 50.5k
Claudio Luchinat Italy 77 12.1k 0.6× 6.7k 1.3× 7.0k 1.4× 1.2k 0.6× 1.8k 1.0× 696 23.7k
Tom Darden United States 28 33.8k 1.7× 9.7k 1.9× 4.3k 0.9× 2.4k 1.3× 487 0.3× 49 55.7k
Jeffry D. Madura United States 37 24.2k 1.2× 8.3k 1.6× 4.2k 0.9× 1.8k 0.9× 437 0.2× 127 43.4k
Barry Honig United States 108 37.5k 1.9× 9.0k 1.7× 4.1k 0.8× 4.2k 2.2× 759 0.4× 347 51.3k
Wei Wang China 65 16.8k 0.8× 6.7k 1.3× 1.8k 0.4× 1.7k 0.9× 1.7k 0.9× 476 33.1k

Countries citing papers authored by John L. Markley

Since Specialization
Citations

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

Fields of papers citing papers by John L. Markley

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by John L. Markley. 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 John L. Markley. The network helps show where John L. Markley may publish in the future.

Co-authorship network of co-authors of John L. Markley

This figure shows the co-authorship network connecting the top 25 collaborators of John L. Markley. A scholar is included among the top collaborators of John L. Markley 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 John L. Markley. John L. Markley 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.
2.
Phillips, Margaret, Marco Tonelli, Gabriel Cornilescu, et al.. (2021). Coordination of Di-Acetylated Histone Ligands by the ATAD2 Bromodomain. International Journal of Molecular Sciences. 22(17). 9128–9128. 10 indexed citations
3.
Phillips, Margaret, Marco Tonelli, Gabriel Cornilescu, et al.. (2020). Structural Insights into the Recognition of Mono- and Diacetylated Histones by the ATAD2B Bromodomain. Journal of Medicinal Chemistry. 63(21). 12799–12813. 13 indexed citations
4.
Cornilescu, Gabriel, Amy Henrickson, Margaret Phillips, et al.. (2020). The BRPF1 bromodomain is a molecular reader of di-acetyllysine. SHILAP Revista de lepidopterología. 2. 104–115. 14 indexed citations
5.
Anderson, John E., et al.. (2020). Metabolic Changes in Synaptosomes in an Animal Model of Schizophrenia Revealed by 1H and 1H,13C NMR Spectroscopy. Metabolites. 10(2). 79–79. 1 indexed citations
6.
Boulton, Stephen, Cristina Olivieri, Madoka Akimoto, et al.. (2020). CHESPA/CHESCA-SPARKY: automated NMR data analysis plugins for SPARKY to map protein allostery. Bioinformatics. 37(8). 1176–1177. 11 indexed citations
7.
Wyche, Thomas P., Jeff S. Piotrowski, Megan Duster, et al.. (2017). Chemical Genomics, Structure Elucidation, and in Vivo Studies of the Marine-Derived Anticlostridial Ecteinamycin. ACS Chemical Biology. 12(9). 2287–2295. 23 indexed citations
8.
Natesan, Senthil, Gabriel Cornilescu, Marco Tonelli, et al.. (2016). Mechanism of Histone H3K4me3 Recognition by the Plant Homeodomain of Inhibitor of Growth 3. Journal of Biological Chemistry. 291(35). 18326–18341. 23 indexed citations
9.
Lee, Woonghee, Jaime L. Stark, & John L. Markley. (2014). PONDEROSA-C/S: client–server based software package for automated protein 3D structure determination. Journal of Biomolecular NMR. 60(2-3). 73–75. 46 indexed citations
10.
Berman, Helen M., Gerard J. Kleywegt, Haruki Nakamura, & John L. Markley. (2012). The Protein Data Bank at 40: Reflecting on the Past to Prepare for the Future. Structure. 20(3). 391–396. 78 indexed citations
11.
Assadi‐Porter, Fariba M., Émeline L. Maillet, James T. Radek, et al.. (2010). Key Amino Acid Residues Involved in Multi-Point Binding Interactions between Brazzein, a Sweet Protein, and the T1R2–T1R3 Human Sweet Receptor. Journal of Molecular Biology. 398(4). 584–599. 93 indexed citations
12.
Lewis, Ian A., et al.. (2009). rNMR: open source software for identifying and quantifying metabolites in NMR spectra. Magnetic Resonance in Chemistry. 47(S1). S123–6. 149 indexed citations
13.
Song, Jikui, Jered V. McGivern, Karl W. Nichols, John L. Markley, & Michael Sheets. (2008). Structural basis for RNA recognition by a type II poly(A)-binding protein. Proceedings of the National Academy of Sciences. 105(40). 15317–15322. 18 indexed citations
14.
Wang, Liya, Hamid R. Eghbalnia, & John L. Markley. (2006). Probabilistic Approach to Determining Unbiased Random-coil Carbon-13 Chemical Shift Values from the Protein Chemical Shift Database. Journal of Biomolecular NMR. 35(3). 155–165. 14 indexed citations
15.
Markley, John L., et al.. (1995). NMR Spectroscopic Studies of Paramagnetic Proteins: Iron-Sulfur Proteins. Annual Review of Biophysics and Biomolecular Structure. 24(1). 209–237. 36 indexed citations
16.
Burkhart, Brian M., et al.. (1995). Structure of the trigonal form of recombinant oxidized flavodoxin fromAnabaena7120 at 1.40 Å resolution. Acta Crystallographica Section D Biological Crystallography. 51(3). 318–330. 17 indexed citations
17.
Edison, Arthur S., Frits Abildgaard, William M. Westler, Ed S. Mooberry, & John L. Markley. (1994). [1] Practical introduction to theory and implementation of multinuclear, multidimensional nuclear magnetic resonance experiments. Methods in enzymology on CD-ROM/Methods in enzymology. 239. 3–79. 73 indexed citations
18.
Macura, Slobodan, William M. Westler, & John L. Markley. (1994). [3] Two-dimensional exchange spectroscopy of proteins. Methods in enzymology on CD-ROM/Methods in enzymology. 239. 106–144. 31 indexed citations
19.
Markley, John L., Andrew P. Hinck, Stewart N. Loh, et al.. (1994). Case study of protein structure, stability, and function: NMR investigations of the proline residues in staphylococcal nuclease. Pure and Applied Chemistry. 66(1). 65–69. 4 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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