James H. Prestegard

16.9k total citations · 2 hit papers
311 papers, 13.7k citations indexed

About

James H. Prestegard is a scholar working on Molecular Biology, Spectroscopy and Materials Chemistry. According to data from OpenAlex, James H. Prestegard has authored 311 papers receiving a total of 13.7k indexed citations (citations by other indexed papers that have themselves been cited), including 236 papers in Molecular Biology, 125 papers in Spectroscopy and 64 papers in Materials Chemistry. Recurrent topics in James H. Prestegard's work include Protein Structure and Dynamics (110 papers), Glycosylation and Glycoproteins Research (82 papers) and Advanced NMR Techniques and Applications (67 papers). James H. Prestegard is often cited by papers focused on Protein Structure and Dynamics (110 papers), Glycosylation and Glycoproteins Research (82 papers) and Advanced NMR Techniques and Applications (67 papers). James H. Prestegard collaborates with scholars based in United States, Canada and Germany. James H. Prestegard's co-authors include Joel R. Tolman, Judit A. Losonczi, Donald M. Engelman, John M. Flanagan, Kevin R. MacKenzie, Hashim M. Al‐Hashimi, Michael A. Kennedy, Charles R. Sanders, Yangmee Kim and Homayoun Valafar and has published in prestigious journals such as Science, Chemical Reviews and Proceedings of the National Academy of Sciences.

In The Last Decade

James H. Prestegard

309 papers receiving 13.3k citations

Hit Papers

align trajectories

What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

A Transmembrane Helix Dimer: Structure and Implications

1997 827 citations James H. Prestegard et al. Science profile →
Nuclear magnetic dipole interactions in field-oriented proteins: information for structure determination in solution.

1995 686 citations Michael A. Kennedy, James H. Prestegard et al. Proceedings of the National Academy of Sciences profile →

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
James H. Prestegard United States	57	10.6k	4.5k	2.7k	1.9k	1.2k	311	13.7k
Robert Kaptein Netherlands	64	14.1k 1.3×	4.0k 0.9×	3.8k 1.4×	1.6k 0.9×	890 0.8×	347	20.1k
David E. Wemmer United States	73	12.4k 1.2×	3.4k 0.8×	2.4k 0.9×	1.5k 0.8×	956 0.8×	281	17.8k
Mark Rance United States	46	8.0k 0.8×	3.6k 0.8×	2.1k 0.8×	724 0.4×	734 0.6×	115	11.1k
Hartmut Oschkinat Germany	63	7.7k 0.7×	6.1k 1.4×	4.1k 1.5×	740 0.4×	1.3k 1.1×	280	14.3k
Harald Schwalbe Germany	64	13.0k 1.2×	3.2k 0.7×	3.6k 1.3×	1.3k 0.7×	644 0.5×	485	16.6k
Rolf Boelens Netherlands	64	13.2k 1.2×	2.3k 0.5×	2.6k 1.0×	682 0.4×	883 0.7×	318	17.1k
Geerten W. Vuister Netherlands	46	15.8k 1.5×	3.0k 0.7×	3.8k 1.4×	721 0.4×	2.0k 1.7×	120	20.2k
Nico Tjandra United States	54	11.1k 1.0×	3.9k 0.9×	3.0k 1.1×	522 0.3×	1.0k 0.9×	172	14.1k
Guang Zhu Hong Kong	32	13.7k 1.3×	2.3k 0.5×	3.1k 1.2×	931 0.5×	1.9k 1.6×	125	18.4k
Gottfried Otting Australia	73	13.3k 1.3×	5.1k 1.1×	5.4k 2.0×	1.1k 0.6×	1.0k 0.9×	326	19.8k

Countries citing papers authored by James H. Prestegard

Since Specialization

Citations

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

Fields of papers citing papers by James H. Prestegard

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by James H. Prestegard. 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 James H. Prestegard. The network helps show where James H. Prestegard may publish in the future.

Co-authorship network of co-authors of James H. Prestegard

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

All Works

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20 of 20 papers shown

Tejero, Roberto, Yuanpeng J. Huang, Theresa A. Ramelot, et al.. (2023). Blind Assessment of Monomeric AlphaFold2 Protein Structure Models with Experimental NMR Data. SSRN Electronic Journal. 1 indexed citations

Williams, Robert V., et al.. (2022). Site-to-site cross-talk in OST-B glycosylation of hCEACAM1-IgV. Proceedings of the National Academy of Sciences. 119(43). e2202992119–e2202992119. 2 indexed citations

Williams, Robert V., et al.. (2022). NMR analysis suggests the terminal domains of Robo1 remain extended but are rigidified in the presence of heparan sulfate. Scientific Reports. 12(1). 14769–14769. 3 indexed citations

Prestegard, James H.. (2021). A perspective on the PDB’s impact on the field of glycobiology. Journal of Biological Chemistry. 296. 100556–100556. 20 indexed citations

Kim, Hyun W., Alexander Eletsky, Hanke van der Wel, et al.. (2020). Skp1 Dimerization Conceals Its F-Box Protein Binding Site. Biochemistry. 59(15). 1527–1536. 12 indexed citations

Kuprov, Ilya, Laura Morris, John Glushka, & James H. Prestegard. (2020). Using molecular dynamics trajectories to predict nuclear spin relaxation behaviour in large spin systems. Journal of Magnetic Resonance. 323. 106891–106891. 6 indexed citations

Gao, Qi, Jeong‐Yeh Yang, Kelley W. Moremen, John G. Flanagan, & James H. Prestegard. (2018). Structural Characterization of a Heparan Sulfate Pentamer Interacting with LAR-Ig1-2. Biochemistry. 57(15). 2189–2199. 14 indexed citations

Eletsky, Alexander, Qi Gao, Laura Morris, et al.. (2018). Paramagnetic Tag for Glycosylation Sites in Glycoproteins: Structural Constraints on Heparan Sulfate Binding to Robo1. ACS Chemical Biology. 13(9). 2560–2567. 13 indexed citations

Xu, Xianzhong, Alexander Eletsky, M. Osman Sheikh, James H. Prestegard, & Christopher M. West. (2017). Glycosylation Promotes the Random Coil to Helix Transition in a Region of a Protist Skp1 Associated with F-Box Binding. Biochemistry. 57(5). 511–515. 14 indexed citations

10.

Gao, Qi, Cheng‐Yu Chen, Chengli Zong, et al.. (2016). Structural Aspects of Heparan Sulfate Binding to Robo1–Ig1–2. ACS Chemical Biology. 11(11). 3106–3113. 22 indexed citations

11.

Chen, Huiling, Victor Olman, Charles K. Mobley, et al.. (2011). Optimal Mutation Sites for PRE Data Collection and Membrane Protein Structure Prediction. Structure. 19(4). 484–495. 20 indexed citations

12.

Raman, Srivatsan, Oliver F. Lange, P. Rossi, et al.. (2010). NMR Structure Determination for Larger Proteins Using Backbone-Only Data. Science. 327(5968). 1014–1018. 201 indexed citations

13.

Liu, Shan, André Venot, Lu Meng, et al.. (2007). Spin-Labeled Analogs of CMP-NeuAc as NMR Probes of the α-2,6-Sialyltransferase ST6Gal I. Chemistry & Biology. 14(4). 409–418. 11 indexed citations

14.

Losonczi, Judit A., Michael Andrec, Mark W.F. Fischer, & James H. Prestegard. (1999). Order Matrix Analysis of Residual Dipolar Couplings Using Singular Value Decomposition. Journal of Magnetic Resonance. 138(2). 334–342. 472 indexed citations

15.

Andrec, Michael, R. Blake Hill, & James H. Prestegard. (1995). Amide exchange rates in Escherichia coli acyl carrier protein: Correlation with protein structure and dynamics. Protein Science. 4(5). 983–993. 57 indexed citations

16.

Hare, Brian, et al.. (1993). Synthesis and characterization of a 13C-labeled α-mannosyl glycolipid analog from [13C]glucose. Chemistry and Physics of Lipids. 66(1-2). 155–158. 4 indexed citations

17.

Aubin, Yves & James H. Prestegard. (1993). Structure and dynamics of sialic acid at the surface of a magnetically oriented membrane system. Biochemistry. 32(13). 3422–3428. 27 indexed citations

18.

Koerner, Theodore A.W., James H. Prestegard, & Robert K. Yu. (1987). [4] Oligosaccharide structure by two-dimensional proton nuclear magnetic resonance spectroscopy. Methods in enzymology on CD-ROM/Methods in enzymology. 138. 38–59. 52 indexed citations

19.

Holak, T.A., et al.. (1987). NMR: pseudoenergy approach to the solution structure of acyl carrier protein. Biochemistry. 26(15). 4652–4660. 31 indexed citations

20.

Cronan, John E. & James H. Prestegard. (1977). Difference decoupling nuclear magnetic resonance: a method to study the exchange of fatty acids between phospholipid molecules. Biochemistry. 16(21). 4738–4742. 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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