John W. Burgner

2.1k total citations
60 papers, 1.7k citations indexed

About

John W. Burgner is a scholar working on Molecular Biology, Materials Chemistry and Cell Biology. According to data from OpenAlex, John W. Burgner has authored 60 papers receiving a total of 1.7k indexed citations (citations by other indexed papers that have themselves been cited), including 38 papers in Molecular Biology, 12 papers in Materials Chemistry and 10 papers in Cell Biology. Recurrent topics in John W. Burgner's work include Protein Structure and Dynamics (13 papers), Enzyme Structure and Function (12 papers) and Hemoglobin structure and function (9 papers). John W. Burgner is often cited by papers focused on Protein Structure and Dynamics (13 papers), Enzyme Structure and Function (12 papers) and Hemoglobin structure and function (9 papers). John W. Burgner collaborates with scholars based in United States, United Kingdom and Switzerland. John W. Burgner's co-authors include William J. Ray, Robert Callender, Hua Deng, Carol Beth Post, Richard Kühn, Jie Zheng, Christopher T. Jones, Lixin Ma, Victor W. Rodwell and Jennifer S. Laurence and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

John W. Burgner

60 papers receiving 1.7k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
John W. Burgner United States 25 1.1k 288 260 202 187 60 1.7k
Mengli Cai United States 26 2.0k 1.9× 335 1.2× 324 1.2× 244 1.2× 79 0.4× 54 2.4k
Paul G. Young New Zealand 26 1.9k 1.8× 359 1.2× 264 1.0× 328 1.6× 243 1.3× 76 2.7k
Irene Luque Spain 27 1.4k 1.3× 406 1.4× 223 0.9× 208 1.0× 69 0.4× 65 2.2k
James R. Appleman United States 26 1.0k 1.0× 244 0.8× 219 0.8× 112 0.6× 108 0.6× 66 1.7k
Tom T. Caradoc-Davies Australia 23 897 0.8× 291 1.0× 191 0.7× 108 0.5× 245 1.3× 45 1.9k
M.R.N. Murthy India 25 1.4k 1.3× 598 2.1× 195 0.8× 150 0.7× 57 0.3× 114 2.4k
Christian Löw Germany 24 1.4k 1.3× 279 1.0× 143 0.6× 190 0.9× 95 0.5× 64 2.1k
Samudrala Gourinath India 25 1.2k 1.2× 264 0.9× 361 1.4× 141 0.7× 121 0.6× 126 2.0k
Pierre Lavigne Canada 33 2.1k 2.0× 273 0.9× 116 0.4× 294 1.5× 80 0.4× 118 4.1k
Jeanne A. Hardy United States 25 1.4k 1.3× 177 0.6× 97 0.4× 193 1.0× 172 0.9× 57 2.1k

Countries citing papers authored by John W. Burgner

Since Specialization
Citations

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

Fields of papers citing papers by John W. Burgner

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of John W. Burgner

This figure shows the co-authorship network connecting the top 25 collaborators of John W. Burgner. A scholar is included among the top collaborators of John W. Burgner 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 W. Burgner. John W. Burgner 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.
Burgner, John W., et al.. (2024). Quantitation of adeno-associated virus in a dual-vector system using sedimentation velocity analytical ultracentrifugation. Journal of Pharmaceutical Sciences. 114(2). 900–910. 1 indexed citations
2.
Burgner, John W., et al.. (2024). BASIS: BioAnalysis SEDFIT integrated software for cGMP analysis of SV-AUC data. European Biophysics Journal. 53(3). 111–121. 2 indexed citations
3.
Burgner, John W., et al.. (2023). AAV analysis by sedimentation velocity analytical ultracentrifugation: beyond empty and full capsids. European Biophysics Journal. 52(4-5). 353–366. 16 indexed citations
4.
Musayev, Faik N., et al.. (2019). Nitrosative stress sensing in Porphyromonas gingivalis: structure of and heme binding by the transcriptional regulator HcpR. Acta Crystallographica Section D Structural Biology. 75(4). 437–450. 6 indexed citations
5.
Musayev, Faik N., et al.. (2015). Structural Insights into the Assembly of the Adeno-associated Virus Type 2 Rep68 Protein on the Integration Site AAVS1. Journal of Biological Chemistry. 290(46). 27487–27499. 23 indexed citations
6.
Steussy, C.N., Tim Schmidt, Jungki Min, et al.. (2013). A Novel Role for Coenzyme A during Hydride Transfer in 3-Hydroxy-3-methylglutaryl-coenzyme A Reductase. Biochemistry. 52(31). 5195–5205. 14 indexed citations
7.
Bardelli, Martino, John W. Burgner, Demet Kekilli, et al.. (2012). The Interdomain Linker of AAV-2 Rep68 Is an Integral Part of Its Oligomerization Domain: Role of a Conserved SF3 Helicase Residue in Oligomerization. PLoS Pathogens. 8(6). e1002764–e1002764. 25 indexed citations
8.
Jose, Joyce, Laralynne Przybyla, Thomas J. Edwards, et al.. (2011). Interactions of the Cytoplasmic Domain of Sindbis Virus E2 with Nucleocapsid Cores Promote Alphavirus Budding. Journal of Virology. 86(5). 2585–2599. 40 indexed citations
9.
Loaiza, Aristobulo, J.A. Ronau, Alexander E. Ribbe, et al.. (2011). Folding dynamics of phenylalanine hydroxylase depends on the enzyme’s metallation state: the native metal, iron, protects against aggregate intermediates. European Biophysics Journal. 40(8). 959–968. 3 indexed citations
10.
Fields, Christopher J., et al.. (2008). pyr RNA binding to the Bacillus caldolyticus PyrR attenuation protein – characterization and regulation by uridine and guanosine nucleotides. FEBS Journal. 275(4). 655–670. 7 indexed citations
11.
Kaddis, Catherine S., et al.. (2007). Similar enzymes, different structures: Phthalate dioxygenase is an α3α3 stacked hexamer, not an α3β3 trimer like “normal” Rieske oxygenases. Archives of Biochemistry and Biophysics. 466(1). 31–39. 11 indexed citations
12.
Burgner, John W., et al.. (2005). Enterococcus faecalis phosphomevalonate kinase. Protein Science. 14(5). 1134–1139. 22 indexed citations
13.
Yu, I-Mei, Jianbo Diao, John W. Burgner, et al.. (2005). Recombinant Severe Acute Respiratory Syndrome (SARS) Coronavirus Nucleocapsid Protein Forms a Dimer through Its C-terminal Domain. Journal of Biological Chemistry. 280(24). 23280–23286. 71 indexed citations
14.
Sinha, Sangita C., et al.. (2004). Crystal Structure of Imidazole Glycerol-phosphate Dehydratase. Journal of Biological Chemistry. 279(15). 15491–15498. 24 indexed citations
15.
Deng, Hua, Jie Zheng, Donald L. Sloan, John W. Burgner, & Robert Callender. (1992). A vibrational analysis of the catalytically important C4-H bonds of NADH bound to lactate or malate dehydrogenase: ground-state effects. Biochemistry. 31(21). 5085–5092. 26 indexed citations
16.
Ray, William J., John W. Burgner, & Carol Beth Post. (1990). Characterization of vanadate-based transition-state-analog complexes of phosphoglucomutase by spectral and NMR techniques. Biochemistry. 29(11). 2770–2778. 33 indexed citations
17.
Deng, Hua, Jie Zheng, John W. Burgner, & Robert Callender. (1989). Hydrogen bonding and reaction specificity in lactate dehydrogenase studied by Raman spectroscopy. The Journal of Physical Chemistry. 93(12). 4710–4713. 12 indexed citations
18.
Burgner, John W., Norman J. Oppenheimer, & William J. Ray. (1987). Remote nitrogen-15 isotope effects on addition of cyanide to NAD. Biochemistry. 26(1). 91–96. 6 indexed citations
19.
Burgner, John W. & William J. Ray. (1984). Acceleration of the NAD-cyanide adduct reaction by lactate dehydrogenase: equilibrium binding effect as a measure of the activation of bound NAD. Biochemistry. 23(16). 3620–3626. 21 indexed citations
20.
Banaszak, Leonard, Patricia A. Andrews, John W. Burgner, E.H. Eylar, & Frank R.N. Gurd. (1963). Carboxymethylation of Sperm Whale Metmyoglobin. Journal of Biological Chemistry. 238(10). 3307–3314. 80 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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