John Orban

4.3k total citations
93 papers, 3.2k citations indexed

About

John Orban is a scholar working on Molecular Biology, Materials Chemistry and Spectroscopy. According to data from OpenAlex, John Orban has authored 93 papers receiving a total of 3.2k indexed citations (citations by other indexed papers that have themselves been cited), including 63 papers in Molecular Biology, 29 papers in Materials Chemistry and 14 papers in Spectroscopy. Recurrent topics in John Orban's work include Protein Structure and Dynamics (34 papers), Enzyme Structure and Function (20 papers) and RNA and protein synthesis mechanisms (19 papers). John Orban is often cited by papers focused on Protein Structure and Dynamics (34 papers), Enzyme Structure and Function (20 papers) and RNA and protein synthesis mechanisms (19 papers). John Orban collaborates with scholars based in United States, Belgium and India. John Orban's co-authors include Philip N. Bryan, Patrick Alexander, Yanan He, Yihong Chen, A. Bellemans, Lisa M. Parsons, Roy A. Mariuzza, Pragati Agnihotri, Prakash Kulkarni and Timothy Lee and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Physical Review Letters.

In The Last Decade

John Orban

92 papers receiving 3.1k 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 Orban United States 32 2.3k 1.0k 286 273 268 93 3.2k
Robert O. Fox United States 28 2.8k 1.2× 707 0.7× 291 1.0× 364 1.3× 436 1.6× 58 3.4k
Carol Beth Post United States 35 2.1k 0.9× 649 0.6× 256 0.9× 385 1.4× 147 0.5× 99 3.8k
Christian Bartels Switzerland 19 2.3k 1.0× 699 0.7× 149 0.5× 463 1.7× 205 0.8× 39 3.1k
Patrice Koehl United States 35 3.8k 1.7× 1.4k 1.3× 158 0.6× 331 1.2× 337 1.3× 127 5.1k
Claus Flensburg Denmark 14 2.3k 1.0× 845 0.8× 267 0.9× 112 0.4× 387 1.4× 23 3.5k
Patrice Vachette France 32 2.4k 1.0× 1.2k 1.2× 231 0.8× 248 0.9× 284 1.1× 100 3.3k
Wayne Boucher United Kingdom 18 2.8k 1.2× 607 0.6× 274 1.0× 538 2.0× 307 1.1× 35 4.3k
Gwyndaf Evans United Kingdom 31 2.5k 1.1× 1.8k 1.7× 129 0.5× 216 0.8× 240 0.9× 102 4.3k
Sanzo Miyazawa Japan 30 4.2k 1.8× 1.6k 1.6× 352 1.2× 320 1.2× 379 1.4× 87 5.2k
Ingemar André Sweden 29 2.4k 1.1× 801 0.8× 186 0.7× 267 1.0× 328 1.2× 59 3.4k

Countries citing papers authored by John Orban

Since Specialization
Citations

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

Fields of papers citing papers by John Orban

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of John Orban

This figure shows the co-authorship network connecting the top 25 collaborators of John Orban. A scholar is included among the top collaborators of John Orban 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 Orban. John Orban 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.
LiWang, Andy & John Orban. (2025). Unveiling the cold reality of metamorphic proteins. Proceedings of the National Academy of Sciences. 122(12). e2422725122–e2422725122. 3 indexed citations
2.
He, Yanan, et al.. (2024). Solution NMR backbone resonance assignment of the full-length resistance-related calcium-binding protein Sorcin. Biomolecular NMR Assignments. 18(2). 253–256. 1 indexed citations
3.
Ruan, Biao, Yanan He, Yingwei Chen, et al.. (2023). Design and characterization of a protein fold switching network. Nature Communications. 14(1). 431–431. 19 indexed citations
4.
Kulkarni, Prakash, Vitor B. P. Leite, Susmita Roy, et al.. (2022). Intrinsically disordered proteins: Ensembles at the limits of Anfinsen's dogma. PubMed. 3(1). 11306–11306. 23 indexed citations
5.
Kulkarni, Prakash, Srisairam Achuthan, S. Bhattacharya, et al.. (2021). Protein conformational dynamics and phenotypic switching. Biophysical Reviews. 13(6). 1127–1138. 10 indexed citations
6.
He, Yanan, Pragati Agnihotri, Sneha Rangarajan, et al.. (2020). Peptide–MHC Binding Reveals Conserved Allosteric Sites in MHC Class I- and Class II-Restricted T Cell Receptors (TCRs). Journal of Molecular Biology. 432(24). 166697–166697. 12 indexed citations
7.
Porter, Lauren L., Yanan He, Yihong Chen, John Orban, & Philip N. Bryan. (2015). Subdomain Interactions Foster the Design of Two Protein Pairs with ∼80% Sequence Identity but Different Folds. Biophysical Journal. 108(1). 154–162. 19 indexed citations
8.
He, Yanan, Yihong Chen, Steven M. Mooney, et al.. (2015). Phosphorylation-induced Conformational Ensemble Switching in an Intrinsically Disordered Cancer/Testis Antigen. Journal of Biological Chemistry. 290(41). 25090–25102. 47 indexed citations
9.
He, Yanan, Yihong Chen, Patrick Alexander, Philip N. Bryan, & John Orban. (2012). Mutational Tipping Points for Switching Protein Folds and Functions. Structure. 20(2). 283–291. 80 indexed citations
10.
Zeng, Yu, Yanan He, Fan Yang, et al.. (2011). The Cancer/Testis Antigen Prostate-associated Gene 4 (PAGE4) Is a Highly Intrinsically Disordered Protein. Journal of Biological Chemistry. 286(16). 13985–13994. 56 indexed citations
11.
Alexander, Patrick, Yanan He, Yihong Chen, John Orban, & Philip N. Bryan. (2009). A minimal sequence code for switching protein structure and function. Proceedings of the National Academy of Sciences. 106(50). 21149–21154. 192 indexed citations
12.
He, Yanan, Yihong Chen, Patrick Alexander, Philip N. Bryan, & John Orban. (2008). NMR structures of two designed proteins with high sequence identity but different fold and function. Proceedings of the National Academy of Sciences. 105(38). 14412–14417. 86 indexed citations
13.
Alexander, Patrick, Yanan He, Yihong Chen, John Orban, & Philip N. Bryan. (2007). The design and characterization of two proteins with 88% sequence identity but different structure and function. Proceedings of the National Academy of Sciences. 104(29). 11963–11968. 140 indexed citations
14.
Ruan, Biao, et al.. (2006). Hydrogen−Deuterium Exchange in Free and Prodomain-Complexed Subtilisin. Biochemistry. 46(3). 652–658. 10 indexed citations
15.
He, Yanan, et al.. (2005). Solution NMR Structures of IgG Binding Domains with Artificially Evolved High Levels of Sequence Identity but Different Folds,. Biochemistry. 44(43). 14055–14061. 26 indexed citations
16.
Tangrea, Michael A., et al.. (2002). Solution Structure of the Pro-hormone Convertase 1 Pro-domain from Mus musculus. Journal of Molecular Biology. 320(4). 801–812. 39 indexed citations
17.
Alexander, Patrick, et al.. (2000). Structure and Dynamics of an Acid-Denatured Protein G Mutant. Biochemistry. 39(5). 965–977. 34 indexed citations
18.
Sverdrup, G.M., et al.. (1991). Conceptual Design of the South Coast Alternative Motor Fuels Demonstration Project. SAE technical papers on CD-ROM/SAE technical paper series. 2 indexed citations
19.
Orban, John & Brian R. Reid. (1989). An improved method for [5′‐2H]‐labelling 3′‐O‐acetylthymidine. Journal of Labelled Compounds and Radiopharmaceuticals. 27(2). 195–198. 6 indexed citations
20.
Bellemans, A., et al.. (1980). Influence of the solvent on the conformation of a chain molecule. The Journal of Chemical Physics. 72(11). 6315–6316. 1 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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