Osman Bilsel

3.0k total citations · 1 hit paper
55 papers, 2.6k citations indexed

About

Osman Bilsel is a scholar working on Molecular Biology, Materials Chemistry and Neurology. According to data from OpenAlex, Osman Bilsel has authored 55 papers receiving a total of 2.6k indexed citations (citations by other indexed papers that have themselves been cited), including 33 papers in Molecular Biology, 30 papers in Materials Chemistry and 7 papers in Neurology. Recurrent topics in Osman Bilsel's work include Protein Structure and Dynamics (27 papers), Enzyme Structure and Function (22 papers) and Mass Spectrometry Techniques and Applications (6 papers). Osman Bilsel is often cited by papers focused on Protein Structure and Dynamics (27 papers), Enzyme Structure and Function (22 papers) and Mass Spectrometry Techniques and Applications (6 papers). Osman Bilsel collaborates with scholars based in United States, United Kingdom and Japan. Osman Bilsel's co-authors include C. Robert Matthews, Jill A. Zitzewitz, Gang Han, Wei Fan, Dewey Holten, Jie Shen, Can Kayatekin, Chun‐Chih Chang, Guanying Chen and Elena Kondrashkina 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

Osman Bilsel

55 papers receiving 2.5k citations

Hit Papers

Dye-Sensitized Core/Active Shell Upconversion Nanoparticl... 2016 2026 2019 2022 2016 100 200 300

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Osman Bilsel United States 28 1.5k 1.2k 504 266 182 55 2.6k
Artem Pliss United States 26 599 0.4× 969 0.8× 694 1.4× 143 0.5× 80 0.4× 70 2.1k
Tetsuro Fujisawa Japan 29 869 0.6× 1.8k 1.5× 210 0.4× 56 0.2× 203 1.1× 80 2.8k
Gregory S. Harms Germany 27 763 0.5× 1.4k 1.1× 538 1.1× 414 1.6× 96 0.5× 66 3.0k
Christian A. Wurm Germany 33 524 0.3× 2.3k 2.0× 1.0k 2.1× 178 0.7× 173 1.0× 49 4.5k
Jiji Chen United States 32 761 0.5× 2.3k 1.9× 937 1.9× 147 0.6× 204 1.1× 52 4.3k
Jens Michaelis Germany 32 556 0.4× 1.8k 1.5× 617 1.2× 297 1.1× 88 0.5× 86 3.2k
Zhen‐Li Huang China 35 1.7k 1.1× 852 0.7× 1.0k 2.1× 606 2.3× 237 1.3× 148 3.7k
Andrey N. Kuzmin United States 32 1.2k 0.8× 599 0.5× 848 1.7× 941 3.5× 134 0.7× 105 3.1k
Brent L. Nannenga United States 21 1.0k 0.7× 988 0.8× 103 0.2× 65 0.2× 226 1.2× 54 1.9k
D.J. van den Heuvel Netherlands 18 849 0.6× 640 0.5× 273 0.5× 409 1.5× 72 0.4× 30 1.8k

Countries citing papers authored by Osman Bilsel

Since Specialization
Citations

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

Fields of papers citing papers by Osman Bilsel

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Osman Bilsel

This figure shows the co-authorship network connecting the top 25 collaborators of Osman Bilsel. A scholar is included among the top collaborators of Osman Bilsel 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 Osman Bilsel. Osman Bilsel 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.
Kayatekin, Can, et al.. (2020). Friction-Limited Folding of Disulfide-Reduced Monomeric SOD1. Biophysical Journal. 118(8). 1992–2000. 2 indexed citations
2.
Peran, Ivan, Alex S. Holehouse, Isaac S. Carrico, et al.. (2019). Unfolded states under folding conditions accommodate sequence-specific conformational preferences with random coil-like dimensions. Proceedings of the National Academy of Sciences. 116(25). 12301–12310. 43 indexed citations
4.
Nawrotek, Agata, Wenhua Zhang, Mahel Zeghouf, et al.. (2019). Structural Organization and Dynamics of Homodimeric Cytohesin Family Arf GTPase Exchange Factors in Solution and on Membranes. Structure. 27(12). 1782–1797.e7. 11 indexed citations
5.
Zitzewitz, Jill A., et al.. (2019). Nonnative structure in a peptide model of the unfolded state of superoxide dismutase 1 (SOD1): Implications for ALS-linked aggregation. Journal of Biological Chemistry. 294(37). 13708–13717. 7 indexed citations
6.
Kathuria, Sagar V., et al.. (2018). Computer design of microfluidic mixers for protein/RNA folding studies. PLoS ONE. 13(6). e0198534–e0198534. 8 indexed citations
7.
Rothstein, Jonathan P., et al.. (2018). High-speed velocimetry in microfluidic protein mixers using confocal fluorescence decay microscopy. Experiments in Fluids. 59(12). 5 indexed citations
8.
Chakravarthy, Srinivas, et al.. (2017). Structural Dynamics Control Allosteric Activation of Cytohesin Family Arf GTPase Exchange Factors. Structure. 26(1). 106–117.e6. 11 indexed citations
9.
Nobrega, R. Paul, Christian R. Schwantes, Sagar V. Kathuria, et al.. (2017). Atomistic structural ensemble refinement reveals non-native structure stabilizes a sub-millisecond folding intermediate of CheY. Scientific Reports. 7(1). 44116–44116. 9 indexed citations
10.
Holehouse, Alex S., et al.. (2017). Simulations and Experiments Provide a Convergent View of Protein Unfolded States under Folding Conditions. Biophysical Journal. 112(3). 315a–315a. 1 indexed citations
11.
Kathuria, Sagar V., Osman Bilsel, Srinivas Chakravarthy, & C. Robert Matthews. (2017). Microfluidic Turbulent Mixers, Time Resolved SAXS and Folding Intermediates of CheY. Biophysical Journal. 112(3). 61a–61a. 1 indexed citations
12.
Chakravarthy, Srinivas, et al.. (2015). Methods for analysis of size-exclusion chromatography–small-angle X-ray scattering and reconstruction of protein scattering. Journal of Applied Crystallography. 48(4). 1102–1113. 42 indexed citations
13.
Rosen, Laura E., Sagar V. Kathuria, C. Robert Matthews, Osman Bilsel, & Susan Marqusee. (2014). Non-Native Structure Appears in Microseconds during the Folding of E. coli RNase H. Journal of Molecular Biology. 427(2). 443–453. 12 indexed citations
14.
Graceffa, Rita, R. Paul Nobrega, Raúl A. Barrea, et al.. (2013). Sub-millisecond time-resolved SAXS using a continuous-flow mixer and X-ray microbeam. Journal of Synchrotron Radiation. 20(6). 820–825. 57 indexed citations
15.
Tiwari, Ashutosh, Amir Liba, Se Hui Sohn, et al.. (2009). Metal Deficiency Increases Aberrant Hydrophobicity of Mutant Superoxide Dismutases That Cause Amyotrophic Lateral Sclerosis. Journal of Biological Chemistry. 284(40). 27746–27758. 68 indexed citations
16.
Arai, Munehito, Elena Kondrashkina, Can Kayatekin, et al.. (2007). Microsecond Hydrophobic Collapse in the Folding of Escherichia coli Dihydrofolate Reductase, an α/β-Type Protein. Journal of Molecular Biology. 368(1). 219–229. 75 indexed citations
18.
Doyle, Shannon M., Osman Bilsel, & Carolyn M. Teschke. (2004). SecA Folding Kinetics: A Large Dimeric Protein Rapidly Forms Multiple Native States. Journal of Molecular Biology. 341(1). 199–214. 14 indexed citations
19.
Bilsel, Osman & C. Robert Matthews. (2000). Barriers in protein folding reactions. Advances in protein chemistry. 53. 153–207. 66 indexed citations
20.
Zitzewitz, Jill A., et al.. (1995). Probing the Folding Mechanism of a Leucine Zipper Peptide by Stopped-Flow Circular Dichroism Spectroscopy. Biochemistry. 34(39). 12812–12819. 150 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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