Xubiao Peng

463 total citations
43 papers, 295 citations indexed

About

Xubiao Peng is a scholar working on Molecular Biology, Atomic and Molecular Physics, and Optics and Materials Chemistry. According to data from OpenAlex, Xubiao Peng has authored 43 papers receiving a total of 295 indexed citations (citations by other indexed papers that have themselves been cited), including 26 papers in Molecular Biology, 12 papers in Atomic and Molecular Physics, and Optics and 12 papers in Materials Chemistry. Recurrent topics in Xubiao Peng's work include Protein Structure and Dynamics (19 papers), Enzyme Structure and Function (7 papers) and Mass Spectrometry Techniques and Applications (5 papers). Xubiao Peng is often cited by papers focused on Protein Structure and Dynamics (19 papers), Enzyme Structure and Function (7 papers) and Mass Spectrometry Techniques and Applications (5 papers). Xubiao Peng collaborates with scholars based in China, Sweden and France. Xubiao Peng's co-authors include Antti J. Niemi, Qing Zhao, Zhicheng Li, Steven S. Plotkin, Neil R. Cashman, Shuangwei Hu, Adam K. Sieradzan, Jin Dai, Yanchun Li and Shijian Li and has published in prestigious journals such as Journal of the American Chemical Society, Nature Communications and The Journal of Chemical Physics.

In The Last Decade

Xubiao Peng

36 papers receiving 289 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Xubiao Peng China 10 130 126 71 53 45 43 295
Ambika Somasundar United States 10 110 0.8× 61 0.5× 77 1.1× 60 1.1× 24 0.5× 11 501
Ram Avinery Israel 11 134 1.0× 82 0.7× 76 1.1× 7 0.1× 17 0.4× 18 339
Perry W. Ellis United States 7 51 0.4× 78 0.6× 18 0.3× 156 2.9× 54 1.2× 14 370
Pengfei Tian United States 17 551 4.2× 185 1.5× 41 0.6× 22 0.4× 53 1.2× 37 757
Miguel A. Ojeda-López United States 8 170 1.3× 61 0.5× 57 0.8× 34 0.6× 44 1.0× 12 427
Lennard van Buren Netherlands 7 155 1.2× 38 0.3× 28 0.4× 35 0.7× 29 0.6× 10 307
Yasunobu Sugimoto Japan 12 211 1.6× 32 0.3× 36 0.5× 16 0.3× 66 1.5× 30 410
Mohsen Sadeghi Iran 12 149 1.1× 142 1.1× 7 0.1× 20 0.4× 93 2.1× 28 429
Shuhei Kawamoto Japan 8 249 1.9× 78 0.6× 29 0.4× 6 0.1× 88 2.0× 18 366
Kin Lam United States 12 251 1.9× 63 0.5× 22 0.3× 27 0.5× 26 0.6× 15 413

Countries citing papers authored by Xubiao Peng

Since Specialization
Citations

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

Fields of papers citing papers by Xubiao Peng

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Xubiao Peng

This figure shows the co-authorship network connecting the top 25 collaborators of Xubiao Peng. A scholar is included among the top collaborators of Xubiao Peng 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 Xubiao Peng. Xubiao Peng 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.
Liwo, Adam, et al.. (2023). Long-Time Dynamics of Selected Molecular-Motor Components Using a Physics-Based Coarse-Grained Approach. Biomolecules. 13(6). 941–941. 1 indexed citations
2.
Gibbs, Ebrima, et al.. (2023). De Novo Design of a β-Helix Tau Protein Scaffold: An Oligomer-Selective Vaccine Immunogen Candidate for Alzheimer’s Disease. ACS Chemical Neuroscience. 14(15). 2603–2617. 3 indexed citations
3.
Peng, Xubiao, et al.. (2023). An mCherry biolaser based on microbubble cavity with ultra-low threshold. Applied Physics Letters. 123(5). 2 indexed citations
4.
Peng, Xubiao, et al.. (2022). In silico study on the effects of disulfide bonds in ORF8 of SARS-CoV-2. Physical Chemistry Chemical Physics. 24(27). 16876–16883. 4 indexed citations
5.
Nijland, Mark J., et al.. (2022). First Principles Calculation of Protein–Protein Dimer Affinities of ALS-Associated SOD1 Mutants. Frontiers in Molecular Biosciences. 9. 845013–845013. 5 indexed citations
6.
Li, Gaoshang, Jiajia Meng, Jiayu Wang, et al.. (2022). Excited-state dynamics of all-trans protonated retinal Schiff base in CRABPII-based rhodopsin mimics. Biophysical Journal. 121(21). 4109–4118. 2 indexed citations
7.
Peng, Xubiao & Antti J. Niemi. (2021). Local topology and bifurcation hot-spots in proteins with SARS-CoV-2 spike protein as an example. PLoS ONE. 16(9). e0257886–e0257886. 1 indexed citations
8.
Peng, Xubiao, et al.. (2020). Application of topological soliton in modeling protein folding: Recent progress and perspective. Chinese Physics B. 29(10). 108705–108705. 2 indexed citations
9.
Li, Shijian, et al.. (2019). Recovering the Missing Regions in Crystal Structures from the Nuclear Magnetic Resonance Measurement Data Using Matrix Completion Method. Journal of Computational Biology. 27(5). 709–717. 3 indexed citations
10.
Zhao, Qing, et al.. (2019). Improved model on fluorescence decay in singlet fission materials. Physical Chemistry Chemical Physics. 21(4). 2153–2165.
11.
Liu, Jiaojiao, et al.. (2019). Study of correlations between protein peptide plane dynamics and side chain dynamics. PLoS ONE. 14(4). e0215141–e0215141.
12.
Peng, Xubiao, Neil R. Cashman, & Steven S. Plotkin. (2018). Prediction of Misfolding-Specific Epitopes in SOD1 Using Collective Coordinates. The Journal of Physical Chemistry B. 122(49). 11662–11676. 22 indexed citations
13.
Dupuis, John H., Hua Yu, Xubiao Peng, et al.. (2018). pH dependent membrane binding of the Solanum tuberosum plant specific insert: An in silico study. Biochimica et Biophysica Acta (BBA) - Biomembranes. 1860(12). 2608–2618. 4 indexed citations
14.
Davidsson, Jan, et al.. (2017). Solution x-ray scattering and structure formation in protein dynamics. Physical review. E. 96(6). 62405–62405. 1 indexed citations
15.
Peng, Xubiao, Adam K. Sieradzan, & Antti J. Niemi. (2016). Thermal unfolding of myoglobin in the Landau-Ginzburg-Wilson approach. Physical review. E. 94(6). 62405–62405. 10 indexed citations
16.
Peng, Xubiao, et al.. (2014). A three dimensional visualisation approach to protein heavy-atom structure reconstruction. BMC Structural Biology. 14(1). 27–27. 18 indexed citations
17.
Krokhotin, A., et al.. (2013). Soliton driven relaxation dynamics and protein collapse in the villin headpiece. Journal of Physics Condensed Matter. 25(32). 325103–325103. 13 indexed citations
18.
Niemi, Antti J., et al.. (2012). Soliton concepts and protein structure. Physical Review E. 85(3). 31906–31906. 30 indexed citations
19.
Hu, Shuangwei, et al.. (2011). Towards quantitative classification of folded proteins in terms of elementary functions. Physical Review E. 83(4). 41907–41907. 18 indexed citations
20.
Peng, Xubiao, Chengming Bai, & Mo‐Lin Ge. (2010). Yangian symmetry in molecule {V6} and four-spin Heisenberg model. Annals of Physics. 326(2). 216–231. 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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