Ivan Peran

2.0k total citations · 2 hit papers
14 papers, 1.2k citations indexed

About

Ivan Peran is a scholar working on Molecular Biology, Materials Chemistry and Spectroscopy. According to data from OpenAlex, Ivan Peran has authored 14 papers receiving a total of 1.2k indexed citations (citations by other indexed papers that have themselves been cited), including 14 papers in Molecular Biology, 6 papers in Materials Chemistry and 2 papers in Spectroscopy. Recurrent topics in Ivan Peran's work include Protein Structure and Dynamics (8 papers), RNA and protein synthesis mechanisms (7 papers) and Enzyme Structure and Function (5 papers). Ivan Peran is often cited by papers focused on Protein Structure and Dynamics (8 papers), RNA and protein synthesis mechanisms (7 papers) and Enzyme Structure and Function (5 papers). Ivan Peran collaborates with scholars based in United States, United Kingdom and India. Ivan Peran's co-authors include Rohit V. Pappu, Erik Martin, Tanja Mittag, Mina Farag, Anne Bremer, Alex S. Holehouse, Andrea Soranno, Christy R. Grace, J. Jeremías Incicco and Wade M. Borcherds and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Ivan Peran

14 papers receiving 1.2k citations

Hit Papers

Valence and patterning of aromatic residues determine the... 2020 2026 2022 2024 2020 2021 200 400 600

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Ivan Peran United States 9 1.1k 165 84 73 61 14 1.2k
Anne Bremer United States 14 1.3k 1.2× 159 1.0× 112 1.3× 104 1.4× 39 0.6× 21 1.6k
Wade M. Borcherds United States 15 1.0k 1.0× 192 1.2× 40 0.5× 90 1.2× 55 0.9× 29 1.2k
Yi‐Hsuan Lin Canada 14 1.4k 1.3× 247 1.5× 152 1.8× 45 0.6× 37 0.6× 25 1.6k
Adiran Garaizar United Kingdom 14 877 0.8× 100 0.6× 72 0.9× 39 0.5× 17 0.3× 20 1.0k
Anastasia C. Murthy United States 8 853 0.8× 76 0.5× 79 0.9× 37 0.5× 29 0.5× 17 994
Rustam Ali United States 7 814 0.8× 72 0.4× 68 0.8× 58 0.8× 26 0.4× 9 902
Dylan T. Murray United States 14 854 0.8× 116 0.7× 46 0.5× 80 1.1× 201 3.3× 21 1.1k
Xiaojie Zhang Germany 4 1.3k 1.2× 81 0.5× 123 1.5× 83 1.1× 15 0.2× 6 1.4k
Alexander Jussupow Germany 16 681 0.6× 128 0.8× 16 0.2× 54 0.7× 49 0.8× 25 843
Ibraheem Alshareedah United States 12 1.1k 1.0× 71 0.4× 109 1.3× 72 1.0× 9 0.1× 20 1.3k

Countries citing papers authored by Ivan Peran

Since Specialization
Citations

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

Fields of papers citing papers by Ivan Peran

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Ivan Peran

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

All Works

14 of 14 papers shown
1.
Bremer, Anne, Mina Farag, Wade M. Borcherds, et al.. (2021). Deciphering how naturally occurring sequence features impact the phase behaviours of disordered prion-like domains. Nature Chemistry. 14(2). 196–207. 302 indexed citations breakdown →
2.
Martin, Erik, Alex S. Holehouse, Ivan Peran, et al.. (2020). Valence and patterning of aromatic residues determine the phase behavior of prion-like domains. Science. 367(6478). 694–699. 713 indexed citations breakdown →
3.
Holehouse, Alex S., Erik Martin, Ivan Peran, Rohit V. Pappu, & Tanja Mittag. (2020). Valence and Patterning of Aromatic Residues Determine the Phase Behavior of Disordered Prion-Like Domains. Bulletin of the American Physical Society. 4 indexed citations
4.
Peran, Ivan, Erik Martin, & Tanja Mittag. (2020). Walking Along a Protein Phase Diagram to Determine Coexistence Points by Static Light Scattering. Methods in molecular biology. 2141. 715–730. 10 indexed citations
5.
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
6.
Zhang, Siwen, Yi Zhang, Junjie Zou, et al.. (2019). Pressure-Temperature Analysis of the Stability of the CTL9 Domain Reveals Hidden Intermediates. Biophysical Journal. 116(3). 445–453. 8 indexed citations
7.
Martin, Erik, Ivan Peran, & Tanja Mittag. (2018). The Collapsed Conformational Landscape of the Hnrnpa1 Low Complexity Region Revealed by SAXS, NMR and Simulation. Biophysical Journal. 114(3). 367a–368a. 1 indexed citations
8.
Sato, Satoshi, et al.. (2017). The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State. Biophysical Journal. 112(9). 1797–1806. 6 indexed citations
9.
Peran, Ivan, et al.. (2017). Selenomethionine Quenching of Tryptophan Fluorescence Provides a Simple Probe of Protein Structure. Biochemistry. 56(8). 1085–1094. 4 indexed citations
10.
Peran, Ivan, et al.. (2016). A Non-perturbing Probe of Coiled Coil Formation Based on Electron Transfer Mediated Fluorescence Quenching. Biochemistry. 55(26). 3685–3691. 11 indexed citations
11.
Zhang, Yi, et al.. (2016). High Pressure ZZ-Exchange NMR Reveals Key Features of Protein Folding Transition States. Journal of the American Chemical Society. 138(46). 15260–15266. 25 indexed citations
12.
Cheng, Xian, et al.. (2016). Positioning the Intracellular Salt Potassium Glutamate in the Hofmeister Series by Chemical Unfolding Studies of NTL9. Biochemistry. 55(15). 2251–2259. 22 indexed citations
13.
Peran, Ivan, et al.. (2015). Selenomethionine, p-cyanophenylalanine pairs provide a convenient, sensitive, non-perturbing fluorescent probe of local helical structure. Chemical Communications. 52(10). 2055–2058. 10 indexed citations
14.
Peran, Ivan, et al.. (2014). General Strategy for the Bioorthogonal Incorporation of Strongly Absorbing, Solvation-Sensitive Infrared Probes into Proteins. The Journal of Physical Chemistry B. 118(28). 7946–7953. 28 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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