Emanuele Paci

16.3k total citations
129 papers, 5.3k citations indexed

About

Emanuele Paci is a scholar working on Molecular Biology, Atomic and Molecular Physics, and Optics and Materials Chemistry. According to data from OpenAlex, Emanuele Paci has authored 129 papers receiving a total of 5.3k indexed citations (citations by other indexed papers that have themselves been cited), including 104 papers in Molecular Biology, 55 papers in Atomic and Molecular Physics, and Optics and 43 papers in Materials Chemistry. Recurrent topics in Emanuele Paci's work include Protein Structure and Dynamics (77 papers), Enzyme Structure and Function (41 papers) and Force Microscopy Techniques and Applications (37 papers). Emanuele Paci is often cited by papers focused on Protein Structure and Dynamics (77 papers), Enzyme Structure and Function (41 papers) and Force Microscopy Techniques and Applications (37 papers). Emanuele Paci collaborates with scholars based in United Kingdom, United States and Switzerland. Emanuele Paci's co-authors include Martin Karplus, Michele Vendruscolo, Christopher M. Dobson, Martin Karplus, Sheena E. Radford, David J. Brockwell, Jane Clarke, Peter D. Olmsted, Massimo Marchi and Robert B. Best and has published in prestigious journals such as Nature, Chemical Reviews and Proceedings of the National Academy of Sciences.

In The Last Decade

Emanuele Paci

128 papers receiving 5.3k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Emanuele Paci United Kingdom 40 4.0k 2.0k 1.7k 669 432 129 5.3k
Shoji Takada Japan 41 5.3k 1.3× 1.1k 0.6× 2.3k 1.3× 432 0.6× 711 1.6× 141 6.3k
Daniel Nettels Switzerland 41 5.0k 1.2× 1.1k 0.6× 2.0k 1.2× 532 0.8× 607 1.4× 96 6.3k
Susan Marqusee United States 46 7.0k 1.7× 1.3k 0.7× 2.6k 1.5× 636 1.0× 1.0k 2.4× 128 8.3k
Changbong Hyeon South Korea 44 3.8k 0.9× 907 0.5× 880 0.5× 746 1.1× 168 0.4× 117 5.0k
Akio Kitao Japan 32 3.4k 0.8× 962 0.5× 1.2k 0.7× 402 0.6× 722 1.7× 135 4.3k
Víctor Muñoz United States 50 7.8k 1.9× 1.2k 0.6× 4.2k 2.5× 759 1.1× 1.1k 2.6× 111 8.6k
Adrian H. Elcock United States 38 4.4k 1.1× 695 0.4× 1.6k 0.9× 389 0.6× 391 0.9× 88 5.4k
Gunnar F. Schröder Germany 41 5.0k 1.3× 483 0.2× 1.2k 0.7× 731 1.1× 538 1.2× 87 7.4k
Florence Tama Japan 34 3.5k 0.9× 701 0.4× 1.6k 1.0× 277 0.4× 347 0.8× 92 4.8k

Countries citing papers authored by Emanuele Paci

Since Specialization
Citations

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

Fields of papers citing papers by Emanuele Paci

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Emanuele Paci

This figure shows the co-authorship network connecting the top 25 collaborators of Emanuele Paci. A scholar is included among the top collaborators of Emanuele Paci 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 Emanuele Paci. Emanuele Paci 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.
Paci, Emanuele, et al.. (2025). Recalibrating Protection Factors Using Millisecond Hydrogen/Deuterium Exchange Mass Spectrometry. Analytical Chemistry. 97(5). 2648–2657. 3 indexed citations
2.
Kaminska, Renata, et al.. (2024). Structural constraints of pyocin S2 import through the ferripyoverdine receptor FpvAI. PNAS Nexus. 3(4). pgae124–pgae124.
3.
Manfield, Iain W., et al.. (2024). The Mutagenic Plasticity of the Cholera Toxin B-Subunit Surface Residues: Stability and Affinity. Toxins. 16(3). 133–133. 2 indexed citations
4.
Whelan, Fiona, Aleix Lafita, Samuel C. Griffiths, et al.. (2021). Periscope Proteins are variable-length regulators of bacterial cell surface interactions. Proceedings of the National Academy of Sciences. 118(23). 14 indexed citations
5.
Ross, James F., Daniel L. Hurdiss, Rebecca F. Thompson, et al.. (2019). Directed Assembly of Homopentameric Cholera Toxin B-Subunit Proteins into Higher-Order Structures Using Coiled-Coil Appendages. Journal of the American Chemical Society. 141(13). 5211–5219. 17 indexed citations
6.
Hao, Yuxin, Luca Bellucci, Emanuele Paci, et al.. (2019). Activation of PKA via asymmetric allosteric coupling of structurally conserved cyclic nucleotide binding domains. Nature Communications. 10(1). 3984–3984. 20 indexed citations
7.
Gruszka, Dominika T., Fiona Whelan, Herman K.H. Fung, et al.. (2015). Cooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein. Nature Communications. 6(1). 7271–7271. 44 indexed citations
8.
Tůma, Roman, et al.. (2014). Functional Dynamics of Hexameric Helicase Probed by Hydrogen Exchange and Simulation. Biophysical Journal. 107(4). 983–990. 13 indexed citations
9.
Batchelor, Matthew, et al.. (2014). Effect of external pulling forces on the length distribution of peptides. Biochimica et Biophysica Acta (BBA) - General Subjects. 1850(5). 903–910. 2 indexed citations
10.
Monteiro, Diana C. F., et al.. (2013). Growth Kinetics of Bacterial Pili from Pairwise Pilin Association Rates. PLoS ONE. 8(5). e63065–e63065. 2 indexed citations
11.
Heidarsson, Pétur O., Luca Bellucci, Alessandro Mossa, et al.. (2013). Single-Molecule Folding Mechanism of an EF-Hand Neuronal Calcium Sensor. Structure. 21(10). 1812–1821. 26 indexed citations
12.
Krivov, Sergei V., et al.. (2009). Analysis of the Free-Energy Surface of Proteins from Reversible Folding Simulations. PLoS Computational Biology. 5(7). e1000428–e1000428. 24 indexed citations
13.
Forman, Julia, et al.. (2009). Non-Native Interactions Are Critical for Mechanical Strength in PKD Domains. Structure. 17(12). 1582–1590. 24 indexed citations
14.
Périole, Xavier, et al.. (2008). Probing the free energy landscape of the FBP28WW domain using multiple techniques. Journal of Computational Chemistry. 30(7). 1059–1068. 6 indexed citations
15.
Olmsted, Peter D., et al.. (2006). Free energy for protein folding from nonequilibrium simulations using the Jarzynski equality. The Journal of Chemical Physics. 125(20). 204910–204910. 38 indexed citations
16.
Best, Robert B., et al.. (2006). Structural Comparison of the Two Alternative Transition States for Folding of TI I27. Biophysical Journal. 91(1). 263–275. 17 indexed citations
17.
Forman, Julia, Seema Qamar, Emanuele Paci, Richard Sandford, & Jane Clarke. (2005). The Remarkable Mechanical Strength of Polycystin-1 Supports a Direct Role in Mechanotransduction. Journal of Molecular Biology. 349(4). 861–871. 81 indexed citations
18.
Paci, Emanuele, et al.. (2005). Characterization of the molten globule state of retinol‐binding protein using a molecular dynamics simulation approach. FEBS Journal. 272(18). 4826–4838. 11 indexed citations
19.
Paci, Emanuele, Kresten Lindorff‐Larsen, Christopher M. Dobson, Martin Karplus, & Michele Vendruscolo. (2005). Transition State Contact Orders Correlate with Protein Folding Rates. Journal of Molecular Biology. 352(3). 495–500. 62 indexed citations
20.
Cavalli, Andrea, Michele Vendruscolo, & Emanuele Paci. (2005). Comparison of Sequence-Based and Structure-Based Energy Functions for the Reversible Folding of a Peptide. Biophysical Journal. 88(5). 3158–3166. 21 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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