Laura S. Itzhaki

6.0k total citations · 1 hit paper
120 papers, 4.8k citations indexed

About

Laura S. Itzhaki is a scholar working on Molecular Biology, Materials Chemistry and Oncology. According to data from OpenAlex, Laura S. Itzhaki has authored 120 papers receiving a total of 4.8k indexed citations (citations by other indexed papers that have themselves been cited), including 112 papers in Molecular Biology, 38 papers in Materials Chemistry and 16 papers in Oncology. Recurrent topics in Laura S. Itzhaki's work include Protein Structure and Dynamics (49 papers), Enzyme Structure and Function (36 papers) and RNA and protein synthesis mechanisms (28 papers). Laura S. Itzhaki is often cited by papers focused on Protein Structure and Dynamics (49 papers), Enzyme Structure and Function (36 papers) and RNA and protein synthesis mechanisms (28 papers). Laura S. Itzhaki collaborates with scholars based in United Kingdom, United States and Singapore. Laura S. Itzhaki's co-authors include Daniel E. Otzen, Alan R. Fersht, Joost Schymkowitz, Alan R. Fersht, Frédéric Rousseau, Albert Perez‐Riba, Alan R. Lowe, Jane Clarke, Hannah Wilkinson and José L. Neira 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

Laura S. Itzhaki

116 papers receiving 4.7k citations

Hit Papers

The Structure of the Transition State for Folding of Chym... 1995 2026 2005 2015 1995 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
Laura S. Itzhaki United Kingdom 37 4.4k 2.0k 599 427 337 120 4.8k
Vincent J. Hilser United States 38 5.0k 1.1× 2.0k 1.0× 477 0.8× 785 1.8× 167 0.5× 97 5.7k
Thomas Kiefhaber Switzerland 43 5.0k 1.1× 2.7k 1.3× 646 1.1× 593 1.4× 168 0.5× 72 5.8k
C. Robert Matthews United States 46 5.1k 1.2× 3.0k 1.5× 613 1.0× 547 1.3× 208 0.6× 148 6.1k
José L. Neira Spain 38 3.5k 0.8× 1.2k 0.6× 354 0.6× 365 0.9× 382 1.1× 195 4.4k
Francisco J. Blanco Spain 42 4.9k 1.1× 1.3k 0.6× 276 0.5× 645 1.5× 413 1.2× 132 5.8k
Pau Bernadó France 44 5.2k 1.2× 2.2k 1.1× 462 0.8× 1.1k 2.6× 271 0.8× 131 6.4k
A.R. Fersht United Kingdom 32 3.6k 0.8× 1.9k 0.9× 410 0.7× 435 1.0× 438 1.3× 50 4.1k
Per Jemth Sweden 43 3.7k 0.8× 1.3k 0.6× 889 1.5× 315 0.7× 218 0.6× 130 4.6k
Robert Fairman United States 38 3.5k 0.8× 976 0.5× 497 0.8× 259 0.6× 292 0.9× 102 4.4k
Martin Billeter Switzerland 8 6.0k 1.4× 1.5k 0.7× 698 1.2× 518 1.2× 445 1.3× 12 7.1k

Countries citing papers authored by Laura S. Itzhaki

Since Specialization
Citations

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

Fields of papers citing papers by Laura S. Itzhaki

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Laura S. Itzhaki. 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 Laura S. Itzhaki. The network helps show where Laura S. Itzhaki may publish in the future.

Co-authorship network of co-authors of Laura S. Itzhaki

This figure shows the co-authorship network connecting the top 25 collaborators of Laura S. Itzhaki. A scholar is included among the top collaborators of Laura S. Itzhaki 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 Laura S. Itzhaki. Laura S. Itzhaki 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.
Šneideris, Tomas, Jan Huertas, Jerelle A. Joseph, et al.. (2025). Tandem-repeat proteins introduce tuneable properties to engineered biomolecular condensates. Chemical Science. 16(23). 10532–10548. 2 indexed citations
2.
Stubbs, Christopher J., Marianne Schimpl, Thomas Tischer, et al.. (2025). Development of D-box peptides to inhibit the anaphase-promoting complex/cyclosome. eLife. 14.
4.
Banerjee, Anupam, Mohsin M. Naqvi, Maria Zacharopoulou, et al.. (2024). Influence of point mutations on PR65 conformational adaptability: Insights from molecular simulations and nanoaperture optical tweezers. Science Advances. 10(22). eadn2208–eadn2208. 5 indexed citations
5.
Itzhaki, Laura S., et al.. (2024). How to target membrane proteins for degradation: Bringing GPCRs into the TPD fold. Journal of Biological Chemistry. 300(12). 107926–107926. 2 indexed citations
6.
Kaur, Veerpal, Demelza Wright, Matthew Peters, et al.. (2024). Portable fiber-based double nanohole optical tweezer for trapping small proteins. Journal of Physics Photonics. 6(3). 35023–35023. 3 indexed citations
7.
Kaynak, Burak, Pemra Doruker, Anupam Banerjee, et al.. (2023). Cooperative mechanics of PR65 scaffold underlies the allosteric regulation of the phosphatase PP2A. Structure. 31(5). 607–618.e3. 8 indexed citations
8.
Ashman, Nicola, et al.. (2023). Red-light modulated ortho -chloro azobenzene photoswitch for peptide stapling via aromatic substitution. RSC Chemical Biology. 5(1). 49–54. 11 indexed citations
9.
Babii, Oleg, Sergii Afonin, Wenshu Xu, et al.. (2020). Diarylethene moiety as an enthalpy-entropy switch: photoisomerizable stapled peptides for modulating p53/MDM2 interaction. Organic & Biomolecular Chemistry. 18(28). 5359–5369. 16 indexed citations
10.
Sharma, Krishna, Elaine Fowler, Wenshu Xu, et al.. (2020). Functionalized Double Strain-Promoted Stapled Peptides for Inhibiting the p53-MDM2 Interaction. ACS Omega. 5(2). 1157–1169. 14 indexed citations
11.
Tan, Yaw Sing, Jessica Iegre, Stephen J. Walsh, et al.. (2019). Targeted covalent inhibitors of MDM2 using electrophile-bearing stapled peptides. Chemical Communications. 55(55). 7914–7917. 26 indexed citations
12.
Wu, Yuteng, Amandeep Kaur, Elaine Fowler, et al.. (2019). Toolbox of Diverse Linkers for Navigating the Cellular Efficacy Landscape of Stapled Peptides. ACS Chemical Biology. 14(3). 526–533. 22 indexed citations
13.
Sharma, Krishna, Elaine Fowler, Xuelu Wang, et al.. (2019). Water-soluble, stable and azide-reactive strained dialkynes for biocompatible double strain-promoted click chemistry. Organic & Biomolecular Chemistry. 17(34). 8014–8018. 16 indexed citations
14.
Garnett, James A., et al.. (2019). Scalable Geometrically Designed Protein Cages Assembled via Genetically Encoded Split Inteins. Structure. 27(5). 776–784.e4. 10 indexed citations
15.
Wiedmann, Mareike M., Yaw Sing Tan, Yuteng Wu, et al.. (2016). Development of Cell‐Permeable, Non‐Helical Constrained Peptides to Target a Key Protein–Protein Interaction in Ovarian Cancer. Angewandte Chemie. 129(2). 539–544. 6 indexed citations
16.
Wiedmann, Mareike M., Yaw Sing Tan, Yuteng Wu, et al.. (2016). Development of Cell‐Permeable, Non‐Helical Constrained Peptides to Target a Key Protein–Protein Interaction in Ovarian Cancer. Angewandte Chemie International Edition. 56(2). 524–529. 36 indexed citations
17.
Ibrahim, Shehu, Pamela J. E. Rowling, Wenshu Xu, et al.. (2015). Single-Molecule FRET Reveals Hidden Complexity in a Protein Energy Landscape. Structure. 23(1). 190–198. 4 indexed citations
18.
Chin, Wee Loong, et al.. (2010). Characterising the Binding Specificities of the Subunits Associated with the KMT2/Set1 Histone Lysine Methyltransferase. Journal of Molecular Biology. 398(4). 481–488. 12 indexed citations
19.
Seeliger, Markus A., et al.. (2002). Weak Cooperativity in the Core Causes a Switch in Folding Mechanism Between Two Proteins of the cks Family. Journal of Molecular Biology. 325(1). 189–199. 20 indexed citations
20.
Clarke, Jane & Laura S. Itzhaki. (1998). Hydrogen exchange and protein folding. Current Opinion in Structural Biology. 8(1). 112–118. 101 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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