Sarah Alamdari

917 total citations · 1 hit paper
20 papers, 547 citations indexed

About

Sarah Alamdari is a scholar working on Molecular Biology, Biomaterials and Biomedical Engineering. According to data from OpenAlex, Sarah Alamdari has authored 20 papers receiving a total of 547 indexed citations (citations by other indexed papers that have themselves been cited), including 12 papers in Molecular Biology, 6 papers in Biomaterials and 4 papers in Biomedical Engineering. Recurrent topics in Sarah Alamdari's work include Chemical Synthesis and Analysis (5 papers), Protein Structure and Dynamics (5 papers) and Supramolecular Self-Assembly in Materials (4 papers). Sarah Alamdari is often cited by papers focused on Chemical Synthesis and Analysis (5 papers), Protein Structure and Dynamics (5 papers) and Supramolecular Self-Assembly in Materials (4 papers). Sarah Alamdari collaborates with scholars based in United States, Denmark and United Kingdom. Sarah Alamdari's co-authors include Jim Pfaendtner, Sijie Yang, Sefaattin Tongay, Steven J. Roeters, Tobias Weidner, T. Amand, Gang Wang, Iann C. Gerber, Aslıhan Süslü and Bin Chen and has published in prestigious journals such as Journal of the American Chemical Society, Nature Communications and Bioinformatics.

In The Last Decade

Sarah Alamdari

20 papers receiving 543 citations

Hit Papers

Protein structure generation via folding diffusion 2024 2026 2025 2024 25 50 75

Peers

Sarah Alamdari
Martin Girard United States
Orion Shih Taiwan
Vyas Ramasubramani United States
Niall M. Mangan United States
Neha Awasthi Germany
J. Wayne Mullinax United States
Handan Arkın Türkiye
Nikolaos V. Mantzaris United States
Martin Girard United States
Sarah Alamdari
Citations per year, relative to Sarah Alamdari Sarah Alamdari (= 1×) peers Martin Girard

Countries citing papers authored by Sarah Alamdari

Since Specialization
Citations

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

Fields of papers citing papers by Sarah Alamdari

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Sarah Alamdari

This figure shows the co-authorship network connecting the top 25 collaborators of Sarah Alamdari. A scholar is included among the top collaborators of Sarah Alamdari 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 Sarah Alamdari. Sarah Alamdari 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.
Alamdari, Sarah, et al.. (2025). ProtNote: a multimodal method for protein–function annotation. Bioinformatics. 41(5). 1 indexed citations
2.
Alamdari, Sarah, et al.. (2025). Toward deep learning sequence–structure co-generation for protein design. Current Opinion in Structural Biology. 91. 103018–103018. 3 indexed citations
3.
Wu, Kevin, Kevin Yang, Rianne van den Berg, et al.. (2024). Protein structure generation via folding diffusion. Nature Communications. 15(1). 1059–1059. 76 indexed citations breakdown →
4.
Zhang, Shuai, Sarah Alamdari, Christopher J. Mundy, et al.. (2023). Computational and Experimental Determination of the Properties, Structure, and Stability of Peptoid Nanosheets and Nanotubes. Biomacromolecules. 24(6). 2618–2632. 7 indexed citations
5.
Alamdari, Sarah, et al.. (2023). Thermodynamic Basis for the Stabilization of Helical Peptoids by Chiral Sidechains. The Journal of Physical Chemistry B. 127(27). 6171–6183. 6 indexed citations
6.
Alamdari, Sarah & Jim Pfaendtner. (2023). Origins of Conformational Heterogeneity in Peptoid Helices Formed by Chiral N-1-Phenylethyl Sidechains. The Journal of Physical Chemistry B. 127(27). 6163–6170. 7 indexed citations
7.
Zhang, Shuai, Sarah Alamdari, Janani Sampath, et al.. (2022). Hierarchical Self-Assembly Pathways of Peptoid Helices and Sheets. Biomacromolecules. 23(3). 992–1008. 30 indexed citations
8.
Lutz, Helmut, Sarah Alamdari, Steven J. Roeters, et al.. (2022). Peptide Mimic of the Marine Sponge Protein Silicatein Fabricates Ultrathin Nanosheets of Silicon Dioxide and Titanium Dioxide. Langmuir. 38(26). 8087–8093. 4 indexed citations
9.
Roeters, Steven J., Thaddeus W. Golbek, Mikkel Bregnhøj, et al.. (2021). Ice-nucleating proteins are activated by low temperatures to control the structure of interfacial water. Nature Communications. 12(1). 1183–1183. 75 indexed citations
10.
11.
Alamdari, Sarah, et al.. (2021). Substitution of distal and active site residues reduces product inhibition of E1 from Acidothermus Cellulolyticus. Protein Engineering Design and Selection. 34. 2 indexed citations
12.
Alamdari, Sarah, et al.. (2020). DiffCapAnalyzer: A Python Package for Quantitative Analysis of Total Differential Capacity Data. The Journal of Open Source Software. 5(54). 2624–2624. 10 indexed citations
13.
Zhao, Mingfei, Janani Sampath, Sarah Alamdari, et al.. (2020). MARTINI-Compatible Coarse-Grained Model for the Mesoscale Simulation of Peptoids. The Journal of Physical Chemistry B. 124(36). 7745–7764. 36 indexed citations
14.
Alamdari, Sarah, Steven J. Roeters, Thaddeus W. Golbek, et al.. (2020). Orientation and Conformation of Proteins at the Air–Water Interface Determined from Integrative Molecular Dynamics Simulations and Sum Frequency Generation Spectroscopy. Langmuir. 36(40). 11855–11865. 38 indexed citations
15.
Alamdari, Sarah, et al.. (2020). Enhanced Activity and Stability of Acidothermus cellulolyticus Endoglucanase 1 in Ionic Liquids via Engineering Active Site Residues and Non-Native Disulfide Bridges. ACS Sustainable Chemistry & Engineering. 8(30). 11299–11307. 13 indexed citations
16.
Sampath, Janani, Sarah Alamdari, & Jim Pfaendtner. (2020). Closing the Gap Between Modeling and Experiments in the Self-Assembly of Biomolecules at Interfaces and in Solution. Chemistry of Materials. 32(19). 8043–8059. 13 indexed citations
17.
Alamdari, Sarah, Harley Pyles, Shuai Zhang, et al.. (2020). Sequence–Structure–Binding Relationships Reveal Adhesion Behavior of the Car9 Solid-Binding Peptide: An Integrated Experimental and Simulation Study. Journal of the American Chemical Society. 142(5). 2355–2363. 28 indexed citations
18.
Alamdari, Sarah & Jim Pfaendtner. (2019). Impact of glutamate carboxylation in the adsorption of the α-1 domain of osteocalcin to hydroxyapatite and titania. Molecular Systems Design & Engineering. 5(3). 620–631. 10 indexed citations
19.
Verreault, Dominique, Sarah Alamdari, Steven J. Roeters, et al.. (2018). Ice-binding site of surface-bound type III antifreeze protein partially decoupled from water. Physical Chemistry Chemical Physics. 20(42). 26926–26933. 17 indexed citations
20.
Wang, Gang, C. Robert, Aslıhan Süslü, et al.. (2015). Spin-orbit engineering in transition metal dichalcogenide alloy monolayers. Nature Communications. 6(1). 10110–10110. 167 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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