Robert V. Stahelin

9.1k total citations · 2 hit papers
155 papers, 7.3k citations indexed

About

Robert V. Stahelin is a scholar working on Molecular Biology, Infectious Diseases and Cell Biology. According to data from OpenAlex, Robert V. Stahelin has authored 155 papers receiving a total of 7.3k indexed citations (citations by other indexed papers that have themselves been cited), including 91 papers in Molecular Biology, 50 papers in Infectious Diseases and 43 papers in Cell Biology. Recurrent topics in Robert V. Stahelin's work include Viral Infections and Outbreaks Research (45 papers), Lipid Membrane Structure and Behavior (38 papers) and Cellular transport and secretion (37 papers). Robert V. Stahelin is often cited by papers focused on Viral Infections and Outbreaks Research (45 papers), Lipid Membrane Structure and Behavior (38 papers) and Cellular transport and secretion (37 papers). Robert V. Stahelin collaborates with scholars based in United States, United Kingdom and South Korea. Robert V. Stahelin's co-authors include Wonhwa Cho, Wonhwa Cho, Diana Murray, Wan‐Seob Cho, Michelle A. Digman, Charles E. Chalfant, Emmanuel Adu‐Gyamfi, Jordan L. Scott, Lenka Bittova and Bharath Ananthanarayanan and has published in prestigious journals such as Nature, Cell and Journal of Biological Chemistry.

In The Last Decade

Robert V. Stahelin

148 papers receiving 7.2k citations

Hit Papers

Membrane-Protein Interactions in Cell Signaling and Membr... 2005 2026 2012 2019 2005 2015 100 200 300 400 500

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Robert V. Stahelin United States 50 4.9k 2.0k 913 850 751 155 7.3k
Matthias Geyer Germany 60 7.1k 1.4× 1.5k 0.7× 918 1.0× 631 0.7× 1.8k 2.4× 201 10.8k
Ronald Frank Germany 46 6.6k 1.3× 1.1k 0.6× 489 0.5× 1.0k 1.2× 962 1.3× 170 9.8k
Marilyn D. Resh United States 62 9.0k 1.8× 2.9k 1.5× 711 0.8× 749 0.9× 1.6k 2.1× 122 12.7k
Chad A. Brautigam United States 47 5.1k 1.0× 1.5k 0.8× 493 0.5× 413 0.5× 950 1.3× 137 7.7k
Kentaro Hanada Japan 55 6.8k 1.4× 2.9k 1.5× 501 0.5× 1.1k 1.3× 702 0.9× 228 9.9k
Laura W. Murray United States 6 8.4k 1.7× 934 0.5× 971 1.1× 775 0.9× 879 1.2× 10 11.7k
Carolyn E. Machamer United States 48 3.2k 0.6× 1.7k 0.9× 1.5k 1.7× 949 1.1× 847 1.1× 91 6.2k
Michael G. Roth United States 52 7.5k 1.5× 3.9k 2.0× 456 0.5× 1.5k 1.8× 958 1.3× 114 10.6k
Evžen Bouřa Czechia 37 2.4k 0.5× 886 0.4× 897 1.0× 431 0.5× 530 0.7× 113 4.0k
Stephen J. Smerdon United Kingdom 50 9.1k 1.8× 3.1k 1.6× 788 0.9× 394 0.5× 885 1.2× 99 11.3k

Countries citing papers authored by Robert V. Stahelin

Since Specialization
Citations

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

Fields of papers citing papers by Robert V. Stahelin

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Robert V. Stahelin. 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 Robert V. Stahelin. The network helps show where Robert V. Stahelin may publish in the future.

Co-authorship network of co-authors of Robert V. Stahelin

This figure shows the co-authorship network connecting the top 25 collaborators of Robert V. Stahelin. A scholar is included among the top collaborators of Robert V. Stahelin 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 Robert V. Stahelin. Robert V. Stahelin 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.
Stahelin, Robert V., et al.. (2025). Heat-induced phosphatidylserine changes drive HSPA1A's plasma membrane localization. Cell Stress and Chaperones. 30(5). 100092–100092.
2.
Liu, Xiao, et al.. (2024). Evaluation of fendiline treatment in VP40 system with nucleation-elongation process: a computational model of Ebola virus matrix protein assembly. Microbiology Spectrum. 12(4). e0309823–e0309823. 1 indexed citations
3.
Bhattarai, Nisha, et al.. (2024). Ebola Virus Matrix Protein VP40 Single Mutations G198R and G201R Significantly Enhance Plasma Membrane Localization. The Journal of Physical Chemistry B. 128(46). 11335–11344. 2 indexed citations
4.
Mukherjee, Angana, Souad Amiar, Dominic Gagnon, et al.. (2022). A Phosphoinositide-Binding Protein Acts in the Trafficking Pathway of Hemoglobin in the Malaria Parasite Plasmodium falciparum. mBio. 13(1). e0323921–e0323921. 9 indexed citations
5.
Norris, Michael, William B. Kiosses, Jieyun Yin, et al.. (2022). Measles and Nipah virus assembly: Specific lipid binding drives matrix polymerization. Science Advances. 8(29). eabn1440–eabn1440. 22 indexed citations
7.
Bhattarai, Nisha, Elumalai Pavadai, Rudramani Pokhrel, et al.. (2021). Ebola virus protein VP40 binding to Sec24c for transport to the plasma membrane. Proteins Structure Function and Bioinformatics. 90(2). 340–350. 4 indexed citations
8.
Wijesinghe, Kaveesha J., Nisha Bhattarai, Jia Ma, et al.. (2020). Mutation of Hydrophobic Residues in the C-Terminal Domain of the Marburg Virus Matrix Protein VP40 Disrupts Trafficking to the Plasma Membrane. Viruses. 12(4). 482–482. 6 indexed citations
9.
Olson, Kenneth R., Yan Gao, Andrea K. Steiger, et al.. (2020). Effects of Manganese Porphyrins on Cellular Sulfur Metabolism. Molecules. 25(4). 980–980. 9 indexed citations
10.
Pavadai, Elumalai, Nisha Bhattarai, Prabin Baral, et al.. (2019). Conformational Flexibility of the Protein–Protein Interfaces of the Ebola Virus VP40 Structural Matrix Filament. The Journal of Physical Chemistry B. 123(43). 9045–9053. 8 indexed citations
11.
Jeevan, B., Shun-ichiro Oda, Bernard S. Gerstman, et al.. (2018). A cationic, C-terminal patch and structural rearrangements in Ebola virus matrix VP40 protein control its interactions with phosphatidylserine. Journal of Biological Chemistry. 293(9). 3335–3349. 32 indexed citations
12.
Bhattacharjee, Souvik, Isabelle Coppens, Alassane Mbengue, et al.. (2018). Remodeling of the malaria parasite and host human red cell by vesicle amplification that induces artemisinin resistance. Blood. 131(11). 1234–1247. 74 indexed citations
13.
Bhattarai, Nisha, B. Jeevan, Bernard S. Gerstman, Robert V. Stahelin, & Prem P. Chapagain. (2017). Plasma membrane association facilitates conformational changes in the Marburg virus protein VP40 dimer. RSC Advances. 7(37). 22741–22748. 14 indexed citations
14.
Adu‐Gyamfi, Emmanuel, et al.. (2014). A Loop Region in the N-Terminal Domain of Ebola Virus VP40 Is Important in Viral Assembly, Budding, and Egress. eScholarship (California Digital Library).
15.
Adu‐Gyamfi, Emmanuel, Smita P. Soni, Yi Xue, et al.. (2013). The Ebola Virus Matrix Protein Penetrates into the Plasma Membrane. Journal of Biological Chemistry. 288(8). 5779–5789. 73 indexed citations
16.
Silkov, Antonina, Youngdae Yoon, Emmanuel Adu‐Gyamfi, et al.. (2011). Genome-wide Structural Analysis Reveals Novel Membrane Binding Properties of AP180 N-terminal Homology (ANTH) Domains. Journal of Biological Chemistry. 286(39). 34155–34163. 20 indexed citations
17.
Smith, Matthew D., et al.. (2009). Modular synthesis of biologically active phosphatidic acid probes using click chemistry. Molecular BioSystems. 5(9). 962–972. 22 indexed citations
18.
Lamour, Nadia F., Preeti Subramanian, Dayanjan S. Wijesinghe, et al.. (2009). Ceramide 1-Phosphate Is Required for the Translocation of Group IVA Cytosolic Phospholipase A2 and Prostaglandin Synthesis. Journal of Biological Chemistry. 284(39). 26897–26907. 85 indexed citations
19.
He, Ju, et al.. (2008). Molecular mechanism of membrane targeting by the GRP1 PH domain*. Journal of Lipid Research. 49(8). 1807–1815. 49 indexed citations
20.
Lamour, Nadia F., Robert V. Stahelin, Dayanjan S. Wijesinghe, et al.. (2007). Ceramide kinase uses ceramide provided by ceramide transport protein: localization to organelles of eicosanoid synthesis. Journal of Lipid Research. 48(6). 1293–1304. 95 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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