Winfríed Weissenhorn

11.0k total citations · 1 hit paper
114 papers, 8.2k citations indexed

About

Winfríed Weissenhorn is a scholar working on Molecular Biology, Virology and Infectious Diseases. According to data from OpenAlex, Winfríed Weissenhorn has authored 114 papers receiving a total of 8.2k indexed citations (citations by other indexed papers that have themselves been cited), including 54 papers in Molecular Biology, 35 papers in Virology and 34 papers in Infectious Diseases. Recurrent topics in Winfríed Weissenhorn's work include Cellular transport and secretion (33 papers), HIV Research and Treatment (30 papers) and Lipid Membrane Structure and Behavior (25 papers). Winfríed Weissenhorn is often cited by papers focused on Cellular transport and secretion (33 papers), HIV Research and Treatment (30 papers) and Lipid Membrane Structure and Behavior (25 papers). Winfríed Weissenhorn collaborates with scholars based in France, United States and Germany. Winfríed Weissenhorn's co-authors include Don C. Wiley, J.J. Skehel, Andréa Dessen, Stephen C. Harrison, Guy Schoehn, Andreas Bracher, Heinrich G. Göttlinger, Rob W.H. Ruigrok, Lesley J. Calder and Joanna Timmins and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

Winfríed Weissenhorn

114 papers receiving 8.1k citations

Hit Papers

Atomic structure of the ectodomain from HIV-1 gp41 1997 2026 2006 2016 1997 400 800 1.2k

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Winfríed Weissenhorn France 47 3.4k 3.0k 2.6k 2.2k 1.9k 114 8.2k
Walther Mothes United States 44 3.6k 1.0× 1.6k 0.5× 2.8k 1.1× 1.9k 0.9× 1.3k 0.7× 102 8.8k
Heinrich G. Göttlinger United States 56 4.5k 1.3× 3.6k 1.2× 6.9k 2.6× 2.5k 1.1× 1.7k 0.9× 95 10.5k
John K. Rose United States 57 5.2k 1.5× 2.7k 0.9× 1.6k 0.6× 4.1k 1.9× 1.9k 1.0× 137 12.1k
Owen Pornillos United States 32 2.8k 0.8× 1.7k 0.6× 2.9k 1.1× 1.0k 0.5× 841 0.4× 52 5.7k
Mark Marsh United Kingdom 68 5.8k 1.7× 2.7k 0.9× 4.3k 1.6× 2.7k 1.3× 2.6k 1.4× 151 14.6k
Thomas J. Hope United States 59 5.9k 1.7× 3.2k 1.1× 5.6k 2.2× 2.5k 1.1× 779 0.4× 206 13.2k
Stephen D. Fuller Germany 41 2.9k 0.8× 2.1k 0.7× 1.5k 0.6× 1.1k 0.5× 799 0.4× 62 6.8k
Thomas R. Fuerst United States 33 2.5k 0.7× 2.5k 0.8× 1.8k 0.7× 2.9k 1.3× 259 0.1× 74 8.0k
Henrik Garoff Sweden 54 3.2k 0.9× 3.7k 1.2× 1.6k 0.6× 2.3k 1.0× 568 0.3× 130 9.2k
Akira Ono United States 34 2.6k 0.8× 1.5k 0.5× 3.4k 1.3× 1.1k 0.5× 469 0.2× 124 5.5k

Countries citing papers authored by Winfríed Weissenhorn

Since Specialization
Citations

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

Fields of papers citing papers by Winfríed Weissenhorn

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Winfríed Weissenhorn

This figure shows the co-authorship network connecting the top 25 collaborators of Winfríed Weissenhorn. A scholar is included among the top collaborators of Winfríed Weissenhorn 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 Winfríed Weissenhorn. Winfríed Weissenhorn 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.
Bally, Isabelle, Marlyse Buisson, Raphaële Germi, et al.. (2024). Anti-SARS-CoV-2 serology based on ancestral RBD antigens does not correlate with the presence of neutralizing antibodies against Omicron variants. Microbiology Spectrum. 13(1). e0156824–e0156824. 2 indexed citations
2.
Sulbarán, Guidenn, et al.. (2023). SARS-CoV-2 S Glycoprotein Stabilization Strategies. Viruses. 15(2). 558–558. 4 indexed citations
3.
Guilligay, Delphine, Cécile Boscheron, Sourav Maity, et al.. (2023). Structural basis of CHMP2A–CHMP3 ESCRT-III polymer assembly and membrane cleavage. Nature Structural & Molecular Biology. 30(1). 81–90. 39 indexed citations
4.
Franceschi, Nicola De, et al.. (2022). The archaeal division protein CdvB1 assembles into polymers that are depolymerized by CdvC. FEBS Letters. 596(7). 958–969. 8 indexed citations
5.
Caillat, Christophe, Delphine Guilligay, Nikolas Friedrich, et al.. (2021). Structure of HIV-1 gp41 with its membrane anchors targeted by neutralizing antibodies. eLife. 10. 22 indexed citations
6.
Carnell, George, Kathrin Held, Guidenn Sulbarán, et al.. (2021). Stepwise Conformational Stabilization of a HIV-1 Clade C Consensus Envelope Trimer Immunogen Impacts the Profile of Vaccine-Induced Antibody Responses. Vaccines. 9(7). 750–750. 9 indexed citations
7.
Bertin, Aurélie, Nicola De Franceschi, E. De la Mora, et al.. (2020). Human ESCRT-III polymers assemble on positively curved membranes and induce helical membrane tube formation. Nature Communications. 11(1). 2663–2663. 77 indexed citations
8.
Franceschi, Nicola De, Nolwenn Miguet, Christophe Caillat, et al.. (2018). The ESCRT protein CHMP2B acts as a diffusion barrier on reconstituted membrane necks. Journal of Cell Science. 132(4). 30 indexed citations
9.
Gray, Eleanor R., Jennifer C. Brookes, Christophe Caillat, et al.. (2017). Unravelling the Molecular Basis of High Affinity Nanobodies against HIV p24: In Vitro Functional, Structural, and in Silico Insights. ACS Infectious Diseases. 3(7). 479–491. 36 indexed citations
10.
Bego, Mariana G., et al.. (2015). Vpu Exploits the Cross-Talk between BST2 and the ILT7 Receptor to Suppress Anti-HIV-1 Responses by Plasmacytoid Dendritic Cells. PLoS Pathogens. 11(7). e1005024–e1005024. 39 indexed citations
11.
Sabin, Charles, Davide Corti, Víctor Buzón, et al.. (2010). Crystal Structure and Size-Dependent Neutralization Properties of HK20, a Human Monoclonal Antibody Binding to the Highly Conserved Heptad Repeat 1 of gp41. PLoS Pathogens. 6(11). e1001195–e1001195. 67 indexed citations
12.
Hinz, Andreas, Nolwenn Miguet, G. Natrajan, et al.. (2010). Structural Basis of HIV-1 Tethering to Membranes by the BST-2/Tetherin Ectodomain. Cell Host & Microbe. 7(4). 314–323. 128 indexed citations
13.
Hock, M. Benjamin, Guy Schoehn, Marc Jamin, et al.. (2009). RNA induced polymerization of the Borna disease virus nucleoprotein. Virology. 397(1). 64–72. 17 indexed citations
14.
Lata, Suman, Guy Schoehn, Ankur Jain, et al.. (2008). Helical Structures of ESCRT-III Are Disassembled by VPS4. Science. 321(5894). 1354–1357. 277 indexed citations
15.
Albertini, Aurélie, Amy K. Wernimont, Tadeusz M. Muzioł, et al.. (2006). Crystal Structure of the Rabies Virus Nucleoprotein-RNA Complex. Science. 313(5785). 360–363. 259 indexed citations
16.
Saiyed, Taslimarif, Ingo Paarmann, Bertram Schmitt, et al.. (2006). Molecular Basis of Gephyrin Clustering at Inhibitory Synapses. Journal of Biological Chemistry. 282(8). 5625–5632. 65 indexed citations
17.
Schibli, David & Winfríed Weissenhorn. (2004). Class I and class II viral fusion protein structures reveal similar principles in membrane fusion (Review). Molecular Membrane Biology. 21(6). 361–371. 80 indexed citations
18.
Bavro, Vassiliy N., Marı́a Solà, Andreas Bracher, et al.. (2002). Crystal structure of the GABA A ‐receptor‐associated protein, GABARAP. EMBO Reports. 3(2). 183–189. 60 indexed citations
19.
Weissenhorn, Winfríed, Andréa Dessen, Lesley J. Calder, et al.. (1999). Structural basis for membrane fusion by enveloped viruses. Molecular Membrane Biology. 16(1). 3–9. 320 indexed citations
20.
Weissenhorn, Winfríed, et al.. (1996). Structural Diversity of Monoclonal CD4 Antibodies and Their Capacity to Block the HIV GP120/CD4 Interaction. Hybridoma. 15(2). 117–124. 2 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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