Andrea Pfeifer
About
Andrea Pfeifer is a scholar working on Physiology, Molecular Biology and Pharmacology.
According to data from OpenAlex, Andrea Pfeifer has authored 51 papers receiving a total of 1.4k indexed citations (citations by other indexed papers that have themselves been cited), including 32 papers in Physiology, 15 papers in Molecular Biology and 13 papers in Pharmacology. Recurrent topics in Andrea Pfeifer's work include Alzheimer's disease research and treatments (32 papers), Cholinesterase and Neurodegenerative Diseases (13 papers) and Computational Drug Discovery Methods (11 papers). Andrea Pfeifer is often cited by papers focused on Alzheimer's disease research and treatments (32 papers), Cholinesterase and Neurodegenerative Diseases (13 papers) and Computational Drug Discovery Methods (11 papers). Andrea Pfeifer collaborates with scholars based in Switzerland, Germany and United States. Andrea Pfeifer's co-authors include Andreas Muhs, Wolfgang Froestl, David T. Hickman, Oskar Adolfsson, Maria Pihlgren, Heiko Kroth, María Pilar López-Deber, Nathalie Chuard, Fred Van Leuven and Asad Jan and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Angewandte Chemie International Edition.
In The Last Decade
Andrea Pfeifer
50 papers receiving 1.4k citations
Peers
Andrea Pfeifer
Andreas Muhs Switzerland
Megan E. McLellan United States
Lee‐Way Jin United States
Sethu Sankaranarayanan United States
Lucía Chávez‐Gutiérrez Belgium
Stephen T. Kajdasz United States
Thomas M. Wengenack United States
Kenneth W. Adams United States
Susanne Aileen Funke Germany
Erene Mina United States
Citations per year, relative to Andrea Pfeifer Andrea Pfeifer (= 1×)
peers
Andreas Muhs
Countries citing papers authored by Andrea Pfeifer
Since
Specialization
Citations
This map shows the geographic impact of Andrea Pfeifer'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 Andrea Pfeifer with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Andrea Pfeifer more than expected).
Fields of papers citing papers by Andrea Pfeifer
Since
Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences
This network shows the impact of papers produced by Andrea Pfeifer. 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 Andrea Pfeifer. The network helps show where Andrea Pfeifer may publish in the future.
Co-authorship network of co-authors of Andrea Pfeifer
This figure shows the co-authorship network connecting the top 25 collaborators of Andrea Pfeifer. A scholar is included among the top collaborators of Andrea Pfeifer 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 Andrea Pfeifer. Andrea Pfeifer is excluded from the visualization to improve readability, since they are connected to all nodes in the network.
All Works
1.
Audrain, Mickaël, Sébastien Menant, Elodie Chevalier, et al.. (2025). A single dose of a vectorized mAb targeting TDP-43 potently inhibits the neuropathology in a model of ALS/FTD. Molecular Therapy. 33(9). 4360–4380.
2.
Chevalier, Elodie, Mickaël Audrain, Aline Fuchs, et al.. (2024). Targeting the TDP-43 low complexity domain blocks spreading of pathology in a mouse model of ALS/FTD. Acta Neuropathologica Communications. 12(1). 156–156.
3.
Overk, Cassia, Emma Fiorini, Marija Vukicevic, et al.. (2023). Modeling Alzheimer’s disease related phenotypes in the Ts65Dn mouse: impact of age on Aβ, Tau, pTau, NfL, and behavior. Frontiers in Neuroscience. 17. 1202208–1202208.
4.
Vukicevic, Marija, Emma Fiorini, Stephan A. Müller, et al.. (2022). Beneficial Effect of ACI-24 Vaccination on Aβ Plaque Pathology and Microglial Phenotypes in an Amyloidosis Mouse Model. Cells. 12(1). 79–79.
5.
Kroth, Heiko, Felix Oden, Jérôme Molette, et al.. (2021). Structure-activity relationship around PI-2620 highlights the importance of the nitrogen atom position in the tricyclic core. Bioorganic & Medicinal Chemistry. 52. 116528–116528.
6.
Gabellieri, Emanuele, Francesca Capotosti, Jérôme Molette, et al.. (2020). Discovery of 2-(4-(2-fluoroethoxy)piperidin-1-yl)-9-methyl-9H-pyrrolo[2,3-b:4,5-c’]dipyridine ([18F]PI-2014) as PET tracer for the detection of pathological aggregated tau in Alzheimer’s disease and other tauopathies. European Journal of Medicinal Chemistry. 204. 112615–112615.
7.
Kroth, Heiko, Felix Oden, Jérôme Molette, et al.. (2019). Discovery and preclinical characterization of [18F]PI-2620, a next-generation tau PET tracer for the assessment of tau pathology in Alzheimer’s disease and other tauopathies. European Journal of Nuclear Medicine and Molecular Imaging. 46(10). 2178–2189.
8.
Chen, Hsu-Hsin, Peter Liu, Seung-Hye Lee, et al.. (2018). Calpain-mediated tau fragmentation is altered in Alzheimer’s disease progression. Scientific Reports. 8(1). 16725–16725.
9.
Sreenivasachary, Nampally, Heiko Kroth, Yvan Varisco, et al.. (2017). Discovery and characterization of novel indole and 7-azaindole derivatives as inhibitors of β-amyloid-42 aggregation for the treatment of Alzheimer’s disease. Bioorganic & Medicinal Chemistry Letters. 27(6). 1405–1411.
10.
Kroth, Heiko, Nampally Sreenivasachary, Yvan Varisco, et al.. (2016). Synthesis and structure–activity relationship of 2,6-disubstituted pyridine derivatives as inhibitors of β-amyloid-42 aggregation. Bioorganic & Medicinal Chemistry Letters. 26(14). 3330–3335.
11.
Ultsch, Mark, Bing Li, Till Maurer, et al.. (2016). Structure of Crenezumab Complex with Aβ Shows Loss of β-Hairpin. Scientific Reports. 6(1). 39374–39374.
12.
Froestl, Wolfgang, Andrea Pfeifer, & Andreas Muhs. (2014). Cognitive Enhancers (Nootropics). Part 3: Drugs Interacting with Targets other than Receptors or Enzymes. Disease-Modifying Drugs. Update 2014. Journal of Alzheimer s Disease. 42(4). 1079–1149.
13.
Hickman, David T., et al.. (2014). Engineering Amyloid-Like Assemblies from Unstructured Peptides via Site-Specific Lipid Conjugation. PLoS ONE. 9(9). e105641–e105641.
14.
Koers, Eline J., María Pilar López-Deber, Markus Weingarth, et al.. (2013). Dynamic Nuclear Polarization NMR Spectroscopy: Revealing Multiple Conformations in Lipid‐Anchored Peptide Vaccines. Angewandte Chemie International Edition. 52(41). 10905–10908.
15.
Pihlgren, Maria, Rime Madani, Valérie Giriens, et al.. (2012). TLR4- and TRIF-dependent stimulation of B lymphocytes by peptide liposomes enables T cell–independent isotype switch in mice. Blood. 121(1). 85–94.
16.
Kroth, Heiko, Annalisa Ansaloni, Yvan Varisco, et al.. (2012). Discovery and Structure Activity Relationship of Small Molecule Inhibitors of Toxic β-Amyloid-42 Fibril Formation. Journal of Biological Chemistry. 287(41). 34786–34800.
17.
Hickman, David T., María Pilar López-Deber, Deepak Nand, et al.. (2011). Sequence-independent Control of Peptide Conformation in Liposomal Vaccines for Targeting Protein Misfolding Diseases. Journal of Biological Chemistry. 286(16). 13966–13976.
18.
Gulyás, Balázs, Christian Spenger, Károly Gulya, et al.. (2011). Distribution and binding of 18F-labeled and 125I-labeled analogues of ACI-80, a prospective molecular imaging biomarker of disease: A whole hemisphere post mortem autoradiography study in human brains obtained from Alzheimer’s disease patients. Neurochemistry International. 60(2). 153–162.
19.
Nag, Sangram, Р. Н. Красикова, Andreas Muhs, et al.. (2011). Fluorine-18 labeling of three novel d-peptides by conjugation with N-succinimidyl-4-[18F]fluorobenzoate and preliminary examination by postmortem whole-hemisphere human brain autoradiography. Nuclear Medicine and Biology. 39(3). 315–323.
20.
Jan, Asad, Oskar Adolfsson, Igor Allaman, et al.. (2010). Aβ42 Neurotoxicity Is Mediated by Ongoing Nucleated Polymerization Process Rather than by Discrete Aβ42 Species. Journal of Biological Chemistry. 286(10). 8585–8596.
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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