Sascha Weggen

7.9k total citations · 2 hit papers
93 papers, 6.2k citations indexed

About

Sascha Weggen is a scholar working on Physiology, Molecular Biology and Pharmacology. According to data from OpenAlex, Sascha Weggen has authored 93 papers receiving a total of 6.2k indexed citations (citations by other indexed papers that have themselves been cited), including 60 papers in Physiology, 37 papers in Molecular Biology and 19 papers in Pharmacology. Recurrent topics in Sascha Weggen's work include Alzheimer's disease research and treatments (60 papers), Cholinesterase and Neurodegenerative Diseases (16 papers) and Drug Transport and Resistance Mechanisms (15 papers). Sascha Weggen is often cited by papers focused on Alzheimer's disease research and treatments (60 papers), Cholinesterase and Neurodegenerative Diseases (16 papers) and Drug Transport and Resistance Mechanisms (15 papers). Sascha Weggen collaborates with scholars based in Germany, United States and Switzerland. Sascha Weggen's co-authors include Claus U. Pietrzik, Edward H. Koo, Jason L. Eriksen, Todd E. Golde, Sarah A. Sagi, Pritam Das, Victor Ozols, Thomas A. Bayer, Dirk Beher and Sandra Baches and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Sascha Weggen

93 papers receiving 6.0k citations

Hit Papers

A subset of NSAIDs lower amyloidogenic Aβ42 independently... 2001 2026 2009 2017 2001 2003 250 500 750 1000
What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

  1. A subset of NSAIDs lower amyloidogenic Aβ42 independently of cyclooxygenase activity
    2001 1.1k citations Sascha Weggen, Jason L. Eriksen et al. profile →
  2. NSAIDs and enantiomers of flurbiprofen target γ-secretase and lower Aβ42 in vivo
    2003 502 citations Jason L. Eriksen, Sarah A. Sagi et al. Journal of Clinical Investigation profile →

Peers

Sascha Weggen
Claus U. Pietrzik Germany
Jason L. Eriksen United States
Pritam Das United States
Patrick C. May United States
Jan Näslund Sweden
Giselle P. Lim United States
Kurt R. Brunden United States
Steffen Roßner Germany
Dennis J. Selkoe United States
Takeshi Kawarabayashi Japan
Claus U. Pietrzik Germany
Sascha Weggen
Citations per year, relative to Sascha Weggen Sascha Weggen (= 1×) peers Claus U. Pietrzik

Countries citing papers authored by Sascha Weggen

Since Specialization
Citations

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

Fields of papers citing papers by Sascha Weggen

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Sascha Weggen

This figure shows the co-authorship network connecting the top 25 collaborators of Sascha Weggen. A scholar is included among the top collaborators of Sascha Weggen 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 Sascha Weggen. Sascha Weggen 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.
2.
Klafki, Hans‐Wolfgang, et al.. (2023). Brain Region-Specific Differences in Amyloid-β Plaque Composition in 5XFAD Mice. Life. 13(4). 1053–1053. 11 indexed citations
3.
Huang, Anfei, Prashant V. Shinde, Jun Huang, et al.. (2019). Progranulin prevents regulatory NK cell cytotoxicity against antiviral T cells. JCI Insight. 4(17). 9 indexed citations
4.
Jumpertz, Thorsten, Isabella Ogorek, David C. Mikles, et al.. (2018). Discovery and validation of 2-styryl substituted benzoxazin-4-ones as a novel scaffold for rhomboid protease inhibitors. Bioorganic & Medicinal Chemistry Letters. 28(8). 1417–1422. 16 indexed citations
5.
Hüttenrauch, Melanie, Isabella Ogorek, Hans‐Wolfgang Klafki, et al.. (2018). Glycoprotein NMB: a novel Alzheimer’s disease associated marker expressed in a subset of activated microglia. Acta Neuropathologica Communications. 6(1). 108–108. 96 indexed citations
6.
Storck, Steffen E., Anika M. S. Hartz, Jessica K. Bernard, et al.. (2018). The concerted amyloid-beta clearance of LRP1 and ABCB1/P-gp across the blood-brain barrier is linked by PICALM. Brain Behavior and Immunity. 73. 21–33. 104 indexed citations
7.
Stäb, Julia, Dominic Docter, Sandra Baches, et al.. (2013). Nanoparticulate flurbiprofen reduces amyloid-β42 generation in an in vitro blood–brain barrier model. Alzheimer s Research & Therapy. 5(6). 51–51. 52 indexed citations
8.
Dieckmann, Marco, et al.. (2013). Stx5 is a novel interactor of VLDL-R to affect its intracellular trafficking and processing. Experimental Cell Research. 319(13). 1956–1972. 12 indexed citations
9.
Bednorz, Mariola, et al.. (2013). LRP1 is critical for the surface distribution and internalization of the NR2B NMDA receptor subtype. Molecular Neurodegeneration. 8(1). 25–25. 46 indexed citations
10.
Čaušević, Mirsada, Thorsten Jumpertz, Lisa Marie Munter, et al.. (2012). The Metalloprotease Meprin β Generates Amino Terminal-truncated Amyloid β Peptide Species. Journal of Biological Chemistry. 287(40). 33304–33313. 107 indexed citations
11.
Jumpertz, Thorsten, Andreas Rennhack, Sandra Baches, et al.. (2012). Presenilin Is the Molecular Target of Acidic γ-Secretase Modulators in Living Cells. PLoS ONE. 7(1). e30484–e30484. 36 indexed citations
12.
Deng, Juan, Huayan Hou, Brian Giunta, et al.. (2011). Autoreactive‐Aβ antibodies promote APP β‐secretase processing. Journal of Neurochemistry. 120(5). 732–740. 23 indexed citations
13.
Munter, Lisa Marie, Peter W. Hildebrand, Muralidhar Dasari, et al.. (2010). Amyloid beta 42 peptide (Aβ42)-lowering compounds directly bind to Aβ and interfere with amyloid precursor protein (APP) transmembrane dimerization. Proceedings of the National Academy of Sciences. 107(33). 14597–14602. 91 indexed citations
14.
Zettl, Heiko, Sascha Weggen, Petra Schneider, & Gisbert Schneider. (2010). Exploring the chemical space of γ-secretase modulators. Trends in Pharmacological Sciences. 31(9). 402–410. 24 indexed citations
15.
Pflanzner, Thorsten, Philip L.S.M. Gordts, Pascale Zimmermann, et al.. (2009). Inactivation of the proximal NPXY motif impairs early steps in LRP1 biosynthesis. Cellular and Molecular Life Sciences. 67(1). 135–145. 26 indexed citations
16.
Kummer, Markus P., et al.. (2008). Formation of Pmel17 Amyloid Is Regulated by Juxtamembrane Metalloproteinase Cleavage, and the Resulting C-terminal Fragment Is a Substrate for γ-Secretase. Journal of Biological Chemistry. 284(4). 2296–2306. 50 indexed citations
17.
Kuhlmann, Christoph, Svenja V. Trossbach, Sébastian Jaeger, et al.. (2008). The Functional Role of the Second NPXY Motif of the LRP1 β-Chain in Tissue-type Plasminogen Activator-mediated Activation of N-Methyl-D-aspartate Receptors. Journal of Biological Chemistry. 283(18). 12004–12013. 86 indexed citations
18.
Leuchtenberger, Stefanie, Markus P. Kummer, Thomas Kukar, et al.. (2005). Inhibitors of Rho‐kinase modulate amyloid‐β (Aβ) secretion but lack selectivity for Aβ42. Journal of Neurochemistry. 96(2). 355–365. 26 indexed citations
19.
Kukar, Thomas, M. Paul Murphy, Jason L. Eriksen, et al.. (2005). Diverse compounds mimic Alzheimer disease–causing mutations by augmenting Aβ42 production. Nature Medicine. 11(5). 545–550. 228 indexed citations
20.
Eriksen, Jason L., Sarah A. Sagi, Sascha Weggen, et al.. (2003). NSAIDs and enantiomers of flurbiprofen target γ-secretase and lower Aβ42 in vivo. Journal of Clinical Investigation. 112(3). 440–449. 502 indexed citations breakdown →

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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