Author

Kenneth Vielsted Christensen

Lundbeck (Denmark)ORCID 0000-0003-1759-8988Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Organism:rat· 2 Organism:human· 1 Research Focus:protein folding & dynamics· 1 Assay:proteomics· 1 Approach:statistical model· 1

Frequent Co-Authors

Anca StoicaiD· 1 shared Douglas S. Williamson· 1 shared Felix S. Oppermann· 1 shared Florence SottyiD· 1 shared Garrick P. Smith· 1 shared Garrick Paul SmithiD· 1 shared Jan Egebjerg· 1 shared Jens Damsgaard MikkelseniD· 1 shared

Activity by Year

2018-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 14 mutual co-author links

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1 shared paperNeuroscience

Anca StoicaORCID

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3 papers

Recent·Most cited

NeuroscienceExperimental NeurologyPeer-reviewedAug 18, 2022

Synergistic Effect of Serotonin 1A and Serotonin 1B/D Receptor Agonists in the Treatment of L-DOPA-Induced Dyskinesia in 6-Hydroxydopamine-Lesioned Rats

Mikael Søndergård Thomsen, Anca Stoica, Kenneth Vielsted Christensen…·John Bondo Hansen

This study evaluates the efficacy and safety of 5-HT1A and 5-HT1B/D agonists in reducing L-DOPA-induced dyskinesia in a rat model, finding synergistic effects and superior performance compared to amantadine.

8 citations

ratexperimental assay

𝕏 PostBluesky

NeuroscienceeNeuroPeer-reviewedNov 1, 2019

Long-term exposure to PFE-360 in the AAV-α-synuclein rat model: findings and implications

Michael Aagaard Andersen, Florence Sotty, Poul Henning Jensen…·Kenneth Vielsted Christensen

This study investigates the long-term effects of PFE-360 treatment in an AAV-α-synuclein rat model to assess its potential as a LRRK2 inhibitor for Parkinson's disease.

8 citations

ratexperimental assay

𝕏 PostBluesky

BiochemistrybioRxivPreprintOct 22, 2018

LRRK2 exonic variants associated with Parkinson’s disease augment phosphorylation levels for LRRK2-Ser1292 and Rab10-Thr73

Kenneth V. Christensen, Morten Hentzer, Felix S. Oppermann…·Garrick P. Smith

This study investigates how LRRK2 exonic variants affect phosphorylation levels of LRRK2 and Rab10, finding increased phosphorylation at Ser1292 for disease-causing variants and Rab10 phosphorylation for both rare and common variants.

DOI 10.1101/447946

humanproteomics

𝕏 PostBluesky