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Nicolai B. Larsen

Researcher at University of Copenhagen

Publications -  26
Citations -  1209

Nicolai B. Larsen is an academic researcher from University of Copenhagen. The author has contributed to research in topics: DNA replication & DNA. The author has an hindex of 12, co-authored 20 publications receiving 862 citations. Previous affiliations of Nicolai B. Larsen include Steno Diabetes Center.

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Book ChapterDOI

RecQ Helicases: Conserved Guardians of Genomic Integrity.

TL;DR: BLM has been shown to play a critical role in homologous recombination at multiple steps, including end-resection, displacement loop formation, branch migration and double Holliday junction dissolution, and recent evidence has revealed a role for BLM/Sgs1 in the stabilisation and repair of replication forks damaged during a perturbed S-phase.
Journal ArticleDOI

Automated detection of fundus photographic red lesions in diabetic retinopathy.

TL;DR: D detection of diabetic retinopathy by automated detection of single fundus lesions can be achieved with a performance comparable to that of experienced ophthalmologists, and the results warrant further investigation of automated fundus image analysis as a tool for diabetic Retinopathy screening.
Journal ArticleDOI

The CMG Helicase Bypasses DNA-Protein Cross-Links to Facilitate Their Repair.

TL;DR: It is shown that when DPC proteolysis is blocked, the replicative DNA helicase CMG (CDC45, MCM2-7, GINS), which travels on the leading strand template, bypasses an intact leading strand DPC.
Journal Article

Diabetic macular edema assessed with optical coherence tomography and stereo fundus photography.

TL;DR: The degree of agreement between subjectively and objectively assessed retinal thickening was very good, implying that changes in diabetic macular edema can be accurately and prospectively measured with OCT.
Journal ArticleDOI

Replication-Coupled DNA-Protein Crosslink Repair by SPRTN and the Proteasome in Xenopus Egg Extracts

TL;DR: It is shown that DPCs can be degraded by SPRTN or the proteasome, which act as independent DPC proteases, and are coupled to DNA replication by distinct mechanisms that promote replication across immovable protein barriers.