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Maarit Hölttä-Vuori

Researcher at Minerva Foundation Institute for Medical Research

Publications -  26
Citations -  5654

Maarit Hölttä-Vuori is an academic researcher from Minerva Foundation Institute for Medical Research. The author has contributed to research in topics: Endosome & Cholesterol. The author has an hindex of 20, co-authored 26 publications receiving 4901 citations. Previous affiliations of Maarit Hölttä-Vuori include University of Helsinki.

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A hexanucleotide repeat expansion in C9ORF72 is the cause of chromosome 9p21-linked ALS-FTD

Alan E. Renton, +85 more
- 20 Oct 2011 - 
TL;DR: The chromosome 9p21 amyotrophic lateral sclerosis-frontotemporal dementia (ALS-FTD) locus contains one of the last major unidentified autosomal-dominant genes underlying these common neurodegenerative diseases, and a large hexanucleotide repeat expansion in the first intron of C9ORF72 is shown.
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Seipin regulates ER-lipid droplet contacts and cargo delivery.

TL;DR: It is suggested that seipin helps to connect newly formed LDs to the ER and that by stabilizing ER–LD contacts seipIn facilitates the incorporation of protein and lipid cargo into growing LDs in human cells.
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BODIPY-Cholesterol: A New Tool to Visualize Sterol Trafficking in Living Cells and Organisms

TL;DR: This study employs atomistic simulations and experiments to characterize a cholesterol compound with fluorescent boron dipyrromethene difluoride linked to sterol carbon‐24 (BODIPY‐cholesterol), and concludes that this new probe closely mimics the membrane partitioning and trafficking of cholesterol and enables the direct monitoring of sterol movement by time‐lapse imaging using trace amounts of the probe.
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Zebrafish: gaining popularity in lipid research.

TL;DR: Basic information on the lipid composition and distribution in zebrafish tissues, including lipoprotein metabolism, intestinal lipid absorption, the yolk lipids and their mobilization, as well as lipids in the nervous system are summarized.
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Modulation of cellular cholesterol transport and homeostasis by Rab11

TL;DR: The results suggest that in Rab11-overexpressing cells, deposition of cholesterol in recycling endosomes results in its impaired esterification, presumably due to defective recycling of cholesterol to the plasma membrane.