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Marja Makarow

Researcher at University of Helsinki

Publications -  50
Citations -  2384

Marja Makarow is an academic researcher from University of Helsinki. The author has contributed to research in topics: Endoplasmic reticulum & Saccharomyces cerevisiae. The author has an hindex of 25, co-authored 50 publications receiving 2310 citations. Previous affiliations of Marja Makarow include European Science Foundation & University of Eastern Finland.

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The cell wall architecture of Candida albicans wild-type cells and cell wall-defective mutants

TL;DR: Observations show that C. albicans follows the same basic rules as S. cerevisiae in constructing a cell wall and indicate that acell wall salvage mechanism is activated when Candida cells are confronted with cell wall weakening.
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GRACILE Syndrome, a Lethal Metabolic Disorder with Iron Overload, Is Caused by a Point Mutation in BCS1L

TL;DR: Interestingly, the British and Turkish patients had complex III deficiency, whereas in the Finnish patients with GRACILE syndrome complex III activity was within the normal range, implying that BCS1L has another cellular function that is uncharacterized but essential and is putatively involved in iron metabolism.
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The contribution of the O-glycosylated protein Pir2p/Hsp150 to the construction of the yeast cell wall in wild-type cells and beta 1,6-glucan-deficient mutants.

TL;DR: Evidence is presented that Pir2p/Hsp150 is attached toβ1,3‐glucan through an alkali‐sensitive linkage, without β1,6‐ glucan as an interconnecting moiety, and it is argued that this is part of a more general compensatory mechanism in response to cell wall weakening caused by low levels of β1,.
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A heat shock gene from Saccharomyces cerevisiae encoding a secretory glycoprotein.

TL;DR: Direct amino acid sequencing of the mature secreted protein showed that an N-terminal sequence of 18 amino acids is removed, and a KEX2 protease-specific site is cleaved to yield two subunits of 53 and 341 amino acids, which remain noncovalently associated during secretion.
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Transmembrane topogenesis of a tail-anchored protein is modulated by membrane lipid composition

TL;DR: This work has developed a highly specific, sensitive, and quantitative in vitro assay for the proper membrane‐spanning topology of a model TA protein, cytochrome b5 (b5), and suggests that selectivity among various intracellular compartments can be imparted by differences in their lipid composition.