ArticleCurrent genetics2009
The Aspergillus nidulans pigP gene encodes a subunit of GPI-N-acetylglucosaminyltransferase which influences filamentation and protein secretion.
Article in Current genetics, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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2 citing papers in PubMed, 8 citations in OpenAlex.
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2 authors at 1 institution in 1 country.
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Abstract
Glycosylphosphatidylinositol (GPI) anchoring is the main mechanism allowing proper localization of secretory proteins in cell membranes. We have isolated an Aspergillus nidulans homolog of the human PIG-P gene, which encodes a subunit of acetylglucosaminyltransferase (GPI-GnT)-an enzyme involved in the synthesis of GPI anchors. A. nidulans pigP mutants have significantly decreased GPI synthesis. On solid media they show strong growth retardation (the "button" phenotype) while in liquid minimal media they show overall good growth but with hyperbranched and bulbous hyphae with impaired septation. Furthermore, the pigP strains, in contrast to the wild-type, abundantly secrete a 33-kDa alkaline serine protease (ALP) into the liquid medium.
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