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Jaap Visser

Researcher at Utrecht University

Publications -  234
Citations -  18133

Jaap Visser is an academic researcher from Utrecht University. The author has contributed to research in topics: Aspergillus niger & Gene. The author has an hindex of 75, co-authored 232 publications receiving 17220 citations. Previous affiliations of Jaap Visser include Wageningen University and Research Centre & Spanish National Research Council.

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Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88

Herman Jan Pel, +70 more
- 01 Feb 2007 - 
TL;DR: The filamentous fungus Aspergillus niger is widely exploited by the fermentation industry for the production of enzymes and organic acids, particularly citric acid, and the sequenced genome revealed a large number of major facilitator superfamily transporters and fungal zinc binuclear cluster transcription factors.
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Aspergillus Enzymes Involved in Degradation of Plant Cell Wall Polysaccharides

TL;DR: This review summarizes the current knowledge of the cell wall polysaccharide-degrading enzymes from aspergilli and the genes by which they are encoded and describes the enzymatic pathways followed by tailored modifications by using specific enzymes purified from these fungi.
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The Endopolygalacturonase Gene Bcpg1 Is Required for Full Virulence of Botrytis cinerea

TL;DR: Results indicate that the Bcpg1 gene, encoding endopolygalacturonase, is required for full virulence in B. cinerea.
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The transcriptional activator XlnR regulates both xylanolytic and endoglucanase gene expression in Aspergillus niger

TL;DR: Genetic expression of genes encoding enzymes involved in xylan degradation and two endoglucanases involved in cellulose degradation was studied at the mRNA level in the filamentous fungus Aspergillus niger, indicating that transcriptional regulation by XlnR goes beyond the genes encoding xylanolytic enzymes and includes regulation of two endglucanase-encoding genes.
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Purification and properties of glutathione reductase of human erythrocytes

TL;DR: Human erythrocyte glutathione reductase (NAD(P)H) was purified 47 000-fold by column chromatography and full restoration of the activity did not guarantee that the original enzyme conformation had been acquired.