about
Aspergillus luchuensis, an industrially important black Aspergillus in East AsiaThe C2H2-type transcription factor, FlbC, is involved in the transcriptional regulation of Aspergillus oryzae glucoamylase and protease genes specifically expressed in solid-state culture.Quantitative evaluation of haze formation of koji and progression of internal haze by drying of koji during koji making.Genomics of Aspergillus oryzae.Effects of codon optimization on the mRNA levels of heterologous genes in filamentous fungi.Signaling pathways for stress responses and adaptation in Aspergillus species: stress biology in the post-genomic era.Reconstitution of biosynthetic machinery for the synthesis of the highly elaborated indole diterpene penitrem.Crawler, a novel Tc1/mariner-type transposable element in Aspergillus oryzae transposes under stress conditions.Functional analysis of FarA transcription factor in the regulation of the genes encoding lipolytic enzymes and hydrophobic surface binding protein for the degradation of biodegradable plastics in Aspergillus oryzae.A defect of LigD (human Lig4 homolog) for nonhomologous end joining significantly improves efficiency of gene-targeting in Aspergillus oryzae.Subcellular localization of aphidicolin biosynthetic enzymes heterologously expressed in Aspergillus oryzae.Cloning and nucleotide sequence of the acid protease-encoding gene (pepA) from Aspergillus oryzae.Endocytosis of a maltose permease is induced when amylolytic enzyme production is repressed in Aspergillus oryzae.Distinct mechanism of activation of two transcription factors, AmyR and MalR, involved in amylolytic enzyme production in Aspergillus oryzae.Rapid reconstitution of biosynthetic machinery for fungal metabolites in Aspergillus oryzae: total biosynthesis of aflatrem.Chaperone complex formation of the transcription factor MalR involved in maltose utilization and amylolytic enzyme production in Aspergillus oryzae.Improved α-amylase production by Aspergillus oryzae after a double deletion of genes involved in carbon catabolite repression.The C-terminal region of the yeast monocarboxylate transporter Jen1 acts as a glucose signal-responding degron recognized by the α-arrestin Rod1Increased production of biomass-degrading enzymes by double deletion of creA and creB genes involved in carbon catabolite repression in Aspergillus oryzaePurification and enzymatic characterization of secretory glycoside hydrolase family 3 (GH3) aryl β-glucosidases screened from Aspergillus oryzae genomeIdentification of potential cell wall component that allows Taka-amylase A adsorption in submerged cultures of Aspergillus oryzaeAtrR Is an Essential Determinant of Azole Resistance in Aspergillus fumigatusUse of a biosynthetic intermediate to explore the chemical diversity of pseudo-natural fungal polyketidesPurification and enzymatic characterization of a novel β-1,6-glucosidase from Aspergillus oryzaeNuclear export-dependent degradation of the carbon catabolite repressor CreA is regulated by a region located near the C-terminus in Aspergillus oryzaeAlternative transcription start sites of the enolase-encoding gene enoA are stringently used in glycolytic/gluconeogenic conditions in Aspergillus oryzaeThe PDR-type ABC transporters AtrA and AtrG are involved in azole drug resistance in Aspergillus oryzaeRegulatory mechanisms for amylolytic gene expression in the koji mold Aspergillus oryzae
P50
Q31118566-C11E2E98-DB85-4E8D-8F5B-B5197B9311A4Q35951489-0994DC4D-0F36-450F-AEDB-0A326F433D92Q36333271-CE9CE353-905C-49C2-900B-4518D69A6582Q36753209-5C851684-4E82-4AB2-AF1F-18D81CFFF190Q38200521-0E466E49-D6B1-420D-BB66-123B7F3B62DEQ38381923-09BE10E7-E40F-40F3-BFEF-66E64BFF77DDQ41127959-1F06BC40-F59D-4F54-AE93-15765403B652Q42614284-E6EFB545-3C24-4C46-AFA0-0118EE7C7624Q44483940-17C22F18-9DBD-4E4B-984D-5596B82316BCQ46746984-89ED654A-1C01-4600-B981-03C7811D6AA4Q47298196-5EDACA8C-3552-4A94-A7FA-820DC6C74906Q48114382-FE6C61DC-D17F-4D5F-91A9-5EEE66B5DA58Q50264144-56E6CB4A-00E8-42FF-9AFC-CAE5303D7704Q50443627-57398D8B-ED5F-47E7-94E6-D76CCC21C152Q51064852-05109454-6C1C-4AEC-BA9F-EF7B21339045Q52363053-D3502741-B9F3-46F8-90A9-7FA212E89B00Q54627955-D69A18A5-600D-44F5-B86F-1A14DB846078Q57663702-D6F260A1-9FFC-4654-9808-52FD520FC938Q57663705-46F64121-1E34-4B9A-8AEA-88523DCB2A9AQ57663719-4A2BC7C6-2095-49D8-9C5C-6AD9BB490EF3Q57663731-40A94361-E63B-4CF0-94D1-8DABD76AEFA5Q64104132-CA22B3CF-D495-4D97-9F97-6C9DFD72CFB2Q85937813-D9FB2FA7-63F4-4493-97E3-B57F77446CAEQ86033992-0C75DB8B-621E-4170-9EAE-716597E4A4A0Q89568072-FCAF1357-A647-410C-9947-6E2E755F364BQ89770760-9CF6E08C-CC89-450B-A267-145A80792415Q90241512-5BE02188-5CF1-4215-AB54-346DBCDEC28FQ92496529-B8695FC7-9010-4014-ACAC-AFA27584C02D
P50
description
onderzoeker
@nl
researcher ORCID ID = 0000-0003-3463-8072
@en
name
Katsuya Gomi
@ast
Katsuya Gomi
@en
Katsuya Gomi
@es
Katsuya Gomi
@nl
type
label
Katsuya Gomi
@ast
Katsuya Gomi
@en
Katsuya Gomi
@es
Katsuya Gomi
@nl
prefLabel
Katsuya Gomi
@ast
Katsuya Gomi
@en
Katsuya Gomi
@es
Katsuya Gomi
@nl
P106
P31
P496
0000-0003-3463-8072