Braus, Gerhard H.

[["dc.bibliographiccitation.firstpage","443"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Fungal Genetics and Biology"],["dc.bibliographiccitation.lastpage","454"],["dc.bibliographiccitation.volume","49"],["dc.contributor.author","Gerke, Jennifer"],["dc.contributor.author","Bayram, Oezguer"],["dc.contributor.author","Braus, Gerhard H."],["dc.date.accessioned","2018-11-07T09:09:40Z"],["dc.date.available","2018-11-07T09:09:40Z"],["dc.date.issued","2012"],["dc.description.abstract","The filamentous fungus Aspergillus nidulans carries a single gene for the S-adenosylmethionine (SAM) synthetase SasA, whereas many other organisms possess multiple SAM synthetases. The conserved enzyme catalyzes the reaction of methionine and ATP to the ubiquitous methyl group donor SAM. SAM is the main methyl group donor for methyltransferases to modify DNA, RNA, protein, metabolites, or phospholipid target substrates. We show here that the single A. nidulans SAM synthetase encoding gene sasA is essential. Overexpression of sasA, encoding a predominantly cytoplasmic protein, led to impaired development including only small sterile fruiting bodies which are surrounded by unusually pigmented auxiliary Hulle cells. Hulle cells are the only fungal cell type which does not contain significant amounts of SasA. Sterigmatocystin production is altered when sasA is overexpressed, suggesting defects in coordination of development and secondary metabolism. SasA interacts with various metabolic proteins including methionine or mitochondrial metabolic enzymes as well as proteins involved in fungal morphogenesis. SasA interaction to histone-2B might reflect a putative epigenetic link to gene expression. Our data suggest a distinct role of SasA in coordinating fungal secondary metabolism and development. (C) 2012 Elsevier Inc. All rights reserved."],["dc.identifier.doi","10.1016/j.fgb.2012.04.003"],["dc.identifier.isi","000305167600004"],["dc.identifier.pmid","22561085"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/26312"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Academic Press Inc Elsevier Science"],["dc.relation.haserratum","/handle/2/72117"],["dc.relation.issn","1087-1845"],["dc.title","Fungal S-adenosylmethionine synthetase and the control of development and secondary metabolism in Aspergillus nidulans"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","8234"],["dc.bibliographiccitation.issue","23"],["dc.bibliographiccitation.journal","Applied and Environmental Microbiology"],["dc.bibliographiccitation.lastpage","8244"],["dc.bibliographiccitation.volume","78"],["dc.contributor.author","Gerke, Jennifer"],["dc.contributor.author","Bayram, Oezguer"],["dc.contributor.author","Feussner, Kirstin"],["dc.contributor.author","Landesfeind, Manuel"],["dc.contributor.author","Shelest, Ekaterina"],["dc.contributor.author","Feussner, Ivo"],["dc.contributor.author","Braus, Gerhard H."],["dc.date.accessioned","2018-11-07T09:03:02Z"],["dc.date.available","2018-11-07T09:03:02Z"],["dc.date.issued","2012"],["dc.description.abstract","The genomes of filamentous fungi comprise numerous putative gene clusters coding for the biosynthesis of chemically and structurally diverse secondary metabolites (SMs), which are rarely expressed under laboratory conditions. Previous approaches to activate these genes were based primarily on artificially targeting the cellular protein synthesis apparatus. Here, we applied an alternative approach of genetically impairing the protein degradation apparatus of the model fungus Aspergillus nidulans by deleting the conserved eukaryotic csnE/CSN5 deneddylase subunit of the COP9 signalosome. This defect in protein degradation results in the activation of a previously silenced gene cluster comprising a polyketide synthase gene producing the antibiotic 2,4-dihydroxy-3-methyl-6-(2-oxopropyl) benzaldehyde (DHMBA). The csnE/CSN5 gene is highly conserved in fungi, and therefore, the deletion is a feasible approach for the identification of new SMs."],["dc.identifier.doi","10.1128/AEM.01808-12"],["dc.identifier.isi","000310915300009"],["dc.identifier.pmid","23001671"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/24811"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Microbiology"],["dc.relation.haserratum","/handle/2/76763"],["dc.relation.issn","1098-5336"],["dc.relation.issn","0099-2240"],["dc.title","Breaking the Silence: Protein Stabilization Uncovers Silenced Biosynthetic Gene Clusters in the Fungus Aspergillus nidulans"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3254"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Molecular Biology of the Cell"],["dc.bibliographiccitation.lastpage","3262"],["dc.bibliographiccitation.volume","19"],["dc.contributor.author","Bayram, Oezguer"],["dc.contributor.author","Biesemann, Christoph"],["dc.contributor.author","Krappmann, Sven"],["dc.contributor.author","Galland, Paul"],["dc.contributor.author","Braus, Gerhard H."],["dc.date.accessioned","2018-11-07T11:12:39Z"],["dc.date.available","2018-11-07T11:12:39Z"],["dc.date.issued","2008"],["dc.description.abstract","Cryptochromes are blue-light receptors that have presumably evolved from the DNA photolyase protein family, and the genomes of many organisms contain genes for both types of molecules. Both protein structures resemble each other, which suggests that light control and light protection share a common ancient origin. In the genome of the filamentous fungus Aspergillus nidulans, however, only one cryptochrome/photolyase-encoding gene, termed cryA, was identified. Deletion of the cryA gene triggers sexual differentiation under inappropriate culture conditions and results in upregulation of transcripts encoding regulators of fruiting body formation. CryA is a protein whose N- and C-terminal synthetic green fluorescent protein fusions localize to the nucleus. CryA represses sexual development under UVA(350-370nm) light both on plates and in submerged culture. Strikingly, CryA exhibits photorepair activity as demonstrated by heterologous complementation of a DNA repair-deficient Escherichia coli strain as well as overexpression in an A. nidulans uvsB Delta genetic background. This is in contrast to the single deletion cryA Delta strain, which does not show increased sensitivity toward UV-induced damage. In A. nidulans, cryA encodes a novel type of cryptochrome/photolyase that exhibits a regulatory function during light-dependent development and DNA repair activity. This represents a paradigm for the evolutionary transition between photolyases and cryptochromes."],["dc.identifier.doi","10.1091/mbc.E08-01-0061"],["dc.identifier.isi","000259160400008"],["dc.identifier.pmid","18495868"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/53714"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Cell Biology"],["dc.relation.issn","1059-1524"],["dc.title","More than a repair enzyme: Aspergillus nidulans photolyase-like CryA is a regulator of sexual development"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1504"],["dc.bibliographiccitation.issue","5882"],["dc.bibliographiccitation.journal","Science"],["dc.bibliographiccitation.lastpage","1506"],["dc.bibliographiccitation.volume","320"],["dc.contributor.author","Bayram, Oezguer"],["dc.contributor.author","Krappmann, Sven"],["dc.contributor.author","Ni, Min"],["dc.contributor.author","Bok, Jin Woo"],["dc.contributor.author","Helmstaedt, Kerstin"],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Braus-Stromeyer, Susanna A."],["dc.contributor.author","Kwon, Nak-Jung"],["dc.contributor.author","Keller, Nancy P."],["dc.contributor.author","Yu, Jae-Hyuk"],["dc.contributor.author","Braus, Gerhard H."],["dc.date.accessioned","2018-11-07T11:14:00Z"],["dc.date.available","2018-11-07T11:14:00Z"],["dc.date.issued","2008"],["dc.description.abstract","Differentiation and secondary metabolism are correlated processes in fungi that respond to light. In Aspergillus nidulans, light inhibits sexual reproduction as well as secondary metabolism. We identified the heterotrimeric velvet complex VelB/VeA/LaeA connecting light-responding developmental regulation and control of secondary metabolism. VeA, which is primarily expressed in the dark, physically interacts with VelB, which is expressed during sexual development. VeA bridges VelB to the nuclear master regulator of secondary metabolism, LaeA. Deletion of either velB or veA results in defects in both sexual fruiting-body formation and the production of secondary metabolites."],["dc.identifier.doi","10.1126/science.1155888"],["dc.identifier.isi","000256676400047"],["dc.identifier.pmid","18556559"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/54029"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Assoc Advancement Science"],["dc.relation.issn","0036-8075"],["dc.title","VelB/VeA/LaeA complex coordinates light signal with fungal development and secondary metabolism"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1278"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Molecular Microbiology"],["dc.bibliographiccitation.lastpage","1295"],["dc.bibliographiccitation.volume","71"],["dc.contributor.author","Bayram, Oezguer"],["dc.contributor.author","Sari, Fatih"],["dc.contributor.author","Braus, Gerhard H."],["dc.contributor.author","Irniger, Stefan"],["dc.date.accessioned","2018-11-07T08:32:21Z"],["dc.date.available","2018-11-07T08:32:21Z"],["dc.date.issued","2009"],["dc.description.abstract","Spore formation is a common process in the developmental cycle of fungi. In the yeast Saccharomyces cerevisiae, Ime2 is a key protein kinase for the meiotic cell cycle, which precedes ascospore formation. Here, we analysed the IME2-related imeB gene of the filamentous ascomycete Aspergillus nidulans. imeB deletion strains are retarded in growth and overproduce fertile sexual fruiting bodies in the presence of light, which normally represses sexual development. imeB mutants also display abnormal differentiation of sexual Hulle cells in submerged cultures. Increased sexual development of imeB mutants is dependent on VeA, a component of the heterotrimeric velvet complex. A combined deletion of imeB with the phytochrome fphA, a red light receptor, results in a complete loss of light response, suggesting that ImeB and FphA cooperate in light-mediated inhibition of sexual development. Furthermore, we found that imeB mutants fail to produce the mycotoxin sterigmatocystin, an aflatoxin precursor, and show that ImeB is needed for expression of the sterigmatocystin gene cluster. ImeB contains a TXY motif conserved in mitogen-activated protein kinases. This sequence element is essential for ImeB function. We conclude that ImeB is a mitogen-activated protein kinase-related protein kinase required for the co-ordinated control of light-dependent development with mycotoxin production."],["dc.identifier.doi","10.1111/j.1365-2958.2009.06606.x"],["dc.identifier.isi","000263522000017"],["dc.identifier.pmid","19210625"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/17324"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell Publishing, Inc"],["dc.relation.issn","0950-382X"],["dc.title","The protein kinase ImeB is required for light-mediated inhibition of sexual development and for mycotoxin production in Aspergillus nidulans"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","495"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Eukaryotic Cell"],["dc.bibliographiccitation.lastpage","510"],["dc.bibliographiccitation.volume","14"],["dc.contributor.author","Jaimes-Arroyo, Rafael"],["dc.contributor.author","Lara-Rojas, Fernando"],["dc.contributor.author","Bayram, Oezguer"],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Braus, Gerhard H."],["dc.contributor.author","Aguirre, Jesus"],["dc.date.accessioned","2018-11-07T09:57:50Z"],["dc.date.available","2018-11-07T09:57:50Z"],["dc.date.issued","2015"],["dc.description.abstract","Fungi and many other eukaryotes use specialized mitogen-activated protein kinases (MAPK) of the Hog1/p38 family to transduce environmental stress signals. In Aspergillus nidulans, the MAPK SakA and the transcription factor AtfA are components of a central multiple stress-signaling pathway that also regulates development. Here we characterize SrkA, a putative MAPK-activated protein kinase, as a novel component of this pathway. Delta srkA and Delta sakA mutants share a derepressed sexual development phenotype. However, Delta srkA mutants are not sensitive to oxidative stress, and in fact, srkA inactivation partially suppresses the sensitivity of Delta sakA mutant conidia to H2O2, tert-butyl-hydroperoxide (t-BOOH), and menadione. In the absence of stress, SrkA shows physical interaction with nonphosphorylated SakA in the cytosol. We show that H2O2 induces a drastic change in mitochondrial morphology consistent with a fission process and the relocalization of SrkA to nuclei and mitochondria, depending on the presence of SakA. SakA-SrkA nuclear interaction is also observed during normal asexual development in dormant spores. Using SakA and SrkA S-tag pulldown and purification studies coupled to mass spectrometry, we found that SakA interacts with SrkA, the stress MAPK MpkC, the PPT1-type phosphatase AN6892, and other proteins involved in cell cycle regulation, DNA damage response, mRNA stability and protein synthesis, mitochondrial function, and other stress-related responses. We propose that oxidative stress induces DNA damage and mitochondrial fission and that SakA and SrkA mediate cell cycle arrest and regulate mitochondrial function during stress. Our results provide new insights into the mechanisms by which SakA and SrkA regulate the remodelling of cell physiology during oxidative stress and development."],["dc.identifier.doi","10.1128/EC.00277-14"],["dc.identifier.isi","000353909500005"],["dc.identifier.pmid","25820520"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/37247"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Microbiology"],["dc.relation.issn","1535-9786"],["dc.relation.issn","1535-9778"],["dc.title","The SrkA Kinase Is Part of the SakA Mitogen-Activated Protein Kinase Interactome and Regulates Stress Responses and Development in Aspergillus nidulans"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","1"],["dc.bibliographiccitation.journal","Frontiers in Microbiology"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Sarikaya-Bayram, Oezlem"],["dc.contributor.author","Palmer, Jonathan M."],["dc.contributor.author","Keller, Nancy P."],["dc.contributor.author","Braus, Gerhard H."],["dc.contributor.author","Bayram, Oezguer"],["dc.date.accessioned","2018-11-07T10:02:05Z"],["dc.date.available","2018-11-07T10:02:05Z"],["dc.date.issued","2015"],["dc.description.abstract","Fungal secondary metabolism has become an important research topic with great biomedical and biotechnological value. In the postgenomic era, understanding the diversity and the molecular control of secondary metabolites (SMs) are two challenging tasks addressed by the research community. Discovery of the LaeA methyltransferase 10 years ago opened up a new horizon on the control of SM research when it was found that expression of many SM gene clusters is controlled by LaeA. While the molecular function of LaeA remains an enigma, discovery of the velvet family proteins as interaction partners further extended the role of the LaeA beyond secondary metabolism. The heterotrimeric VeIB-VeA-LaeA complex plays important roles in development, sporulation, secondary metabolism, and pathogenicity. Recently, three other methyltransferases have been found to associate with the velvet complex, the LaeA-like methyltransferase F and the methyltransferase heterodimers VipC-VapB. Interaction of VeA with at least four methyltransferase proteins indicates a molecular hub function for VeA that questions: Is there a VeA supercornplex or is VeA part of a highly dynamic cellular control network with many different partners?"],["dc.identifier.doi","10.3389/fmicb.2015.00001"],["dc.identifier.isi","000348859100001"],["dc.identifier.pmid","25653648"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/38158"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Frontiers Research Foundation"],["dc.relation.issn","1664-302X"],["dc.title","One Juliet and four Romeos: VeA and its methyltransferases"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","42"],["dc.bibliographiccitation.journal","Fungal Genetics and Biology"],["dc.bibliographiccitation.lastpage","53"],["dc.bibliographiccitation.volume","56"],["dc.contributor.author","Suzuki, Satoshi"],["dc.contributor.author","Bayram, Oezlem Sarikaya"],["dc.contributor.author","Bayram, Oezguer"],["dc.contributor.author","Braus, Gerhard H."],["dc.date.accessioned","2018-11-07T09:23:05Z"],["dc.date.available","2018-11-07T09:23:05Z"],["dc.date.issued","2013"],["dc.description.abstract","Light induces various responses in fungi including formation of asexual and sexual reproductive structures. The formation of conidia in the filamentous fungus Aspergillus nidulans is regulated by red and blue light receptors. Expression of conidia associated con genes, which are widely spread in the fungal kingdom, increases upon exposure to light. We have characterized the light-inducible conF and conj genes of A. nidulans which are homologs of con-6 and con-10 of Neurospora crassa. con genes are expressed during conidia formation in asexual development. Five minutes light exposure are sufficient to induce conF or conj expression in vegetative mycelia. Similar to N. crassa there were no significant phenotypes of single con mutations. A double conF and conJ deletion resulted in significantly increased cellular amounts of glycerol or erythritol. This leads to a delayed germination phenotype combined with increased resistance against desiccation. These defects were rescued by complementation of the double mutant strain with either conF or conj. This suggests that fungal con genes exhibit redundant functions in controlling conidia germination and adjusting cellular levels of substances which protect conidia against dryness. (C) 2013 Elsevier Inc. All rights reserved."],["dc.identifier.doi","10.1016/j.fgb.2013.04.008"],["dc.identifier.isi","000321534600006"],["dc.identifier.pmid","23644150"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/29494"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Academic Press Inc Elsevier Science"],["dc.relation.issn","1096-0937"],["dc.relation.issn","1087-1845"],["dc.title","conF and conJ contribute to conidia germination and stress response in the filamentous fungus Aspergillus nidulans"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","406"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Developmental Cell"],["dc.bibliographiccitation.lastpage","420"],["dc.bibliographiccitation.volume","29"],["dc.contributor.author","Sarikaya-Bayram, Oezlem"],["dc.contributor.author","Bayram, Oezguer"],["dc.contributor.author","Feussner, Kirstin"],["dc.contributor.author","Kim, Jong-Hwa"],["dc.contributor.author","Kim, Hee-Seo"],["dc.contributor.author","Kaever, Alexander"],["dc.contributor.author","Feussner, Ivo"],["dc.contributor.author","Chae, Keon-Sang"],["dc.contributor.author","Han, Dong-Min"],["dc.contributor.author","Han, Kap-Hoon"],["dc.contributor.author","Braus, Gerhard H."],["dc.date.accessioned","2018-11-07T09:39:57Z"],["dc.date.available","2018-11-07T09:39:57Z"],["dc.date.issued","2014"],["dc.description.abstract","Epigenetic and transcriptional control of gene expression must be coordinated in response to external signals to promote alternative multicellular developmental programs. The membrane-associated trimeric complex VapA-VipC-VapB controls a signal transduction pathway for fungal differentiation. The VipC-VapB methyltransferases are tethered to the membrane by the FYVE-like zinc finger protein VapA, allowing the nuclear VelB-VeA-LaeA complex to activate transcription for sexual development. Once the release from VapA is triggered, VipC-VapB is transported into the nucleus. VipC-VapB physically interacts with VeA and reduces its nuclear import and protein stability, thereby reducing the nuclear VelB-VeA-LaeA complex. Nuclear VapB methyltransferase diminishes the establishment of facultative heterochromatin by decreasing histone 3 lysine 9 trimethylation (H3K9me3). This favors activation of the regulatory genes brlA and abaA, which promote the asexual program. The VapA-VipC-VapB methyltransferase pathway combines control of nuclear import and stability of transcription factors with histone modification to foster appropriate differentiation responses."],["dc.identifier.doi","10.1016/j.devcel.2014.03.020"],["dc.identifier.isi","000336608600005"],["dc.identifier.pmid","24871947"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/33407"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.relation.issn","1878-1551"],["dc.relation.issn","1534-5807"],["dc.title","Membrane-Bound Methyltransferase Complex VapA-VipC-VapB Guides Epigenetic Control of Fungal Development"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","900"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Fungal Genetics and Biology"],["dc.bibliographiccitation.lastpage","908"],["dc.bibliographiccitation.volume","47"],["dc.contributor.author","Bayram, Oezguer"],["dc.contributor.author","Braus, Gerhard H."],["dc.contributor.author","Fischer, Reinhard X."],["dc.contributor.author","Rodriguez-Romero, Julio"],["dc.date.accessioned","2018-11-07T08:37:31Z"],["dc.date.available","2018-11-07T08:37:31Z"],["dc.date.issued","2010"],["dc.description.abstract","Aspergilli are ubiquitous soil-borne fungi growing within or on the surface of numerous organic substrates. Growth within a substrate or growth on the surface correlates to different growth conditions for the hyphae due to significant changes in oxygen or reactive oxygen species levels and variations in humidity or temperature. The production of air-borne spores is supported by the substrate-air interphase and also requires a sensing system to adapt appropriately. Here we focus on light as important parameter for the mycelium to discriminate between different habitats. The fungal 'eye' includes several light sensors which react to a broad plethora of wavelengths. Aspergillus nidulans light receptors comprise a phytochrome for red-light sensing, white collar-like blue-light signaling proteins, a putative green-light sensing opsin and a cryptochrome/photolyase as distinct sensory systems. Red- and blue-light receptors are assembled into a light-sensing protein complex. Light receptors transmit their signal to a number of other regulatory proteins including a bridging protein, VeA, as part of a trimeric complex. VeA plays a central role in the balance of asexual and sexual development and in the coordination of morphogenesis and secondary metabolism. (C) 2010 Elsevier Inc. All rights reserved."],["dc.identifier.doi","10.1016/j.fgb.2010.05.008"],["dc.identifier.isi","000283007700004"],["dc.identifier.pmid","20573560"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/18553"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Academic Press Inc Elsevier Science"],["dc.relation.issn","1087-1845"],["dc.title","Spotlight on Aspergillus nidulans photosensory systems"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]