Now showing 1 - 10 of 16
  • 2019Journal Article Research Paper
    [["dc.bibliographiccitation.firstpage","37"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Acta Edulis Fungi"],["dc.bibliographiccitation.lastpage","50"],["dc.bibliographiccitation.volume","26"],["dc.contributor.author","Majcherczyk, Andrzej"],["dc.contributor.author","Dörnte, Bastian"],["dc.contributor.author","Subba, Shanta"],["dc.contributor.author","Zomorrodi, Mojtaba"],["dc.contributor.author","Kües, Ursula"],["dc.date.accessioned","2022-02-16T13:25:56Z"],["dc.date.available","2022-02-16T13:25:56Z"],["dc.date.issued","2019"],["dc.description.abstract","Fruiting body formation of Coprinopsis cinerea takes place at 25 ℃ under a 12 h day/12 h night regime. It starts by intense local hyphal branching with production of primary hyphal knots in the dark. A first light signal induces the transfer into the compact secondary hyphal knots. In these secondary hyphal knots, cap and stipe tissue begin to differentiate. This process underlies distinct patterns of light and dark regulated events over the following 5 days and then the mushrooms mature on the next day. To gain insight into the complex cytological processes during the cap and stipe tissue development, we isolated total proteomes from distinct primordia stages for MS/MS analysis. Between 1672 and 2663 proteins were detected in the different samples with at least two peptides at a confidence level of 99%, among which 1401 proteins were shared by all the samples. Known proteins in primordia development were identified in the samples."],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/99923"],["dc.relation.doi","10.16488/j.cnki.1005-9873.2019.03.005"],["dc.relation.orgunit","Abteilung Molekulare Holzbiotechnologie und technische Mykologie"],["dc.title","Proteomes in Primordia Development of Coprinopsis cinerea"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]
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  • 2007Journal Article
    [["dc.bibliographiccitation.firstpage","694"],["dc.bibliographiccitation.issue","6-7"],["dc.bibliographiccitation.journal","Enzyme and Microbial Technology"],["dc.bibliographiccitation.lastpage","701"],["dc.bibliographiccitation.volume","41"],["dc.contributor.author","Kellner, Harald"],["dc.contributor.author","Jehmlich, Nico"],["dc.contributor.author","Benndorf, Dirk"],["dc.contributor.author","Hoffmann, Ralf"],["dc.contributor.author","Ruehl, Martin"],["dc.contributor.author","Hoegger, Patrick J."],["dc.contributor.author","Majcherczyk, Andrzej"],["dc.contributor.author","Kuees, Ursula"],["dc.contributor.author","von Bergen, Martin"],["dc.contributor.author","Buscot, Francois"],["dc.date.accessioned","2018-11-07T10:56:06Z"],["dc.date.available","2018-11-07T10:56:06Z"],["dc.date.issued","2007"],["dc.description.abstract","This study presents a combined method to analyze extracellular fungal laccases using a new anti-laccase antibody together with the identification of tryptic laccase peptides by mass spectrometry (nanoLC-ESI-MS/MS). The polyclonal anti-laccase antibody LccCbr2 was raised against peptides designed from the copper binding region 11 of fungal laccases using in silico data obtained from GenBank database. As a consequence, detection requires denaturation of the enzymes due to the stable conformation of the copper binding region II. The specificity of the antibody was shown with denatured laccase Lcc1 of Coprinopsis cinerea and laccase of Hypholoma fasciculare. LccCbr2 detected amounts as low as 5 ng of highly purified laccase, indicating a possible use of the antibody for quantification of laccase proteins. Denatured extracellular laccases from culture supernatants of the basidiomycetes C. cinerea, H. fasciculare, Lentinula edodes, Mycena sp., Piriformospora indica, Pleurotus cornucopiae, Pleurotus ostreatus, Pycnoporus cinnabarinus, Trametes versicolor and furthermore the ascomycete Verpa conica were detected with apparent molecular masses between 60 and 70 kDa by LccCbr2. The identity of extracellular laccases from C cinerea, H. fasciculare, P ostreatus, P. cinnabarinus and T versicolor were verified by tryptic peptides using nanoLC-ESI-MS/MS. (C) 2007 Elsevier Inc. All rights reserved."],["dc.identifier.doi","10.1016/j.enzmictec.2007.06.002"],["dc.identifier.isi","000250042000005"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/49936"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Inc"],["dc.relation.issn","1879-0909"],["dc.relation.issn","0141-0229"],["dc.title","Detection, quantification and identification of fungal extracellular laccases using polyclonal antibody and mass spectrometry"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]
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  • 2007Journal Article
    [["dc.bibliographiccitation.firstpage","1423"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Tree Physiology"],["dc.bibliographiccitation.lastpage","1431"],["dc.bibliographiccitation.volume","27"],["dc.contributor.author","Blödner, Constanze"],["dc.contributor.author","Majcherczyk, Andrzej"],["dc.contributor.author","Kües, Ursula"],["dc.contributor.author","Polle, Andrea"],["dc.date.accessioned","2017-09-07T11:49:13Z"],["dc.date.available","2017-09-07T11:49:13Z"],["dc.date.issued","2007"],["dc.description.abstract","To elucidate early drought responses in needles of Norway spruce (Picea abies (Karst.) L.), we subjected 1-year-old seedlings to gradual desiccation for 6 weeks. Four weeks of drought treatment caused a small but significant decrease in photosystem II quantum yield of light-adapted needles (Φa) compared with that of well-watered controls. Six weeks of drought treatment reduced Φa and the photosystem II quantum yield of dark-adapted needles (Φ) by 50 and 8%, respectively, and reduced shoot water potential by 0.7 MPa, but had no measurable effect on needle relative water content. After two weeks of drought treatment, and before there was a discernible effect of drought on Φ or a statistically significant effect on shoot water potential, needles were analyzed for changes in protein composition. Five out of several hundred detected proteins in needles of drought-treated plants showed consistent changes compared with control leaves. The proteins were identified by LC-MS/MS as components of the oxygen-evolving complex (oxygen evolving enhancer protein 2), ribulose-1,5-bisphosphate carboxylase/oxgenase large subunit, and one protein of unknown function, whose mRNA was found in a previous screen of wound- and methyl-jasmonate-induced bark proteins."],["dc.identifier.doi","10.1093/treephys/27.10.1423"],["dc.identifier.gro","3147211"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/4843"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.notes.submitter","chake"],["dc.relation.issn","0829-318X"],["dc.title","Early drought-induced changes to the needle proteome of Norway spruce"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]
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  • 2008Journal Article
    [["dc.bibliographiccitation.artnumber","129"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","BMC Plant Biology"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Floerl, Saskia"],["dc.contributor.author","Druebert, Christine"],["dc.contributor.author","Majcherczyk, Andrzej"],["dc.contributor.author","Karlovsky, Petr"],["dc.contributor.author","Kües, Ursula"],["dc.contributor.author","Polle, Andrea"],["dc.date.accessioned","2017-09-07T11:50:34Z"],["dc.date.available","2017-09-07T11:50:34Z"],["dc.date.issued","2008"],["dc.description.abstract","Background Verticillium longisporum is one of the most important pathogens of Brassicaceae that remains strictly in the xylem during most stages of its development. It has been suggested that disease symptoms are associated with clogging of xylem vessels. The aim of our study was to investigate extracellular defence reactions induced by V. longisporum in the xylem sap and leaf apoplast of Brassica napus var. napus in relation to the development of disease symptoms, photosynthesis and nutrient status. Results V. longisporum (strain VL43) did not overcome the hypocotyl barrier until 3 weeks after infection although the plants showed massive stunting of the stem and mild leaf chlorosis. During this initial infection phase photosynthetic carbon assimilation, transpiration rate and nutrient elements in leaves were not affected in VL43-infected compared to non-infected plants. Proteome analysis of the leaf apoplast revealed 170 spots after 2-D-protein separation, of which 12 were significantly enhanced in response to VL43-infection. LS-MS/MS analysis and data base searches revealed matches of VL43-responsive proteins to an endochitinase, a peroxidase, a PR-4 protein and a β-1,3-glucanase. In xylem sap three up-regulated proteins were found of which two were identified as PR-4 and β-1,3-glucanase. Xylem sap of infected plants inhibited the growth of V. longisporum. Conclusion V. longisporum infection did not result in drought stress or nutrient limitations. Stunting and mild chlorosis were, therefore, not consequences of insufficient water and nutrient supply due to VL43-caused xylem obstruction. A distinct array of extracellular PR-proteins was activated that might have limited Verticillium spreading above the hypocotyl. In silico analysis suggested that ethylene was involved in up-regulating VL43-responsive proteins."],["dc.identifier.doi","10.1186/1471-2229-8-129"],["dc.identifier.gro","3147701"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/5107"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.notes.submitter","chake"],["dc.relation.issn","1471-2229"],["dc.title","Defence reactions in the apoplastic proteome of oilseed rape (Brassica napus var. napus) attenuate Verticillium longisporum growth but not disease symptoms"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]
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  • 2009Journal Article Research Paper
    [["dc.bibliographiccitation.firstpage","2431"],["dc.bibliographiccitation.issue","14"],["dc.bibliographiccitation.journal","Electrophoresis"],["dc.bibliographiccitation.lastpage","2441"],["dc.bibliographiccitation.volume","30"],["dc.contributor.author","Fragner, Dorothea"],["dc.contributor.author","Zomorrodi, Mojtaba"],["dc.contributor.author","Kües, Ursula"],["dc.contributor.author","Majcherczyk, Andrzej"],["dc.date.accessioned","2018-11-07T08:28:07Z"],["dc.date.available","2018-11-07T08:28:07Z"],["dc.date.issued","2009"],["dc.description.abstract","Basidiomycetes inhabiting lignocellulose comprise an important class of filamentous fungi with ecological and biotechnological relevance. Extracellular enzymes of wood-degrading fungi such as laccases, manganese-dependent (or independent) peroxidases, cellulases and xylanases are of considerable interest for biotechnological applications. Still, proteomic studies of fungal secretomes based on 2-DE can be very challenging due to low protein concentrations and variable amounts of fungal metabolites. Comparison of different standard methods for protein precipitation has demonstrated their limited applicability to fungal secretomes. The extracellular metabolites impair standard methods for protein quantification and can result in a strong overestimation of total protein. We have developed an optimized protocol for the precipitation of extracellular proteins from liquid cultures of Coprinopsis cinerea growing in an exponential phase on a complex media. We found that a considerable amount of gelatinous material can be removed from the liquid culture supernatants by high-speed centrifugation. Fungal proteins can be effectively enriched by TCA precipitation and coprecipitated metabolites hampering 2-DE can be removed through the application of Tris/acetone. Following our protocol makes it possible to concentrate proteins from culture supernatants and to simultaneously remove most of the impeding compounds from a given sample. We have applied this procedure in the 2-DE of secretomes from the model organism C. cinerea as well as other basidiomycetes such as Pleurotus ostreatus, Phanerochaete chrysosporium, Polyporus brumalis and Schizophyllum commune."],["dc.description.sponsorship","Ministry of Science and Culture in Hannover, Germany [ZN 2043]"],["dc.identifier.doi","10.1002/elps.200800770"],["dc.identifier.isi","000269041500004"],["dc.identifier.pmid","19593751"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/16346"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","0173-0835"],["dc.title","Optimized protocol for the 2-DE of extracellular proteins from higher basidiomycetes inhabiting lignocellulose"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]
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  • 2012Journal Article
    [["dc.bibliographiccitation.artnumber","e31435"],["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","PLoS ONE"],["dc.bibliographiccitation.lastpage","14"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Floerl, Saskia"],["dc.contributor.author","Majcherczyk, Andrzej"],["dc.contributor.author","Possienke, Mareike"],["dc.contributor.author","Feussner, Kirstin"],["dc.contributor.author","Tappe, Hella"],["dc.contributor.author","Gatz, Christiane"],["dc.contributor.author","Feussner, I."],["dc.contributor.author","Kües, Ursula"],["dc.contributor.author","Polle, Andrea"],["dc.date.accessioned","2017-09-07T11:49:18Z"],["dc.date.available","2017-09-07T11:49:18Z"],["dc.date.issued","2012"],["dc.description.abstract","Verticillium longisporum (VL) is one of the most devastating diseases in important oil crops from the family of Brassicaceae. The fungus resides for much time of its life cycle in the extracellular fluid of the vascular system, where it cannot be controlled by conventional fungicides. To obtain insights into the biology of VL-plant interaction in the apoplast, the secretome consisting of the extracellular proteome and metabolome as well as cell wall properties were studied in the model Brassicaceae, Arabidopsis thaliana. VL infection resulted in increased production of cell wall material with an altered composition of carbohydrate polymers and increased lignification. The abundance of several hundred soluble metabolites changed in the apoplast of VL-infected plants including signalling and defence compounds such as glycosides of salicylic acid, lignans and dihydroxybenzoic acid as well as oxylipins. The extracellular proteome of healthy leaves was enriched in antifungal proteins. VL caused specific increases in six apoplast proteins (three peroxidases PRX52, PRX34, P37, serine carboxypeptidase SCPL20, α-galactosidase AGAL2 and a germin-like protein GLP3), which have functions in defence and cell wall modification. The abundance of a lectin-like, chitin-inducible protein (CILLP) was reduced. Since the transcript levels of most of the induced proteins were not elevated until late infection time points (>20 dpi), whereas those of CILLP and GLP3 were reduced at earlier time points, our results may suggest that VL enhances its virulence by rapid down-regulation and delay of induction of plant defence genes."],["dc.identifier.doi","10.1371/journal.pone.0031435"],["dc.identifier.gro","3147253"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/7889"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/4884"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","chake"],["dc.relation.issn","1932-6203"],["dc.rights","CC BY 2.5"],["dc.rights.uri","https://creativecommons.org/licenses/by/2.5"],["dc.title","Verticillium longisporum Infection Affects the Leaf Apoplastic Proteome, Metabolome, and Cell Wall Properties in Arabidopsis thaliana"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]
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  • 2013Journal Article
    [["dc.bibliographiccitation.firstpage","1029"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","ANTONIE VAN LEEUWENHOEK INTERNATIONAL JOURNAL OF GENERAL AND MOLECULAR MICROBIOLOGY"],["dc.bibliographiccitation.lastpage","1039"],["dc.bibliographiccitation.volume","103"],["dc.contributor.author","Ruehl, Martin"],["dc.contributor.author","Majcherczyk, Andrzej"],["dc.contributor.author","Kuees, Ursula"],["dc.date.accessioned","2018-11-07T09:25:02Z"],["dc.date.available","2018-11-07T09:25:02Z"],["dc.date.issued","2013"],["dc.description.abstract","The litter-degrading dung fungus Coprinopsis cinerea has the high number of seventeen different laccase genes. In this work, ten different monokaryons were compared in their ability to produce laccases in two different complete media at different temperatures. Few strains showed laccase activity at the optimal growth temperature of 37 degrees C. Nine of the strains gave laccase activities between 0.2 and 5.9 U mL(-1) at the suboptimal temperature of 25 degrees C in mKjalke medium. Laccase activities in YMG/T medium were detected for only three strains (0.5-4.5 U mL(-1)). Zymograms of supernatants from mKjalke medium resulted in total in 10 different laccase bands but strains differed in distribution. LC-MS/MS analysis with Mascot searches of the annotated C. cinerea genome identified isoenzymes from five different genes (Lcc1, Lcc2, Lcc5, Lcc9 and Lcc10) and of Lcc1 three and of Lcc5 two distinct electrophoretical forms. Lcc1 and Lcc5 were expressed in all laccase positive strains, but not all forms were found in all of the strains. Lcc2, Lcc9 and Lcc10 occurred only in three strains as minor laccases, indicating that Lcc1 and Lcc5 are the main laccases of C. cinerea secreted in liquid mKjalke medium."],["dc.description.sponsorship","Ministry of Science and Culture of Lower Saxony [ZN 2043]"],["dc.identifier.doi","10.1007/s10482-013-9883-7"],["dc.identifier.isi","000319268600010"],["dc.identifier.pmid","23340718"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10338"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/29973"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.relation.issn","0003-6072"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Lcc1 and Lcc5 are the main laccases secreted in liquid cultures of Coprinopsis cinerea strains"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]
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  • 2011Journal Article
    [["dc.bibliographiccitation.firstpage","136"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Diversity"],["dc.bibliographiccitation.lastpage","154"],["dc.bibliographiccitation.volume","3"],["dc.contributor.author","Badalyan, Susanna M."],["dc.contributor.author","Szafranski, Karol"],["dc.contributor.author","Hoegger, Patrik J."],["dc.contributor.author","Navarro-González, Monica"],["dc.contributor.author","Majcherczyk, Andrzej"],["dc.contributor.author","Kües, Ursula"],["dc.date.accessioned","2019-07-09T11:54:15Z"],["dc.date.available","2019-07-09T11:54:15Z"],["dc.date.issued","2011"],["dc.description.abstract","Coprinoid mushrooms grown on wood of broad-leaf species were collected for the first time in Armenia and dikaryotic mycelial cultures were established. ITS (internal transcribed spacer) sequences identified one species as Coprinopsis strossmayeri and the other as a species closely related to Coprinellus radians. Mycelial growth and morphological features on different media are described. The pearl-white-silky colonies of C. strossmayeri are characterized by mycelial strands and by a light-yellow agar colorization. The species forms chlamydospores intercalary in its hyphae. Some hyphal ends form hyphal loops. Colonies of C. aff. radians have a characteristic yellow pigmentation and stain the agar yellowish. Hyphae are mostly clampless but at some septa, pseudoclamps are seen from which side-branches develop growing along the parental hyphae. In the mycelium of C. aff. radians, hyphal loops, hyphal swellings, cystidia and typical allocysts were observed. Both new species from Armenia show growth optima at temperatures of 25 to 30 °C and pHs of 6.0 to 7.0. Both grow in alkaline conditions up to pH 12.0 but not at pHs 3.0 and 4.0, classifying them with other coprinoid mushrooms as ―ammonia fungi‖. Both species grew on a variety of lignocellulosic substrates and both show polyphenol oxidase activities."],["dc.identifier.doi","10.3390/d3010136"],["dc.identifier.fs","576359"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/8672"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/60605"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.issn","1424-2818"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","New Armenian Wood-Associated Coprinoid Mushrooms: Coprinopsis strossmayeri and Coprinellus aff. radians"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]
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  • 2006Journal Article Research Paper
    [["dc.bibliographiccitation.firstpage","200"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Applied Microbiology and Biotechnology"],["dc.bibliographiccitation.lastpage","210"],["dc.bibliographiccitation.volume","71"],["dc.contributor.author","Kilaru, Sreedhar"],["dc.contributor.author","Hoegger, Patrick J."],["dc.contributor.author","Majcherczyk, Andrzej"],["dc.contributor.author","Burns, Claire"],["dc.contributor.author","Shishido, Kazuo"],["dc.contributor.author","Bailey, Andrew M."],["dc.contributor.author","Foster, Gary D."],["dc.contributor.author","Kües, Ursula"],["dc.date.accessioned","2018-11-07T09:42:54Z"],["dc.date.available","2018-11-07T09:42:54Z"],["dc.date.issued","2006"],["dc.description.abstract","Coprinopsis cinerea laccase gene lcc1 was expressed in this basidiomycete under naturally non-inductive conditions using various homologous and heterologous promoters. Laccase expression was achieved in solid and liquid media with promoter sequences from the C cinerea tub1 gene, the Agaricus bisporus gpdII gene, the Lentinus edodes priA gene and the Schizophyllum commune Sc3 gene. As measured by enzyme activity in liquid cultures, a 277-bp gpdII promoter fragment, followed by a 423-bp priA fragment, was most efficient. A shorter priA sequence of 372 bp was inactive. tub1 promoter fragments were reasonably active, whereas the S. commune Sc3 promoter sequence was less active, in comparison. Irrespective of the promoter used, addition of copper to the medium increased enzymatic activities for highly active transformants by 10- to 50-fold and for less active transformants for 2- to 7-fold. The highest enzymatic activities (3 U/ml) were reached with the gpdII promoter in the presence of 0.1 mM CuSO4."],["dc.identifier.doi","10.1007/s00253-005-0128-1"],["dc.identifier.isi","000239207800010"],["dc.identifier.pmid","16158283"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/34069"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","0175-7598"],["dc.title","Expression of laccase gene lcc1 in Coprinopsis cinerea under control of various basidiomycetous promoters"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]
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  • 2006Book Chapter
    [["dc.bibliographiccitation.firstpage","151"],["dc.bibliographiccitation.lastpage","163"],["dc.contributor.author","Peddireddi, S."],["dc.contributor.author","Velagapudi, R."],["dc.contributor.author","Hoegger, P. J."],["dc.contributor.author","Majcherczyk, A."],["dc.contributor.author","Naumann, A."],["dc.contributor.author","Olbrich, A."],["dc.contributor.author","Polle, A."],["dc.contributor.author","Kües, Ursula"],["dc.contributor.editor","Pisabarro, Antonio G."],["dc.contributor.editor","Ramírez, Lucía"],["dc.date.accessioned","2017-09-07T11:49:56Z"],["dc.date.available","2017-09-07T11:49:56Z"],["dc.date.issued","2006"],["dc.identifier.gro","3149774"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/6472"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.notes.submitter","chake"],["dc.publisher","Universidad Pública de Navarra"],["dc.publisher.place","Pamplona"],["dc.relation.isbn","84-9769-107-5"],["dc.relation.ispartof","VI Meeting on Genetic and Cellular Biology of Basidiomycetes"],["dc.title","Multiple Hydrophobin Genes in Mushroom"],["dc.type","book_chapter"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]
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