Majcherczyk, Andrzej

[["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"]]

[["dc.bibliographiccitation.firstpage","29"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","AGRO FOOD INDUSTRY HI-TECH"],["dc.bibliographiccitation.lastpage","32"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Huttermann, A."],["dc.contributor.author","Hamza, A. S."],["dc.contributor.author","Chet, I."],["dc.contributor.author","Majcherczyk, Andrzej"],["dc.contributor.author","Fouad, T."],["dc.contributor.author","Badr, A."],["dc.contributor.author","Cohen, R."],["dc.contributor.author","Persky, L."],["dc.contributor.author","Hadar, Y."],["dc.date.accessioned","2018-11-07T11:05:20Z"],["dc.date.available","2018-11-07T11:05:20Z"],["dc.date.issued","2000"],["dc.identifier.isi","000165673000008"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/52047"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Teknoscienze Publ"],["dc.relation.issn","1120-6012"],["dc.title","Recycling of agricultural wastes by white-rot fungi for the production of fodder for ruminants"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","193"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Journal of Biotechnology"],["dc.bibliographiccitation.lastpage","199"],["dc.bibliographiccitation.volume","78"],["dc.contributor.author","Johannes, C."],["dc.contributor.author","Majcherczyk, Andrzej"],["dc.date.accessioned","2018-11-07T08:46:26Z"],["dc.date.available","2018-11-07T08:46:26Z"],["dc.date.issued","2000"],["dc.description.abstract","Sulfhydryl organic compounds described as laccase inhibitors: dithiothreitol, thioglycolic acid, cysteine, diethyldithiocarbamic acid, and sodium azide were tested for their activity toward laccase of Trametes versicolor in different test systems utilising 2,2'-azino-bis-(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS) and 2,6-dimethoxyphenol as enzyme substrates. Only sodium azide acted as a true laccase inhibitor and showed no significant interference with the enzyme tests. All other substances did not significantly inhibit the laccase activity and the previously reported inhibitory effects result from the reductions of the reaction products such as ABTS radical cation and diquinone or subsequent non-enzymatic interactions during substrate oxidation. The latter apparently forms a complex with unreacted ABTS displaying varied spectral characteristics and resulting in am underestimation of enzyme activity. (C) 2000 Elsevier Science B.V. All rights reserved."],["dc.identifier.doi","10.1016/S0168-1656(00)00208-X"],["dc.identifier.isi","000086333200010"],["dc.identifier.pmid","10725542"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/20691"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Bv"],["dc.relation.issn","1873-4863"],["dc.relation.issn","0168-1656"],["dc.title","Laccase activity tests and laccase inhibitors"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["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"]]

[["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"]]

[["dc.bibliographiccitation.artnumber","tpj.15802"],["dc.bibliographiccitation.journal","The Plant Journal"],["dc.contributor.author","Kasper, Karl"],["dc.contributor.author","Abreu, Ilka N."],["dc.contributor.author","Feussner, Kirstin"],["dc.contributor.author","Zienkiewicz, Krzysztof"],["dc.contributor.author","Herrfurth, Cornelia"],["dc.contributor.author","Ischebeck, Till"],["dc.contributor.author","Janz, Dennis"],["dc.contributor.author","Majcherczyk, Andrzej"],["dc.contributor.author","Schmitt, Kerstin"],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Polle, Andrea"],["dc.date.accessioned","2022-06-01T09:39:32Z"],["dc.date.available","2022-06-01T09:39:32Z"],["dc.date.issued","2022"],["dc.identifier.doi","10.1111/tpj.15802"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/108504"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-572"],["dc.relation.eissn","1365-313X"],["dc.relation.issn","0960-7412"],["dc.title","Multi‐omics analysis of xylem sap uncovers dynamic modulation of poplar defenses by ammonium and nitrate"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","524"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Applied and Environmental Microbiology"],["dc.bibliographiccitation.lastpage","528"],["dc.bibliographiccitation.volume","66"],["dc.contributor.author","Johannes, C."],["dc.contributor.author","Majcherczyk, Andrzej"],["dc.date.accessioned","2018-11-07T10:10:31Z"],["dc.date.available","2018-11-07T10:10:31Z"],["dc.date.issued","2000"],["dc.description.abstract","The oxidation of polycyclic aromatic compounds was studied in systems consisting of laccase from Trametes versicolor and so-called mediator compounds, The enzymatic oxidation of acenaphthene, acenaphthylene, anthracene, and fluorene was mediated by various laccase substrates (phenols and aromatic amines) or compounds produced and secreted by white rot fungi. The best natural mediators, such as phenol, aniline, 4-hydroxybenzoic acid, and 4-hydroxybenzyl alcohol were as efficient as the previously described synthetic compounds ABTS [2,2'-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid)] and 1-hydroxybenzotriazole. The oxidation efficiency increased proportionally with the redox potentials of the phenolic mediators up to a maximum value of 0.9 V and decreased thereafter,vith redox potentials exceeding this value. Natural compounds such as methionine, cysteine, and reduced glutathione, containing sulfhydryl groups, were also active as mediator compounds."],["dc.identifier.doi","10.1128/AEM.66.2.524-528.2000"],["dc.identifier.isi","000085125900010"],["dc.identifier.pmid","10653713"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/39869"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Microbiology"],["dc.relation.issn","0099-2240"],["dc.title","Natural mediators in the oxidation of polycyclic aromatic hydrocarbons by laccase mediator systems"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1192"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Cells"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Beißbarth, Tim"],["dc.contributor.author","Bohrer, Rainer"],["dc.contributor.author","Feussner, Kirstin"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Schmitt, Kerstin"],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Asif, Abdul R."],["dc.contributor.author","Dihazi, Hassan"],["dc.contributor.author","Majcherczyk, Andrzej"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Lenz, Christof"],["dc.date.accessioned","2020-04-02T10:32:12Z"],["dc.date.available","2020-04-02T10:32:12Z"],["dc.date.issued","2019"],["dc.description.abstract","Mass spectrometry-based proteomics methods are finding increasing use in structural biology research. Beyond simple interaction networks, information about stable protein-protein complexes or spatially proximal proteins helps to elucidate the biological functions of proteins in a wider cellular context. To shed light on new developments in this field, the Göttingen Proteomics Forum organized a one-day symposium focused on complexome profiling and proximity labeling, two emerging technologies that are gaining significant attention in biomolecular research. The symposium was held in Göttingen, Germany on 23 May, 2019, as part of a series of regular symposia organized by the Göttingen Proteomics Forum."],["dc.identifier.doi","10.3390/cells8101192"],["dc.identifier.pmid","31581721"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16914"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/63512"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/95"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.publisher","MDPI"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | Z02: Massenspektrometrie-basierte Proteomanalyse"],["dc.relation.conference","Seventh Symposium of the Göttingen Proteomics Forum"],["dc.relation.eissn","2073-4409"],["dc.relation.eventlocation","Göttingen"],["dc.relation.eventstart","2019-05-23"],["dc.relation.issn","2073-4409"],["dc.relation.orgunit","Gesellschaft für wissenschaftliche Datenverarbeitung"],["dc.relation.workinggroup","RG Urlaub (Bioanalytische Massenspektrometrie)"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Mapping Cellular Microenvironments: Proximity Labeling and Complexome Profiling"],["dc.type","conference_paper"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["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"]]

[["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"]]