Großhans, Jörg

[["dc.bibliographiccitation.firstpage","21000"],["dc.bibliographiccitation.issue","52"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences of the United States of America"],["dc.bibliographiccitation.lastpage","21005"],["dc.bibliographiccitation.volume","110"],["dc.contributor.author","Schulz, Olaf"],["dc.contributor.author","Pieper, Christoph"],["dc.contributor.author","Clever, Michaela"],["dc.contributor.author","Pfaff, Janine"],["dc.contributor.author","Ruhlandt, Aike"],["dc.contributor.author","Kehlenbach, Ralph H."],["dc.contributor.author","Wouters, Fred Silvester"],["dc.contributor.author","Großhans, Jörg"],["dc.contributor.author","Bunt, Gertrude"],["dc.contributor.author","Enderlein, Jörg"],["dc.date.accessioned","2018-04-23T11:49:28Z"],["dc.date.available","2018-04-23T11:49:28Z"],["dc.date.issued","2013"],["dc.description.abstract","We demonstrate how a conventional confocal spinning-disk (CSD) microscope can be converted into a doubly resolving image scanning microscopy (ISM) system without changing any part of its optical or mechanical elements. Making use of the intrinsic properties of a CSD microscope, we illuminate stroboscopically, generating an array of excitation foci that are moved across the sample by varying the phase between stroboscopic excitation and rotation of the spinning disk. ISM then generates an image with nearly doubled resolution. Using conventional fluorophores, we have imaged single nuclear pore complexes in the nuclear membrane and aggregates of GFP-conjugated Tau protein in three dimensions. Multicolor ISM was shown on cytoskeletal-associated structural proteins and on 3D four-color images including MitoTracker and Hoechst staining. The simple adaptation of conventional CSD equipment allows superresolution investigations of a broad variety of cell biological questions."],["dc.identifier.doi","10.1073/pnas.1315858110"],["dc.identifier.gro","3142124"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/13705"],["dc.language.iso","en"],["dc.notes.intern","lifescience updates Crossref Import"],["dc.notes.status","final"],["dc.relation.doi","10.1073/pnas.1315858110"],["dc.relation.issn","0027-8424"],["dc.title","Resolution doubling in fluorescence microscopy with confocal spinning-disk image scanning microscopy"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2305"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","G3 (Bethesda, Md.)"],["dc.bibliographiccitation.lastpage","2314"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Winkler, Franziska"],["dc.contributor.author","Kriebel, Maria"],["dc.contributor.author","Clever, Michaela"],["dc.contributor.author","Gröning, Stephanie"],["dc.contributor.author","Großhans, Jörg"],["dc.date.accessioned","2019-07-09T11:43:38Z"],["dc.date.available","2019-07-09T11:43:38Z"],["dc.date.issued","2017-07-05"],["dc.description.abstract","Many metabolic enzymes are evolutionarily highly conserved and serve a central function in the catabolism and anabolism of cells. The serine hydroxymethyl transferase (SHMT) catalyzing the conversion of serine and glycine and vice versa feeds into tetrahydrofolate (THF)-mediated C1 metabolism. We identified a Drosophila mutation in SHMT (CG3011) in a screen for blastoderm mutants. Embryos from SHMT mutant germline clones specifically arrest the cell cycle in interphase 13 at the time of the midblastula transition (MBT) and prior to cellularization. The phenotype is due to a loss of enzymatic activity as it cannot be rescued by an allele with a point mutation in the catalytic center but by an allele based on the SHMT coding sequence from Escherichia coli The onset of zygotic gene expression and degradation of maternal RNAs in SHMT mutant embryos are largely similar to that in wild-type embryos. The specific timing of the defects in SHMT mutants indicates that at least one of the SHMT-dependent metabolites becomes limiting in interphase 13, if it is not produced by the embryo. Our data suggest that mutant eggs contain maternally-provided and SHMT-dependent metabolites in amounts that suffice for early development until interphase 13."],["dc.identifier.doi","10.1534/g3.117.043133"],["dc.identifier.pmid","28515048"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14608"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/58933"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.issn","2160-1836"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject.ddc","610"],["dc.title","Essential Function of the Serine Hydroxymethyl Transferase (SHMT) Gene During Rapid Syncytial Cell Cycles in Drosophila."],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]