Neumann, Daniel

[["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.lastpage","19"],["dc.bibliographiccitation.seriesnr","124"],["dc.contributor.author","Jakobs, Stefan"],["dc.contributor.author","Stoldt, Stefan"],["dc.contributor.author","Neumann, Daniel"],["dc.contributor.editor","Müller, Susann"],["dc.contributor.editor","Bley, Thomas"],["dc.date.accessioned","2017-09-07T11:45:03Z"],["dc.date.available","2017-09-07T11:45:03Z"],["dc.date.issued","2011"],["dc.description.abstract","Heterogeneity in the shapes of individual multicellular organisms is a daily experience. Likewise, even a quick glance through the ocular of a light microscope reveals the morphological heterogeneities in genetically identical cultured cells, whereas heterogeneities on the level of the organelles are much less obvious. This short review focuses on intracellular heterogeneities at the example of the mitochondria and their analysis by fluorescence microscopy. The overall mitochondrial shape as well as mitochondrial dynamics can be studied by classical (fluorescence) light microscopy. However, with an organelle diameter generally close to the resolution limit of light, the heterogeneities within mitochondria cannot be resolved with conventional light microscopy. Therefore, we briefly discuss here the potential of subdiffraction light microscopy (nanoscopy) to study inner-mitochondrial heterogeneities."],["dc.identifier.doi","10.1007/10_2010_81"],["dc.identifier.gro","3142799"],["dc.identifier.isi","000288919400001"],["dc.identifier.pmid","21072702"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/243"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Springer"],["dc.publisher.place","Berlin"],["dc.relation.crisseries","Advances in Biochemical Engineering, Biotechnology"],["dc.relation.isbn","978-3-642-16886-4"],["dc.relation.ispartof","High Resolution Microbial Single Cell Analytics"],["dc.relation.ispartofseries","Advances in Biochemical Engineering, Biotechnology; 124"],["dc.relation.issn","0724-6145"],["dc.relation.issn","0724-6145"],["dc.title","Light Microscopic Analysis of Mitochondrial Heterogeneity in Cell Populations and Within Single Cells"],["dc.type","book_chapter"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","185"],["dc.bibliographiccitation.lastpage","199"],["dc.bibliographiccitation.seriesnr","591"],["dc.contributor.author","Wurm, Christian Andreas"],["dc.contributor.author","Neumann, Daniel"],["dc.contributor.author","Schmidt, Christoph"],["dc.contributor.author","Egner, Alexander"],["dc.contributor.author","Jakobs, Stefan"],["dc.date.accessioned","2017-09-07T11:53:08Z"],["dc.date.available","2017-09-07T11:53:08Z"],["dc.date.issued","2009"],["dc.identifier.doi","10.1007/978-1-60761-404-3_11"],["dc.identifier.gro","3145045"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2738"],["dc.language.iso","en"],["dc.notes.intern","Crossref Import"],["dc.notes.status","final"],["dc.publisher","Springer Nature"],["dc.relation.crisseries","Methods in Molecular Biology"],["dc.relation.isbn","978-1-60761-403-6"],["dc.relation.ispartof","Live Cell Imaging: Methods and Protocols"],["dc.relation.ispartofseries","Methods in Molecular Biology; 591"],["dc.relation.issn","1064-3745"],["dc.title","Sample Preparation for STED Microscopy"],["dc.type","book_chapter"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","13546"],["dc.bibliographiccitation.issue","33"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences"],["dc.bibliographiccitation.lastpage","13551"],["dc.bibliographiccitation.volume","108"],["dc.contributor.author","Wurm, Christian Andreas"],["dc.contributor.author","Neumann, Daniel"],["dc.contributor.author","Lauterbach, Marcel A."],["dc.contributor.author","Harke, Benjamin"],["dc.contributor.author","Egner, Alexander"],["dc.contributor.author","Hell, Stefan"],["dc.contributor.author","Jakobs, Stefan"],["dc.date.accessioned","2017-09-07T11:43:26Z"],["dc.date.available","2017-09-07T11:43:26Z"],["dc.date.issued","2011"],["dc.description.abstract","The translocase of the mitochondrial outer membrane (TOM) complex is the main import pore for nuclear-encoded proteins into mitochondria, yet little is known about its spatial distribution within the outer membrane. Super-resolution stimulated emission depletion microscopy was used to determine quantitatively the nanoscale distribution of Tom20, a subunit of the TOM complex, in more than 1,000 cells. We demonstrate that Tom20 is located in clusters whose nanoscale distribution is finely adjusted to the cellular growth conditions as well as to the specific position of a cell within a microcolony. The density of the clusters correlates to the mitochondrial membrane potential. The distributions of clusters of Tom20 and of Tom22 follow an inner-cellular gradient from the perinuclear to the peripheral mitochondria. We conclude that the nanoscale distribution of the TOM complex is finely adjusted to the cellular conditions, resulting in distribution gradients both within single cells and between adjacent cells."],["dc.identifier.doi","10.1073/pnas.1107553108"],["dc.identifier.gro","3142687"],["dc.identifier.isi","000293895100042"],["dc.identifier.pmid","21799113"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/118"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Natl Acad Sciences"],["dc.relation.issn","0027-8424"],["dc.title","Nanoscale distribution of mitochondrial import receptor Tom20 is adjusted to cellular conditions and exhibits an inner-cellular gradient"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","119"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","The Journal of Cell Biology"],["dc.bibliographiccitation.lastpage","130"],["dc.bibliographiccitation.volume","181"],["dc.contributor.author","Altmann, Katrin"],["dc.contributor.author","Frank, Martina"],["dc.contributor.author","Neumann, Daniel"],["dc.contributor.author","Jakobs, Stefan"],["dc.contributor.author","Westermann, Benedikt"],["dc.date.accessioned","2017-09-07T11:48:45Z"],["dc.date.available","2017-09-07T11:48:45Z"],["dc.date.issued","2008"],["dc.description.abstract","The actin cytoskeleton is essential for polarized, bud-directed movement of cellular membranes in Saccharomyces cerevisiae and thus ensures accurate inheritance of organelles during cell division. Also, mitochondrial distribution and inheritance depend on the actin cytoskeleton, though the precise molecular mechanisms are unknown. Here, we establish the class V myosin motor protein, Myo2, as an important mediator of mitochondrial motility in budding yeast. We found that mutants with abnormal expression levels of Myo2 or its associated light chain, Mlc1, exhibit aberrant mitochondrial morphology and loss of mitochondrial DNA. Specific mutations in the globular tail of Myo2 lead to aggregation of mitochondria in the mother cell. Isolated mitochondria lacking functional Myo2 are severely impaired in their capacity to bind to actin. laments in vitro. Time-resolved. uorescence microscopy revealed a block of bud-directed anterograde mitochondrial movement in cargo binding-defective myo2 mutant cells. We conclude that Myo2 plays an important and direct role for mitochondrial motility and inheritance in budding yeast."],["dc.identifier.doi","10.1083/jcb.200709099"],["dc.identifier.gro","3143317"],["dc.identifier.isi","000254746500013"],["dc.identifier.pmid","18391073"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/818"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0021-9525"],["dc.title","The class V myosin motor protein, Myo2, plays a major role in mitochondrial motility in Saccharomyces cerevisiae"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]