Schuh, Melina

[["dc.bibliographiccitation.firstpage","841"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Scheffler, Kathleen"],["dc.contributor.author","Uraji, Julia"],["dc.contributor.author","Jentoft, Ida"],["dc.contributor.author","Cavazza, Tommaso"],["dc.contributor.author","Mönnich, Eike"],["dc.contributor.author","Mogessie, Binyam"],["dc.contributor.author","Schuh, Melina"],["dc.date.accessioned","2022-02-21T16:28:14Z"],["dc.date.available","2022-02-21T16:28:14Z"],["dc.date.issued","2021"],["dc.description.abstract","A new life begins with the unification of the maternal and paternal chromosomes upon fertilization. The parental chromosomes first become enclosed in two separate pronuclei near the surface of the fertilized egg. The mechanisms that then move the pronuclei inwards for their unification are only poorly understood in mammals. Here, we report two mechanisms that act in concert to unite the parental genomes in fertilized mouse eggs. The male pronucleus assembles within the fertilization cone and is rapidly moved inwards by the flattening cone. Rab11a recruits the actin nucleation factors Spire and Formin-2 into the fertilization cone, where they locally nucleate actin and further accelerate the pronucleus inwards. In parallel, a dynamic network of microtubules assembles that slowly moves the male and female pronuclei towards the cell centre in a dynein-dependent manner. Both mechanisms are partially redundant and act in concert to unite the parental pronuclei in the zygote's centre."],["dc.identifier.doi","10.1038/s41467-021-21020-x"],["dc.identifier.pmid","33547291"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/100161"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/234"],["dc.language.iso","en"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation.issn","2041-1723"],["dc.relation.workinggroup","RG Schuh"],["dc.rights","CC BY 4.0"],["dc.title","Two mechanisms drive pronuclear migration in mouse zygotes"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","135"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Cell"],["dc.bibliographiccitation.lastpage","146"],["dc.bibliographiccitation.volume","126"],["dc.contributor.author","Kudo, Nobuaki R."],["dc.contributor.author","Wassmann, Katja"],["dc.contributor.author","Anger, Martin"],["dc.contributor.author","Schuh, Melina"],["dc.contributor.author","Wirth, Karin G."],["dc.contributor.author","Xu, Huiling"],["dc.contributor.author","Helmhart, Wolfgang"],["dc.contributor.author","Kudo, Hiromi"],["dc.contributor.author","Mckay, Michael"],["dc.contributor.author","Maro, Bernard"],["dc.contributor.author","Ellenberg, Jan"],["dc.contributor.author","Boer, Peter de"],["dc.contributor.author","Nasmyth, Kim"],["dc.date.accessioned","2017-09-07T11:52:38Z"],["dc.date.available","2017-09-07T11:52:38Z"],["dc.date.issued","2006"],["dc.description.abstract","In yeast, resolution of chiasmata in meiosis I requires proteolytic cleavage along chromosome arms of cohesin's Rec8 subunit by separase. Since activation of separase by the anaphase-promoting complex (APC/C) is supposedly not required for meiosis I in Xenopus oocytes, it has been suggested that animal cells might resolve chiasmata by a separase-independent mechanism related to the so-called \"prophase pathway\" that removes cohesin from chromosome arms during mitosis. By expressing Cre recombinase from a zona pellucida promoter, we have deleted a floxed allele of separase specifically in mouse oocytes. This prevents removal of Rec8 from chromosome arms and resolution of chiasmata. It also hinders extrusion of the first polar body (PBE) and causes female sterility. mRNA encoding wild-type but not catalytically inactive separase restores chiasma resolution. Both types of mRNA restore PBE. Proteolytic activity of separase is therefore essential for Rec8's removal from chromosome arms and for chiasma resolution but not for PBE."],["dc.identifier.doi","10.1016/j.cell.2006.05.033"],["dc.identifier.gro","3143657"],["dc.identifier.isi","000239224800022"],["dc.identifier.pmid","16839882"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1195"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Medical Research Council [G0901046]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0092-8674"],["dc.title","Resolution of Chiasmata in Oocytes Requires Separase-Mediated Proteolysis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1426"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Cell Reports"],["dc.bibliographiccitation.lastpage","1437"],["dc.bibliographiccitation.volume","17"],["dc.contributor.author","Tischer, Thomas"],["dc.contributor.author","Schuh, Melina"],["dc.date.accessioned","2017-09-07T11:44:32Z"],["dc.date.available","2017-09-07T11:44:32Z"],["dc.date.issued","2016"],["dc.description.abstract","Mammalian oocytes are stored in the ovary, where they are arrested in prophase for prolonged periods. The mechanisms that abrogate the prophase arrest in mammalian oocytes and reinitiate meiosis are not well understood. Here, we identify and characterize an essential pathway for the resumption of meiosis that relies on the protein phosphatase DUSP7. DUSP7-depleted oocytes either fail to resume meiosis or resume meiosis with a significant delay. In the absence of DUSP7, Cdk1/CycB activity drops below the critical level required to reinitiate meiosis, precluding or delaying nuclear envelope breakdown. Our data suggest that DUSP7 drives meiotic resumption by dephosphorylating and thereby inactivating cPKC isoforms. In addition to controlling meiotic resumption, DUSP7 has a second function in chromosome segregation: DUSP7-depleted oocytes that enter meiosis show severe chromosome alignment defects and progress into anaphase prematurely. Altogether, these findings establish the phosphatase DUSP7 as an essential regulator of multiple steps in oocyte meiosis."],["dc.identifier.doi","10.1016/j.celrep.2016.10.007"],["dc.identifier.gro","3141601"],["dc.identifier.isi","000386527100019"],["dc.identifier.pmid","27783954"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/12"],["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","2211-1247"],["dc.title","The Phosphatase Dusp7 Drives Meiotic Resumption and Chromosome Alignment in Mouse Oocytes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","128"],["dc.bibliographiccitation.issue","6398"],["dc.bibliographiccitation.journal","Science"],["dc.bibliographiccitation.lastpage","129"],["dc.bibliographiccitation.volume","361"],["dc.contributor.author","Zielinska, Agata P."],["dc.contributor.author","Schuh, Melina"],["dc.date.accessioned","2022-03-01T11:47:19Z"],["dc.date.available","2022-03-01T11:47:19Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1126/science.aau3216"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103989"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","1095-9203"],["dc.relation.issn","0036-8075"],["dc.title","Double trouble at the beginning of life"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1986"],["dc.bibliographiccitation.issue","24"],["dc.bibliographiccitation.journal","Current Biology"],["dc.bibliographiccitation.lastpage","1992"],["dc.bibliographiccitation.volume","18"],["dc.contributor.author","Schuh, Melina"],["dc.contributor.author","Ellenberg, Jan"],["dc.date.accessioned","2017-09-07T11:47:37Z"],["dc.date.available","2017-09-07T11:47:37Z"],["dc.date.issued","2008"],["dc.description.abstract","An oocyte matures into an egg by extruding half of the chromosomes in a small polar body. This extremely asymmetric division enables the oocyte to retain sufficient storage material for the development of the embryo after fertilization. To divide asymmetrically, mammalian oocytes relocate the spindle from their center to the cortex. In all mammalian species analyzed so far, including human [1], mouse [2], cow [3], pig [4], and hamster [5], spindle relocation depends on filamentous actin (F-actin). However, even though spindle relocation is essential for fertility [6], the involved F-actin structures and the mechanism by which they relocate the spindle are unknown. Here we show in live mouse oocytes that spindle relocation requires a continuously reorganizing cytoplasmic actin network nucleated by Formin-2 (Fmn2). We found that the spindle poles were enriched in activated myosin and pulled on this network. Inhibition of myosin activation by myosin light chain kinase (MLCK) stopped pulling and spindle relocation, indicating that myosin pulling creates the force that drives spindle movement. Based on these results, we propose the first mechanistic model for asymmetric spindle positioning in mammalian oocytes and validate five of its key predictions experimentally."],["dc.identifier.doi","10.1016/j.cub.2008.11.022"],["dc.identifier.gro","3143189"],["dc.identifier.isi","000262089700037"],["dc.identifier.pmid","19062278"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/675"],["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","0960-9822"],["dc.title","A New Model for Asymmetric Spindle Positioning in Mouse Oocytes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","eabq4835"],["dc.bibliographiccitation.issue","6617"],["dc.bibliographiccitation.journal","Science"],["dc.bibliographiccitation.volume","378"],["dc.contributor.author","Cheng, Shiya"],["dc.contributor.author","Altmeppen, Gerrit"],["dc.contributor.author","So, Chun"],["dc.contributor.author","Welp, Luisa M."],["dc.contributor.author","Penir, Sarah"],["dc.contributor.author","Ruhwedel, Torben"],["dc.contributor.author","Menelaou, Katerina"],["dc.contributor.author","Harasimov, Katarina"],["dc.contributor.author","Stützer, Alexandra"],["dc.contributor.author","Blayney, Martyn"],["dc.contributor.author","Schuh, Melina"],["dc.date.accessioned","2022-11-01T10:17:06Z"],["dc.date.available","2022-11-01T10:17:06Z"],["dc.date.issued","2022"],["dc.description.abstract","Full-grown oocytes are transcriptionally silent and must stably maintain the messenger RNAs (mRNAs) needed for oocyte meiotic maturation and early embryonic development. However, where and how mammalian oocytes store maternal mRNAs is unclear. Here, we report that mammalian oocytes accumulate mRNAs in a mitochondria-associated ribonucleoprotein domain (MARDO). MARDO assembly around mitochondria was promoted by the RNA-binding protein ZAR1 and directed by an increase in mitochondrial membrane potential during oocyte growth. MARDO foci coalesced into hydrogel-like matrices that clustered mitochondria. Maternal mRNAs stored in the MARDO were translationally repressed. Loss of ZAR1 disrupted the MARDO, dispersed mitochondria, and caused a premature loss of MARDO-localized mRNAs. Thus, a mitochondria-associated membraneless compartment controls mitochondrial distribution and regulates maternal mRNA storage, translation, and decay to ensure fertility in mammals."],["dc.description.abstract","Oocytes store mRNAs around mitochondria\n \n Mammalian oocytes stop transcribing DNA into messenger RNA (mRNA) during the final stages of their development. The oocyte’s meiotic divisions and early embryo development occur in the absence of transcription and rely instead on maternal mRNAs that are stored in the oocyte. However, where and how mammalian oocytes store mRNAs has remained elusive. Cheng\n et al\n . discovered that mammalian oocytes, including those in humans, store maternal mRNAs around the mitochondria in a membraneless compartment with hydrogel-like properties. The RNA-binding protein ZAR1 drives the assembly of this compartment, which clusters the mitochondria and protects the mRNAs against degradation. —SMH"],["dc.description.abstract","A membraneless compartment clusters mitochondria and stores maternal mRNAs in oocytes of various mammalian species."],["dc.description.abstract","INTRODUCTION\n Mammalian oocytes accumulate a large number of messenger RNAs (mRNAs) through active transcription as they grow. Transcription ceases during the final stages of oocyte growth and only resumes when the embryonic genome is activated after fertilization. During this period, the oocyte and the embryo can only use the stored mRNAs to synthesize new proteins. Proper storage of maternal mRNAs is thus critical for the maturation of oocytes into fertilizable eggs through meiosis and for early embryonic development after fertilization. However, where and how maternal mRNAs are stored in mammalian oocytes, including human oocytes, has remained elusive.\n \n \n RATIONALE\n \n RNAs are often stored in membraneless compartments that form by spontaneous phase separation of proteins and/or nucleic acids. Previous studies identified different types of membraneless compartments that store mRNAs in non-mammalian oocytes, such as P granules in\n Caenorhabditis elegans\n and Polar granules in\n Drosophila\n . We thus set out to identify potential RNA storage compartments in mammalian oocytes.\n \n \n \n RESULTS\n We analyzed the localization of RNA-binding proteins that were highly expressed in mouse oocytes. We found that the RNA-binding proteins ZAR1, YBX2, DDX6, LSM14B, and 4E-T (EIF4ENIF1) co-localized with mitochondria, forming clusters throughout the cytoplasm. By contrast, they did not co-localize with the Golgi apparatus, recycling endosomes, or lysosomes, and only partially co-localized with the endoplasmic reticulum. Additionally, we stained mRNAs using RNA fluorescence in situ hybridization and found that they were stored in this mitochondria-associated domain. This domain was also present in oocytes of other mammalian species, including humans. Because this domain was distinct from any known RNA-containing compartment, we named it mitochondria-associated ribonucleoprotein domain, or MARDO for short.\n \n MARDO assembly around mitochondria was directed by an increase in mitochondrial membrane potential during oocyte growth. The MARDO gradually appeared as oocytes grew and became most prominent in full-grown oocytes, the mitochondria of which are also the most active. Among the MARDO-localized RNA-binding proteins, ZAR1 played a major role in the assembly of the MARDO. ZAR1, but not other RNA-binding proteins, promoted the coalescence of MARDO foci into hydrogel-like matrices when overexpressed. MARDO coalescence drove the aggregation of mitochondria into giant clusters. Through a series of in vivo and in vitro experiments, we found that the unstructured N-terminal domain of ZAR1 was essential for MARDO assembly and its association with mitochondria. We depleted ZAR1 by gene knockout, RNA interference, and Trim-Away and found that both MARDO formation and mitochondrial clustering were impaired. MARDO formation and mitochondrial clustering were restored by expressing ZAR1 in\n Zar1\n -knockout oocytes. These results confirmed that ZAR1 is essential for MARDO assembly and mitochondrial clustering. Furthermore, live-cell imaging analyses showed that loss of ZAR1 caused severe defects in spindle assembly, chromosome alignment, and cytokinesis during oocyte meiotic maturation.\n \n The MARDO stored translationally repressed mRNAs, some of which are known to become translationally activated during the maturation of oocytes into fertilizable eggs or after fertilization. Loss of ZAR1 not only disrupted the MARDO, but also caused a premature loss of MARDO-localized mRNAs. Maternal mRNAs need to be progressively degraded and replaced by mRNAs transcribed from the embryonic genome to ensure proper embryonic development. The MARDO dissolved during the transition from meiosis I to meiosis II because of proteasomal degradation of ZAR1, which was essential for the timely degradation of maternal mRNAs.\n \n \n CONCLUSION\n In this study, we identified the MARDO, a mitochondria-associated membraneless compartment that stores maternal mRNAs in oocytes of various mammalian species, including humans. Our data reveal how the MARDO coordinates maternal mRNA storage, translation, and degradation to ensure fertility in mammals. The RNA-binding protein ZAR1 promotes MARDO assembly and coalescence into clusters. The MARDO stores translationally repressed mRNAs, some of which are translated during later stages of development. Proteasomal degradation of ZAR1 drives MARDO dissolution in mature eggs to ensure the timely degradation of maternal mRNAs.\n Our data also reveal physical and functional interactions between the membraneless MARDO and membrane-bound mitochondria, both of which are maternally contributed compounds that accumulate during oocyte growth.\n \n \n The MARDO in a mouse oocyte.\n The MARDO (ZAR1, green) assembles around mitochondria (cytochrome c, magenta), where it stores maternal mRNAs. Insets are magnifications of outlined regions showing the accumulation of the MARDO around an individual mitochondrion. Scale bar, 2 μm."],["dc.identifier.doi","10.1126/science.abq4835"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/116734"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-605"],["dc.relation.eissn","1095-9203"],["dc.relation.issn","0036-8075"],["dc.title","Mammalian oocytes store mRNAs in a mitochondria-associated membraneless compartment"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","627"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Astronomy and Astrophysics"],["dc.bibliographiccitation.lastpage","640"],["dc.bibliographiccitation.volume","477"],["dc.contributor.author","Costa, J. E. S."],["dc.contributor.author","Kepler, S. O."],["dc.contributor.author","Winget, D. E."],["dc.contributor.author","O'Brien, M. S."],["dc.contributor.author","Kawaler, S. D."],["dc.contributor.author","Costa, A. F. M."],["dc.contributor.author","Giovannini, O."],["dc.contributor.author","Kanaan, A."],["dc.contributor.author","Mukadam, A. S."],["dc.contributor.author","Mullally, F."],["dc.contributor.author","Nitta, A."],["dc.contributor.author","Provençal, J. L."],["dc.contributor.author","Shipman, H."],["dc.contributor.author","Wood, M. A."],["dc.contributor.author","Ahrens, T. J."],["dc.contributor.author","Grauer, A."],["dc.contributor.author","Kilic, M."],["dc.contributor.author","Bradley, P. A."],["dc.contributor.author","Sekiguchi, K."],["dc.contributor.author","Crowe, R."],["dc.contributor.author","Jiang, X. J."],["dc.contributor.author","Sullivan, D."],["dc.contributor.author","Sullivan, T."],["dc.contributor.author","Rosen, R."],["dc.contributor.author","Clemens, J. C."],["dc.contributor.author","Janulis, R."],["dc.contributor.author","O'Donoghue, D."],["dc.contributor.author","Ogloza, W."],["dc.contributor.author","Baran, A."],["dc.contributor.author","Silvotti, R."],["dc.contributor.author","Marinoni, S."],["dc.contributor.author","Vauclair, G."],["dc.contributor.author","Dolez, N."],["dc.contributor.author","Chevreton, M."],["dc.contributor.author","Dreizler, S."],["dc.contributor.author","Schuh, S."],["dc.contributor.author","Deetjen, J."],["dc.contributor.author","Nagel, T."],["dc.contributor.author","Solheim, J.-E."],["dc.contributor.author","Gonzalez Perez, J. M."],["dc.contributor.author","Ulla, A."],["dc.contributor.author","Barstow, M."],["dc.contributor.author","Burleigh, M."],["dc.contributor.author","Good, S."],["dc.contributor.author","Metcalfe, T. S."],["dc.contributor.author","Kim, S.-L."],["dc.contributor.author","Lee, H."],["dc.contributor.author","Sergeev, A."],["dc.contributor.author","Akan, M. C."],["dc.contributor.author","Çakırlı, Ö."],["dc.contributor.author","Paparo, M."],["dc.contributor.author","Viraghalmy, G."],["dc.contributor.author","Ashoka, B. N."],["dc.contributor.author","Handler, G."],["dc.contributor.author","Hürkal, Ö."],["dc.contributor.author","Johannessen, F."],["dc.contributor.author","Kleinman, S. J."],["dc.contributor.author","Kalytis, R."],["dc.contributor.author","Krzesinski, J."],["dc.contributor.author","Klumpe, E."],["dc.contributor.author","Larrison, J."],["dc.contributor.author","Lawrence, T."],["dc.contributor.author","Meištas, E."],["dc.contributor.author","Martinez, P."],["dc.contributor.author","Nather, R. E."],["dc.contributor.author","Fu, J.-N."],["dc.contributor.author","Pakštienė, E."],["dc.contributor.author","Romero-Colmenero, E."],["dc.contributor.author","Riddle, R."],["dc.contributor.author","Seetha, S."],["dc.contributor.author","Silvestri, N. M."],["dc.contributor.author","Vučković, M."],["dc.contributor.author","Warner, B."],["dc.contributor.author","Zola, S."],["dc.contributor.author","Althaus, L. G."],["dc.contributor.author","Córsico, A. H."],["dc.contributor.author","Montgomery, M. H."],["dc.date.accessioned","2019-07-09T11:53:29Z"],["dc.date.available","2019-07-09T11:53:29Z"],["dc.date.issued","2008"],["dc.description.abstract","Context. PG 1159-035, a pre-white dwarf with Teff 140 000 K, is the prototype of both two classes: the PG 1159 spectroscopic class and the DOV pulsating class. Previous studies of PG 1159-035 photometric data obtained with the Whole Earth Telescope (WET) showed a rich frequency spectrum allowing the identification of 122 pulsation modes. Analyzing the periods of pulsation, it is possible to measure the stellar mass, the rotational period and the inclination of the rotation axis, to estimate an upper limit for the magnetic field, and even to obtain information about the inner stratification of the star. Aims. We have three principal aims: to increase the number of detected and identified pulsation modes in PG 1159-035, study trapping of the star’s pulsation modes, and to improve or constrain the determination of stellar parameters. Methods. We used all available WET photometric data from 1983, 1985, 1989, 1993 and 2002 to identify the pulsation periods. Results. We identified 76 additional pulsation modes, increasing to 198 the number of known pulsation modes in PG 1159-035, the largest number of modes detected in any star besides the Sun. From the period spacing we estimated a mass M/M = 0.59 ± 0.02 for PG 1159-035, with the uncertainty dominated by the models, not the observation. Deviations in the regular period spacing suggest that some of the pulsation modes are trapped, even though the star is a pre-white dwarf and the gravitational settling is ongoing. The position of the transition zone that causes the mode trapping was calculated at rc/R = 0.83 ± 0.05. From the multiplet splitting, we calculated the rotational period Prot = 1.3920 ± 0.0008 days and an upper limit for the magnetic field, B < 2000 G. The total power of the pulsation modes at the stellar surface changed less than 30% for = 1 modes and less than 50% for = 2 modes. We find no evidence of linear combinations between the 198 pulsation mode frequencies. PG 1159-035 models have not significative convection zones, supporting the hypothesis that nonlinearity arises in the convection zones in cooler pulsating white dwarf stars."],["dc.identifier.doi","10.1051/0004-6361:20053470"],["dc.identifier.fs","513378"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/7676"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/60434"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.orgunit","Fakultät für Physik"],["dc.rights","Goescholar"],["dc.rights.access","openAccess"],["dc.rights.uri","https://goedoc.uni-goettingen.de/licenses"],["dc.title","The pulsation modes of the pre-white dwarf PG 1159-035"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","381"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Annual Review of Cell and Developmental Biology"],["dc.bibliographiccitation.lastpage","403"],["dc.bibliographiccitation.volume","34"],["dc.contributor.author","Mogessie, Binyam"],["dc.contributor.author","Scheffler, Kathleen"],["dc.contributor.author","Schuh, Melina"],["dc.date.accessioned","2022-03-01T11:43:45Z"],["dc.date.available","2022-03-01T11:43:45Z"],["dc.date.issued","2018"],["dc.description.abstract","Fertilizable eggs develop from diploid precursor cells termed oocytes. Once every menstrual cycle, an oocyte matures into a fertilizable egg in the ovary. To this end, the oocyte eliminates half of its chromosomes into a small cell termed a polar body. The egg is then released into the Fallopian tube, where it can be fertilized. Upon fertilization, the egg completes the second meiotic division, and the mitotic division of the embryo starts. This review highlights recent work that has shed light on the cytoskeletal structures that drive the meiotic divisions of the oocyte in mammals. In particular, we focus on how mammalian oocytes assemble a microtubule spindle in the absence of centrosomes, how they position the spindle in preparation for polar body extrusion, and how the spindle segregates the chromosomes. We primarily focus on mouse oocytes as a model system but also highlight recent insights from human oocytes."],["dc.description.abstract","Fertilizable eggs develop from diploid precursor cells termed oocytes. Once every menstrual cycle, an oocyte matures into a fertilizable egg in the ovary. To this end, the oocyte eliminates half of its chromosomes into a small cell termed a polar body. The egg is then released into the Fallopian tube, where it can be fertilized. Upon fertilization, the egg completes the second meiotic division, and the mitotic division of the embryo starts. This review highlights recent work that has shed light on the cytoskeletal structures that drive the meiotic divisions of the oocyte in mammals. In particular, we focus on how mammalian oocytes assemble a microtubule spindle in the absence of centrosomes, how they position the spindle in preparation for polar body extrusion, and how the spindle segregates the chromosomes. We primarily focus on mouse oocytes as a model system but also highlight recent insights from human oocytes."],["dc.identifier.doi","10.1146/annurev-cellbio-100616-060553"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/102834"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","1530-8995"],["dc.relation.issn","1081-0706"],["dc.title","Assembly and Positioning of the Oocyte Meiotic Spindle"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","572"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Obstetrical & Gynecological Survey"],["dc.bibliographiccitation.lastpage","573"],["dc.bibliographiccitation.volume","70"],["dc.contributor.author","Holubcová, Zuzana"],["dc.contributor.author","Blayney, Martyn"],["dc.contributor.author","Elder, Kay"],["dc.contributor.author","Schuh, Melina"],["dc.date.accessioned","2022-03-01T11:46:52Z"],["dc.date.available","2022-03-01T11:46:52Z"],["dc.date.issued","2015"],["dc.identifier.doi","10.1097/OGX.0000000000000240"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103828"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.issn","0029-7828"],["dc.title","Error-Prone Chromosome-Mediated Spindle Assembly Favors Chromosome Segregation Defects in Human Oocytes"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","410"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Nature Reviews Molecular Cell Biology"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Schuh, Melina"],["dc.date.accessioned","2017-09-07T11:48:50Z"],["dc.date.available","2017-09-07T11:48:50Z"],["dc.date.issued","2012"],["dc.identifier.doi","10.1038/nrm3370"],["dc.identifier.gro","3142504"],["dc.identifier.isi","000305809700008"],["dc.identifier.pmid","22644453"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8863"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Medical Research Council [MC_U105192711]"],["dc.notes.intern","unklar, ob ein so kurzer Artikel peer-reviewed ist"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1471-0072"],["dc.title","Goodbye homunculus"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","letter_note"],["dspace.entity.type","Publication"]]