Now showing 1 - 2 of 2
  • 2018Journal Article Research Paper
    [["dc.bibliographiccitation.firstpage","130"],["dc.bibliographiccitation.journal","F1000Research"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Gabay-Maskit, Shiran"],["dc.contributor.author","Schuldiner, Maya"],["dc.contributor.author","Zalckvar, Einat"],["dc.date.accessioned","2022-07-04T13:17:12Z"],["dc.date.available","2022-07-04T13:17:12Z"],["dc.date.issued","2018"],["dc.description.abstract","Malate dehydrogenases (Mdhs) reversibly convert malate to oxaloacetate and serve as important enzymes in several metabolic pathways. In the yeast Saccharomyces cerevisiae there are three Mdh isozymes, localized to different compartments in the cell. In order to identify specifically the Mdh2 isozyme, GenScript USA produced three different antibodies that we further tested by western blot. All three antibodies recognized the S. cerevisiae Mdh2 with different background and specificity properties. One of the antibodies had a relatively low background and high specificity and thus can be used for specific identification of Mdh2 in various experimental settings."],["dc.identifier.doi","10.12688/f1000research.13396.2"],["dc.identifier.pmid","29568493"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/112376"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/21"],["dc.language.iso","en"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P11: Zuordnung zellulärer Kontaktstellen und deren Zusammenspiel"],["dc.relation.eissn","2046-1402"],["dc.relation.workinggroup","RG Schuldiner (Functional Genomics of Organelles)"],["dc.rights","CC BY 4.0"],["dc.title","Validation of a yeast malate dehydrogenase 2 (Mdh2) antibody tested for use in western blots"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]
    Details DOI PMID PMC
  • 2018Journal Article Research Paper
    [["dc.bibliographiccitation.firstpage","1761"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Shai, Nadav"],["dc.contributor.author","Yifrach, Eden"],["dc.contributor.author","van Roermund, Carlo W. T."],["dc.contributor.author","Cohen, Nir"],["dc.contributor.author","Bibi, Chen"],["dc.contributor.author","IJlst, Lodewijk"],["dc.contributor.author","Cavellini, Laetitia"],["dc.contributor.author","Meurisse, Julie"],["dc.contributor.author","Schuster, Ramona"],["dc.contributor.author","Zada, Lior"],["dc.contributor.author","Mari, Muriel C."],["dc.contributor.author","Reggiori, Fulvio M."],["dc.contributor.author","Hughes, Adam L."],["dc.contributor.author","Escobar-Henriques, Mafalda"],["dc.contributor.author","Cohen, Mickael M."],["dc.contributor.author","Waterham, Hans R."],["dc.contributor.author","Wanders, Ronald J. A."],["dc.contributor.author","Schuldiner, Maya"],["dc.contributor.author","Zalckvar, Einat"],["dc.date.accessioned","2022-07-04T13:23:53Z"],["dc.date.available","2022-07-04T13:23:53Z"],["dc.date.issued","2018"],["dc.description.abstract","The understanding that organelles are not floating in the cytosol, but rather held in an organized yet dynamic interplay through membrane contact sites, is altering the way we grasp cell biological phenomena. However, we still have not identified the entire repertoire of contact sites, their tethering molecules and functions. To systematically characterize contact sites and their tethering molecules here we employ a proximity detection method based on split fluorophores and discover four potential new yeast contact sites. We then focus on a little-studied yet highly disease-relevant contact, the Peroxisome-Mitochondria (PerMit) proximity, and uncover and characterize two tether proteins: Fzo1 and Pex34. We genetically expand the PerMit contact site and demonstrate a physiological function in β-oxidation of fatty acids. Our work showcases how systematic analysis of contact site machinery and functions can deepen our understanding of these structures in health and disease."],["dc.identifier.doi","10.1038/s41467-018-03957-8"],["dc.identifier.pmid","29720625"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/112378"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/29"],["dc.language.iso","en"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P11: Zuordnung zellulärer Kontaktstellen und deren Zusammenspiel"],["dc.relation.issn","2041-1723"],["dc.relation.workinggroup","RG Schuldiner (Functional Genomics of Organelles)"],["dc.rights","CC BY 4.0"],["dc.title","Systematic mapping of contact sites reveals tethers and a function for the peroxisome-mitochondria contact"],["dc.type","journal_article"],["dc.type.internalPublication","no"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]
    Details DOI PMID PMC