Neumann, Heinz

[["dc.bibliographiccitation.firstpage","453"],["dc.bibliographiccitation.journal","Metabolic Engineering"],["dc.bibliographiccitation.lastpage","462"],["dc.bibliographiccitation.volume","47"],["dc.contributor.author","Heitmüller, Svenja"],["dc.contributor.author","Neumann-Staubitz, Petra"],["dc.contributor.author","Herrfurth, Cornelia"],["dc.contributor.author","Feussner, Ivo"],["dc.contributor.author","Neumann, Heinz"],["dc.date.accessioned","2020-12-10T15:21:49Z"],["dc.date.available","2020-12-10T15:21:49Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1016/j.ymben.2018.04.022"],["dc.identifier.issn","1096-7176"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/73173"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Cellular substrate limitations of lysine acetylation turnover by sirtuins investigated with engineered futile cycle enzymes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","131"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Pathogens and Disease"],["dc.bibliographiccitation.lastpage","137"],["dc.bibliographiccitation.volume","72"],["dc.contributor.author","Rakebrandt, Nikolas"],["dc.contributor.author","Lentes, Sabine"],["dc.contributor.author","Neumann, Heinz"],["dc.contributor.author","James, Leo C."],["dc.contributor.author","Neumann-Staubitz, Petra"],["dc.date.accessioned","2018-11-07T09:33:05Z"],["dc.date.available","2018-11-07T09:33:05Z"],["dc.date.issued","2014"],["dc.description.abstract","TRIM21 (tripartite motif-containing protein 21', Ro52) is a ubiquitously expressed cytosolic Fc receptor, which has a potent role in protective immunity against nonenveloped viruses. TRIM21 mediates intracellular neutralisation of antibody-coated viruses, a process called ADIN (antibody-dependent intracellular neutralisation). Our results reveal a similar mechanism to fight bacterial infections. TRIM21 is recruited to the intracellular pathogen Salmonella enterica in epithelial cells early in infection. TRIM21 does not bind directly to S.enterica, but to antibodies opsonising it. Most importantly, bacterial restriction is dependent on TRIM21 as well as on the opsonisation state of the bacteria. Finally, Salmonella and TRIM21 colocalise with the autophagosomal marker LC3, and intracellular defence is enhanced in starved cells suggesting an involvement of the autophagocytic pathway. Our data extend the protective role of TRIM21 from viruses to bacteria and thereby strengthening the general role of ADIN in cellular immunity."],["dc.description.sponsorship","'Fonds der Chemischen Industrie'"],["dc.identifier.doi","10.1111/2049-632X.12192"],["dc.identifier.isi","000345151900006"],["dc.identifier.pmid","24920099"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/31890"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","2049-632X"],["dc.title","Antibody- and TRIM21-dependent intracellular restriction of Salmonella enterica"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","119"],["dc.bibliographiccitation.journal","Current Opinion in Structural Biology"],["dc.bibliographiccitation.lastpage","128"],["dc.bibliographiccitation.volume","38"],["dc.contributor.author","Neumann-Staubitz, Petra"],["dc.contributor.author","Neumann, Heinz"],["dc.date.accessioned","2018-11-07T10:13:00Z"],["dc.date.available","2018-11-07T10:13:00Z"],["dc.date.issued","2016"],["dc.description.abstract","The expansion of the genetic code for the incorporation of unnatural amino acids (UAAs) in proteins of bacteria, yeasts, mammalian cells or whole animals provides molecular and structural biologists with an amazing kit of novel tools. UAAs can be used to investigate the structure and dynamics of proteins, to study their interactions or to control their activity in living cells. Incorporation of UAAs with bioorthogonal reactivity facilitates the site-specific installation of labels for spectroscopy and microscopy. Light-activatable crosslinker UAAs can be used to trap interacting molecules in living cells with a precision almost at the structural level. Post-translational modifications such as lysine acetylation and serine phosphorylation can be directly encoded to analyse their impact on protein function, and caging groups can be installed on critical residues to create light-activatable proteins. In this review we highlight recent applications of this technology to investigate protein function."],["dc.identifier.doi","10.1016/j.sbi.2016.06.006"],["dc.identifier.isi","000383301900017"],["dc.identifier.pmid","27318816"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/40349"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Current Biology Ltd"],["dc.relation.issn","1879-033X"],["dc.relation.issn","0959-440X"],["dc.title","The use of unnatural amino acids to study and engineer protein function"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]