Lytovchenko, Oleksandr

[["dc.bibliographiccitation.firstpage","643"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","The Journal of Cell Biology"],["dc.bibliographiccitation.lastpage","656"],["dc.bibliographiccitation.volume","195"],["dc.contributor.author","Schulz, Christian"],["dc.contributor.author","Lytovchenko, Oleksandr"],["dc.contributor.author","Melin, Jonathan"],["dc.contributor.author","Chacinska, Agnieszka"],["dc.contributor.author","Guiard, Bernard"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2017-09-07T11:43:19Z"],["dc.date.available","2017-09-07T11:43:19Z"],["dc.date.issued","2011"],["dc.description.abstract","N-terminal targeting signals (presequences) direct proteins across the TOM complex in the outer mitochondrial membrane and the TIM23 complex in the inner mitochondrial membrane. Presequences provide directionality to the transport process and regulate the transport machineries during translocation. However, surprisingly little is known about how presequence receptors interact with the signals and what role these interactions play during preprotein transport. Here, we identify signal-binding sites of presequence receptors through photo-affinity labeling. Using engineered presequence probes, photo cross-linking sites on mitochondrial proteins were mapped mass spectrometrically, thereby defining a presequence-binding domain of Tim50, a core subunit of the TIM23 complex that is essential for mitochondrial protein import. Our results establish Tim50 as the primary presequence receptor at the inner membrane and show that targeting signals and Tim50 regulate the Tim23 channel in an antagonistic manner."],["dc.identifier.doi","10.1083/jcb.201105098"],["dc.identifier.gro","3142630"],["dc.identifier.isi","000297206400012"],["dc.identifier.pmid","22065641"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/8033"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/55"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Rockefeller Univ Press"],["dc.relation.issn","0021-9525"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Tim50's presequence receptor domain is essential for signal driven transport across the TIM23 complex"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","247"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Molecular Biology of the Cell"],["dc.bibliographiccitation.lastpage","257"],["dc.bibliographiccitation.volume","23"],["dc.contributor.author","Alkhaja, Alwaleed K."],["dc.contributor.author","Jans, Daniel C."],["dc.contributor.author","Nikolov, Miroslav"],["dc.contributor.author","Vukotic, Milena"],["dc.contributor.author","Lytovchenko, Oleksandr"],["dc.contributor.author","Ludewig, Fabian"],["dc.contributor.author","Schliebs, Wolfgang"],["dc.contributor.author","Riedel, Dietmar"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Jakobs, Stefan"],["dc.contributor.author","Deckers, Markus"],["dc.date.accessioned","2017-09-07T11:49:01Z"],["dc.date.available","2017-09-07T11:49:01Z"],["dc.date.issued","2012"],["dc.description.abstract","The inner membrane of mitochondria is especially protein rich and displays a unique morphology characterized by large invaginations, the mitochondrial cristae, and the inner boundary membrane, which is in proximity to the outer membrane. Mitochondrial inner membrane proteins appear to be not evenly distributed in the inner membrane, but instead organize into functionally distinct subcompartments. It is unknown how the organization of the inner membrane is achieved. We identified MINOS1/MIO10 (C1orf151/YCL057C-A), a conserved mitochondrial inner membrane protein. mio10-mutant yeast cells are affected in growth on nonfermentable carbon sources and exhibit altered mitochondrial morphology. At the ultrastructural level, mutant mitochondria display loss of inner membrane organization. Proteomic analyses reveal MINOS1/Mio10 as a novel constituent of Mitofilin/Fcj1 complexes in human and yeast mitochondria. Thus our analyses reveal new insight into the composition of the mitochondrial inner membrane organizing machinery."],["dc.identifier.doi","10.1091/mbc.E11-09-0774"],["dc.identifier.gro","3142588"],["dc.identifier.isi","000299108000002"],["dc.identifier.pmid","22114354"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/7823"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8955"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1059-1524"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","MINOS1 is a conserved component of mitofilin complexes and required for mitochondrial function and cristae organization"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1624"],["dc.bibliographiccitation.issue","15"],["dc.bibliographiccitation.journal","EMBO Journal"],["dc.bibliographiccitation.lastpage","1727"],["dc.bibliographiccitation.volume","33"],["dc.contributor.author","Lytovchenko, Oleksandr"],["dc.contributor.author","Naumenko, Nataliia"],["dc.contributor.author","Oeljeklaus, Silke"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","von der Malsburg, Karina"],["dc.contributor.author","Deckers, Markus"],["dc.contributor.author","Warscheid, Bettina"],["dc.contributor.author","van der Laan, Martin"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2017-09-07T11:45:41Z"],["dc.date.available","2017-09-07T11:45:41Z"],["dc.date.issued","2014"],["dc.description.abstract","Mitochondrial F1Fo-ATP synthase generates the bulk of cellular ATP. This molecular machine assembles from nuclear- and mitochondria-encoded subunits. Whereas chaperones for formation of the matrix-exposed hexameric F-1-ATPase core domain have been identified, insight into how the nuclear-encoded F-1-domain assembles with the membrane-embedded F-o-region is lacking. Here we identified the INA complex (INAC) in the inner membrane of mitochondria as an assembly factor involved in this process. Ina22 and Ina17 are INAC constituents that physically associate with the F-1-module and peripheral stalk, but not with the assembled F1Fo-ATP synthase. Our analyses show that loss of Ina22 and Ina17 specifically impairs formation of the peripheral stalk that connects the catalytic F-1-module to the membrane embedded F-o-domain. We conclude that INAC represents a matrix-exposed inner membrane protein complex that facilitates peripheral stalk assembly and thus promotes a key step in the biogenesis of mitochondrial F1Fo-ATP synthase."],["dc.identifier.doi","10.15252/embj.201488076"],["dc.identifier.gro","3142082"],["dc.identifier.isi","000339917000005"],["dc.identifier.pmid","24942160"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/4345"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1460-2075"],["dc.relation.issn","0261-4189"],["dc.title","The INA complex facilitates assembly of the peripheral stalk of the mitochondrial F1Fo-ATP synthase"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","660"],["dc.bibliographiccitation.issue","17-18"],["dc.bibliographiccitation.journal","Wiener klinische Wochenschrift"],["dc.bibliographiccitation.lastpage","661"],["dc.bibliographiccitation.volume","124"],["dc.contributor.author","Fromm-Dornieden, Carolin"],["dc.contributor.author","Heyde, Silvia von der"],["dc.contributor.author","Lytovchenko, Oleksandr"],["dc.contributor.author","Salinas-Riester, Gabriela"],["dc.contributor.author","Brenig, Bertram B."],["dc.contributor.author","Beißbarth, Tim"],["dc.contributor.author","Baumgartner, Bernhard G."],["dc.date.accessioned","2018-11-07T09:06:27Z"],["dc.date.available","2018-11-07T09:06:27Z"],["dc.date.issued","2012"],["dc.identifier.isi","000309233400021"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/25562"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","Wien"],["dc.title","Identification of new translationally regulated genes in early Adipogenesis"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","9"],["dc.bibliographiccitation.journal","BMC Molecular Biology"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Fromm-Dornieden, Carolin"],["dc.contributor.author","Heyde, Silvia von der"],["dc.contributor.author","Lytovchenko, Oleksandr"],["dc.contributor.author","Salinas-Riester, Gabriela"],["dc.contributor.author","Brenig, Bertram B."],["dc.contributor.author","Beißbarth, Tim"],["dc.contributor.author","Baumgartner, Bernhard G."],["dc.date.accessioned","2018-11-07T09:12:11Z"],["dc.date.available","2018-11-07T09:12:11Z"],["dc.date.issued","2012"],["dc.description.abstract","Background: Control of translation allows for rapid adaptation of the cell to stimuli, rather than the slower transcriptional control. We presume that translational control is an essential process in the control of adipogenesis, especially in the first hours after hormonal stimulation. 3T3-L1 preadipocytes were cultured to confluency and adipogenesis was induced by standard protocols using a hormonal cocktail. Cells were harvested before and 6 hours after hormonal induction. mRNAs attached to ribosomes (polysomal mRNAs) were separated from unbound mRNAs by velocity sedimentation. Pools of polysomal and unbound mRNA fractions were analyzed by microarray analysis. Changes in relative abundance in unbound and polysomal mRNA pools were calculated to detect putative changes in translational activity. Changes of expression levels of selected genes were verified by qPCR and Western blotting. Results: We identified 43 genes that shifted towards the polysomal fraction (up-regulated) and 2 genes that shifted towards free mRNA fraction (down-regulated). Interestingly, we found Ghrelin to be down-regulated. Upregulated genes comprise factors that are nucleic acid binding (eIF4B, HSF1, IRF6, MYC, POLR2a, RPL18, RPL27a, RPL6, RPL7a, RPS18, RPSa, TSC22d3), form part of ribosomes (RPL18, RPL27a, RPL6, RPL7a, RPS18, RPSa), act on the regulation of translation (eIF4B) or transcription (HSF1, IRF6, MYC, TSC22d3). Others act as chaperones (BAG3, HSPA8, HSP90ab1) or in other metabolic or signals transducing processes. Conclusions: We conclude that a moderate reorganisation of the functionality of the ribosomal machinery and translational activity are very important steps for growth and gene expression control in the initial phase of adipogenesis."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2012"],["dc.identifier.doi","10.1186/1471-2199-13-9"],["dc.identifier.isi","000303817800001"],["dc.identifier.pmid","22436005"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/7594"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/26895"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Biomed Central Ltd"],["dc.relation.issn","1471-2199"],["dc.rights","CC BY 2.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/2.0"],["dc.title","Novel polysome messages and changes in translational activity appear after induction of adipogenesis in 3T3-L1 cells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1850"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Biochimica et Biophysica Acta (BBA) - Molecular Cell Research"],["dc.bibliographiccitation.lastpage","1859"],["dc.bibliographiccitation.volume","1853"],["dc.contributor.author","Melin, Jonathan"],["dc.contributor.author","Kilisch, Markus"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Lytovchenko, Oleksandr"],["dc.contributor.author","Gomkale, Ridhima"],["dc.contributor.author","Schendzielorz, Alexander Benjamin"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Liepold, Thomas"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Schulz, Christian"],["dc.date.accessioned","2017-09-07T11:43:40Z"],["dc.date.available","2017-09-07T11:43:40Z"],["dc.date.issued","2015"],["dc.description.abstract","The translocase of the outer mitochondrial membrane (TOM complex) is the general entry gate into mitochondria for almost all imported proteins. A variety of specific receptors allow the TOM complex to recognize targeting signals of various precursor proteins that are transported along different import pathways. Aside from the well-characterized presequence receptors Tom20 and Tom22 a third TOM receptor, Tom70, binds proteins of the carrier family containing multiple transmembrane segments. Here we demonstrate that Tom70 directly binds to presequence peptides using a dedicated groove. A single point mutation in the cavity of this pocket (M551R) reduces the presequence binding affinity of Tom70 ten-fold and selectively impairs import of the presequence-containing precursor Mdl1 but not the ADP/ATP carrier (MC). Hence Tom70 contributes to the presequence import pathway by recognition of the targeting signal of the Mdl1 precursor. (C) 2015 Elsevier B.V. All rights reserved."],["dc.identifier.doi","10.1016/j.bbamcr.2015.04.021"],["dc.identifier.gro","3141858"],["dc.identifier.isi","000356209600009"],["dc.identifier.pmid","25958336"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1856"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","0006-3002"],["dc.relation.issn","0167-4889"],["dc.title","A presequence-binding groove in Tom70 supports import of Mdl1 into mitochondria"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","86"],["dc.bibliographiccitation.journal","Nutrition & Metabolism"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Fromm-Dornieden, Carolin"],["dc.contributor.author","Lytovchenko, Oleksandr"],["dc.contributor.author","Heyde, Silvia von der"],["dc.contributor.author","Behnke, Nina"],["dc.contributor.author","Hogl, Sebastian"],["dc.contributor.author","Berghoff, Janina"],["dc.contributor.author","Koepper, Frederik"],["dc.contributor.author","Opitz, Lennart"],["dc.contributor.author","Renne, Ulla"],["dc.contributor.author","Hoeflich, Andreas"],["dc.contributor.author","Beißbarth, Tim"],["dc.contributor.author","Brenig, Bertram B."],["dc.contributor.author","Baumgartner, Bernhard G."],["dc.date.accessioned","2018-11-07T09:05:46Z"],["dc.date.available","2018-11-07T09:05:46Z"],["dc.date.issued","2012"],["dc.description.abstract","Background: DOR/TP53INP2 acts both at the chromosomal level as a nuclear co-factor e.g. for the thyroid hormone receptor and at the extrachromosomal level as an organizing factor of the autophagosome. In a previous study, DOR was shown to be down-regulated in skeletal muscle of obese diabetic Zucker fa/fa rats. Methods: To identify sites of differential DOR expression in metabolically active tissues, we measured differences in DOR expression in white adipose tissue (WAT), brown adipose tissue (BAT), skeletal muscle (SM) and heart muscle (HM) by qPCR. To assess whether DOR expression is influenced in the short term by nutritional factors, NMRI mice were fed different fat rich diets (fat diet, FD: 18% or high fat diet, HFD: 80% fat) for one week and DOR expression was compared to NMRI mice fed a control diet (normal diet, ND: 3.3% fat). Additionally, DOR expression was measured in young (45 days old) and adult (100 days old) genetically obese (DU6/DU6i) mice and compared to control (DUKs/DUKsi) animals. Results: ANOVA results demonstrate a significant influence of diet, tissue type and sex on DOR expression in adipose and muscle tissues of FD and HFD mice. In SM, DOR expression was higher in HFD than in FD male mice. In WAT, DOR expression was increased compared to BAT in male FD and HFD mice. In contrast, expression levels in female mice were higher in BAT for both dietary conditions. DOR expression levels in all tissues of 100 days old genetically obese animals were mainly influenced by sex. In HM, DOR expression was higher in male than female animals. Conclusions: DOR expression varies under the influence of dietary fat content, tissue type and sex. We identified target tissues for further studies to analyze the specific function of DOR in obesity. DOR might be part of a defense mechanism against fat storage in high fat diets or obesity."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2012"],["dc.identifier.doi","10.1186/1743-7075-9-86"],["dc.identifier.isi","000311434000001"],["dc.identifier.pmid","22995226"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/8284"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/25404"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Biomed Central Ltd"],["dc.relation.issn","1743-7075"],["dc.rights","CC BY 2.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/2.0"],["dc.title","Extrinsic and intrinsic regulation of DOR/TP53INP2 expression in mice: effects of dietary fat content, tissue type and sex in adipose and muscle tissues"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","886"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","EMBO Journal"],["dc.bibliographiccitation.lastpage","898"],["dc.bibliographiccitation.volume","32"],["dc.contributor.author","Lytovchenko, Oleksandr"],["dc.contributor.author","Melin, Jonathan"],["dc.contributor.author","Schulz, Christian"],["dc.contributor.author","Kilisch, Markus"],["dc.contributor.author","Hutu, Dana P."],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2017-09-07T11:47:45Z"],["dc.date.available","2017-09-07T11:47:45Z"],["dc.date.issued","2013"],["dc.description.abstract","The mitochondrial presequence translocase interacts with presequence-containing precursors at the intermembrane space (IMS) side of the inner membrane to mediate their translocation into the matrix. Little is known as too how these matrix-targeting signals activate the translocase in order to initiate precursor transport. Therefore, we analysed how signal recognition by the presequence translocase initiates reorganization among Tim-proteins during import. Our analyses revealed that the presequence receptor Tim50 interacts with Tim21 in a signal-sensitive manner in a process that involves the IMS-domain of the Tim23 channel. The signal-driven release of Tim21 from Tim50 promotes recruitment of Pam17 and thus triggers formation of the motor-associated form of the TIM23 complex required for matrix transport. The EMBO Journal (2013) 32, 886-898. doi:10.1038/emboj.2013.23; Published online 12 February 2013"],["dc.identifier.doi","10.1038/emboj.2013.23"],["dc.identifier.gro","3142372"],["dc.identifier.isi","000316463600013"],["dc.identifier.pmid","23403928"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/7552"],["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","0261-4189"],["dc.title","Signal recognition initiates reorganization of the presequence translocase during protein import"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Wiener klinische Wochenschrift"],["dc.bibliographiccitation.volume","123"],["dc.contributor.author","Fromm-Dornieden, Carolin"],["dc.contributor.author","Lytovchenko, Oleksandr"],["dc.contributor.author","Salinas-Riester, Gabriela"],["dc.contributor.author","Heyde, Silvia von der"],["dc.contributor.author","Beißbarth, Tim"],["dc.contributor.author","Brenig, Bertram B."],["dc.contributor.author","Baumgartner, Bernhard G."],["dc.date.accessioned","2018-11-07T08:50:04Z"],["dc.date.available","2018-11-07T08:50:04Z"],["dc.date.issued","2011"],["dc.identifier.isi","000298356200044"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/21605"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","Wien"],["dc.title","Management of early Adipogenesis through Translational Control"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2905"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Infection and Immunity"],["dc.bibliographiccitation.lastpage","2912"],["dc.bibliographiccitation.volume","76"],["dc.contributor.author","Hippe, Diana"],["dc.contributor.author","Lytovchenko, Oleksandr"],["dc.contributor.author","Schmitz, Ingo"],["dc.contributor.author","Lueder, Carsten Guenter Kurt"],["dc.date.accessioned","2018-11-07T11:13:30Z"],["dc.date.available","2018-11-07T11:13:30Z"],["dc.date.issued","2008"],["dc.description.abstract","The intracellular protozoan Toxoplasma gondii induces persistent infections in various hosts and is an important opportunistic pathogen of humans with immature or deficient immune responses. The ability to survive intracellularly largely depends on the blocking of different proapoptotic signaling cascades of its host cell. Fas/CD95 triggers an apoptotic cascade that is crucial for immunity and the outcome of infectious diseases. We have determined the mechanism by which T. gondii counteracts death receptor-mediated cell death in type II cells that transduce Fas/CD95 ligation via caspase 8-mediated activation of the mitochondrial amplification loop. The results showed that infection with T. gondii significantly reduced Fas/CD95-triggered apoptosis in HeLa cells by inhibiting the activities of initiator caspases 8 and 9 and effector caspase 3/7. Parasitic infection dose dependently diminished cleavage of caspase 8, the BH3-only protein Bid, and the downstream caspases 9 and 3. Importantly, interference with Fas/CD95-triggered caspase 8 and caspase 3/7 activities after parasitic infection was largely dependent on the presence of caspase 9. Within the mitochondrial amplification loop, T. gondii significantly inhibited the Fas/CD95-triggered release of cytochrome c into the host cell cytosol. These results indicate that T. gondii inhibits Fas/CD95-mediated apoptosis in type II cells primarily by decreasing the apoptogenic function of mitochondria."],["dc.identifier.doi","10.1128/IAI.01546-07"],["dc.identifier.isi","000257172300011"],["dc.identifier.pmid","18411295"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/53912"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Microbiology"],["dc.relation.issn","0019-9567"],["dc.title","Fas/CD95-mediated apoptosis of type II cells is blocked by Toxoplasma gondii primarily via interference with the mitochondrial amplification loop"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]