Katschinski, Dörthe Magdalena

[["dc.bibliographiccitation.firstpage","700"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Microcirculation"],["dc.bibliographiccitation.lastpage","710"],["dc.bibliographiccitation.volume","22"],["dc.contributor.author","Czepluch, Frauke S."],["dc.contributor.author","Vogler, Melanie"],["dc.contributor.author","Kuschicke, Hendrik"],["dc.contributor.author","Meier, Julia"],["dc.contributor.author","Gogiraju, Rajinikanth"],["dc.contributor.author","Katschinski, Dörthe M."],["dc.contributor.author","Riggert, Joachim"],["dc.contributor.author","Hasenfuß, Gerd"],["dc.contributor.author","Schaefer, Katrin"],["dc.date.accessioned","2017-09-07T11:43:27Z"],["dc.date.available","2017-09-07T11:43:27Z"],["dc.date.issued","2015"],["dc.description.abstract","Objective: The zinc finger transcription factor KLF4 is known to control diverse EC functions. Methods: The functional role of KLF4 for angiogenesis and its association with CAD was examined in HUVECs and human CECs. Results: In two different angiogenesis assays, siRNA-mediated KLF4 downregulation impaired HUVEC sprouting and network formation. Conversely, KLF4 overexpression increased HUVEC sprouting and network formation. Similar findings were observed after incubation of HUVECs with CdM from KLF4 cDNA-transfected cells, suggesting a role of paracrine factors for mediating angiogenic KLF4 effects. In this regard, VEGF expression was increased in KLF4-overexpressing HUVECs, whereas its expression was reduced in HUVECs transfected with KLF4 siRNA. To examine the relevance of our in vitro findings for human endothelial dysfunction, we analyzed the expression of KLF4 in CECs of patients with stable CAD. Flow cytometry analyses revealed decreased numbers of KLF4-positive CECs in peripheral blood from CAD patients compared to healthy controls. Conclusions: Our findings suggest that KLF4 may represent a potential biomarker for EC dysfunction. In the future, (therapeutic) modulation of KLF4 may be useful in regulating EC function during vascular disease processes."],["dc.identifier.doi","10.1111/micc.12226"],["dc.identifier.gro","3141793"],["dc.identifier.isi","000365387200003"],["dc.identifier.pmid","26214161"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1135"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1549-8719"],["dc.relation.issn","1073-9688"],["dc.title","Circulating Endothelial Cells Expressing the Angiogenic Transcription Factor Kruppel-Like Factor 4 are Decreased in Patients with Coronary Artery Disease"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3758"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Molecular and Cellular Biology"],["dc.bibliographiccitation.lastpage","3768"],["dc.bibliographiccitation.volume","27"],["dc.contributor.author","Barth, Sandra"],["dc.contributor.author","Nesper, Jutta"],["dc.contributor.author","Hasgall, Philippe A."],["dc.contributor.author","Wirthner, Renato"],["dc.contributor.author","Nytko, Katarzyna J."],["dc.contributor.author","Edlich, Frank"],["dc.contributor.author","Katschinski, Doerthe Magdalena"],["dc.contributor.author","Stiehl, Daniel P."],["dc.contributor.author","Wenger, Roland H."],["dc.contributor.author","Camenisch, Gieri"],["dc.date.accessioned","2018-11-07T11:02:54Z"],["dc.date.available","2018-11-07T11:02:54Z"],["dc.date.issued","2007"],["dc.description.abstract","The heterodimeric hypoxia-inducible transcription factors (HIFs) are central regulators of the response to low oxygenation. HIF-alpha subunits are constitutively expressed but rapidly degraded under normoxic conditions. Oxygen-dependent hydroxylation of two conserved prolyl residues by prolyl-4-hydroxylase domain-containing enzymes (PHDs) targets HIF-alpha for proteasomal destruction. We identified the peptidyl prolyl cis/trans isomerase FK506-binding protein 38 (FKBP38) as a novel interactor of PHD2. Yeast two-hybrid, glutathione S-transferase pull-down, coimmunoprecipitation, colocalization, and mammalian two-hybrid studies confirmed specific FKBP38 interaction with PHD2, but not with PHD1 or PHD3. PHD2 and FKBP38 associated with their N-terminal regions, which contain no known interaction motifs. Neither FKBP38 mRNA nor protein levels were regulated under hypoxic conditions or after PHD inhibition, suggesting that FKBP38 is not a HIF/PHD target. Stable RNA interference-mediated depletion of FKBP38 resulted in increased PHD hydroxylation activity and decreased HIF protein levels and transcriptional activity. Reconstitution of FKBP38 expression abolished these effects, which were independent of the peptidyl prolyl cis/trans isomerase activity. Downregulation of FKBP38 did not affect PHD2 mRNA levels but prolonged PHD2 protein stability, suggesting that FKBP38 is involved in PHD2 protein regulation."],["dc.identifier.doi","10.1128/MCB.01324-06"],["dc.identifier.isi","000246269400018"],["dc.identifier.pmid","17353276"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/51495"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Microbiology"],["dc.relation.issn","0270-7306"],["dc.title","The peptidyl prolyl cis/trans isomerase FKBP38 determines hypoxia-inducible transcription factor prolyl-4-hydroxylase PHD2 protein stability"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Acta Physiologica"],["dc.bibliographiccitation.volume","216"],["dc.contributor.author","Jatho, Aline"],["dc.contributor.author","Hartmann, S."],["dc.contributor.author","Kittana, Naim"],["dc.contributor.author","Muegge, F."],["dc.contributor.author","Wuertz, Christina"],["dc.contributor.author","Tiburcy, Malte"],["dc.contributor.author","Zimmermann, Wolfram-Hubertus"],["dc.contributor.author","Katschinski, Doerthe Magdalena"],["dc.contributor.author","Lutz, S."],["dc.date.accessioned","2018-11-07T10:17:27Z"],["dc.date.available","2018-11-07T10:17:27Z"],["dc.date.issued","2016"],["dc.identifier.isi","000372285400124"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/41230"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.publisher.place","Hoboken"],["dc.relation.issn","1748-1716"],["dc.relation.issn","1748-1708"],["dc.title","RhoA ambivalently controls prominent myofibroblast characteristics by involving distinct signaling routes"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Frontiers in Physiology"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Trautsch, Irina"],["dc.contributor.author","Heta, Eriona"],["dc.contributor.author","Soong, Poh Loong"],["dc.contributor.author","Levent, Elif"],["dc.contributor.author","Nikolaev, Viacheslav O."],["dc.contributor.author","Bogeski, Ivan"],["dc.contributor.author","Katschinski, Dörthe M."],["dc.contributor.author","Mayr, Manuel"],["dc.contributor.author","Zimmermann, Wolfram-Hubertus"],["dc.date.accessioned","2020-12-10T18:44:38Z"],["dc.date.available","2020-12-10T18:44:38Z"],["dc.date.issued","2019"],["dc.description.abstract","Redox signaling affects all aspects of cardiac function and homeostasis. With the development of genetically encoded fluorescent redox sensors, novel tools for the optogenetic investigation of redox signaling have emerged. Here, we sought to develop a human heart muscle model for in-tissue imaging of redox alterations. For this, we made use of (1) the genetically-encoded Grx1-roGFP2 sensor, which reports changes in cellular glutathione redox status (GSH/GSSG), (2) human embryonic stem cells (HES2), and (3) the engineered heart muscle (EHM) technology. We first generated HES2 lines expressing Grx1-roGFP2 in cytosol or mitochondria compartments by TALEN-guided genomic integration. Grx1-roGFP2 sensor localization and function was verified by fluorescence imaging. Grx1-roGFP2 HES2 were then subjected to directed differentiation to obtain high purity cardiomyocyte populations. Despite being able to report glutathione redox potential from cytosol and mitochondria, we observed dysfunctional sarcomerogenesis in Grx1-roGFP2 expressing cardiomyocytes. Conversely, lentiviral transduction of Grx1-roGFP2 in already differentiated HES2-cardiomyocytes and human foreskin fibroblast was possible, without compromising cell function as determined in EHM from defined Grx1-roGFP2-expressing cardiomyocyte and fibroblast populations. Finally, cell-type specific GSH/GSSG imaging was demonstrated in EHM. Collectively, our observations suggests a crucial role for redox signaling in cardiomyocyte differentiation and provide a solution as to how this apparent limitation can be overcome to enable cell-type specific GSH/GSSG imaging in a human heart muscle context."],["dc.identifier.doi","10.3389/fphys.2019.00272"],["dc.identifier.pmid","31024328"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/78535"],["dc.identifier.url","https://sfb1002.med.uni-goettingen.de/production/literature/publications/265"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/67"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.relation","SFB 1002: Modulatorische Einheiten bei Herzinsuffizienz"],["dc.relation","SFB 1002 | C04: Fibroblasten-Kardiomyozyten Interaktion im gesunden und erkrankten Herzen: Mechanismen und therapeutische Interventionen bei Kardiofibroblastopathien"],["dc.relation","SFB 1002 | S01: In vivo und in vitro Krankheitsmodelle"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P17: Die Rolle mitochondrialer Kontaktstellen im Rahmen tumorrelevanter Calcium- und Redox-Signalwege"],["dc.relation.eissn","1664-042X"],["dc.relation.workinggroup","RG Nikolaev (Cardiovascular Research Center)"],["dc.relation.workinggroup","RG Zimmermann (Engineered Human Myocardium)"],["dc.relation.workinggroup","RG Bogeski"],["dc.rights","http://creativecommons.org/licenses/by/4.0/"],["dc.title","Optogenetic Monitoring of the Glutathione Redox State in Engineered Human Myocardium"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3610"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Blood"],["dc.bibliographiccitation.lastpage","3617"],["dc.bibliographiccitation.volume","110"],["dc.contributor.author","Koditz, Jens"],["dc.contributor.author","Nesper, Jutta"],["dc.contributor.author","Wottawa, Marieke"],["dc.contributor.author","Stiehl, Daniel P."],["dc.contributor.author","Camenisch, Gieri"],["dc.contributor.author","Franke, Corinna"],["dc.contributor.author","Myllyharju, Johanna"],["dc.contributor.author","Wenger, Roland H."],["dc.contributor.author","Katschinski, Doerthe Magdalena"],["dc.date.accessioned","2018-11-07T10:53:15Z"],["dc.date.available","2018-11-07T10:53:15Z"],["dc.date.issued","2007"],["dc.description.abstract","The activating transcription factor-4 (ATF-4) is translationally induced under anoxic conditions, mediates part of the unfolded protein response following endoplasmic reticulum (ER) stress, and is a critical regulator of cell fate. Here, we identified the zipper 11 domain of ATF-4 to interact with the oxygen sensor prolyl-4-hydroxylase domain 3 (PHD3). The PHD inhibitors dimethyloxalylglycine (DMOG) and hypoxia, or proteasomal inhibition, all induced ATF-4 protein levels. Hypoxic induction of ATF-4 was due to increased protein stability, but was independent of the ubiquitin ligase von Hippel-Lindau protein (pVHL).,A novel oxygen-dependent degradation (ODD) domain was identified adjacent to the zipper 11 domain. Mutations of 5 prolyl residues within this ODD domain or siRNA-mediated down-regulation of PHD3, but not of PHD2, was sufficient to stabilize ATF-4 under normoxic conditions. These data demonstrate that PHD-dependent oxygen-sensing recruits both the hypoxia-inducible factor (HIF) and ATF-4 systems, and hence not only confers adaptive responses but also cell fate decisions."],["dc.identifier.doi","10.1182/blood-2007-06-094441"],["dc.identifier.isi","000250946300026"],["dc.identifier.pmid","17684156"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/49312"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Hematology"],["dc.relation.issn","0006-4971"],["dc.title","Oxygen-dependent ATF-4 stability is mediated by the PHD3 oxygen sensor"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","jcs223230"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Journal of Cell Science"],["dc.bibliographiccitation.volume","132"],["dc.contributor.author","Leinhos, Lisa"],["dc.contributor.author","Peters, Johannes"],["dc.contributor.author","Krull, Sabine"],["dc.contributor.author","Helbig, Lena"],["dc.contributor.author","Vogler, Melanie"],["dc.contributor.author","Levay, Magdolna"],["dc.contributor.author","van Belle, Gijsbert J."],["dc.contributor.author","Ridley, Anne J."],["dc.contributor.author","Lutz, Susanne"],["dc.contributor.author","Katschinski, Dörthe M."],["dc.contributor.author","Zieseniss, Anke"],["dc.date.accessioned","2020-12-10T18:41:53Z"],["dc.date.available","2020-12-10T18:41:53Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1242/jcs.223230"],["dc.identifier.eissn","1477-9137"],["dc.identifier.issn","0021-9533"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/77715"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Hypoxia suppresses myofibroblast differentiation by changing RhoA activity"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2048"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Cell Reports"],["dc.bibliographiccitation.lastpage","2055"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Siegert, Isabel"],["dc.contributor.author","Schoedel, Johannes"],["dc.contributor.author","Nairz, Manfred"],["dc.contributor.author","Schatz, Valentin"],["dc.contributor.author","Dettmer, Katja"],["dc.contributor.author","Dick, Christopher"],["dc.contributor.author","Kalucka, Joanna"],["dc.contributor.author","Franke, Kristin"],["dc.contributor.author","Ehrenschwender, Martin"],["dc.contributor.author","Schley, Gunnar"],["dc.contributor.author","Beneke, Angelika"],["dc.contributor.author","Sutter, Joerg"],["dc.contributor.author","Moll, Matthias"],["dc.contributor.author","Hellerbrand, Claus"],["dc.contributor.author","Wielockx, Ben"],["dc.contributor.author","Katschinski, Doerthe Magdalena"],["dc.contributor.author","Lang, Roland"],["dc.contributor.author","Galy, Bruno"],["dc.contributor.author","Hentze, Matthias W."],["dc.contributor.author","Koivunen, Peppi"],["dc.contributor.author","Oefner, Peter J."],["dc.contributor.author","Bogdan, Christian"],["dc.contributor.author","Weiss, Guenter"],["dc.contributor.author","Willam, Carsten"],["dc.contributor.author","Jantsch, Jonathan"],["dc.date.accessioned","2018-11-07T09:47:29Z"],["dc.date.available","2018-11-07T09:47:29Z"],["dc.date.issued","2015"],["dc.description.abstract","Both hypoxic and inflammatory conditions activate transcription factors such as hypoxia-inducible factor (HIF)-1 alpha and nuclear factor (NF)-kappa B, which play a crucial role in adaptive responses to these challenges. In dendritic cells (DC), lipopolysaccharide (LPS)-induced HIF1 alpha accumulation requires NF-kappa B signaling and promotes inflammatory DC function. The mechanisms that drive LPS-induced HIF1 alpha accumulation under normoxia are unclear. Here, we demonstrate that LPS inhibits prolyl hydroxylase domain enzyme (PHD) activity and thereby blocks HIF1 alpha degradation. Of note, LPS-induced PHD inhibition was neither due to cosubstrate depletion (oxygen or alpha-ketoglutarate) nor due to increased levels of reactive oxygen species, fumarate, and succinate. Instead, LPS inhibited PHD activity through NF-kappa B-mediated induction of the iron storage protein ferritin and subsequent decrease of intracellular available iron, a critical cofactor of PHD. Thus, hypoxia and LPS both induce HIF1 alpha accumulation via PHD inhibition but deploy distinct molecular mechanisms (lack of cosubstrate oxygen versus deprivation of co-factor iron)."],["dc.identifier.doi","10.1016/j.celrep.2015.11.005"],["dc.identifier.isi","000366534300002"],["dc.identifier.pmid","26628374"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/12739"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/35125"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.relation.issn","2211-1247"],["dc.rights","CC BY-NC-ND 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-nd/4.0"],["dc.title","Ferritin-Mediated Iron Sequestration Stabilizes Hypoxia-Inducible Factor-1 alpha upon LPS Activation in the Presence of Ample Oxygen"],["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.artnumber","e0137519"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","PLoS ONE"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Jatho, Aline"],["dc.contributor.author","Hartmann, Svenja"],["dc.contributor.author","Kittana, Naim"],["dc.contributor.author","Muegge, Felicitas"],["dc.contributor.author","Wuertz, Christina M."],["dc.contributor.author","Tiburcy, Malte"],["dc.contributor.author","Zimmermann, Wolfram-Hubertus"],["dc.contributor.author","Katschinski, Dörthe M."],["dc.contributor.author","Lutz, Susanne"],["dc.date.accessioned","2017-09-07T11:43:28Z"],["dc.date.available","2017-09-07T11:43:28Z"],["dc.date.issued","2015"],["dc.description.abstract","Introduction RhoA has been shown to be beneficial in cardiac disease models when overexpressed in cardiomyocytes, whereas its role in cardiac fibroblasts (CF) is still poorly understood. During cardiac remodeling CF undergo a transition towards a myofibroblast phenotype thereby showing an increased proliferation and migration rate. Both processes involve the remodeling of the cytoskeleton. Since RhoA is known to be a major regulator of the cytoskeleton, we analyzed its role in CF and its effect on myofibroblast characteristics in 2 D and 3D models. Results Downregulation of RhoA was shown to strongly affect the actin cytoskeleton. It decreased the myofibroblast marker alpha-sm-actin, but increased certain fibrosis-associated factors like TGF-beta and collagens. Also, the detailed analysis of CTGF expression demonstrated that the outcome of RhoA signaling strongly depends on the involved stimulus. Furthermore, we show that proliferation of myofibroblasts rely on RhoA and tubulin acetylation. In assays accessing three different types of migration, we demonstrate that RhoA/ROCK/Dia1 are important for 2D migration and the repression of RhoA and Dia1 signaling accelerates 3D migration. Finally, we show that a downregulation of RhoA in CF impacts the viscoelastic and contractile properties of engineered tissues. Conclusion RhoA positively and negatively influences myofibroblast characteristics by differential signaling cascades and depending on environmental conditions. These include gene expression, migration and proliferation. Reduction of RhoA leads to an increased viscoelasticity and a decrease in contractile force in engineered cardiac tissue."],["dc.description.sponsorship","Open-Access Publikationsfonds 2015"],["dc.identifier.doi","10.1371/journal.pone.0137519"],["dc.identifier.gro","3141809"],["dc.identifier.isi","000362511000003"],["dc.identifier.pmid","26448568"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/12214"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1312"],["dc.identifier.url","https://sfb1002.med.uni-goettingen.de/production/literature/publications/118"],["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","SFB 1002: Modulatorische Einheiten bei Herzinsuffizienz"],["dc.relation","SFB 1002 | C02: RhoGTPasen und ihre Bedeutung für die Last-abhängige Myokardfibrose"],["dc.relation","SFB 1002 | C04: Fibroblasten-Kardiomyozyten Interaktion im gesunden und erkrankten Herzen: Mechanismen und therapeutische Interventionen bei Kardiofibroblastopathien"],["dc.relation","SFB 1002 | C06: Mechanismen und Regulation der koronaren Gefäßneubildung"],["dc.relation.issn","1932-6203"],["dc.relation.workinggroup","RG Lutz (G Protein-Coupled Receptor Mediated Signaling)"],["dc.relation.workinggroup","RG Tiburcy (Stem Cell Disease Modeling)"],["dc.relation.workinggroup","RG Zimmermann (Engineered Human Myocardium)"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","RhoA Ambivalently Controls Prominent Myofibroblast Characteritics by Involving Distinct Signaling Routes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","407"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Acta Physiologica"],["dc.bibliographiccitation.lastpage","414"],["dc.bibliographiccitation.volume","195"],["dc.contributor.author","Katschinski, Doerthe Magdalena"],["dc.date.accessioned","2018-11-07T08:30:49Z"],["dc.date.available","2018-11-07T08:30:49Z"],["dc.date.issued","2009"],["dc.description.abstract","The prolyl-4-hydroxylase domain (PHD) 1-3 enzymes have been identified based on their ability to regulate the stability of hypoxia-inducible factor a subunits and thus to modify hypoxia-inducible gene expression. Transgenic mouse models provided insights into the isoform-specific functions of these oxygen sensors with physiological implications for angiogenesis, erythropoiesis/oxygen transport, cardiovascular function, metabolism and tissue homeostasis. This knowledge is important for the ongoing development of small molecule PHD inhibitors that are currently tested in preclinical and clinical trials for the treatment of anaemia and for cytoprotection. This review aims at summarizing the insights obtained from key mouse knock-out models as well as first experiences in the therapeutic application of PHD inhibitors."],["dc.identifier.doi","10.1111/j.1748-1716.2008.01952.x"],["dc.identifier.isi","000263965500001"],["dc.identifier.pmid","19183336"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/16983"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell Publishing, Inc"],["dc.relation.issn","1748-1708"],["dc.title","In vivo functions of the prolyl-4-hydroxylase domain oxygen sensors: direct route to the treatment of anaemia and the protection of ischaemic tissues"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Annals of Oncology"],["dc.bibliographiccitation.volume","27"],["dc.contributor.author","Kozlova, Nina"],["dc.contributor.author","Wottawa, Marieke"],["dc.contributor.author","Katschinski, Doerthe Magdalena"],["dc.contributor.author","Kristiansen, Glen"],["dc.contributor.author","Kietzmann, Thomas"],["dc.date.accessioned","2018-11-07T10:07:18Z"],["dc.date.available","2018-11-07T10:07:18Z"],["dc.date.issued","2016"],["dc.identifier.doi","10.1093/annonc/mdw362.27"],["dc.identifier.isi","000393912500028"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/39250"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Oxford Univ Press"],["dc.publisher.place","Oxford"],["dc.relation.conference","41st Congress of the European-Society-for-Medical-Oncology (ESMO)"],["dc.relation.eventlocation","Copenhagen, DENMARK"],["dc.relation.issn","1569-8041"],["dc.relation.issn","0923-7534"],["dc.title","Hypoxia inducible factor prolyl hydroxylase 2 (PHD2) is a direct regulator of epidermal growth factor receptor (EGFR) signaling in breast cancer"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]