Burckhardt, Birgitta-Christina

[["dc.bibliographiccitation.firstpage","E843"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","AMERICAN JOURNAL OF PHYSIOLOGY-RENAL PHYSIOLOGY"],["dc.bibliographiccitation.lastpage","E851"],["dc.bibliographiccitation.volume","309"],["dc.contributor.author","Henjakovic, Maja"],["dc.contributor.author","Hagos, Yohannes"],["dc.contributor.author","Krick, Wolfgang"],["dc.contributor.author","Burckhardt, Gerhard"],["dc.contributor.author","Burckhardt, Birgitta-Christina"],["dc.date.accessioned","2018-11-07T09:48:54Z"],["dc.date.available","2018-11-07T09:48:54Z"],["dc.date.issued","2015"],["dc.description.abstract","Phylogentically, organic anion transporter (OAT)1 and OAT3 are closely related, whereas OAT2 is more distant. Experiments with human embryonic kidney-293 cells stably transfected with human OAT1, OAT2, or OAT3 were performed to compare selected transport properties. Common to OAT1, OAT2, and OAT3 is their ability to transport cGMP. OAT2 interacted with prostaglandins, and cGMP uptake was inhibited by PGE(2) and PGF(2 alpha) with IC50 values of 40.8 and 12.7 mu M, respectively. OAT1 (IC50: 23.7 mu M), OAT2 (IC50: 9.5 mu M), and OAT3 (IC50: 1.6 mu M) were potently inhibited by MK571, an established multidrug resistance protein inhibitor. OAT2-mediated cGMP uptake was not inhibited by short-chain monocarboxylates and, as opposed to OAT1 and OAT3, not by dicarboxylates. Consequently, OAT2 showed no cGMP/glutarate exchange. OAT1 and OAT3 exhibited a pH and a Cl- dependence with higher substrate uptake at acidic pH and lower substrate uptake in the absence of Cl-, respectively. Such pH and Cl- dependencies were not observed with OAT2. Depolarization of membrane potential by high K-1 concentrations in the presence of the K-1 ionophore valinomycin left cGMP uptake unaffected. In addition to cGMP, OAT2 transported urate and glutamate, but cGMP/glutamate exchange could not be demonstrated. These experiments suggest that OAT2-mediated cGMP uptake does not occur via exchange with monocarboxylates, dicarboxylates, and hydroxyl ions. The counter anion for electroneutral cGMP uptake remains to be identified."],["dc.identifier.doi","10.1152/ajprenal.00140.2015"],["dc.identifier.isi","000365896300005"],["dc.identifier.pmid","26377792"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/35401"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Physiological Soc"],["dc.relation.issn","1522-1466"],["dc.relation.issn","1931-857X"],["dc.title","Human organic anion transporter 2 is distinct from organic anion transporters 1 and 3 with respect to transport function"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","The FASEB Journal"],["dc.bibliographiccitation.volume","25"],["dc.contributor.author","Hagos, Yohannes"],["dc.contributor.author","Willam, Carsten"],["dc.contributor.author","Krick, Wolfgang"],["dc.contributor.author","Burckhardt, Gerhard"],["dc.contributor.author","Burckhardt, Birgitta-Christina"],["dc.date.accessioned","2018-11-07T08:57:48Z"],["dc.date.available","2018-11-07T08:57:48Z"],["dc.date.issued","2011"],["dc.identifier.isi","000310708405863"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/23487"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Federation Amer Soc Exp Biol"],["dc.publisher.place","Bethesda"],["dc.relation.conference","Experimental Biology Meeting 2011"],["dc.relation.eventlocation","Washington, DC"],["dc.relation.issn","0892-6638"],["dc.title","Inhibitors of prolyl hydroxlase are substrates of the organic anion transporter 1 (OAT1)"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","F145"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","AMERICAN JOURNAL OF PHYSIOLOGY-RENAL PHYSIOLOGY"],["dc.bibliographiccitation.lastpage","F154"],["dc.bibliographiccitation.volume","297"],["dc.contributor.author","Krick, Wolfgang"],["dc.contributor.author","Schnedler, Nina"],["dc.contributor.author","Burckhardt, Gerhard"],["dc.contributor.author","Burckhardt, Birgitta-Christina"],["dc.date.accessioned","2018-11-07T08:27:52Z"],["dc.date.available","2018-11-07T08:27:52Z"],["dc.date.issued","2009"],["dc.description.abstract","Krick W, Schnedler N, Burckhardt G, Burckhardt BC. Ability of sat-1 to transport sulfate, bicarbonate, or oxalate under physiological conditions. Am J Physiol Renal Physiol 297: F145-F154, 2009. First published April 15, 2009; doi:10.1152/ajprenal.90401.2008.-Tubular reabsorption of sulfate is achieved by the sodium-dependent sulfate transporter, NaSi-1, located at the apical membrane, and the sulfate-anion exchanger, sat-1, located at the basolateral membrane. To delineate the physiological role of rat sat-1, [(35)S] sulfate and [(14)C] oxalate uptake into sat-1-expressing oocytes was determined under various experimental conditions. Influx of [(35)S] sulfate was inhibited by bicarbonate, thiosulfate, sulfite, and oxalate, but not by sulfamate and sulfide, in a competitive manner with K(i) values of 2.7 +/- 1.3 mM, 101.7 +/- 9.7 mu M, 53.8 +/- 10.9 mu M, and 63.5 +/- 38.7 mu M, respectively. Vice versa, [(14)C] oxalate uptake was inhibited by sulfate with a Ki of 85.9 +/- 9.5 mu M. The competitive type of inhibition indicates that these compounds are most likely substrates of sat-1. Physiological plasma bicarbonate concentrations ( 25 mM) reduced sulfate and oxalate uptake by more than 75%. Simultaneous application of sulfate, bicarbonate, and oxalate abolished sulfate as well as oxalate uptake. These data and electrophysiological studies using a two-electrode voltage-clamp device provide evidence that sat-1 preferentially works as an electroneutral sulfate-bicarbonate or oxalate-bicarbonate exchanger. In kidney proximal tubule cells, sat-1 likely completes sulfate reabsorption from the ultrafiltrate across the basolateral membrane in exchange for bicarbonate. In hepatocytes, oxalate extrusion is most probably mediated either by an exchange for sulfate or bicarbonate."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft [BU 998/4-1]"],["dc.identifier.doi","10.1152/ajprenal.90401.2008"],["dc.identifier.isi","000267341800017"],["dc.identifier.pmid","19369292"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/6067"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/16296"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Physiological Soc"],["dc.relation.issn","1931-857X"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Ability of sat-1 to transport sulfate, bicarbonate, or oxalate under physiological conditions"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","367"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Pflügers Archiv - European Journal of Physiology"],["dc.bibliographiccitation.lastpage","374"],["dc.bibliographiccitation.volume","464"],["dc.contributor.author","Hagos, Yohannes"],["dc.contributor.author","Schley, Gunnar"],["dc.contributor.author","Schoedel, Johannes"],["dc.contributor.author","Krick, Wolfgang"],["dc.contributor.author","Burckhardt, Gerhard"],["dc.contributor.author","Willam, Carsten"],["dc.contributor.author","Burckhardt, Birgitta-Christina"],["dc.date.accessioned","2018-11-07T09:05:27Z"],["dc.date.available","2018-11-07T09:05:27Z"],["dc.date.issued","2012"],["dc.description.abstract","2-Oxoglutarate or alpha-ketoglutarate (alpha KG) is a substrate of HIF prolyl hydroxylases 1-3 that decrease cellular levels of the hypoxia-inducible factor 1 alpha (HIF-1 alpha) in the presence of oxygen. alpha KG analogs are applied to stabilize HIF-1 alpha even in the presence of oxygen and thus provide a novel therapeutic option in treating kidney diseases. In the kidneys, the organic anion transporters 1 and 3 (OAT1 and OAT3, respectively) in cooperation with the sodium-dependent dicarboxylate transporter 3 (NaDC3) and the OAT4 might be responsible for the uptake of alpha KG analogs into and the efflux out of the tubular cells. Using the radiolabelled substrates p-aminohippurate (PAH, OAT1), estrone-3-sulfate (ES; OAT3, OAT4), and succinate (NaDC3), N-oxalylglycine (NOG), dimethyloxalyl glycine (DMOG), 2,4-diethylpyridine dicarboxylate (2,4-DPD), and pyridine-2,4-dicarboxylic acid (PDCA) were tested in cis-inhibition and trans-stimulation experiments. None of these alpha KG analogs interacted with NaDC3. 2,4-DPD and PDCA inhibited ES uptake by OAT3 moderately. NOG, 2,4-DPD and PDCA, but not DMOG, inhibited PAH uptake by OAT1 significantly. trans-Stimulation experiments and experiments demonstrating stabilization of HIF-1 alpha revealed that NOG and PDCA, but not 2,4-DPD, are translocated by OAT1. All compounds trans-stimulated ES uptake by OAT4, but only PDCA stabilized HIF-1 alpha. The data suggest that OAT1 is involved in the uptake of NOG and PDCA across the basolateral membrane of proximal tubule cells, whereas OAT4 may release these compounds into the primary urine."],["dc.description.sponsorship","German Research Council [BU998/5-1]"],["dc.identifier.doi","10.1007/s00424-012-1140-9"],["dc.identifier.isi","000309178600004"],["dc.identifier.pmid","22875277"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/8812"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/25320"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.relation.issn","0031-6768"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","alpha-Ketoglutarate-related inhibitors of HIF prolyl hydroxylases are substrates of renal organic anion transporters 1 (OAT1) and 4 (OAT4)"],["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","F1026"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","AMERICAN JOURNAL OF PHYSIOLOGY-RENAL PHYSIOLOGY"],["dc.bibliographiccitation.lastpage","F1034"],["dc.bibliographiccitation.volume","301"],["dc.contributor.author","Kaufhold, Marcel"],["dc.contributor.author","Schulz, Katharina"],["dc.contributor.author","Breljak, Davorka"],["dc.contributor.author","Gupta, Shivangi"],["dc.contributor.author","Henjakovic, Maja"],["dc.contributor.author","Krick, Wolfgang"],["dc.contributor.author","Hagos, Yohannes"],["dc.contributor.author","Sabolic, Ivan"],["dc.contributor.author","Burckhardt, Birgitta-Christina"],["dc.contributor.author","Burckhardt, Gerhard"],["dc.date.accessioned","2018-11-07T08:50:00Z"],["dc.date.available","2018-11-07T08:50:00Z"],["dc.date.issued","2011"],["dc.description.abstract","Kaufhold M, Schulz K, Breljak D, Gupta S, Henjakovic M, Krick W, Hagos Y, Sabolic I, Burckhardt BC, Burckhardt G. Differential interaction of dicarboxylates with human sodium-dicarboxylate cotransporter 3 and organic anion transporters 1 and 3. Am J Physiol Renal Physiol 301: F1026-F1034, 2011. First published August 24, 2011; doi:10.1152/ajprenal.00169.2011.-Organic anions are taken up from the blood into proximal tubule cells by organic anion transporters 1 and 3 (OAT1 and OAT3) in exchange for dicarboxylates. The released dicarboxylates are recycled by the sodium dicarboxylate cotransporter 3 (NaDC3). In this study, we tested the substrate specificities of human NaDC3, OAT1, and OAT3 to identify those dicarboxylates for which the three cooperating transporters have common high affinities. All transporters were stably expressed in HEK293 cells, and extracellularly added dicarboxylates were used as inhibitors of [(14)C] succinate (NaDC3), p-[(3)H] aminohippurate (OAT1), or [(3)H] estrone-3-sulfate (OAT3) uptake. Human NaDC3 was stably expressed as proven by immunochemical methods and by sodium-dependent uptake of succinate (K(0.5) for sodium activation, 44.6 mM; Hill coefficient, 2.1; K(m) for succinate, 18 mu M). NaDC3 was best inhibited by succinate (IC(50) 25.5 mu M) and less by alpha-ketoglutarate (IC(50) 69.2 mu M) and fumarate (IC(50) 95.2 mu M). Dicarboxylates with longer carbon backbones (adipate, pimelate, suberate) had low or no affinity for NaDC3. OAT1 exhibited the highest affinity for glutarate, alpha-ketoglutarate, and adipate (IC(50) between 3.3 and 6.2 mu M), followed by pimelate (18.6 mu M) and suberate (19.3 mu M). The affinity of OAT1 to succinate and fumarate was low. OAT3 showed the same dicarboxylate selectivity with similar to 13-fold higher IC(50) values compared with OAT1. The data 1) reveal alpha-ketoglutarate as a common high-affinity substrate of NaDC3, OAT1, and OAT3 and 2) suggest potentially similar molecular structures of the binding sites in OAT1 and OAT3 for dicarboxylates."],["dc.identifier.doi","10.1152/ajprenal.00169.2011"],["dc.identifier.isi","000298151700013"],["dc.identifier.pmid","21865262"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/21591"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Physiological Soc"],["dc.relation.issn","1931-857X"],["dc.title","Differential interaction of dicarboxylates with human sodium-dicarboxylate cotransporter 3 and organic anion transporters 1 and 3"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1381"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Pflügers Archiv - European Journal of Physiology"],["dc.bibliographiccitation.lastpage","1392"],["dc.bibliographiccitation.volume","457"],["dc.contributor.author","Brzica, Hrvoje"],["dc.contributor.author","Breljak, Davorka"],["dc.contributor.author","Krick, Wolfgang"],["dc.contributor.author","Lovric, Mila"],["dc.contributor.author","Burckhardt, Gerhard"],["dc.contributor.author","Burckhardt, Birgitta-Christina"],["dc.contributor.author","Sabolic, Ivan"],["dc.date.accessioned","2018-11-07T08:31:22Z"],["dc.date.available","2018-11-07T08:31:22Z"],["dc.date.issued","2009"],["dc.description.abstract","The sulfate anion transporter (sat-1, Slc26a1) has been cloned from rat liver, functionally characterized, and localized to the sinusoidal membrane in hepatocytes and basolateral membrane (BLM) in proximal tubules (PT). Here, we confirm previously described localization of sat-1 protein in rat liver and kidneys and report on gender differences (GD) in its expression by immunochemical, transport, and excretion studies in rats. The similar to 85-kDa sat-1 protein was localized to the sinusoidal membrane in hepatocytes and BLM in renal cortical PT, with the male-dominant expression. However, the real-time reverse-transcription polymerase chain reaction data indicated no GD at the level of sat-1 mRNA. In agreement with the protein data, isolated membranes from both organs exhibited the male-dominant exchange of radiolabeled sulfate for oxalate, whereas higher oxalate in plasma and 24-h urine indicated higher oxalate production and excretion in male rats. Furthermore, the expression of liver, but not renal, sat-1 protein was: unaffected by castration, upregulated by ovariectomy, and downregulated by estrogen or progesterone treatment in males. Therefore, GD (males > females) in the expression of sat-1 protein in rat liver (and, possibly, kidneys) are caused by the female sex-hormone-driven inhibition at the posttranscriptional level. The male-dominant abundance of sat-1 protein in liver may conform to elevated uptake of sulfate and extrusion of oxalate, causing higher plasma oxalate in males. Oxalate is then excreted by the kidneys via the basolateral sat-1 (males > females) and the apical CFEX (Slc26a6; GD unknown) in PT and eliminated in the urine (males > females), where it may contribute to the male-prevailing development of oxalate urolithiasis."],["dc.identifier.doi","10.1007/s00424-008-0611-5"],["dc.identifier.isi","000264184300015"],["dc.identifier.pmid","19002488"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/3531"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/17108"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.relation.issn","0031-6768"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","The liver and kidney expression of sulfate anion transporter sat-1 in rats exhibits male-dominant gender differences"],["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","223"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Pflügers Archiv"],["dc.bibliographiccitation.lastpage","231"],["dc.bibliographiccitation.volume","457"],["dc.contributor.author","Hagos, Yohannes"],["dc.contributor.author","Krick, Wolfgang"],["dc.contributor.author","Braulke, Thomas"],["dc.contributor.author","Mühlhausen, Chris"],["dc.contributor.author","Burckhardt, Gerhard"],["dc.contributor.author","Burckhardt, Birgitta C."],["dc.date.accessioned","2019-07-09T11:52:00Z"],["dc.date.available","2019-07-09T11:52:00Z"],["dc.date.issued","2008"],["dc.description.abstract","Glutaric acidurias are rare inherited neurodegenerative disorders accompanied by accumulation of the metabolites glutarate (GA) and 3-hydroxyglutarate (3OHGA), glutaconate, L-, or D-2-hydroxyglutarate (L-2OHGA, D-2OHGA) in all body fluids. Oocytes expressing the human (h) sodium-dicarboxylate cotransporter (NaDC3) showed sodium-dependent inward currents mediated by GA, 3OHGA, L-, and D-2OHGA. The organic anion transporters (OATs) were examined as additional transporters for GA derivatives. The uptake of [3H]p-aminohippurate in hOAT1-transfected human embryonic kidney (HEK293) cells was inhibited by GA, 3OHGA, D-, or L-2OHGA in a concentration-dependent manner. None of these compounds affected the hOAT3-mediated uptake of [3H]estrone sulfate (ES). In hOAT4-expressing cells and oocytes, ES uptake was strongly increased by intracellular GA derivatives. The data provide a model for the concerted action of OAT1 and NaDC3 mediating the basolateral uptake, and OAT4 mediating apical secretion of GA derivatives from proximal tubule cells and therefore contribute to the renal clearance of these compounds."],["dc.identifier.doi","10.1007/s00423-008-0489-2"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/3098"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/60065"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.publisher","Springer"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject.ddc","571"],["dc.title","Organic anion transporters OAT1 and OAT4 mediate the high affinity transport of glutarate derivatives accumulating in patients with glutaric acidurias"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.issue","1-2"],["dc.bibliographiccitation.journal","Nephron Physiology"],["dc.bibliographiccitation.lastpage","5"],["dc.bibliographiccitation.volume","124"],["dc.contributor.author","Schorbach, Lena"],["dc.contributor.author","Krick, Wolfgang"],["dc.contributor.author","Burckhardt, Gerhard"],["dc.contributor.author","Burckhardt, Birgitta-Christina"],["dc.date.accessioned","2018-11-07T09:29:22Z"],["dc.date.available","2018-11-07T09:29:22Z"],["dc.date.issued","2013"],["dc.description.abstract","Background/Aims: During a single pass through the kidneys, more than 80% of glutathione (GSH) is excreted, indicating not only glomerular filtration, but also tubular secretion. The first step in tubular secretion is the uptake of a substance across the basolateral membrane of proximal tubule cells by sodium-dependent and -independent transporters. Due to the dicarboxylate-like structure, we postulated that GSH uptake across the basolateral membrane is mediated by the sodium-dependent dicarboxylate transporter 3 (NaDC3). Methods: Tracer uptake and electrophysiologic measurements using a two-electrode voltage clamp device were performed in Xenopus laevis oocytes expressing the human (h) NaDC3. Results: Uptake of succinate, the reference substrate of hNaDC3, was inhibited by GSH in a dose-dependent manner with an IC50 of 1.88 m M. GSH evoked potential-dependent inward currents, which were abolished under sodium-free conditions. At -60 mV, GSH currents showed saturation kinetics with a K-M of 1.65 mM. Conclusion: hNaDC3 present at the basolateral membrane of proximal tubule cells mediates sodium-dependent GSH uptake. The kinetic data show that NaDC3 is a low-affinity GSH transporter. (C) 2013 S. Karger AG, Basel"],["dc.description.sponsorship","German Research Council [BU998/5-1]"],["dc.identifier.doi","10.1159/000356419"],["dc.identifier.isi","000330134200001"],["dc.identifier.pmid","24247155"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10823"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/31012"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Karger"],["dc.relation.issn","1660-2137"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Glutathione Is a Low-Affinity Substrate of the Human Sodium-Dependent Dicarboxylate Transporter"],["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","16332"],["dc.bibliographiccitation.issue","24"],["dc.bibliographiccitation.journal","Journal of Biological Chemistry"],["dc.bibliographiccitation.lastpage","16341"],["dc.bibliographiccitation.volume","283"],["dc.contributor.author","Bahn, Andrew"],["dc.contributor.author","Hagos, Yohannes"],["dc.contributor.author","Reuter, Stefan"],["dc.contributor.author","Balen, Daniela"],["dc.contributor.author","Brzica, Hrvoje"],["dc.contributor.author","Krick, Wolfgang"],["dc.contributor.author","Burckhardt, Birgitta C."],["dc.contributor.author","Sabolić, Ivan"],["dc.contributor.author","Burckhardt, Gerhard"],["dc.date.accessioned","2021-06-01T10:51:08Z"],["dc.date.available","2021-06-01T10:51:08Z"],["dc.date.issued","2008"],["dc.identifier.doi","10.1074/jbc.M800737200"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/6066"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/86903"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-425"],["dc.notes.intern","Merged from goescholar"],["dc.relation.issn","0021-9258"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Identification of a New Urate and High Affinity Nicotinate Transporter, hOAT10 (SLC22A13)"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]