Wallbach, Manuel

[["dc.bibliographiccitation.firstpage","344"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Cellular Signalling"],["dc.bibliographiccitation.lastpage","353"],["dc.bibliographiccitation.volume","23"],["dc.contributor.author","Do Thanh Phu, Do Thanh Phu"],["dc.contributor.author","Wallbach, Manuel"],["dc.contributor.author","Depatie, Chantal"],["dc.contributor.author","Fu, Accalia"],["dc.contributor.author","Screaton, Robert A."],["dc.contributor.author","Oetjen, Elke"],["dc.date.accessioned","2018-11-07T08:59:34Z"],["dc.date.available","2018-11-07T08:59:34Z"],["dc.date.issued","2011"],["dc.description.abstract","CREB is a ubiquitously expressed transcription factor regulating gene expression via binding to a CRE DNA element. Previous work showed that the dual leucine zipper kinase (DLK) reduced CREB-dependent gene transcription at least in part via inhibition of the coactivator CBP. Here we demonstrate that DLK also inhibits CREB activity by affecting the interaction of CREB with its second coactivator TORC. DLK acted on TORC-dependent transcription by distinct mechanisms. An interaction between DLK and all three TORC isoforms was demonstrated by in vitro protein-protein interaction assays and in cells by coimmunoprecipitation that required the N-terminus of TORC and the leucine zipper of dimerized DLK. Overexpressed DLK induced the phosphorylation of TORC2 and TORC1 on Ser-171 and 167, respectively and on additional residues. Since a kinase-dead DLK mutant did not prevent the nuclear localization of TORC and did not reduce TORC transcriptional activity to the same extent as wild-type DLK, we suggest that DLK-induced phosphorylation of TORC contributes to DLK's inhibitory action. Both the interaction with and the phosphorylation of TORC by DLK might account for the reduced recruitment of TORC to a CRE containing promoter as revealed by chromatin immunoprecipitation assay. These results show for the first time the inhibition of TORC function by a mitogen-activated kinase. Given the dependence on TORC in CREB-directed gene transcription, DLK and its downstream kinases thus contribute to the finely tuned regulation of CREB-dependent effects. (C) 2010 Elsevier Inc. All rights reserved."],["dc.identifier.doi","10.1016/j.cellsig.2010.10.001"],["dc.identifier.isi","000286539600005"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/23933"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Inc"],["dc.relation.issn","0898-6568"],["dc.title","Regulation of the CREB coactivator TORC by the dual leucine zipper kinase at different levels"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","257"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Hypertension"],["dc.bibliographiccitation.lastpage","264"],["dc.bibliographiccitation.volume","75"],["dc.contributor.author","Heusser, Karsten"],["dc.contributor.author","Thöne, Arvo"],["dc.contributor.author","Lipp, Axel"],["dc.contributor.author","Menne, Jan"],["dc.contributor.author","Beige, Joachim"],["dc.contributor.author","Reuter, Hannes"],["dc.contributor.author","Hoffmann, Fabian"],["dc.contributor.author","Halbach, Marcel"],["dc.contributor.author","Eckert, Siegfried"],["dc.contributor.author","Wallbach, Manuel"],["dc.contributor.author","Koziolek, Michael"],["dc.contributor.author","Haarmann, Helge"],["dc.contributor.author","Joyner, Michael J."],["dc.contributor.author","Paton, Julian F.R."],["dc.contributor.author","Diedrich, André"],["dc.contributor.author","Haller, Hermann"],["dc.contributor.author","Jordan, Jens"],["dc.contributor.author","Tank, Jens"],["dc.date.accessioned","2020-12-10T18:38:04Z"],["dc.date.available","2020-12-10T18:38:04Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1161/HYPERTENSIONAHA.119.13925"],["dc.identifier.eissn","1524-4563"],["dc.identifier.issn","0194-911X"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/77177"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Efficacy of Electrical Baroreflex Activation Is Independent of Peripheral Chemoreceptor Modulation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Journal of Nephrology"],["dc.contributor.author","Hakroush, Samy"],["dc.contributor.author","Lehnig, Luca-Yves"],["dc.contributor.author","Wallbach, Manuel"],["dc.contributor.author","Schanz, Julie"],["dc.contributor.author","Koziolek, Michael Johann"],["dc.date.accessioned","2021-08-12T07:46:15Z"],["dc.date.available","2021-08-12T07:46:15Z"],["dc.date.issued","2021"],["dc.identifier.doi","10.1007/s40620-021-01109-8"],["dc.identifier.pii","1109"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/88657"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-448"],["dc.relation.eissn","1724-6059"],["dc.relation.issn","1121-8428"],["dc.title","Renal involvement of intravascular large B-cell lymphoma: a challenging diagnosis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","718"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","JAMA Ophthalmology"],["dc.bibliographiccitation.lastpage","720"],["dc.bibliographiccitation.volume","133"],["dc.contributor.author","Koziolek, Michael Johann"],["dc.contributor.author","Patschan, Daniel"],["dc.contributor.author","Desel, Herbert"],["dc.contributor.author","Wallbach, Manuel"],["dc.contributor.author","Callizo, Josep"],["dc.date.accessioned","2018-11-07T09:56:31Z"],["dc.date.available","2018-11-07T09:56:31Z"],["dc.date.issued","2015"],["dc.identifier.doi","10.1001/jamaophthalmol.2015.191"],["dc.identifier.isi","000356044400026"],["dc.identifier.pmid","25742635"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/36970"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Medical Assoc"],["dc.relation.issn","2168-6173"],["dc.relation.issn","2168-6165"],["dc.title","Closantel Poisoning Treated With Plasma Exchange"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.subtype","letter_note"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","829"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Acta Diabetologica"],["dc.bibliographiccitation.lastpage","835"],["dc.bibliographiccitation.volume","52"],["dc.contributor.author","Wallbach, Manuel"],["dc.contributor.author","Lehnig, Luca-Yves"],["dc.contributor.author","Helms, Hans-Joachim"],["dc.contributor.author","Schroer, Charlotte"],["dc.contributor.author","Mueller, Georg Anton"],["dc.contributor.author","Wachter, R. Rolf"],["dc.contributor.author","Koziolek, Michael Johann"],["dc.date.accessioned","2018-11-07T09:51:13Z"],["dc.date.available","2018-11-07T09:51:13Z"],["dc.date.issued","2015"],["dc.description.abstract","Aims Sympathetic overactivity is one critical factor associated with the development of arterial hypertension, impaired insulin secretion and resistance. Some antihypertensives exert beneficial effects on glucose metabolism, whereas others lead to an impairment of metabolic state with consecutive weight gain. In resistant hypertension, baroreflex activation therapy (BAT) reduces arterial blood pressure (BP) by inhibition of the sympathetic nervous system. The objective of this study was to evaluate whether BAT influences metabolic state in patients with resistant hypertension. Methods Thirty patients with resistant hypertension (10 with known diabetes mellitus) were prospectively included into this study. Blood pressure, BMI, weight, fasting glucose, insulin, C-peptide, hemoglobin A1c, HOMA-IR, HOMA-beta, ISQuickI, and glucose levels during oral glucose tolerance test were measured at baseline and 6 months after BAT activation. Results Fasting glucose was significantly reduced after 6 months of BAT, whereas mean 2-h glucose levels during oral glucose tolerance test, fasting insulin levels, C-peptide levels, hemoglobin A1c, HOMA-IR, HOMA-beta, ISQuickI, weight, and BMI remained unchanged. Conclusion Despite improvement in fasting glucose, BAT exerts neither sustained additional beneficial effects nor an impairment of metabolic state. Thus, chronic BAT might be an effective interventional method to reduce BP without metabolic disadvantages."],["dc.description.sponsorship","CVRx"],["dc.identifier.doi","10.1007/s00592-014-0679-7"],["dc.identifier.isi","000361346500002"],["dc.identifier.pmid","25539879"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/35870"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.relation.issn","1432-5233"],["dc.relation.issn","0940-5429"],["dc.title","Long-term effects of baroreflex activation therapy on glucose metabolism"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","578"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Der Internist"],["dc.bibliographiccitation.lastpage","586"],["dc.bibliographiccitation.volume","60"],["dc.contributor.author","Wallbach, M."],["dc.contributor.author","Tampe, B."],["dc.contributor.author","Dihazi, H."],["dc.contributor.author","Koziolek, M. J."],["dc.date.accessioned","2020-12-10T14:08:25Z"],["dc.date.available","2020-12-10T14:08:25Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1007/s00108-019-0602-y"],["dc.identifier.eissn","1432-1289"],["dc.identifier.issn","0020-9554"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/70458"],["dc.language.iso","de"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Akute Nierenschädigung: von Kreatinin zu KIM‑1?"],["dc.title.alternative","Acute kidney injury: from creatinine to KIM‑1?"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Journal of Artificial Organs"],["dc.contributor.author","Rademacher, Jan-Gerd"],["dc.contributor.author","Wulf, Gerald"],["dc.contributor.author","Koziolek, Michael J."],["dc.contributor.author","Zeisberg, Michael"],["dc.contributor.author","Wallbach, Manuel"],["dc.date.accessioned","2021-04-14T08:30:38Z"],["dc.date.available","2021-04-14T08:30:38Z"],["dc.date.issued","2021"],["dc.identifier.doi","10.1007/s10047-020-01244-2"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/83319"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation.eissn","1619-0904"],["dc.relation.issn","1434-7229"],["dc.title","Cytokine adsorption therapy in lymphoma-associated hemophagocytic lymphohistiocytosis and allogeneic stem cell transplantation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","International Urology and Nephrology"],["dc.contributor.author","Wenzel, Mike"],["dc.contributor.author","Yu, Hang"],["dc.contributor.author","Uhlig, Annemarie"],["dc.contributor.author","Würnschimmel, Christoph"],["dc.contributor.author","Wallbach, Manuel"],["dc.contributor.author","Becker, Andreas"],["dc.contributor.author","Fisch, Margit"],["dc.contributor.author","Chun, Felix K. H."],["dc.contributor.author","Meyer, Christian P."],["dc.contributor.author","Leitsmann, Marianne"],["dc.date.accessioned","2021-08-12T07:46:14Z"],["dc.date.available","2021-08-12T07:46:14Z"],["dc.date.issued","2021"],["dc.description.abstract","Abstract Purpose To test the value of preoperative and postoperative cystatin C (CysC) as a predictor on kidney function after partial (PN) or radical nephrectomy (RN) in renal cell carcinoma (RCC) patients with normal preoperative renal function. Methods From 01/2011 to 12/2014, 195 consecutive RCC patients with a preoperative estimated glomerular filtration rate (eGFR) > 60 ml/min/1.73m 2 underwent surgical RCC treatment with either PN or RN. Logistic and linear regression models tested for the effect of CysC as a predictor of new-onset chronic kidney disease in follow-up (eGFR < 60 ml/min/1.73m 2 ). Moreover, postoperative CysC and creatinine values were compared for kidney function estimation. Results Of 195 patients, 129 (66.2%) underwent PN. In postoperative and in follow-up setting (median 14 months, IQR 10–20), rates of eGFR < 60 ml/min/1.73m 2 were 55.9 and 30.2%. In multivariable logistic regression models, preoperative CysC [odds ratio (OR): 18.3] and RN (OR: 13.5) were independent predictors for a reduced eGFR < 60 ml/min/1.73m 2 in follow-up (both p  < 0.01), while creatinine was not. In multivariable linear regression models, a difference of the preoperative CysC level of 0.1 mg/dl estimated an eGFR decline in follow-up of about 5.8 ml/min/1.73m 2 . Finally, we observed a plateau of postoperative creatinine values in the range of 1.2–1.3 mg/dl, when graphically depicted vs. postoperative CysC values (‘creatinine blind area’). Conclusion Preoperative CysC predicts renal function impairment following RCC surgery. Furthermore, CysC might be superior to creatinine for renal function monitoring in the early postoperative setting."],["dc.description.abstract","Abstract Purpose To test the value of preoperative and postoperative cystatin C (CysC) as a predictor on kidney function after partial (PN) or radical nephrectomy (RN) in renal cell carcinoma (RCC) patients with normal preoperative renal function. Methods From 01/2011 to 12/2014, 195 consecutive RCC patients with a preoperative estimated glomerular filtration rate (eGFR) > 60 ml/min/1.73m 2 underwent surgical RCC treatment with either PN or RN. Logistic and linear regression models tested for the effect of CysC as a predictor of new-onset chronic kidney disease in follow-up (eGFR < 60 ml/min/1.73m 2 ). Moreover, postoperative CysC and creatinine values were compared for kidney function estimation. Results Of 195 patients, 129 (66.2%) underwent PN. In postoperative and in follow-up setting (median 14 months, IQR 10–20), rates of eGFR < 60 ml/min/1.73m 2 were 55.9 and 30.2%. In multivariable logistic regression models, preoperative CysC [odds ratio (OR): 18.3] and RN (OR: 13.5) were independent predictors for a reduced eGFR < 60 ml/min/1.73m 2 in follow-up (both p  < 0.01), while creatinine was not. In multivariable linear regression models, a difference of the preoperative CysC level of 0.1 mg/dl estimated an eGFR decline in follow-up of about 5.8 ml/min/1.73m 2 . Finally, we observed a plateau of postoperative creatinine values in the range of 1.2–1.3 mg/dl, when graphically depicted vs. postoperative CysC values (‘creatinine blind area’). Conclusion Preoperative CysC predicts renal function impairment following RCC surgery. Furthermore, CysC might be superior to creatinine for renal function monitoring in the early postoperative setting."],["dc.identifier.doi","10.1007/s11255-021-02957-w"],["dc.identifier.pii","2957"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/88653"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-448"],["dc.relation.eissn","1573-2584"],["dc.relation.issn","0301-1623"],["dc.title","Cystatin C predicts renal function impairment after partial or radical tumor nephrectomy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","272"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Cellular Signalling"],["dc.bibliographiccitation.lastpage","283"],["dc.bibliographiccitation.volume","28"],["dc.contributor.author","Wallbach, Manuel"],["dc.contributor.author","Escobar, Jorge Duque"],["dc.contributor.author","Babaeikelishomi, Rohollah"],["dc.contributor.author","Stahnke, Marie-Jeannette"],["dc.contributor.author","Blume, Roland"],["dc.contributor.author","Schroeder, Sabine"],["dc.contributor.author","Kruegel, Jenny"],["dc.contributor.author","Maedler, Kathrin"],["dc.contributor.author","Kluth, Oliver"],["dc.contributor.author","Kehlenbach, Ralph H."],["dc.contributor.author","Miosge, Nicolai"],["dc.contributor.author","Oetjen, Elke"],["dc.date.accessioned","2018-11-07T10:16:38Z"],["dc.date.available","2018-11-07T10:16:38Z"],["dc.date.issued","2016"],["dc.description.abstract","The dual leucine zipper kinase DLK induces beta-cell apoptosis by inhibiting the transcriptional activity conferred by the beta-cell protective transcription factor cAMP response element binding protein CREB. This action might contribute to beta-cell loss and ultimately diabetes. Within its kinase domain DLK shares high homology with the mixed lineage kinase (MLK) 3, which is activated by tumor necrosis factor (TNF) alpha and interleukin (IL)-1 beta, known prediabetic signals. In the present study, the regulation of DLK in beta-cells by these cytokines was investigated. Both, TNF alpha and IL-1 beta induced the nuclear translocation of DLK. Mutations within a putative nuclear localization signal (NLS) prevented basal and cytokine-induced nuclear localization of DLK and binding to the importin receptor importin alpha, thereby demonstrating a functional NLS within DLK. DLK NLS mutants were catalytically active as they phosphorylated their down-stream kinase c-Jun N-terminal kinase to the same extent as DLK wild-type but did neither inhibit CREB-dependent gene transcription nor transcription conferred by the promoter of the anti-apoptotic protein BCL-xL In addition, the beta-cell apoptosis-inducing effect of DLK was severely diminished by mutation of its NLS. In a murine model of prediabetes, enhanced nuclear DLK was found. These data demonstrate that DLK exerts distinct functions, depending on its subcellular localization and thus provide a novel level of regulating DLK action. Furthermore, the prevention of the nuclear localization of DLK as induced by prediabetic signals with consecutive suppression of beta-cell apoptosis might constitute a novel target in the therapy of diabetes mellitus. (C) 2016 Elsevier Inc. All rights reserved."],["dc.identifier.doi","10.1016/j.cellsig.2016.01.002"],["dc.identifier.isi","000371188000005"],["dc.identifier.pmid","26776303"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/41072"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Inc"],["dc.relation.issn","1873-3913"],["dc.relation.issn","0898-6568"],["dc.title","Distinct functions of the dual leucine zipper kinase depending on its subcellular localization"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1287"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Clinical Research in Cardiology"],["dc.bibliographiccitation.lastpage","1296"],["dc.bibliographiccitation.volume","108"],["dc.contributor.author","Lipphardt, Mark"],["dc.contributor.author","Koziolek, Michael J."],["dc.contributor.author","Lehnig, Luca-Yves"],["dc.contributor.author","Schäfer, Ann-Kathrin"],["dc.contributor.author","Müller, Gerhard A."],["dc.contributor.author","Lüders, Stephan"],["dc.contributor.author","Wallbach, Manuel"],["dc.date.accessioned","2020-12-10T14:10:22Z"],["dc.date.available","2020-12-10T14:10:22Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1007/s00392-019-01464-4"],["dc.identifier.eissn","1861-0692"],["dc.identifier.issn","1861-0684"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/70741"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Effect of baroreflex activation therapy on renal sodium excretion in patients with resistant hypertension"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]