Klafki, Hans-Wolfgang

[["dc.bibliographiccitation.firstpage","355"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","ELECTROPHORESIS"],["dc.bibliographiccitation.lastpage","362"],["dc.bibliographiccitation.volume","36"],["dc.contributor.author","Halbgebauer, Steffen"],["dc.contributor.author","Haußmann, Ute"],["dc.contributor.author","Klafki, Hans"],["dc.contributor.author","Tumani, Hayrettin"],["dc.contributor.author","Wiltfang, Jens"],["dc.contributor.author","Otto, Markus"],["dc.date.accessioned","2017-09-07T11:44:42Z"],["dc.date.available","2017-09-07T11:44:42Z"],["dc.date.issued","2014"],["dc.description.abstract","The detection of oligoclonal bands (OCBs) in cerebrospinal fluid is an indicator of intrathecal synthesis of immunoglobulins which is a neurochemical sign of chronic inflammatory brain diseases. Intrathecally synthesized IgGs are typically observed in patients with multiple sclerosis. The current standard protocol for the detection of OCBs is IEF on agarose or polyacrylamide gels followed by immunoblotting or silver staining. These methods are time consuming, show substantial interlaboratory variation and cannot be used in a high throughput-approach. We have developed a new nanoscale method for the detection of OCBs based on automated capillary IEF followed by immunological detection. Evidence for intrathecal IgG synthesis was found in all tested patients (n = 27) with multiple sclerosis, even in two subjects who did not have oligoclonal bands according to standard methods. The test specificity was at 97.5% (n = 19). Our findings indicate that the novel OCB-CIEF-immunoassay is suitable for the rapid and highly sensitive detection of OCBs in clinical samples. Furthermore, the method allows for a higher sample throughput than the current standard methods."],["dc.identifier.doi","10.1002/elps.201400339"],["dc.identifier.gro","3151730"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8550"],["dc.language.iso","en"],["dc.notes.status","public"],["dc.notes.submitter","chake"],["dc.relation.issn","0173-0835"],["dc.title","Capillary isoelectric focusing immunoassay as a new nanoscale approach for the detection of oligoclonal bands"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","849"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Journal of Alzheimer's Disease"],["dc.bibliographiccitation.lastpage","858"],["dc.bibliographiccitation.volume","67"],["dc.contributor.author","Hornung, Karen"],["dc.contributor.author","Zampar, Silvia"],["dc.contributor.author","Engel, Nadine"],["dc.contributor.author","Klafki, Hans"],["dc.contributor.author","Liepold, Thomas"],["dc.contributor.author","Bayer, Thomas A."],["dc.contributor.author","Wiltfang, Jens"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Wirths, Oliver"],["dc.date.accessioned","2020-12-10T18:44:12Z"],["dc.date.available","2020-12-10T18:44:12Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.3233/JAD-181134"],["dc.identifier.eissn","1875-8908"],["dc.identifier.issn","1387-2877"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/78365"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","N-Terminal Truncated Aβ4-42 Is a Substrate for Neprilysin Degradation in vitro and in vivo"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","101"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Journal of Alzheimer s Disease"],["dc.bibliographiccitation.lastpage","110"],["dc.bibliographiccitation.volume","49"],["dc.contributor.author","Savastano, Adriana"],["dc.contributor.author","Klafki, Hans"],["dc.contributor.author","Haussman, Ute"],["dc.contributor.author","Oberstein, Timo Jan"],["dc.contributor.author","Mueller, Petr"],["dc.contributor.author","Wirths, Oliver"],["dc.contributor.author","Wiltfang, Jens"],["dc.contributor.author","Bayer, Thomas A."],["dc.date.accessioned","2018-11-07T10:21:48Z"],["dc.date.available","2018-11-07T10:21:48Z"],["dc.date.issued","2016"],["dc.description.abstract","According to the modified amyloid hypothesis, the key event in the pathogenesis of Alzheimer's disease (AD) is the deposition of neurotoxic amyloid beta-peptides (A beta s) in plaques and cerebral blood vessels. Additionally to full-length peptides, a great diversity of N-truncated A beta variants is derived from the larger amyloid-beta protein precursor (A beta PP). Vast evidence suggests that A beta(x-42) isoforms play an important role in triggering neurodegeneration due to their high abundance, amyloidogenic propensity and toxicity. Although N-truncated Ap peptides and A beta(x-42) species appear to be the crucial players in AD etiology, the A beta(2-x) isoforms did not receive much attention yet. The present study is the first to show immunohistochemical evidence of A beta(2-x) in cases of AD and its distribution in Al3PP/PS 1KI and 5XFAD transgenic mouse models using a novel antibody pAB77 that has been developed using A132-14 as antigen. Positive plaques and congophilic amyloid angiopathy (CAA) were observed in AD cases and in both mouse models. While in AD cases, abundant CAA and less pronounced plaque pathology was evident, the two mouse models showed predominantly extracellular Ap deposits and minor CAA staining. Western blotting and a capillary isoelectric focusing immunoassay demonstrated the high specificity of the antibody pAb77 against A13-variants starting with the N-terminal Alanine-2."],["dc.identifier.doi","10.3233/JAD-150394"],["dc.identifier.isi","000364409100012"],["dc.identifier.pmid","26529393"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/42160"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Ios Press"],["dc.relation.issn","1875-8908"],["dc.relation.issn","1387-2877"],["dc.title","N-Truncated A beta(2-X) Starting with Position Two in Sporadic Alzheimer's Disease Cases and Two Alzheimer Mouse Models"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","112"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Journal of Neurochemistry"],["dc.bibliographiccitation.lastpage","121"],["dc.bibliographiccitation.volume","137"],["dc.contributor.author","van Waalwijk van Doorn, Linda J. C."],["dc.contributor.author","Koel-Simmelink, Marleen J."],["dc.contributor.author","Haußmann, Ute"],["dc.contributor.author","Klafki, Hans"],["dc.contributor.author","Struyfs, Hanne"],["dc.contributor.author","Linning, Philipp"],["dc.contributor.author","Knölker, Hans-Joachim"],["dc.contributor.author","Twaalfhoven, Harry"],["dc.contributor.author","Kuiperij, H. Bea"],["dc.contributor.author","Engelborghs, Sebastiaan"],["dc.contributor.author","Scheltens, Philip"],["dc.contributor.author","Verbeek, Marcel M."],["dc.contributor.author","Vanmechelen, Eugeen"],["dc.contributor.author","Wiltfang, Jens"],["dc.contributor.author","Teunissen, Charlotte E."],["dc.date.accessioned","2017-09-07T11:44:31Z"],["dc.date.available","2017-09-07T11:44:31Z"],["dc.date.issued","2016"],["dc.description.abstract","Analytical validation of a biomarker assay is essential before implementation in clinical practice can occur. In this study, we analytically validated the performance of assays detecting soluble amyloid-β precursor protein (sAPP) α and β in CSF in two laboratories according to previously standard operating procedures serving this goal. sAPPα and sAPPβ ELISA assays from two vendors (IBL-international, Meso Scale Diagnostics) were validated. The performance parameters included precision, sensitivity, dilutional linearity, recovery, and parallelism. Inter-laboratory variation, biomarker comparison (sAPPα vs. sAPPβ) and clinical performance was determined in three laboratories using 60 samples of patients with subjective memory complaints, Alzheimer's disease, or frontotemporal dementia. All performance parameters of the assays were similar between labs and within predefined acceptance criteria. The only exceptions were minor out-of-range results for recovery at low concentrations and, despite being within predefined acceptance criteria, non-comparability of the results for evaluation of the dilutional linearity and hook-effect. Based on the inter-laboratory correlation between Lab #1 and Lab #2, the IBL-international assays were more robust (sAPPα: r2 = 0.92, sAPPβ: r2 = 0.94) than the Meso Scale Diagnostics (MSD) assay (sAPPα: r2 = 0.70, sAPPβ: r2 = 0.80). Specificity of assays was confirmed using assay-specific peptide competitors. Clinical validation showed consistent results across the clinical groups in the different laboratories for all assays. The validated sAPP assays appear to be of sufficient technical quality and perform well. Moreover, the study shows that the newly developed standard operating procedures provide highly useful tools for the validation of new biomarker assays. A recommendation was made for renewed instructions to evaluate the dilutional linearity and hook-effect."],["dc.identifier.doi","10.1111/jnc.13527"],["dc.identifier.gro","3151694"],["dc.identifier.pmid","26748905"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8513"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.notes.submitter","chake"],["dc.relation.issn","0022-3042"],["dc.title","Validation of soluble amyloid-β precursor protein assays as diagnostic CSF biomarkers for neurodegenerative diseases"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","203"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Journal of Alzheimer's Disease"],["dc.bibliographiccitation.lastpage","212"],["dc.bibliographiccitation.volume","62"],["dc.contributor.author","Vogelgsang, Jonathan"],["dc.contributor.author","Wedekind, Dirk"],["dc.contributor.author","Bouter, Caroline"],["dc.contributor.author","Klafki, Hans-W."],["dc.contributor.author","Wiltfang, Jens"],["dc.date.accessioned","2020-12-10T18:44:11Z"],["dc.date.available","2020-12-10T18:44:11Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.3233/JAD-170793"],["dc.identifier.eissn","1875-8908"],["dc.identifier.issn","1387-2877"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/78359"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Reproducibility of Alzheimer’s Disease Cerebrospinal Fluid-Biomarker Measurements under Clinical Routine Conditions"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3136"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Molecular Neurobiology"],["dc.bibliographiccitation.lastpage","3145"],["dc.bibliographiccitation.volume","53"],["dc.contributor.author","Gronewold, Janine"],["dc.contributor.author","Klafki, Hans-Wolfgang"],["dc.contributor.author","Baldelli, Enrico"],["dc.contributor.author","Kaltwasser, Britta"],["dc.contributor.author","Seidel, Ulla K."],["dc.contributor.author","Todica, Olga"],["dc.contributor.author","Volsek, Michaela"],["dc.contributor.author","Haußmann, Ute"],["dc.contributor.author","Wiltfang, Jens"],["dc.contributor.author","Kribben, Andreas"],["dc.contributor.author","Bruck, Heike"],["dc.contributor.author","Hermann, Dirk M."],["dc.date.accessioned","2017-09-07T11:44:30Z"],["dc.date.available","2017-09-07T11:44:30Z"],["dc.date.issued","2016"],["dc.description.abstract","Disturbed brain-to-blood elimination of β-amyloid (Aβ) promotes cerebral Aβ accumulation in Alzheimer’s disease. Considering that the kidneys are involved in Aβ elimination from the blood, we evaluated how chronic kidney disease (CKD) affects plasma Aβ. In 106 CKD patients stages 3–5 (including 19 patients on hemodialysis and 15 kidney recipients), 53 control subjects with comparable vascular risk profile and 10 kidney donors, plasma Aβ was determined using electrochemiluminescence immunoassay and gel electrophoresis followed by Western blotting. Plasma Aβ increased with CKD stage (control = 182.98 ± 76.73 pg/ml; CKD3A = 248.34 ± 103.77 pg/ml; CKD3B = 259.25 ± 97.74 pg/ml; CKD4 = 489.16 ± 154.16 pg/ml; CKD5 = 721.19 ± 291.69 pg/ml) and was not influenced by hemodialysis (CKD5D = 697.97 ± 265.91 pg/ml). Renal transplantation reduced plasma Aβ (332.57 ± 162.82 pg/ml), whereas kidney donation increased it (251.51 ± 34.34 pg/ml). Gel electrophoresis confirmed stage-dependent elevation namely of Aβ1-40, the most abundant Aβ peptide. In a multivariable regression including age, sex, estimated glomerular filtration rate (eGFR), potassium, hemoglobin, urine urea, and urine total protein, the factors eGFR (β = −0.42, p < 0.001), hemoglobin (β = −0.17, p = 0.020), and urine protein (β = 0.26, p = 0.008) were associated with plasma Aβ. In a regression including age, sex, eGFR, potassium, hemoglobin and the vascular risk factors systolic blood pressure, smoking, LDL, HDL, HbA1c, body mass index, brain-derived natriuretic peptide and fibrinogen, the factors eGFR (β = −0.53, p < 0.001), body mass index (β = −0.17, p = 0.022), and fibrinogen (β = 0.18, p = 0.024) were associated with plasma Aβ. Our results demonstrate a stage-dependent plasma Aβ increase that is augmented by loss of glomerulotubular integrity, low body weight, and inflammation, demonstrating a multifaceted role of renal dysfunction in Aβ retention."],["dc.identifier.doi","10.1007/s12035-015-9218-y"],["dc.identifier.gro","3151675"],["dc.identifier.pmid","26019016"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8493"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.notes.submitter","chake"],["dc.relation.issn","0893-7648"],["dc.title","Factors Responsible for Plasma β-Amyloid Accumulation in Chronic Kidney Disease"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2797"],["dc.bibliographiccitation.issue","18"],["dc.bibliographiccitation.journal","Lab on a Chip"],["dc.bibliographiccitation.lastpage","2805"],["dc.bibliographiccitation.volume","18"],["dc.contributor.author","Kunding, Andreas H."],["dc.contributor.author","Busk, Louise L."],["dc.contributor.author","Webb, Helen"],["dc.contributor.author","Klafki, Hans W."],["dc.contributor.author","Otto, Markus"],["dc.contributor.author","Kutter, Jörg P."],["dc.contributor.author","Dufva, Martin"],["dc.date.accessioned","2020-12-10T18:11:23Z"],["dc.date.available","2020-12-10T18:11:23Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1039/C8LC00608C"],["dc.identifier.eissn","1473-0189"],["dc.identifier.issn","1473-0197"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/73991"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Micro-droplet arrays for micro-compartmentalization using an air/water interface"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","93"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Obesity Facts"],["dc.bibliographiccitation.lastpage","108"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Giuranna, Johanna"],["dc.contributor.author","Volckmar, Anna-Lena"],["dc.contributor.author","Heinen, Anna"],["dc.contributor.author","Peters, Triinu"],["dc.contributor.author","Schmidt, Börge"],["dc.contributor.author","Spieker, Anne"],["dc.contributor.author","Straub, Helena"],["dc.contributor.author","Grallert, Harald"],["dc.contributor.author","Müller, Timo D."],["dc.contributor.author","Antel, Jochen"],["dc.contributor.author","Haußmann, Ute"],["dc.contributor.author","Klafki, Hans"],["dc.contributor.author","Liangyou, Rui"],["dc.contributor.author","Hebebrand, Johannes"],["dc.contributor.author","Hinney, Anke"],["dc.date.accessioned","2020-12-10T18:37:49Z"],["dc.date.available","2020-12-10T18:37:49Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1159/000486962"],["dc.identifier.eissn","1662-4033"],["dc.identifier.issn","1662-4025"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/77104"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","The Effect of SH2B1 Variants on Expression of Leptin- and Insulin-Induced Pathways in Murine Hypothalamus"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","101"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Journal of Alzheimer's Disease"],["dc.bibliographiccitation.lastpage","110"],["dc.bibliographiccitation.volume","49"],["dc.contributor.author","Savastano, Adriana"],["dc.contributor.author","Klafki, Hans"],["dc.contributor.author","Haußmann, Ute"],["dc.contributor.author","Oberstein, Timo Jan"],["dc.contributor.author","Muller, Petr"],["dc.contributor.author","Wirths, Oliver"],["dc.contributor.author","Wiltfang, Jens"],["dc.contributor.author","Bayer, Thomas A."],["dc.date.accessioned","2017-09-07T11:44:34Z"],["dc.date.available","2017-09-07T11:44:34Z"],["dc.date.issued","2015"],["dc.description.abstract","According to the modified amyloid hypothesis, the key event in the pathogenesis of Alzheimer’s disease (AD) is the deposition of neurotoxic amyloid β-peptides (Aβs) in plaques and cerebral blood vessels. Additionally to full-length peptides, a great diversity of N-truncated Aβ variants is derived from the larger amyloid-β protein precursor (AβPP). Vast evidence suggests that Aβx-42 isoforms play an important role in triggering neurodegeneration due to their high abundance, amyloidogenic propensity and toxicity. Although N-truncated Aβ peptides and Aβx-42 species appear to be the crucial players in AD etiology, the Aβ2-X isoforms did not receive much attention yet. The present study is the first to show immunohistochemical evidence of Aβ2-X in cases of AD and its distribution in AβPP/PS1KI and 5XFAD transgenic mouse models using a novel antibody pAB77 that has been developed using Aβ2-14 as antigen. Positive plaques and congophilic amyloid angiopathy (CAA) were observed in AD cases and in both mouse models. While in AD cases, abundant CAA and less pronounced plaque pathology was evident, the two mouse models showed predominantly extracellular Aβ deposits and minor CAA staining. Western blotting and a capillary isoelectric focusing immunoassay demonstrated the high specificity of the antibody pAb77 against Aβ-variants starting with the N-terminal Alanine-2."],["dc.identifier.doi","10.3233/jad-150394"],["dc.identifier.gro","3151701"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8520"],["dc.language.iso","en"],["dc.notes.status","public"],["dc.notes.submitter","chake"],["dc.relation.issn","1387-2877"],["dc.title","N-Truncated Aβ2-X Starting with Position Two in Sporadic Alzheimer’s Disease Cases and Two Alzheimer Mouse Models"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Pharmacopsychiatry"],["dc.bibliographiccitation.volume","38"],["dc.contributor.author","Maler, Juan Manuel"],["dc.contributor.author","Esselmann, Herrmann"],["dc.contributor.author","Dyrks, T."],["dc.contributor.author","Klafki, H."],["dc.contributor.author","Fiszer, M."],["dc.contributor.author","Paul, S."],["dc.contributor.author","Reulbach, Udo"],["dc.contributor.author","Lewczuk, Piotr"],["dc.contributor.author","Ruther, Eckart"],["dc.contributor.author","Kornhuber, Johannes"],["dc.contributor.author","Wiltfang, J."],["dc.date.accessioned","2018-11-07T10:56:36Z"],["dc.date.available","2018-11-07T10:56:36Z"],["dc.date.issued","2005"],["dc.format.extent","262"],["dc.identifier.isi","000232591900164"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/50051"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Georg Thieme Verlag Kg"],["dc.publisher.place","Stuttgart"],["dc.relation.conference","24th Symposium of the Arbeitsgemeinschaft-fur-Neuropsychopharmakologie-und-Pharmakopsychiatrie (AGNP)"],["dc.relation.eventlocation","Munich, GERMANY"],["dc.relation.issn","0176-3679"],["dc.title","Specific inhibition of beta-amyloid peptide secretion by ZK808762 mimicks the effect of non-steroidal antiinflammatory drugs"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]