Ahsen, Nicolas von

[["dc.bibliographiccitation.firstpage","156"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Clinical Chemistry"],["dc.bibliographiccitation.lastpage","161"],["dc.bibliographiccitation.volume","46"],["dc.contributor.author","von Ahsen, Nicolas"],["dc.contributor.author","Oellerich, M."],["dc.contributor.author","Schutz, Ekkehard"],["dc.date.accessioned","2018-11-07T10:16:50Z"],["dc.date.available","2018-11-07T10:16:50Z"],["dc.date.issued","2000"],["dc.description.abstract","Background: alpha(1)-Antitrypsin is the major plasma serine protease inhibitor. Its deficiency is mainly associated with the alleles PI S and PI Z and can lead to obstructive lung disease in adults and to liver cirrhosis during childhood. Methods: A multiplex PCR method has been established that uses two sets of primers to amplify the gene regions covering the PI S or PI Z mutations sites. Mutation detection was performed on the LightCycler by melting curve analysis of detection probes labeled with two different fluorescent dyes, LC-Red640 and LC-Red705. Results: Unequivocal genotyping results were obtained for all investigated samples in an assay time of similar to 30 min. The color compensation procedure greatly improved the readability of the resulting diagnostic melting curves. Conclusions: To our knowledge, this is the first report of simultaneous detection of two mutations in a single tube by PCR of genomic DNA and the use of two different reporter dyes with the LightCycler color compensation feature. This approach is a rapid, convenient, and economic alternative to other methods described to date for the detection of alpha(1)-antitrypsin deficiency alleles. (C) 2000 American Association for Clinical Chemistry."],["dc.identifier.isi","000085288500004"],["dc.identifier.pmid","10657370"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/41113"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Assoc Clinical Chemistry"],["dc.publisher.place","Washington"],["dc.relation.conference","Meeting of the Deutsche-Gesellschaft-fur-Klinische-Chemie / Deutsche-Gesellschaft-fur-Laboratoriumsmedizin"],["dc.relation.eventlocation","REGENSBURG, GERMANY"],["dc.relation.issn","0009-9147"],["dc.title","Use of two reporter dyes without interference in a single-tube rapid-cycle PCR: alpha(1)-antitrypsin genotyping by multiplex real-time fluorescence PCR with the LightCycler"],["dc.type","conference_paper"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","297"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Therapeutic Drug Monitoring"],["dc.bibliographiccitation.lastpage","304"],["dc.bibliographiccitation.volume","27"],["dc.contributor.author","El Desoky, E. S."],["dc.contributor.author","Abdelsalam, Y. M."],["dc.contributor.author","Salama, R. H."],["dc.contributor.author","El Akkad, M. A."],["dc.contributor.author","Atanasova, Srebrena"],["dc.contributor.author","von Ahsen, Nicolas"],["dc.contributor.author","Armstrong, Victor William"],["dc.contributor.author","Oellerich, M."],["dc.date.accessioned","2018-11-07T10:58:59Z"],["dc.date.available","2018-11-07T10:58:59Z"],["dc.date.issued","2005"],["dc.description.abstract","Arylarnine N-acetyl transferase (NAT2) displays extensive genetic polymorphisms that affect the rates of acetylation of drugs and genotoxic compounds such as amine carcinogens. To investigate whether the slow acetylator genotype is a risk factor for development of bladder cancer following schistosomal infection of the urinary tract, the authors determined the frequencies of 3 common polymorphisms in the NAT2 gene (341T > C, 590G > A, and 282C > T), which are associated with impaired acetylation activity, in control subjects (n = 61; mean age 34.3 +/- 9.2 years) and in schistosomiasis-associated bladder cancer patients (n = 55; 52 +/- 10.9 years) from the Egyptian population. Genotyping was carried out using rapid cycle PCR on the LightCycler, and subjects were assigned to a slow, intermediate, or rapid acetylator phenotype on the basis of the genotypes. The frequencies of the mutant alleles observed in the controls from the present study were similar to those reported previously for both the Egyptian population and other Arab populations. Patients showed a higher prevalence (78.2%) of slow acetylator phenotype than controls (67.2%), but this did not reach statistical significance (P = 0.19). However, there were significantly more individuals who were carriers of 2 mutant 341T > C alleles (NAT2 5/ 5 genotype) in the patient group compared with controls (odds ratio 2.6, CI 1.02-6.67, P = 0.026). The alloenzyme encoded by this allele has been shown to display a large reduction in its catalytic activity. In conclusion, these data suggest that the NAT2 5/ 5 genotype is a potential risk factor for development of urinary bladder cancer in patients with prior schistosomiasis infection."],["dc.identifier.doi","10.1097/01.ftd.0000164197.95494.aa"],["dc.identifier.isi","000229592500009"],["dc.identifier.pmid","15905799"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/50593"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Lippincott Williams & Wilkins"],["dc.relation.issn","0163-4356"],["dc.title","NAT2 5/ 5 genotype (341T > C) is a potential risk factor for schistosomiasis-associated bladder cancer in Egyptians"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","586"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Blood"],["dc.bibliographiccitation.lastpage","593"],["dc.bibliographiccitation.volume","103"],["dc.contributor.author","von Ahsen, Nicolas"],["dc.contributor.author","Oellerich, M."],["dc.date.accessioned","2018-11-07T10:51:46Z"],["dc.date.available","2018-11-07T10:51:46Z"],["dc.date.issued","2004"],["dc.description.abstract","The common prothrombin gene cleavage site mutation 20210G>A is associated with elevated prothrombin levels and thrombosis. The pathomechanism of the 20210G>A mutation was explained by increased mRNA formation and/or more efficient translation. Human studies also showed an influence of the intronic 19911A>G polymorphism on prothrombin activity. We established HepG2 cell lines stably transfected with prothrombin mini-genes containing the last 2 prothrombin exons, the last intron, 3' untranslated region (UTR), and flanking sequence. The highest mRNA expression and protein activity resulted from the mutant haplotype 19911A-20210A. Haplotypes with wild-type cleavage site (19911A-20210G, 19911G-20210G) also differed significantly as a consequence of the intronic 19911 mutation; the 19911G-2021OG haplotype showed lower expression than the 19911A-20210G haplotype, whereas previous clinical studies have reported elevated prothrombin activity with the 19911G-2021OG haplotype. The cleavage site pattern was homogeneous with 20210A, which may cause a favorable intracellular processing, and heterogeneous with 20210G. In an independent assay for splicing efficiency, 19911G showed about 30% higher efficiency than 19911A. We conclude that the intronic 19911A>G single nucleotide polymorphism is itself functional and changes splicing efficiency by altering a known functional pentamer motif. Further studies are needed to define the value of additional prothrombin 19911 genotyping for thrombophilia screening, especially in cases heterozygous for 20210G>A."],["dc.identifier.doi","10.1182/blood-2003-02-0419"],["dc.identifier.isi","000187954000042"],["dc.identifier.pmid","14504098"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/48961"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Hematology"],["dc.publisher.place","Washington"],["dc.relation.conference","47th Annual Meeting of the Society-of-Thrombosis-and-Haemostasis-Research"],["dc.relation.eventlocation","INNSBRUCK, AUSTRIA"],["dc.relation.issn","0006-4971"],["dc.title","The intronic prothrombin 19911 A > G polymorphism influences splicing efficiency and modulates effects of the 20210G > A polymorphism on mRNA amount and expression in a stable reporter gene assay system"],["dc.type","conference_paper"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","155"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Journal of Medical Primatology"],["dc.bibliographiccitation.lastpage","164"],["dc.bibliographiccitation.volume","35"],["dc.contributor.author","Atanasova, Srebrena"],["dc.contributor.author","von Ahsen, Nicolas"],["dc.contributor.author","Schlumbohm, Christina"],["dc.contributor.author","Wieland, Eberhard"],["dc.contributor.author","Oellerich, M."],["dc.contributor.author","Armstrong, Victor William"],["dc.date.accessioned","2018-11-07T09:45:57Z"],["dc.date.available","2018-11-07T09:45:57Z"],["dc.date.issued","2006"],["dc.description.abstract","Background Dysfunction of the cellular antioxidant system and accumulation of reactive oxygen species are involved in the pathophysiology of diseases such as cardiovascular disease, neurodegenerative disorders, tumors, male infertility and aging. Two gluthathione peroxidases play key roles in the cellular protection against oxidative damage. Glutathione peroxidase (GPx-1) removes cytosolic hydroperoxides while phospholipid-hydroperoxide glutathione peroxidase (GPx-4) is a unique enzyme that reduces phospholipid peroxides in membranes. Methods We cloned and sequenced the full-length cDNA for GPx-1 (GenBank: AY966403) and GPx-4 (GenBank: AY966404) from the common marmoset (Callithrix jacchus) in order to create a suitable model for studying human diseases related with oxidative stress. Results The cDNAs encode a 202 amino acid protein for GPx-1 and a 197 amino acid protein for GPx-4. Both proteins include selenocysteine (Sec, in Gpx-1 at position 48; in GPx-4 at position 73) and showed high homology (> 90%) with other mammalian GPxs. The relative levels of mRNA expression for GPx-1 and GPx-4 were determined in different marmoset tissues by quantitative real-time reverse transcriptase-polymerase chain reaction using transcription elongation factor-2 as a reference gene. GPx-1 showed increased levels of expression in the liver, heart and kidney while the highest mRNA levels for GPx-4 were detected in the testis, followed by the liver, lung, kidney and spinal cord. Conclusions These findings will be of value for studies designed to assess the role of glutathione peroxidases in non-human primate models for a variety of diseases in which increased oxidative stress has been implicated."],["dc.identifier.doi","10.1111/j.1600-0684.2006.00158.x"],["dc.identifier.isi","000237352700007"],["dc.identifier.pmid","16764674"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/34757"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Blackwell Publishing"],["dc.relation.issn","0047-2565"],["dc.title","Marmoset glutathione peroxidases: cDNA sequences, molecular evolution, and gene expression"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","56"],["dc.bibliographiccitation.journal","Transplant International"],["dc.bibliographiccitation.lastpage","57"],["dc.bibliographiccitation.volume","23"],["dc.contributor.author","Rother, A."],["dc.contributor.author","Glander, Petra"],["dc.contributor.author","Vitt, Esther"],["dc.contributor.author","Feneberg, Reinhard"],["dc.contributor.author","von Ahsen, Nicolas"],["dc.contributor.author","Armstrong, Victor William"],["dc.contributor.author","Oellerich, M."],["dc.contributor.author","Budde, C."],["dc.contributor.author","Toenshoff, Burkhardt"],["dc.contributor.author","Weber, Lutz T."],["dc.date.accessioned","2018-11-07T08:39:02Z"],["dc.date.available","2018-11-07T08:39:02Z"],["dc.date.issued","2010"],["dc.identifier.isi","000281666000228"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/18893"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell Publishing, Inc"],["dc.publisher.place","Malden"],["dc.relation.issn","0934-0874"],["dc.title","INOSINE 5-MONOPHOSPHATE DEHYDROGENASE (IMPDH) ACTIVITY IN CHILDREN AND ADOLESCENTS: PHYSIOLOGICAL REGULATION AND RESPONSE TO MYCOPHENOLIC ACID (MPA) THERAPY"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2995"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Blood"],["dc.bibliographiccitation.lastpage","2996"],["dc.bibliographiccitation.volume","105"],["dc.contributor.author","von Ahsen, Nicolas"],["dc.contributor.author","Oellerich, M."],["dc.date.accessioned","2018-11-07T11:09:46Z"],["dc.date.available","2018-11-07T11:09:46Z"],["dc.date.issued","2005"],["dc.identifier.isi","000228042900064"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/53081"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Hematology"],["dc.relation.issn","0006-4971"],["dc.title","Prothrombin 19911A > G as a functional noncoding variant: the evidence remains"],["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","438"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Therapeutic Drug Monitoring"],["dc.bibliographiccitation.lastpage","443"],["dc.bibliographiccitation.volume","24"],["dc.contributor.author","Wigger, M."],["dc.contributor.author","Armstrong, Victor William"],["dc.contributor.author","Shipkova, Maria"],["dc.contributor.author","Wacke, R."],["dc.contributor.author","Nizze, H."],["dc.contributor.author","Streit, Frank"],["dc.contributor.author","von Ahsen, Nicolas"],["dc.contributor.author","Muscheites, J."],["dc.contributor.author","Glasenapp, S."],["dc.contributor.author","Stolpe, H. J."],["dc.contributor.author","Oellerich, M."],["dc.date.accessioned","2018-11-07T10:29:47Z"],["dc.date.available","2018-11-07T10:29:47Z"],["dc.date.issued","2002"],["dc.description.abstract","A juvenile, female renal transplant recipient suffered two acute rejection episodes: the first on posttransplant day 31 while taking cyclosporine, prednisone, and mycophenolate mofetil (MMF); and the second on posttransplant clay 67, when she was taking tacrolimus, prednisone, and MMF. Dosage of MMF was initially started at 2 g/d (corresponding to 600 mg MMF/m(2) twice daily) but was reduced to 250 mg/d to 500 mg/d after severe diarrhea and a paralytic ileus on posttransplant day 16. During therapy with tacrolimus, prednisone, and MMF, predose plasma mycophenolic acid (MPA) concentrations varied from 1.1 mg/L to 8.2 mg/L (median 3.0 mg/L). On posttransplant day 91, a 12-hour pharmacokinetic profile was obtained. The concentrations of MPA and its metabolites were determined with a validated high-performance liquid chromatography (HPLC) procedure. After oral MMIF (250 mg) administration, the MPA concentration showed an atypical decline front a predose concentration of 6.0 mg/L to a value of 3.8 mg/L at 75 minutes postdose, and 3.4 mg/L at 6 hours postdose, before returning to 6.0 mg/L after 12 hours. The 12-hour area under the concentration-time curve (AUC) values for MPA and its major metabolite the phenolic glucuronide MPAG were 55.1 mg.h/L and 800 mg.h/L, respectively. An unusually high concentration (12-h AUC, 165 mg.h/L) of the phenolic glucose conjugate of MPA was found. The apparent renal clearance of MPAG was only 2.2 mL/min. Her creatinine clearance was 30 mL/min. MPAG clearances have been reported to range from approximately. 5.5 m:/min to 35 mL/min at a creatinine clearance of approximately 30 mL/min in renal transplant recipients. The authors' findings suggest that conjugation and clearance of MPA through the kidney is strongly impaired in this patient. The relatively high preclose MPA concentrations could result from an enhanced enterohepatic circulation of MPA and its metabolites."],["dc.identifier.doi","10.1097/00007691-200206000-00019"],["dc.identifier.isi","000175866900019"],["dc.identifier.pmid","12021639"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/43715"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Lippincott Williams & Wilkins"],["dc.relation.issn","0163-4356"],["dc.title","Atypical pharmacokinetics and metabolism of mycophenolic acid in a young kidney transplant recipient with impaired renal function"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","223"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Clinical Biochemistry"],["dc.bibliographiccitation.lastpage","228"],["dc.bibliographiccitation.volume","38"],["dc.contributor.author","Atanasova, S. Y."],["dc.contributor.author","von Ahsen, Nicolas"],["dc.contributor.author","Toncheva, D. I."],["dc.contributor.author","Dimitrov, T. G."],["dc.contributor.author","Oellerich, M."],["dc.contributor.author","Armstrong, Victor William"],["dc.date.accessioned","2018-11-07T11:18:35Z"],["dc.date.available","2018-11-07T11:18:35Z"],["dc.date.issued","2005"],["dc.description.abstract","Objectives: The concept of multifactorial etiology of BEN anticipates that a combination of polymorphic gene variants and various environmental factors causes an increased risk for the disease. CYP enzymes play a key role in the metabolic activation of environmental chemicals and toxins. CYP3A enzymes are particularly relevant for xenobiotic metabolism because of their broad substrate specificity and abundant expression in the human liver, intestine, and kidney. Previous phenotyping analysis on CYP2D6 enzyme activity in BEN patients proposed a modifying effect of CYP2D6 gene variants on BEN risk, but it was not approved with molecular-genetic methods. The aim of the current case-control study was to compare the frequency of CYP2D6 and CYP3A5 polymorphisms, as well as one CYP3A4 promoter variant in BEN patients and controls in order to investigate a possible association between individual genetic variations in these genes and susceptibility to BEN. Design and methods: Ninety-six nonrelated Bulgarian BEN patients from endemic villages in the Vratza district and 112 healthy Bulgarians from nonendemic areas (controls) were genotyped. Identification of alleles was done by allele-specific PCR or by rapid-cycle amplification on the LightCycler, followed by sequence-specific detection. Results: The UM, PM, and EM + IM genotype frequencies of CYP2D6 did not differ significantly between the two groups (P > 0.05). The CYP3A4 1B allele was only found in the heterozygous form, with allelic frequencies of 5.21% in the patients and 2.23% in the healthy individuals (P = 0.11). The CYP3A5 1 allele was more prevalent in BEN patients with a frequency of 9.38% compared to 5.36% in the controls and was associated with a higher risk for BEN (OR 2.41, 95% CI 1.09-5.33) (P = 0.02). Conclusions: Our results demonstrate that the CYP3A5 1 allele, previously reported as a marker for CYP3A5 expression in human kidney, is associated with increased risk for BEN, while CYP3A4 1B and CYP2D6 genotypes do not significantly modify the risk for the disease. (C) 2005 The Canadian Society of Clinical Chemists. All rights reserved."],["dc.identifier.doi","10.1016/j.clinbiochem.2004.12.002"],["dc.identifier.isi","000227206700003"],["dc.identifier.pmid","15708542"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/55070"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Pergamon-elsevier Science Ltd"],["dc.relation.issn","0009-9120"],["dc.title","Genetic polymorphisms of cytochrome P450 among patients with Balkan endemic nephropathy (BEN)"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","220"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Therapeutic Drug Monitoring"],["dc.bibliographiccitation.lastpage","226"],["dc.bibliographiccitation.volume","26"],["dc.contributor.author","Armstrong, Victor William"],["dc.contributor.author","Shipkova, Maria"],["dc.contributor.author","von Ahsen, Nicolas"],["dc.contributor.author","Oellerich, M."],["dc.date.accessioned","2018-11-07T10:50:10Z"],["dc.date.available","2018-11-07T10:50:10Z"],["dc.date.issued","2004"],["dc.description.abstract","The thiopurine medications 6-mercaptopurine (6-MP), 6-thioguanine (6-TG), and azathioprine are used in treatment of childhood acute lymphoblastic leukemia, amoimmune diseases, and, in the case of azathioprine, in solid organ transplantation. They are converted in vivo to the active 6-thioguanine nucleotides (6-TGN). One person in 300 in white populations has low or undetectable TPMT activity and is at risk for accumulating 6-TGN with the consequence of severe, life-threatening myelosuppression. A rational therapeutic strategy for thiopurine drug use is to first determine TPMT phenotype/genotype and then to adjust the dosage on an individual basis. Determination of erythrocyte 6-TGN levels can further help to optimize therapy. TPMT activity (phenotype) is determined in erythrocytes using radiochemical or HPLC procedures. Recent HPLC procedures show good agreement with the original radiochemical method, while offering simplified sample pretreatment and improved precision. To date, 12 mutant alleles responsible for TPMT deficiency have been published. Restriction fragment length polymorphism PCR and allele-specific PCR have been used for detection of TPMT mutations. Genotyping methods that allow a higher throughput include real-time PCR (LightCycler) and denaturing HPLC. Numerous HPLC methods have been reported for quantification of 6-TGN. The majority involve acid hydrolysis to 6-TG at high temperature. There are substantial differences in the hydrolysis step, extraction procedure, chromatographic conditions and method of detection. Erythrocyte 6-TGN concentrations can vary up to 2.6-fold depending on the HPLC method. The method that has found the greatest application in clinical studies is that of Lennard.(46) This has served as the basis for the establishment of treatment-related therapeutic ranges for thiopurine therapy. These ranges will not necessarily be applicable when other methodology is used. There is an urgent need to harmonize the analytic procedures for 6-TGN."],["dc.identifier.doi","10.1097/00007691-200404000-00024"],["dc.identifier.isi","000223147100025"],["dc.identifier.pmid","15228169"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/48594"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Lippincott Williams & Wilkins"],["dc.publisher.place","Philadelphia"],["dc.relation.conference","8th International Congress of Therapeutic Drug Monitoring and Clinical Toxicology"],["dc.relation.eventlocation","BASEL, SWITZERLAND"],["dc.relation.issn","0163-4356"],["dc.title","Analytic aspects of monitoring therapy with thiopurine medications"],["dc.type","conference_paper"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","European Journal of Human Genetics"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Atanasova, Srebrena"],["dc.contributor.author","von Ahsen, Nicolas"],["dc.contributor.author","Dimitrov, T."],["dc.contributor.author","Oellerich, M."],["dc.contributor.author","Toncheva, D."],["dc.date.accessioned","2018-11-07T10:30:09Z"],["dc.date.available","2018-11-07T10:30:09Z"],["dc.date.issued","2002"],["dc.format.extent","179"],["dc.identifier.isi","000187166100586"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/43800"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Nature Publishing Group"],["dc.publisher.place","London"],["dc.relation.conference","European-Society-of-Human-Genetics European Human Genetics Conference in Conjuction With European Meeting on Psychosocial Aspects of Genetics"],["dc.relation.eventlocation","STRASBOURG, FRANCE"],["dc.relation.issn","1018-4813"],["dc.title","NAT polymorphisms in Bulgarian patients with Balkan endemic nephropathy (BEN)"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]