Krätzner, Ralph

[["dc.bibliographiccitation.firstpage","2100"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","European Journal of Organic Chemistry"],["dc.bibliographiccitation.lastpage","2106"],["dc.contributor.author","Pitulescu, Marian"],["dc.contributor.author","Grapp, Marcel"],["dc.contributor.author","Kraetzner, Ralph"],["dc.contributor.author","Knepel, Willhart"],["dc.contributor.author","Diederichsen, Ulf"],["dc.date.accessioned","2018-11-07T11:16:29Z"],["dc.date.available","2018-11-07T11:16:29Z"],["dc.date.issued","2008"],["dc.description.abstract","Two formacetal-linked dinucleotides TT and TT were synthesized as phosphoramidite building blocks for solid-phase synthesis. Incorporated in a 29-mer DNA, the oligomers P3(TT) and P3(TA) were studied with respect to the binding activity towards the Pax6 homeodomain. Substitution of the negatively charged phosphodiester by a neutral formacetal linker facilitates the bent conformation of double-stranded DNA. The duplex stability was affected more significantly by the TT formacetal modification, whereas destabilization induced by TA was less pronounced. Based on CD spectroscopy, the TA formacetal-modified oligomer P3(TA) A has mainly B-DNA topology, whereas the P3(TT) modified oligomet significantly deviated from B-form DNA. The binding affinity of the P3 oligomer towards Pax6 HD was investigated by in vitro EMSA experiments providing even a small increase in binding affinity for the P3(TA) T oligomer. ((C) Wiley-VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2008)."],["dc.identifier.doi","10.1002/ejoc.200701178"],["dc.identifier.isi","000255508600010"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/54599"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","1434-193X"],["dc.title","Synthesis of formacetal-linked dinucleotides to facilitate dsDNA bending and binding to the homeodomain of Pax6"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","515"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Circulation"],["dc.bibliographiccitation.lastpage","525"],["dc.bibliographiccitation.volume","116"],["dc.contributor.author","Knoell, Ralph"],["dc.contributor.author","Postel, Ruben"],["dc.contributor.author","Wang, Jianming"],["dc.contributor.author","Kraetzner, Ralph"],["dc.contributor.author","Hennecke, Gerrit"],["dc.contributor.author","Vacaru, Andrei M."],["dc.contributor.author","Vakeel, Padmanabhan"],["dc.contributor.author","Schubert, Cornelia"],["dc.contributor.author","Murthy, Kenton"],["dc.contributor.author","Rana, Brinda K."],["dc.contributor.author","Kube, Dieter"],["dc.contributor.author","Knoell, Gudrun"],["dc.contributor.author","Schaefer, Katrin"],["dc.contributor.author","Hayashi, Takeharu"],["dc.contributor.author","Holm, Torbjorn"],["dc.contributor.author","Kimura, Akinori"],["dc.contributor.author","Schork, Nicholas"],["dc.contributor.author","Toliat, Mohammad Reza"],["dc.contributor.author","Nürnberg, Peter"],["dc.contributor.author","Schultheiss, Heinz-Peter"],["dc.contributor.author","Schaper, Wolfgang"],["dc.contributor.author","Schaper, Jutta"],["dc.contributor.author","Bos, Erik"],["dc.contributor.author","Hertog, Jeroen den"],["dc.contributor.author","van Eeden, Fredericus J. M."],["dc.contributor.author","Peters, Peter J."],["dc.contributor.author","Hasenfuß, Gerd"],["dc.contributor.author","Chien, Kenneth R."],["dc.contributor.author","Bakkers, Jeroen"],["dc.date.accessioned","2017-09-07T11:49:27Z"],["dc.date.available","2017-09-07T11:49:27Z"],["dc.date.issued","2007"],["dc.description.abstract","Background - Extracellular matrix proteins, such as laminins, and endothelial cells are known to influence cardiomyocyte performance; however, the underlying molecular mechanisms remain poorly understood. Methods and Results - We used a forward genetic screen in zebrafish to identify novel genes required for myocardial function and were able to identify the lost-contact (loc) mutant, which encodes a nonsense mutation in the integrin-linked kinase ( ilk) gene. This loc/ilk mutant is associated with a severe defect in cardiomyocytes and endothelial cells that leads to severe myocardial dysfunction. Additional experiments revealed the epistatic regulation between laminin-alpha 4 (Lama4), integrin, and Ilk, which led us to screen for mutations in the human ILK and LAMA4 genes in patients with severe dilated cardiomyopathy. We identified 2 novel amino acid residue - altering mutations (2828C > T [Pro943Leu] and 3217C > T [Arg1073X]) in the integrin-interacting domain of the LAMA4 gene and 1 mutation (785C > T [Ala262Val]) in the ILK gene. Biacore quantitative protein/protein interaction data, which have been used to determine the equilibrium dissociation constants, point to the loss of integrin-binding capacity in case of the Pro943Leu (K-d = 5 +/- 3 mu mol/L) and Arg1073X LAMA4 (K-d=1 +/- 0.2 mu mol/L) mutants compared with the wild-type LAMA4 protein (K-d=440 +/- 20nmol/L). Additional functional data point to the loss of endothelial cells in affected patients as a direct consequence of the mutant genes, which ultimately leads to heart failure. Conclusions - This is the first report on mutations in the laminin, integrin, and ILK system in human cardiomyopathy, which has consequences for endothelial cells as well as for cardiomyocytes, thus providing a new genetic basis for dilated cardiomyopathy in humans."],["dc.identifier.doi","10.1161/CIRCULATIONAHA.107.689984"],["dc.identifier.gro","3143464"],["dc.identifier.isi","000248456000009"],["dc.identifier.pmid","17646580"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/981"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0009-7322"],["dc.title","Laminin-alpha 4 and integrin-linked kinase mutations cause human cardiomyopathy via simultaneous defects in cardiomyocytes and endothelial cells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Naunyn-Schmiedeberg s Archives of Pharmacology"],["dc.bibliographiccitation.volume","375"],["dc.contributor.author","Oetjen, Elke"],["dc.contributor.author","Blume, Roland"],["dc.contributor.author","Cierny, I."],["dc.contributor.author","Kutschenko, Anna"],["dc.contributor.author","Kraetzner, Ralph"],["dc.contributor.author","Stein, R."],["dc.contributor.author","Knepel, Willhart"],["dc.date.accessioned","2018-11-07T11:04:44Z"],["dc.date.available","2018-11-07T11:04:44Z"],["dc.date.issued","2007"],["dc.format.extent","49"],["dc.identifier.isi","000245997000216"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/51901"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","New york"],["dc.relation.conference","48th Spring Meeting of the Deutsche-Gesellschaft-fur Experimentelle-ung-Klinische-Pharmakologie-und-Toxikologie"],["dc.relation.eventlocation","Mainz, GERMANY"],["dc.relation.issn","0028-1298"],["dc.title","Inhibition of MafA transcriptional activity contributes to the inhibition of human insulin gene transcription by MEKK1 and interleukin-1beta"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1255"],["dc.bibliographiccitation.journal","ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY"],["dc.bibliographiccitation.lastpage","1262"],["dc.bibliographiccitation.volume","61"],["dc.contributor.author","Kratzner, R."],["dc.contributor.author","Debreczeni, J. E."],["dc.contributor.author","Pape, T."],["dc.contributor.author","Schneider, Thomas R."],["dc.contributor.author","Wentzel, A."],["dc.contributor.author","Kolmar, Harald"],["dc.contributor.author","Sheldrick, George M."],["dc.contributor.author","Uson, I."],["dc.date.accessioned","2018-11-07T10:55:49Z"],["dc.date.available","2018-11-07T10:55:49Z"],["dc.date.issued","2005"],["dc.description.abstract","The Ecballium elaterium trypsin inhibitor II (EETI-II) belongs to the family of squash inhibitors and is one of the strongest inhibitors known for trypsin. The eight independent molecules of EETI-II in the crystal structure reported here provide a good opportunity to test the hypothesis that this small cystine-knot protein (knottin) is sufficiently rigid to be used as a molecular scaffold for protein-engineering purposes. To extend this test, the structures of two complexes of EETI-II with trypsin have also been determined, one carrying a four-amino-acid mutation of EETI-II. The remarkable similarity of these structures confirms the rigidity of the molecular framework and hence its suitability as a molecular scaffold."],["dc.identifier.doi","10.1107/S0907444905021207"],["dc.identifier.isi","000231243400011"],["dc.identifier.pmid","16131759"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/49872"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Blackwell Publishing"],["dc.relation.issn","0907-4449"],["dc.title","Structure of Ecballium elaterium trypsin inhibitor II (EETI-II): a rigid molecular scaffold"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2125"],["dc.bibliographiccitation.journal","ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY"],["dc.bibliographiccitation.lastpage","2132"],["dc.bibliographiccitation.volume","59"],["dc.contributor.author","Debreczeni, J. E."],["dc.contributor.author","Girmann, B."],["dc.contributor.author","Zeeck, Axel"],["dc.contributor.author","Kratzner, R."],["dc.contributor.author","Sheldrick, George M."],["dc.date.accessioned","2018-11-07T10:34:08Z"],["dc.date.available","2018-11-07T10:34:08Z"],["dc.date.issued","2003"],["dc.description.abstract","The crystal structure of viscotoxin A3 (VT A3) extracted from European mistletoe ( Viscum album L.) has been solved using the anomalous diffraction of the native S atoms measured in-house with Cu Kalpha radiation to a resolution of 2.2 Angstrom and truncated to 2.5 Angstrom. A 1.75 Angstrom resolution synchrotron data set was used for phase expansion and refinement. An innovation in the dual-space substructure-solution program SHELXD enabled the individual S atoms of the disulfide bonds to be located using the Cu Kalpha data; this resulted in a marked improvement in the phasing compared with the use of super-S atoms. The VT A3 monomer consists of 46 amino acids with three disulfide bridges and has an overall fold resembling the canonical architecture of the alpha- and beta-thionins, a capital letter L. The asymmetric unit consists of two monomers related by a local twofold axis and held together by hydrophobic interactions between the monomer units. One phosphate anion (confirmed by P-31-NMR and MS) is associated with each monomer."],["dc.identifier.doi","10.1107/S0907444903018973"],["dc.identifier.isi","000186884000010"],["dc.identifier.pmid","14646070"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/44789"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Blackwell Munksgaard"],["dc.relation.issn","0907-4449"],["dc.title","Structure of viscotoxin A3: disulfide location from weak SAD data"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2803"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","American Journal of Medical Genetics Part A"],["dc.bibliographiccitation.lastpage","2807"],["dc.bibliographiccitation.volume","173"],["dc.contributor.author","Weissbach, Susann"],["dc.contributor.author","Reinert, Marie-Christine"],["dc.contributor.author","Altmüller, Janine"],["dc.contributor.author","Krätzner, Ralph"],["dc.contributor.author","Thiele, Holger"],["dc.contributor.author","Rosenbaum, Thorsten"],["dc.contributor.author","Nürnberg, Peter"],["dc.contributor.author","Gärtner, Jutta"],["dc.date.accessioned","2018-04-23T11:47:26Z"],["dc.date.available","2018-04-23T11:47:26Z"],["dc.date.issued","2017"],["dc.description.abstract","Cabezas type of X‐linked syndromic intellectual disability (MRXSC; MIM300354) is a rare X‐linked recessive intellectual disability characterized primarily by intellectual disability, short stature, hypogonadism, and gait abnormalities. It is caused by a wide spectrum of hemizygous variants in CUL4B. In a 10‐year‐old boy with an exceptional leukoencephalopathy pattern, we identified a new missense variant p.Leu329Gln in CUL4B using “Mendeliome” sequencing. However, his phenotype does not include the severe characteristics currently known for MRXSC. We discuss the divergent phenotype and propose a potential connection between the different CUL4B variants and corresponding phenotypes in the context of the current literature as well as 3D homology modeling."],["dc.identifier.doi","10.1002/ajmg.a.38390"],["dc.identifier.gro","3142217"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/13339"],["dc.language.iso","en"],["dc.notes.intern","lifescience updates Crossref Import"],["dc.notes.status","final"],["dc.relation.issn","1552-4825"],["dc.title","A new CUL4B variant associated with a mild phenotype and an exceptional pattern of leukoencephalopathy"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2845"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","American Journal of Medical Genetics"],["dc.bibliographiccitation.lastpage","2849"],["dc.bibliographiccitation.volume","152A"],["dc.contributor.author","Gronborg, Sabine"],["dc.contributor.author","Kraetzner, Ralph"],["dc.contributor.author","Spiegler, Juliane"],["dc.contributor.author","Ferdinandusse, Sacha"],["dc.contributor.author","Wanders, Ronald J. A."],["dc.contributor.author","Waterham, Hans R."],["dc.contributor.author","Gärtner, Jutta"],["dc.date.accessioned","2017-09-07T11:45:12Z"],["dc.date.available","2017-09-07T11:45:12Z"],["dc.date.issued","2010"],["dc.description.abstract","D-bifunctional protein deficiency (DBPD) is an autosomal recessive disease caused by a defect in peroxisomal beta-oxidation. The majority of patients suffer from a severe neurological disease with neonatal hypotonia and seizures and die within the first 2 years of life. Few patients show milder clinical phenotypes with prolonged survival. The diagnosis relies on the clinical presentation, measurement of peroxisomal markers, including very long chain fatty acids (VLCFA) in plasma, followed by enzymatic studies in fibroblasts and genetic testing. Diagnosis can be difficult to establish in milder cases, especially if VLCFA concentration in plasma is not or only mildly elevated. We report on siblings in which initial measurement of plasma VLCFA did not indicate a peroxisomal disease. Nevertheless, cMRI showed a pattern typical for an inborn peroxisomal disease with cerebral and cerebellar leukencephalopathy, perisylvic polymicrogyria, and frontoparietal pachygyria. Repeated measurements of peroxisomal metabolites in plasma prompted by the cMRI findings showed values in the upper normal or mildly elevated range and led to further diagnostic steps. The diagnosis of a type III DBPD with a missense mutation (T15A) in the HSD17B4 gene, coding for D-bifunctional protein (DBP), could be established. We conclude that a typical \"peroxisomal pattern'' in cMRI including cerebral and cerebellar leukencephalopathy, perisylvic polymicrogyria and pachygyria is a valuable clue to the diagnosis of DBPD, especially in cases with no or only very mild abnormalities in plasma. (C) 2010 Wiley-Liss, Inc."],["dc.identifier.doi","10.1002/ajmg.a.33677"],["dc.identifier.gro","3142834"],["dc.identifier.isi","000284005700028"],["dc.identifier.pmid","20949532"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/282"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Wiley-liss"],["dc.relation.issn","1552-4825"],["dc.title","Typical cMRI Pattern as Diagnostic Clue for D-Bifunctional Protein Deficiency Without Apparent Biochemical Abnormalities in Plasma"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","16"],["dc.bibliographiccitation.journal","Circulation"],["dc.bibliographiccitation.volume","116"],["dc.contributor.author","Knoll, Ralph"],["dc.contributor.author","Postel, Ruben"],["dc.contributor.author","Kratzner, Ralph"],["dc.contributor.author","Hennecke, Gerrit"],["dc.contributor.author","Vacaru, Andrei M."],["dc.contributor.author","Vakeel, Padmanabhan"],["dc.contributor.author","Knoll, Gudrun"],["dc.contributor.author","Schafer, Katrin"],["dc.contributor.author","Bos, Erik"],["dc.contributor.author","Den Hertog, Jeroen"],["dc.contributor.author","Peters, Peter J."],["dc.contributor.author","van Eeden, Fredericus"],["dc.contributor.author","Schaper, Jutta"],["dc.contributor.author","Hasenfuß, Gerd"],["dc.contributor.author","Schultheiss, Heinz-Peter"],["dc.contributor.author","Chien, Kenneth R."],["dc.contributor.author","Bakkers, Jeroen"],["dc.contributor.author","Schaper, Wolfgang"],["dc.date.accessioned","2018-11-07T10:57:43Z"],["dc.date.available","2018-11-07T10:57:43Z"],["dc.date.issued","2007"],["dc.format.extent","221"],["dc.identifier.isi","000250394301030"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/50317"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Lippincott Williams & Wilkins"],["dc.publisher.place","Philadelphia"],["dc.relation.conference","80th Annual Scientific Session of the American-Heart-Association"],["dc.relation.eventlocation","Orlando, FL"],["dc.relation.issn","0009-7322"],["dc.title","Integrin-linked kinase and laminin alpha 4 mutations cause human cardiomyopathy"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","91"],["dc.bibliographiccitation.journal","JIMD reports"],["dc.bibliographiccitation.lastpage","99"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Dreha-Kulaczewski, S."],["dc.contributor.author","Kalscheuer, V."],["dc.contributor.author","Tzschach, A."],["dc.contributor.author","Hu, H."],["dc.contributor.author","Helms, G."],["dc.contributor.author","Brockmann, K."],["dc.contributor.author","Weddige, A."],["dc.contributor.author","Dechent, P."],["dc.contributor.author","Schlüter, G."],["dc.contributor.author","Krätzner, R."],["dc.contributor.author","Ropers, H. H."],["dc.contributor.author","Gärtner, J."],["dc.contributor.author","Zirn, B."],["dc.date.accessioned","2018-02-15T10:23:08Z"],["dc.date.available","2018-02-15T10:23:08Z"],["dc.date.issued","2013"],["dc.description.abstract","X-linked creatine transport (CRTR) deficiency, caused by mutations in the SLC6A8 gene, leads to intellectual disability, speech delay, epilepsy, and autistic behavior in hemizygous males. Additional diagnostic features are depleted brain creatine levels and increased creatine/creatinine ratio (cr/crn) in urine. In heterozygous females the phenotype is highly variable and diagnostic hallmarks might be inconclusive. This survey aims to explore the intrafamilial variability of clinical and brain proton Magnetic Resonance Spectroscopy (MRS) findings in males and females with CRTR deficiency. X-chromosome exome sequencing identified a novel missense mutation in the SLC6A8 gene (p.G351R) in a large family with X-linked intellectual disability. Detailed clinical investigations including neuropsychological assessment, measurement of in vivo brain creatine concentrations using quantitative MRS, and analyses of creatine metabolites in urine were performed in five clinically affected family members including three heterozygous females and one hemizygous male confirming the diagnosis of CRTR deficiency. The severe phenotype of the hemizygous male was accompanied by most distinct aberrations of brain creatine concentrations (-83% in gray and -79% in white matter of age-matched normal controls) and urinary creatine/creatinine ratio. In contrast, the heterozygous females showed varying albeit generally milder phenotypes with less severe brain creatine (-50% to -33% in gray and -45% to none in white matter) and biochemical urine abnormalities. An intrafamilial correlation between female phenotype, brain creatine depletion, and urinary creatine abnormalities was observed. The combination of powerful new technologies like exome-next-generation sequencing with thorough systematic evaluation of patients will further expand the clinical spectrum of neurometabolic diseases."],["dc.identifier.doi","10.1007/8904_2013_261"],["dc.identifier.pmid","24190795"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/12255"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.isbn","978-3-642-54148-3"],["dc.relation.isbn","978-3-642-54149-0"],["dc.title","A Novel SLC6A8 Mutation in a Large Family with X-Linked Intellectual Disability: Clinical and Proton Magnetic Resonance Spectroscopy Data of Both Hemizygous Males and Heterozygous Females"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","13"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","European Journal of Inorganic Chemistry"],["dc.bibliographiccitation.lastpage","16"],["dc.contributor.author","Mosch-Zanetti, Nadia C."],["dc.contributor.author","Kratzner, R."],["dc.contributor.author","Lehmann, C."],["dc.contributor.author","Schneider, Thomas R."],["dc.contributor.author","Uson, I."],["dc.date.accessioned","2018-11-07T11:04:04Z"],["dc.date.available","2018-11-07T11:04:04Z"],["dc.date.issued","2000"],["dc.description.abstract","The reduction of [L2TiCl2] (1) (L = 3,5-tert-butylpyrazolate) with 1% Na/Hg in tetrahydrofuran (THP) affords the complex [L2TiCl(THF)(2)] (2), which crystallizes from hexane in moderate yield. The analogous reduction carried out in toluene gives dimeric [(L2TiCl)(2)] (3) in high yield. If the reduction time is extended to 3 days, the complex [L3Ti] (4) is isolated as light blue crystals in low yield. An alternative procedure for preparing compound 4 requires mixing [TiCl3(THF)(3)] with 3 equivalents of potassium 3,5-tert-butylpyrazolate in toluene. Crystallization from hexane affords 4 in high yield. Crystallographic data for 2, 3 and 4 are presented."],["dc.identifier.isi","000084534300004"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/51751"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-v C H Verlag Gmbh"],["dc.relation.issn","1434-1948"],["dc.title","Titanium(III) compounds with eta(2)-pyrazolato ligands"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]