Krätzner, Ralph

[["dc.bibliographiccitation.firstpage","1174"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Journal of Inherited Metabolic Disease"],["dc.bibliographiccitation.lastpage","1185"],["dc.bibliographiccitation.volume","44"],["dc.contributor.affiliation","Klemp, Henry; 1\r\nDepartment of Pediatrics and Adolescent Medicine, Division of Pediatric Neurology, University Medical Center Göttingen\r\nGeorg August University\r\nGöttingen Germany"],["dc.contributor.affiliation","Nessler, Stefan; 2\r\nInstitute of Neuropathology, University Medical Center Göttingen\r\nGeorg August University\r\nGöttingen Germany"],["dc.contributor.affiliation","Streit, Frank; 3\r\nInstitute for Clinical Chemistry, University Medical Center Göttingen\r\nGeorg August University\r\nGöttingen Germany"],["dc.contributor.affiliation","Krätzner, Ralph; 1\r\nDepartment of Pediatrics and Adolescent Medicine, Division of Pediatric Neurology, University Medical Center Göttingen\r\nGeorg August University\r\nGöttingen Germany"],["dc.contributor.affiliation","Rosewich, Hendrik; 1\r\nDepartment of Pediatrics and Adolescent Medicine, Division of Pediatric Neurology, University Medical Center Göttingen\r\nGeorg August University\r\nGöttingen Germany"],["dc.contributor.affiliation","Gärtner, Jutta; 1\r\nDepartment of Pediatrics and Adolescent Medicine, Division of Pediatric Neurology, University Medical Center Göttingen\r\nGeorg August University\r\nGöttingen Germany"],["dc.contributor.author","Kettwig, Matthias"],["dc.contributor.author","Klemp, Henry"],["dc.contributor.author","Nessler, Stefan"],["dc.contributor.author","Streit, Frank"],["dc.contributor.author","Krätzner, Ralph"],["dc.contributor.author","Rosewich, Hendrik"],["dc.contributor.author","Gärtner, Jutta"],["dc.date.accessioned","2021-06-01T09:42:02Z"],["dc.date.available","2021-06-01T09:42:02Z"],["dc.date.issued","2021"],["dc.date.updated","2022-03-21T01:43:41Z"],["dc.description.abstract","Abstract X‐linked adrenoleukodystrophy (X‐ALD) is the most common leukodystrophy. Despite intensive research in recent years, it remains unclear, what drives the different clinical disease courses. Due to this missing pathophysiological link, therapy for the childhood cerebral disease course of X‐ALD (CCALD) remains symptomatic; the allogenic hematopoietic stem cell transplantation or hematopoietic stem‐cell gene therapy is an option for early disease stages. The inclusion of dried blood spot (DBS) C26:0‐lysophosphatidylcholine to newborn screening in an increasing number of countries is leading to an increasing number of X‐ALD patients diagnosed at risk for CCALD. Current follow‐up in asymptomatic boys with X‐ALD requires repetitive cerebral MRIs under sedation. A reliable and easily accessible biomarker that predicts CCALD would therefore be of great value. Here we report the application of targeted metabolomics by AbsoluteIDQ p180‐Kit from Biocrates to search for suitable biomarkers in X‐ALD. LysoPC a C20:3 and lysoPC a C20:4 were identified as metabolites that indicate neuroinflammation after induction of experimental autoimmune encephalitis in the serum of Abcd1tm1Kds mice. Analysis of serum from X‐ALD patients also revealed different concentrations of these lipids at different disease stages. Further studies in a larger cohort of X‐ALD patient sera are needed to prove the diagnostic value of these lipids for use as early biomarkers for neuroinflammation in CCALD patients."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft http://dx.doi.org/10.13039/501100001659"],["dc.description.sponsorship","Niedersächsisches Ministerium für Wissenschaft und Kultur http://dx.doi.org/10.13039/501100010570"],["dc.description.sponsorship","Germany's Excellence Strategy"],["dc.description.sponsorship","Transregional Collaborative Research Center"],["dc.identifier.doi","10.1002/jimd.12389"],["dc.identifier.pmid","33855724"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/85119"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/270"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-425"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation.eissn","1573-2665"],["dc.relation.issn","0141-8955"],["dc.relation.workinggroup","RG Gärtner"],["dc.rights","This is an open access article under the terms of the Creative Commons Attribution‐NonCommercial License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes."],["dc.title","Targeted metabolomics revealed changes in phospholipids during the development of neuroinflammation in Abcd1 tm1Kds mice and X‐linked adrenoleukodystrophy patients"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1321"],["dc.bibliographiccitation.journal","Acta Crystallographica Section D Biological Crystallography"],["dc.bibliographiccitation.lastpage","1335"],["dc.bibliographiccitation.volume","70"],["dc.contributor.author","Sidhu, Navdeep S."],["dc.contributor.author","Schreiber, Kathrin"],["dc.contributor.author","Proepper, Kevin"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Uson, Isabel"],["dc.contributor.author","Sheldrick, George M."],["dc.contributor.author","Gärtner, Jutta"],["dc.contributor.author","Kraetzner, Ralph"],["dc.contributor.author","Steinfeld, Robert"],["dc.date.accessioned","2017-09-07T11:46:15Z"],["dc.date.available","2017-09-07T11:46:15Z"],["dc.date.issued","2014"],["dc.description.abstract","Mucopolysaccharidosis type IIIA (Sanfilippo A syndrome), a fatal childhood-onset neurodegenerative disease with mild facial, visceral and skeletal abnormalities, is caused by an inherited deficiency of the enzyme N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase). More than 100 mutations in the SGSH gene have been found to reduce or eliminate its enzymatic activity. However, the molecular understanding of the effect of these mutations has been confined by a lack of structural data for this enzyme. Here, the crystal structure of glycosylated SGSH is presented at 2 A resolution. Despite the low sequence identity between this unique N-sulfatase and the group of O-sulfatases, they share a similar overall fold and active-site architecture, including a catalytic formylglycine, a divalent metal-binding site and a sulfate-binding site. However, a highly conserved lysine in O-sulfatases is replaced in SGSH by an arginine (Arg282) that is positioned to bind the N-linked sulfate substrate. The structure also provides insight into the diverse effects of pathogenic mutations on SGSH function in mucopolysaccharidosis type IIIA and convincing evidence for the molecular consequences of many missense mutations. Further, the molecular characterization of SGSH mutations will lay the groundwork for the development of structure-based drug design for this devastating neurodegenerative disorder."],["dc.identifier.doi","10.1107/S1399004714002739"],["dc.identifier.gro","3142131"],["dc.identifier.isi","000335952500014"],["dc.identifier.pmid","24816101"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/12116"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/4888"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","1399-0047"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Structure of sulfamidase provides insight into the molecular pathology of mucopolysaccharidosis IIIA"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["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.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.journal","Journal of Inherited Metabolic Disease"],["dc.bibliographiccitation.volume","33"],["dc.contributor.author","Kraetzner, Ralph"],["dc.contributor.author","Pal, A."],["dc.contributor.author","Grune, Tim"],["dc.contributor.author","Grapp, Marcel"],["dc.contributor.author","Schreiber, K."],["dc.contributor.author","Gaertner, J."],["dc.contributor.author","Sheldrick, George M."],["dc.contributor.author","Steinfeld, Robert"],["dc.date.accessioned","2018-11-07T08:40:54Z"],["dc.date.available","2018-11-07T08:40:54Z"],["dc.date.issued","2010"],["dc.format.extent","S141"],["dc.identifier.isi","000281735000448"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/19348"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","Dordrecht"],["dc.relation.issn","0141-8955"],["dc.title","STRUCTURE OF TRIPEPTIDYL-PEPTIDASE I (TPP1) PROVIDES INSIGHT INTO THE MOLECULAR BASIS OF LATE INFANTILE NEURONAL CEROID LIPOFUSCINOSIS"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","29"],["dc.bibliographiccitation.journal","JIMD reports"],["dc.bibliographiccitation.lastpage","36"],["dc.bibliographiccitation.volume","1"],["dc.contributor.author","Grønborg, S."],["dc.contributor.author","Krätzner, R."],["dc.contributor.author","Rosewich, H."],["dc.contributor.author","Gärtner, J."],["dc.date.accessioned","2018-02-13T12:37:43Z"],["dc.date.available","2018-02-13T12:37:43Z"],["dc.date.issued","2011"],["dc.description.abstract","Peroxisome biogenesis disorders (PBDs) are a group of autosomal-recessive developmental and progressive metabolic diseases leading to the Zellweger spectrum (ZS) phenotype in most instances. Diagnosis of clinically suspected cases can be difficult because of extensive genetic heterogeneity and large spectrum of disease severity. Furthermore, a second group of peroxisomal diseases caused by deficiencies of single peroxisomal enzymes can show an indistinguishable clinical phenotype. The diagnosis of these peroxisomal disorders relies on the clinical presentation, the biochemical parameters in plasma and erythrocyte membranes, and genetic testing as the final step. Analysis of patients' cells is frequently required during the diagnostic process, e.g., for complementation analysis to identify the affected gene before sequencing. In the cases with unclear clinical or biochemical presentation, patients' cells are analyzed to prove PBD or to demonstrate biochemical abnormalities that might be elusive in plasma. Cell lines from skin fibroblast that are usually generated for diagnostic workup are not available in all instances, mainly because the required skin biopsy is invasive and sometimes denied by parents. An alternative cellular system has not been analyzed sufficiently. In this study, we evaluated the alternative use of lymphoblastoid cell lines (LCLs), derived from a peripheral blood sample, in the diagnostic process for PBD. LCLs were suitable for immunofluorescence visualization of peroxisomal enzymes, complementation analysis, and the biochemical analysis to differentiate between control and PBD LCL. LCLs are therefore an easily obtainable alternative cellular system for a detailed PBD diagnostic workup with a reliability of diagnostic results equal to those of skin fibroblasts."],["dc.identifier.doi","10.1007/8904_2011_12"],["dc.identifier.pmid","23430824"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/12224"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.isbn","978-3-642-17707-1"],["dc.relation.isbn","978-3-642-17708-8"],["dc.title","Lymphoblastoid cell lines for diagnosis of peroxisome biogenesis disorders"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Journal of Inherited Metabolic Disease"],["dc.bibliographiccitation.volume","33"],["dc.contributor.author","Steinfeld, Robert"],["dc.contributor.author","Grapp, Marcel"],["dc.contributor.author","Kraetzner, Ralph"],["dc.contributor.author","Dreha-Kulaczewski, S. F."],["dc.contributor.author","Wevers, Ron A."],["dc.contributor.author","Gaertner, J."],["dc.date.accessioned","2018-11-07T08:40:55Z"],["dc.date.available","2018-11-07T08:40:55Z"],["dc.date.issued","2010"],["dc.format.extent","S158"],["dc.identifier.isi","000281735000507"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/19350"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","Dordrecht"],["dc.relation.issn","0141-8955"],["dc.title","CEREBRAL FOLATE TRANSPORT DEFICIENCY: A NOVEL INHERITED DISORDER OF FOLATE METABOLISM"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3976"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Journal of biological chemistry"],["dc.bibliographiccitation.lastpage","3984"],["dc.bibliographiccitation.volume","284"],["dc.contributor.author","Pal, Aritra"],["dc.contributor.author","Kraetzner, Ralph"],["dc.contributor.author","Gruene, Tim"],["dc.contributor.author","Grapp, Marcel"],["dc.contributor.author","Schreiber, Kathrin"],["dc.contributor.author","Gronborg, Mads"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Asif, Abdul R."],["dc.contributor.author","Gärtner, Jutta"],["dc.contributor.author","Sheldrick, George M."],["dc.contributor.author","Steinfeld, Robert"],["dc.date.accessioned","2017-09-07T11:47:33Z"],["dc.date.available","2017-09-07T11:47:33Z"],["dc.date.issued","2009"],["dc.description.abstract","Late infantile neuronal ceroid lipofuscinosis, a fatal neurodegenerative disease of childhood, is caused by mutations in the TPP1 gene that encodes tripeptidyl-peptidase I. We show that purified TPP1 requires at least partial glycosylation for in vitro autoprocessing and proteolytic activity. We crystallized the fully glycosylated TPP1 precursor under conditions that implied partial autocatalytic cleavage between the prosegment and the catalytic domain. X-ray crystallographic analysis at 2.35 angstrom resolution reveals a globular structure with a subtilisin-like fold, a Ser(475) -Glu(272) -Asp(360) catalytic triad, and an octahedrally coordinated Ca(2+) -binding site that are characteristic features of the S53 sedolisin family of peptidases. In contrast to other S53 peptidases, the TPP1 structure revealed steric constraints on the P4 substrate pocket explaining its preferential cleavage of tripeptides from the unsubstituted N terminus of proteins. Two alternative conformations of the catalytic Asp(276) are associated with the activation status of TPP1. 28 disease-causing missense mutations are analyzed in the light of the TPP1 structure providing insight into the molecular basis of late infantile neuronal ceroid lipofuscinosis."],["dc.identifier.doi","10.1074/jbc.M806947200"],["dc.identifier.gro","3143151"],["dc.identifier.isi","000262872500066"],["dc.identifier.pmid","19038966"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/633"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Fonds der Chemischen Industrie"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Amer Soc Biochemistry Molecular Biology Inc"],["dc.relation.issn","0021-9258"],["dc.title","Structure of Tripeptidyl-peptidase I Provides Insight into the Molecular Basis of Late Infantile Neuronal Ceroid Lipofuscinosis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Journal of Inherited Metabolic Disease"],["dc.bibliographiccitation.volume","34"],["dc.contributor.author","Steinfeld, Robert"],["dc.contributor.author","Grapp, Marcel"],["dc.contributor.author","Kraetzner, Ralph"],["dc.contributor.author","Gärtner, Jutta"],["dc.date.accessioned","2018-11-07T09:00:10Z"],["dc.date.available","2018-11-07T09:00:10Z"],["dc.date.issued","2011"],["dc.format.extent","S119"],["dc.identifier.isi","000309837800148"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/24087"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","Dordrecht"],["dc.relation.issn","0141-8955"],["dc.title","THE EXTENDED CLINICAL SPECTRUM OF CEREBRAL FOLATE TRANSPORT DEFICIENCY"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]