Gärtner, Jutta

[["dc.bibliographiccitation.firstpage","268"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Neuropediatrics"],["dc.bibliographiccitation.lastpage","271"],["dc.bibliographiccitation.volume","44"],["dc.contributor.author","Shoukier, Moneef"],["dc.contributor.author","Fuchs, Sigrid"],["dc.contributor.author","Schwaibold, Eva"],["dc.contributor.author","Lingen, Michael"],["dc.contributor.author","Gärtner, Jutta"],["dc.contributor.author","Brockmann, Knut"],["dc.contributor.author","Zirn, Birgit"],["dc.date.accessioned","2017-09-07T11:47:08Z"],["dc.date.available","2017-09-07T11:47:08Z"],["dc.date.issued","2013"],["dc.description.abstract","Terminal deletions of chromosome 3p26.3 confined to the CHL1 gene have previously been described in children with intellectual disability and epilepsy. Here, we report for the first time, a 3p26.3 duplication including only the CHL1 gene in an intellectually disabled girl with epilepsy. The penetrance of both deletions and duplications in 3p26.3 is reduced because all chromosomal imbalances were inherited from healthy parents. Further studies are needed to specify the pathogenic mechanism of 3p26.3 imbalances and to estimate recurrence risks in genetic counseling. However, the description of both deletions and duplications of chromosome 3p26.3 in nonsyndromic intellectual disability suggests that CHL1 is a dosage-sensitive gene with an important role for normal cognitive development."],["dc.identifier.doi","10.1055/s-0033-1333874"],["dc.identifier.gro","3142278"],["dc.identifier.isi","000324755000006"],["dc.identifier.pmid","23436495"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/6509"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Georg Thieme Verlag Kg"],["dc.relation.issn","0174-304X"],["dc.title","Microduplication of 3p26.3 in Nonsyndromic Intellectual Disability Indicates an Important Role of CHL1 for Normal Cognitive Function"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","2123"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","4"],["dc.contributor.author","Grapp, Marcel"],["dc.contributor.author","Wrede, Arne"],["dc.contributor.author","Schweizer, Michaela"],["dc.contributor.author","Huewel, Sabine"],["dc.contributor.author","Galla, Hans-Joachim"],["dc.contributor.author","Snaidero, Nicolas"],["dc.contributor.author","Simons, Mikael"],["dc.contributor.author","Bueckers, Johanna"],["dc.contributor.author","Low, Philip S."],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Gärtner, Jutta"],["dc.contributor.author","Steinfeld, Robert"],["dc.date.accessioned","2017-09-07T11:47:39Z"],["dc.date.available","2017-09-07T11:47:39Z"],["dc.date.issued","2013"],["dc.description.abstract","Loss of folate receptor-alpha function is associated with cerebral folate transport deficiency and childhood-onset neurodegeneration. To clarify the mechanism of cerebral folate transport at the blood-cerebrospinal fluid barrier, we investigate the transport of 5-methyltetrahydrofolate in polarized cells. Here we identify folate receptor-alpha-positive intralumenal vesicles within multivesicular bodies and demonstrate the directional cotransport of human folate receptor-alpha, and labelled folate from the basolateral to the apical membrane in rat choroid plexus cells. Both the apical medium of folate receptor-alpha-transfected rat choroid plexus cells and human cerebrospinal fluid contain folate receptor-alpha-positive exosomes. Loss of folate receptor-alpha-expressing cerebrospinal fluid exosomes correlates with severely reduced 5-methyltetrahydrofolate concentration, corroborating the importance of the folate receptor-alpha-mediated folate transport in the cerebrospinal fluid. Intraventricular injections of folate receptor-alpha-positive and -negative exosomes into mouse brains demonstrate folate receptor-alpha-dependent delivery of exosomes into the brain parenchyma. Our results unravel a new pathway of folate receptor-alpha-dependent exosome-mediated folate delivery into the brain parenchyma and opens new avenues for cerebral drug targeting."],["dc.identifier.doi","10.1038/ncomms3123"],["dc.identifier.gro","3142330"],["dc.identifier.isi","000323715900003"],["dc.identifier.pmid","23828504"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/9774"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/7086"],["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","Nature Publishing Group"],["dc.relation.issn","2041-1723"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Choroid plexus transcytosis and exosome shuttling deliver folate into brain parenchyma"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","submitted_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","European Journal of Pediatrics"],["dc.bibliographiccitation.volume","168"],["dc.contributor.author","Klinge, Lars"],["dc.contributor.author","Thoms, Sven"],["dc.contributor.author","Cierny, Irmgard"],["dc.contributor.author","Straub, Volker"],["dc.contributor.author","Bushby, Kate"],["dc.contributor.author","Gärtner, Jutta"],["dc.date.accessioned","2018-11-07T08:31:59Z"],["dc.date.available","2018-11-07T08:31:59Z"],["dc.date.issued","2009"],["dc.identifier.isi","000262826600054"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/17244"],["dc.language.iso","en"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","New york"],["dc.title","Defective membrane tubulation in dysferlin-deficient muscular dystrophy"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","774"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Journal of biological chemistry"],["dc.bibliographiccitation.lastpage","784"],["dc.bibliographiccitation.volume","277"],["dc.contributor.author","Brosius, U."],["dc.contributor.author","Dehmel, T."],["dc.contributor.author","Gärtner, Jutta"],["dc.date.accessioned","2017-09-07T11:45:57Z"],["dc.date.available","2017-09-07T11:45:57Z"],["dc.date.issued","2002"],["dc.description.abstract","The 22-kDa peroxisomal membrane protein (PMP22) is a major component of peroxisomal membranes in mammals. Although its precise role in peroxisome function is poorly understood, it seems to be involved in pore forming activity and may contribute to the unspecific permeability of the organelle membrane. PMP22 is synthesized on free cytosolic ribosomes and then directed to the peroxisome membrane by specific targeting information. Previous studies in rats revealed that PMP22 contains one distinct peroxisomal membrane targeting signal in the amino-terminal cytoplasmic tail. We cloned and characterized the targeting signal of human PMP22 and compared it with the already described characteristics of the corresponding rat protein. Amino acid sequence alignment of rat and human protein revealed 77% identity including a high conservation of several protein motifs. We expressed various deletion constructs of PMP22 in fusion with the green fluorescent protein in COS-7 cells and determined their intracellular localization. In contrast to previous studies on rat PMP22 and most other peroxisomal membrane proteins, we showed that human as well as rat PMP22 contains two distinct and nonoverlapping peroxisomal membrane targeting signals, one in the amino-terminal and the other in the carboxyl-terminal protein region. They consist of two transmembrane domains and adjacent protein loops with almost identical basic clusters. Both of these peroxisomal targeting regions interact with PEX19, a factor required for peroxisome membrane synthesis. In addition, we observed that fusing the green fluorescent protein immediately adjacent to the targeting region completely abolishes targeting function and mislocalizes PMP22 to the cytosol."],["dc.identifier.doi","10.1074/jbc.M108155200"],["dc.identifier.gro","3144228"],["dc.identifier.isi","000173087900100"],["dc.identifier.pmid","11590176"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1829"],["dc.notes.intern","WoS Import 2017-03-10"],["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","Two different targeting signals direct human peroxisomal membrane protein 22 to peroxisomes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","833"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Child's Nervous System"],["dc.bibliographiccitation.lastpage","841"],["dc.bibliographiccitation.volume","35"],["dc.contributor.author","Bock, Hans C."],["dc.contributor.author","Dreha-Kulaczewski, Steffi F."],["dc.contributor.author","Alaid, Awad"],["dc.contributor.author","Gärtner, Jutta"],["dc.contributor.author","Ludwig, Hans C."],["dc.date.accessioned","2020-12-10T14:10:20Z"],["dc.date.available","2020-12-10T14:10:20Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1007/s00381-019-04119-x"],["dc.identifier.eissn","1433-0350"],["dc.identifier.issn","0256-7040"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/70732"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Upward movement of cerebrospinal fluid in obstructive hydrocephalus—revision of an old concept"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","61"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","American journal of human genetics"],["dc.bibliographiccitation.lastpage","68"],["dc.bibliographiccitation.volume","90"],["dc.contributor.author","Huppke, Peter"],["dc.contributor.author","Brendel, Cornelia"],["dc.contributor.author","Kalscheuer, Vera"],["dc.contributor.author","Korenke, Georg Christoph"],["dc.contributor.author","Marquardt, Iris"],["dc.contributor.author","Freisinger, Peter"],["dc.contributor.author","Christodoulou, John"],["dc.contributor.author","Hillebrand, Merle"],["dc.contributor.author","Pitelet, Gaele"],["dc.contributor.author","Wilson, Callum"],["dc.contributor.author","Gruber-Sedlmayr, Ursula"],["dc.contributor.author","Ullmann, Reinhard"],["dc.contributor.author","Haas, Stefan"],["dc.contributor.author","Elpeleg, Orly"],["dc.contributor.author","Nürnberg, Gudrun"],["dc.contributor.author","Nürnberg, Peter"],["dc.contributor.author","Dad, Shzeena"],["dc.contributor.author","Moller, Lisbeth Birk"],["dc.contributor.author","Kaler, Stephen G."],["dc.contributor.author","Gärtner, Jutta"],["dc.date.accessioned","2017-09-07T11:49:01Z"],["dc.date.available","2017-09-07T11:49:01Z"],["dc.date.issued","2012"],["dc.description.abstract","Low copper and ceruloplasmin in serum are the diagnostic hallmarks for Menkes disease, Wilson disease, and aceruloplasminemia. We report on five patients from four unrelated families with these biochemical findings who presented with a lethal autosomal-recessive syndrome of congenital cataracts, hearing loss, and severe developmental delay. Cerebral MRI showed pronounced cerebellar hypoplasia and hypomyelination. Homozygosity mapping was performed and displayed a region of commonality among three families at chromosome 3q25. Deep sequencing and conventional sequencing disclosed homozygous or compound heterozygous mutations for all affected subjects in SLC33A1 encoding a highly conserved acetylCoA transporter (AT-1) required for acetylation of multiple gangliosides and glycoproteins. The mutations were found to cause reduced or absent AT-1 expression and abnormal intracellular localization of the protein. We also showed that AT-1 knockdown in HepG2 cells leads to reduced ceruloplasmin secretion, indicating that the low copper in serum is due to reduced ceruloplasmin levels and is not a sign of copper deficiency. The severity of the phenotype implies an essential role of AT-1 in proper posttranslational modification of numerous proteins, without which normal lens and brain development is interrupted. Furthermore, AT-1 defects are a new and important differential diagnosis in patients with low copper and ceruloplasmin in serum."],["dc.identifier.doi","10.1016/j.ajhg.2011.11.030"],["dc.identifier.gro","3142590"],["dc.identifier.isi","000299409100005"],["dc.identifier.pmid","22243965"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8957"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0002-9297"],["dc.title","Mutations in SLC33A1 Cause a Lethal Autosomal-Recessive Disorder with Congenital Cataracts, Hearing Loss, and Low Serum Copper and Ceruloplasmin"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","89"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Neuropädiatrie in Klinik und Praxis"],["dc.bibliographiccitation.lastpage","91"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Müller-Wielsch, K."],["dc.contributor.author","Huppke, P."],["dc.contributor.author","Gärtner, J."],["dc.date.accessioned","2018-02-15T09:50:25Z"],["dc.date.available","2018-02-15T09:50:25Z"],["dc.date.issued","2011"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/12253"],["dc.language.iso","de"],["dc.notes.status","final"],["dc.relation.issn","1619-3873"],["dc.title","Entwicklungsverzögerung im Säuglingsalter durch alimentären Vitamin B12-Mangel."],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","772"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Journal of Medical Genetics"],["dc.bibliographiccitation.lastpage","775"],["dc.bibliographiccitation.volume","50"],["dc.contributor.author","Banne, Ehud"],["dc.contributor.author","Atawneh, Osama"],["dc.contributor.author","Henneke, Marco"],["dc.contributor.author","Brockmann, Knut"],["dc.contributor.author","Gärtner, Jutta"],["dc.contributor.author","Elpeleg, Orly"],["dc.contributor.author","Edvardson, Simon"],["dc.date.accessioned","2017-09-07T11:47:04Z"],["dc.date.available","2017-09-07T11:47:04Z"],["dc.date.issued","2013"],["dc.description.abstract","West syndrome (WS) is an epileptic encephalopathy of childhood, defined by the presence of clustered spasms usually occurring before the age of 1year, hypsarrhythmia on EEG that is notoriously difficult to define, and developmental arrest or regression. The incidence of WS is 1:3200 live births with an aetiology-dependent prognosis. Up to 80% of children with symptomatic WS suffer from mental retardation, and approximately 50% develop Lennox-Gastaut syndrome. Using homozygosity mapping followed by exome sequencing, we identified a ADP-ribosylation factor (ARF) guanine nucleotide-exchange factor two (brefeldin A-inhibited) (ARFGEF2) mutation in five related infants with WS. ARFGEF2 is involved in the activation of ARFs by accelerating replacement of bound guanosine diphosphate (GDP) with Guanosine triphosphate (GTP), and is involved in Golgi transport. A mutation in ARFGEF2 has been previously described only once, causing microcephaly and periventricular heterotopia. Here, we describe a novel ARFGEF2 mutation in five related patients presenting with WS, microcephaly, periventricular heterotopia and thin corpus callosum."],["dc.identifier.doi","10.1136/jmedgenet-2013-101752"],["dc.identifier.gro","3142256"],["dc.identifier.isi","000328141400009"],["dc.identifier.pmid","23812912"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/6265"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: German Research Foundation [Ga354/9-1]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Bmj Publishing Group"],["dc.relation.eissn","1468-6244"],["dc.relation.issn","0022-2593"],["dc.title","West syndrome, microcephaly, grey matter heterotopia and hypoplasia of corpus callosum due to a novel ARFGEF2 mutation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","10"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","European Journal of Paediatric Neurology"],["dc.bibliographiccitation.lastpage","16"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Huppke, Peter"],["dc.contributor.author","Koehler, Karola"],["dc.contributor.author","Brockmann, Knut"],["dc.contributor.author","Stettner, Georg M."],["dc.contributor.author","Gärtner, Jutta"],["dc.date.accessioned","2017-09-07T11:49:52Z"],["dc.date.available","2017-09-07T11:49:52Z"],["dc.date.issued","2007"],["dc.description.abstract","Introduction: Epilepsy is very frequent in Rett syndrome (RTT) patients and often difficult to treat. Because most cases of RTT are caused by mutations in the MECP2 gene it is reasonable to assume that convulsions are based on common pathogenetic mechanisms and thus should have a similar response to antiepileptic drugs. Purpose: To find the optimal treatment for epilepsy in RTT. Methods: We performed a retrospective study on 110 female patients with confirmed MECP2 mutations. Results: The median age was 10 years, 58% had a history of epilepsy and 55% received antiepileptic drugs (AEDs). Only sulthiame, carbamazepine and valproate were administered in an adequate frequency to allow statistical analysis. The best anticonvulsive results were seen in the RTT group that was treated with carbamazepine. Sulthiame was slightly less effective while valproate was significantly less effective. The rate of side effects was equivalent in all groups. In conclusion, carbamazepine should be recommended as first choice AED in RTT. If carbamazepine is not effective or not well tolerated sulthiame ought to be taken as second choice AED. (c) 2006 European Paediatric Neurology Society. Published by Elsevier Ltd. All rights reserved."],["dc.identifier.doi","10.1016/j.ejpn.2006.09.003"],["dc.identifier.gro","3143557"],["dc.identifier.isi","000244178200002"],["dc.identifier.pmid","17178248"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1084"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Elsevier Sci Ltd"],["dc.relation.issn","1090-3798"],["dc.title","Treatment of epilepsy in Rett syndrome"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","741"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.lastpage","748"],["dc.bibliographiccitation.volume","28"],["dc.contributor.author","Gärtner, Jutta"],["dc.contributor.author","Dehmel, T."],["dc.contributor.author","Klusmann, A."],["dc.contributor.author","Roerig, Peter"],["dc.date.accessioned","2017-09-07T11:45:58Z"],["dc.date.available","2017-09-07T11:45:58Z"],["dc.date.issued","2002"],["dc.description.abstract","X-linked adrenoleukodystrophy (X-AILD) is the most common peroxisomal disorder characterized by abnormal accumulation of saturated very long chain fatty acids in tissues and body fluids with predominance in brain white matter and adrenal cortex. The clinical phenotype is highly variable ranging from the severe childhood cerebral form to asymptomatic persons. The responsible ALD gene encodes the adrenoleukodystrophy protein (ALDP), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The patient gene mutations. are heterogeneously distributed over the functional domains of ALDP. The extreme variability in clinical phenotype, even within one affected family, indicates that besides the ALD gene mutations other factors strongly influence the clinical phenotype. To understand the cell biology and function of mammalian peroxisomal ABC transporters and to determine their role in the pathogenesis of X-ALD we developed a system for expressing functional ABC protein domains in fusion with the maltose binding protein. Wild type and mutant fusion proteins of the nucleotide-binding fold were overexpressed, purified, and characterized by photoaffinity labeling with 8-azido ATP or 8-azido GTP and a coupled ATP regenerating enzyme assay for ATPase activity. Our studies provide evidence that peroxisomal ABC transporters utilize ATP to become a functional transporter and that ALD gene mutations alter peroxisomal transport function. The established disease model will be used further to study the influence of possible disease modifier proteins on ALDP function."],["dc.identifier.doi","10.1081/ERC-120016999"],["dc.identifier.gro","3144232"],["dc.identifier.isi","000180213900075"],["dc.identifier.pmid","12530690"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1833"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Marcel Dekker Inc"],["dc.publisher.place","New york"],["dc.relation.conference","10th Conference on the Adrenal Cortex"],["dc.relation.eventlocation","SAN FRANCISCO, CALIFORNIA"],["dc.relation.ispartof","Endocrine Research"],["dc.relation.issn","0743-5800"],["dc.title","Functional characterization of the adrenoleukodystrophy protein (ALDP) and disease pathogenesis"],["dc.type","conference_paper"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]