Kermer, Pawel

[["dc.bibliographiccitation.firstpage","551"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Journal of Alzheimer's Disease"],["dc.bibliographiccitation.lastpage","565"],["dc.bibliographiccitation.volume","38"],["dc.contributor.author","Schmitz, M."],["dc.contributor.author","Wulf, K."],["dc.contributor.author","Signore, S. C."],["dc.contributor.author","Schulz-Schaeffer, W. J."],["dc.contributor.author","Kermer, P."],["dc.contributor.author","Baehr, M."],["dc.contributor.author","Wouters, F. S."],["dc.contributor.author","Zafar, S."],["dc.contributor.author","Zerr, I."],["dc.date.accessioned","2017-09-07T11:46:57Z"],["dc.date.available","2017-09-07T11:46:57Z"],["dc.date.issued","2014"],["dc.description.abstract","Previous studies indicate an important role for the cellular prion protein (PrPC) in the development of Alzheimer's disease (AD) pathology. In the present study, we analyzed the involvement of PrPC in different pathological mechanisms underlying AD: the processing of the amyloid-beta protein precursor (A beta PP) and its interaction with A beta PP, tau, and different phosphorylated forms of the tau protein (p-tau). The effect of PrPC on tau expression was investigated in various cellular compartments using a HEK293 cell model expressing a tau mutant (3PO-tau) or wild type (WT)-tau. We could show that PrPC reduces A beta PP cleavage, leading to decreased levels of A beta(40) and sA beta PP without changing the protein expression of A beta PP, beta-secretase, or gamma-secretase. Tau and its phosphorylated forms were identified as interactions partners for PrPC, raising the question as to whether PrPC might also be involved in tau pathology. Overexpression of PrPC in PRNP and 3PO-tau transfected cells resulted in a reduction of 3PO-tau and p-tau as well as a decrease of 3PO-tau-related toxicity. In addition, we used the transgenic PrPC knockout (Prnp0/0) mouse line to study the dynamics of tau phosphorylation, an important pathological hallmark in the pathogenesis of AD in vivo. There, an effect of PrPC on tau expression could be observed under oxidative stress conditions but not during aging. In summary, we provide further evidence for interactions of PrPC with proteins that are known to be the key players in AD pathogenesis. We identified tau and its phosphorylated forms as potential PrP-interactors and report a novel protective function of PrPC in AD-like tau pathology."],["dc.identifier.doi","10.3233/JAD-130566"],["dc.identifier.gro","3142228"],["dc.identifier.isi","000327598500009"],["dc.identifier.pmid","24028865"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10657"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/5954"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1875-8908"],["dc.relation.issn","1387-2877"],["dc.rights","CC BY 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/3.0"],["dc.title","Impact of the Cellular Prion Protein on Amyloid-beta and 3PO-Tau Processing"],["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","521"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Neurobiology of Disease"],["dc.bibliographiccitation.lastpage","531"],["dc.bibliographiccitation.volume","26"],["dc.contributor.author","Esposito, Alessandro"],["dc.contributor.author","Dohm, Christoph P."],["dc.contributor.author","Kermer, Pawel"],["dc.contributor.author","Bähr, Mathias"],["dc.contributor.author","Wouters, Fred S."],["dc.date.accessioned","2017-09-07T11:49:47Z"],["dc.date.available","2017-09-07T11:49:47Z"],["dc.date.issued","2007"],["dc.description.abstract","alpha-Synuclein is a primarily neuronal protein that is enriched at the presynapse. alpha-Synuclein and the microtubule binding protein tau have been implicated in neurodegenerative diseases. alpha-Synuclein is known to associate with phospholipid vesicles, regulates dopamine metabolism and exhibits chaperone activity, but its main role remains largely unknown. Furthermore, knowledge on its interactions and posttranslational modifications is essential for a molecular understanding of alpha-synucleinopathies. We investigated alpha-synuclein mutations, causative for autosomal dominant forms of Parkinson's disease (A30P, A53T and E46K), and phosphorylation mutants at serine 129 (S129A and S129D) using fluorescently labelled alpha-synuclein, actin and tau. The investigation of colocalizafion, and protein-protein interactions by Forster resonance energy transfer and fluorescence lifetime imaging showed that alpha-synuclein associates with the actin cytoskeleton and interacts with tau. The A30P mutation and cytoskeletal destabilization decreased this interaction. Given the concurrent loss of membrane binding by this mutation, we propose a membrane- bound functional complex with tau that might involve the actin cytoskeleton. (c) 2007 Elsevier Inc. All rights reserved."],["dc.identifier.doi","10.1016/j.nbd.2007.01.014"],["dc.identifier.gro","3143496"],["dc.identifier.isi","000247146400003"],["dc.identifier.pmid","17408955"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1017"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0969-9961"],["dc.title","Alpha-synuclein and its disease-related mutants interact differentially with the microtubule protein tau and associate with the actin cytoskeleton"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1013"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Journal of Neurochemistry"],["dc.bibliographiccitation.lastpage","1023"],["dc.bibliographiccitation.volume","129"],["dc.contributor.author","Liman, Jan"],["dc.contributor.author","Deeg, S."],["dc.contributor.author","Voigt, A."],["dc.contributor.author","Voßfeldt, H."],["dc.contributor.author","Dohm, C. P."],["dc.contributor.author","Karch, A."],["dc.contributor.author","Weishaupt, Jochen"],["dc.contributor.author","Schulz, J. B."],["dc.contributor.author","Bähr, M."],["dc.contributor.author","Kermer, P."],["dc.date.accessioned","2017-09-07T11:46:13Z"],["dc.date.available","2017-09-07T11:46:13Z"],["dc.date.issued","2014"],["dc.description.abstract","Spinocerebellar ataxia type 3 (SCA3) is one of at least nine inherited neurodegenerative diseases caused by an expansion of a polyglutamine tract within corresponding disease-specific proteins. In case of SCA3, mutation of Ataxin-3 results in aggregation of misfolded protein, formation of intranuclear as well as cytosolic inclusion bodies and cell death in distinct neuronal populations. Since cyclin-dependent kinase-5 (CDK5) has been shown to exert beneficial effects on aggregate formation and cell death in various polyglutamine diseases, we tested its therapeutic potential for SCA3. Our data show increased caspase-dependent Ataxin-3 cleavage, aggregation, and neurodegeneration in the absence of sufficient CDK5 activity. This disease-propagating effect could be reversed by mutation of the caspase cleavage site in Ataxin-3. Moreover, reduction of CDK5 expression levels by RNAi in vivo enhances SCA3 toxicity as assayed in a Drosophila model for SCA3. In summary, we present CDK5 as a potent neuroprotectant, regulating cleavage and thereby toxicity of Ataxin-3 and other polyglutamine proteins. We propose that increased caspase-dependent cleavage of mutated Ataxin-3, because of missing CDK5 shielding, leads to aggregation and cell death. Moreover, reduction of CDK5 expression levels by RNAi in vivo enhances SCA3 toxicity as assayed in a Drosophila model for SCA3. We think that CDK5 functions as a shield against cleavage-induced toxification and thereby is an interesting target for therapeutic intervention in polyQ disease in general."],["dc.identifier.doi","10.1111/jnc.12684"],["dc.identifier.gro","3142111"],["dc.identifier.isi","000337760500011"],["dc.identifier.pmid","24548080"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/4666"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1471-4159"],["dc.relation.issn","0022-3042"],["dc.title","CDK5 protects from caspase-induced Ataxin-3 cleavage and neurodegeneration"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","117"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Neuroscience Letters"],["dc.bibliographiccitation.lastpage","120"],["dc.bibliographiccitation.volume","315"],["dc.contributor.author","Kermer, Pawel"],["dc.contributor.author","Klocker, N."],["dc.contributor.author","Bähr, Mathias"],["dc.date.accessioned","2017-09-07T11:45:59Z"],["dc.date.available","2017-09-07T11:45:59Z"],["dc.date.issued","2001"],["dc.description.abstract","Both optic nerve (ON) transection and intraocular injection of N-methyl-D-aspartate (NMDA) are established lesion models to cause death of retinal ganglion cells (RGCs) in the adult rat. Excitotoxic effects via glutamate receptors resulting in secondary neuronal death are discussed as possible initiators in both types of RGC damage. We examined whether modulating glutamatergic transmission through metabotropic glutamate receptors rescues RGCs from lesion-induced degeneration in vivo. Unexpectedly, repeated intraocular injection of four different agonists/antagonists on the various subtypes of mGluRs did not decrease retinal damage in both lesion paradigms as revealed by measurement of visual performance and RGC survival. We conclude that activation/inactivation of retinal mGluRs does not play an important role for the initiation and execution of secondary RGC loss after ON transection and NMDA lesion in the adult rat. (C) 2001 Elsevier Science Ltd. All rights reserved."],["dc.identifier.doi","10.1016/S0304-3940(01)02318-7"],["dc.identifier.gro","3144243"],["dc.identifier.isi","000172603100002"],["dc.identifier.pmid","11716977"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1846"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Elsevier Sci Ireland Ltd"],["dc.relation.issn","0304-3940"],["dc.title","Modulation of metabotropic glutamate receptors fails to prevent the loss of adult rat retinal ganglion cells following axotomy or N-methyl-D-aspartate lesion in vivo"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","21"],["dc.bibliographiccitation.journal","Brain Research"],["dc.bibliographiccitation.lastpage","26"],["dc.bibliographiccitation.volume","1198"],["dc.contributor.author","Liman, Jan"],["dc.contributor.author","Faida, Lena"],["dc.contributor.author","Dohm, Christoph P."],["dc.contributor.author","Reed, John C."],["dc.contributor.author","Bähr, Mathias"],["dc.contributor.author","Kermer, Pawel"],["dc.date.accessioned","2017-09-07T11:48:46Z"],["dc.date.available","2017-09-07T11:48:46Z"],["dc.date.issued","2008"],["dc.description.abstract","BAG1 is a potent neuroprotectant as well as a marker of differentiation in neuronal cells. It is known that BAG1 mainly localizes to the nucleus during neuronal development, whereas BAG1 shifts to the cytosol upon neuronal differentiation suggesting that distinct BAG1 functions depend on its subcellular localization. Here, we show that forced BAG1 expression within the nucleus when compared to full-length BAG1 expression and to control cells completely abolishes the neuroprotective effects of BAG1 supporting the notion that cytosolic interaction with Hsp70 is mandatory for BAG1 mediated neuroprotection. At the same time, we observed that cells can no longer differentiate into post-mitotic neurons when BAG1 is only present in the nucleus. In addition, phospho-Erk levels are decreased in those cells indicating that BAG1 has to translocate to the cytosol for Raf-dependent MAPK activation. (C) 2008 Elsevier B.V. All rights reserved."],["dc.identifier.doi","10.1016/j.brainres.2008.01.010"],["dc.identifier.gro","3143337"],["dc.identifier.isi","000254106400003"],["dc.identifier.pmid","18242589"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/840"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0006-8993"],["dc.title","Subcellular distribution affects BAG1 function"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","674"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Der Ophthalmologe"],["dc.bibliographiccitation.lastpage","678"],["dc.bibliographiccitation.volume","102"],["dc.contributor.author","Kermer, P."],["dc.contributor.author","Bähr, M."],["dc.date.accessioned","2018-04-23T11:48:03Z"],["dc.date.available","2018-04-23T11:48:03Z"],["dc.date.issued","2005"],["dc.description.abstract","Das zelluläre Suizidprogramm (Apoptose) ist sowohl für viele physiologische Vorgänge von der embryonalen Entwicklung bis zum Altern, als auch für die Pathogenese und den Verlauf eines weiten Spektrums von Krankheiten von großer Wichtigkeit. Hierzu zählen nicht zuletzt auch chronisch neurodegenerative Prozesse, zu denen auch die erworbene und erbliche Degeneration von Photorezeptorzellen und retinalen Ganglienzellen, wie z. B. bei der Retinitis pigmentosa, der Makuladegeneration, der Neuritis nervi optici oder dem Glaukom gehören. In der vorliegenden Übersicht werden die grundlegenden pro- und antiapoptotischen Regulationsmechanismen in der Zelle geschildert, ihre Relevanz für die Degeneration retinaler Zelltypen unter Fokussierung auf retinale Ganglienzellen dargestellt und daraus hervorgehende, neue Therapieansätze aufgezeigt."],["dc.identifier.doi","10.1007/s00347-005-1187-5"],["dc.identifier.gro","3142088"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/13455"],["dc.language.iso","de"],["dc.notes.intern","lifescience updates Crossref Import"],["dc.notes.status","final"],["dc.relation.issn","0941-293X"],["dc.title","Programmierter Zelltod in der Netzhaut: Molekulare Mechanismen und therapeutische Ansätze"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","190"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Journal of Medical Case Reports"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Liman, Jan"],["dc.contributor.author","von Gottberg, Philipp"],["dc.contributor.author","Bähr, Mathias"],["dc.contributor.author","Kermer, Pawel"],["dc.date.accessioned","2018-03-08T09:21:27Z"],["dc.date.available","2018-03-08T09:21:27Z"],["dc.date.issued","2011"],["dc.description.abstract","Introduction Infectious ileopectineal bursitis is a rare complication after total hip replacement and is associated mainly with rheumatoid arthritis. The main complications are local swelling and pain, but communication of the inflamed bursa with the joint can occur, leading to subsequent cartilage damage and bone destruction. Case presentation We report a case of a 47-year-old Caucasian woman without rheumatoid arthritis who reported pain and palsy in her left leg almost one year after total hip replacement. She was diagnosed with an ileopectineal bursitis after total hip replacement, leading to femoral nerve palsy. The diagnosis was obtained by thorough clinical examination, the results of focused computed tomography and magnetic resonance imaging. Conclusion To the best of our knowledge, this is the first report of non-infectious ileopectineal bursitis in a patient without rheumatoid arthritis as a complication of total hip replacement. This rare case underlines the importance of proper neurologic examination of persistent conditions after orthopedic intervention in otherwise healthy individuals. We believe this case should be useful for a broad spectrum of medical specialties, including orthopedics, neurology, radiology, and general practice."],["dc.identifier.doi","10.1186/1752-1947-5-190"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/6375"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/12889"],["dc.language.iso","en"],["dc.notes.intern","GRO-Li-Import"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.relation.doi","10.1186/1752-1947-5-190"],["dc.relation.issn","1752-1947"],["dc.relation.issn","1752-1947"],["dc.rights","CC BY 2.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/2.0"],["dc.title","Femoral nerve palsy caused by ileopectineal bursitis after total hip replacement: a case report"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","312"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Cell Death and Differentiation"],["dc.bibliographiccitation.lastpage","321"],["dc.bibliographiccitation.volume","15"],["dc.contributor.author","Ganesan, S."],["dc.contributor.author","Rohde, G."],["dc.contributor.author","Eckermann, K."],["dc.contributor.author","Sroka, K."],["dc.contributor.author","Schaefer, M. K. E."],["dc.contributor.author","Dohm, C. P."],["dc.contributor.author","Kermer, P."],["dc.contributor.author","Haase, G."],["dc.contributor.author","Wouters, F."],["dc.contributor.author","Bähr, M."],["dc.contributor.author","Weishaupt, J. H."],["dc.date.accessioned","2017-09-07T11:48:47Z"],["dc.date.available","2017-09-07T11:48:47Z"],["dc.date.issued","2008"],["dc.description.abstract","Mutant superoxide dismutase 1 (mtSOD1) causes dominantly inherited amyotrophic lateral sclerosis (ALS). The mechanism for mtSOD1 toxicity remains unknown. Two main hypotheses are the impairment of proteasomal function and chaperone depletion by misfolded mtSOD1. Here, we employed FRET/FLIM and biosensor imaging to quantitatively localize ubiquitination, as well as chaperone binding of mtSOD1, and to assess their effect on proteasomal and protein folding activities. We found large differences in ubiquitination and chaperone interaction levels for wild-type (wt) SOD1 versus mtSOD1 in intact single cells. Moreover, SOD1 ubiquitination levels differ between proteasomal structures and cytoplasmic material. Hsp70 binding and ubiquitination of wt and mtSOD1 species are highly correlated, demonstrating the coupled upregulation of both cellular detoxification mechanisms upon mtSOD1 expression. Biosensor imaging in single cells revealed that mtSOD1 expression alters cellular protein folding activity but not proteasomal function in the neuronal cell line examined. Our results provide the first cell-bycell- analysis of SOD1 ubiquitination and chaperone interaction. Moreover, our study opens new methodological avenues for cell biological research on ALS."],["dc.identifier.doi","10.1038/sj.cdd.4402262"],["dc.identifier.gro","3143350"],["dc.identifier.isi","000252387900011"],["dc.identifier.pmid","17992192"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/854"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1350-9047"],["dc.title","Mutant SOD1 detoxification mechanisms in intact single cells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","4656"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","The Journal of neuroscience"],["dc.bibliographiccitation.lastpage","4662"],["dc.bibliographiccitation.volume","18"],["dc.contributor.author","Kermer, Pawel"],["dc.contributor.author","Klocker, N."],["dc.contributor.author","Labes, M."],["dc.contributor.author","Bähr, Mathias"],["dc.date.accessioned","2017-09-07T11:48:10Z"],["dc.date.available","2017-09-07T11:48:10Z"],["dc.date.issued","1998"],["dc.description.abstract","The majority of retinal ganglion cells (RGCs) degenerate and die after transection of the optic nerve (ON) in the adult rat. This secondary cell death can primarily be ascribed to apoptosis, Recent work strongly suggests a decisive role for a family of cysteine proteases, termed caspases, as mediators of neuronal apoptosis. In this study, we investigated whether activation of caspases contributes to delayed death of RGCs after axotomy. Intraocular application of various caspase inhibitors rescued up to 34% of RGCs that would otherwise have died 14 d after ON transection. Using a modified affinity-labeling technique, we detected a 17 kDa protease subunit upregulated after axotomy. Upregulation was prevented by caspase inhibitor treatment. The 17 kDa protein was identified as a CPP32-like protease by Western blot analysis and affinity labeling with biotinylated acetyl-Asp-Glu-Val-Asp-aldehyde, which specifically inhibits CPP32-like caspases. In vivo application of the irreversible caspase inhibitor benzyloxycarbonyl-Asp-Glu-Val-Asp-chloromethylketone revealed CPP32-like proteases to be major mediators of caspase-induced apoptosis in axotomized RGCs, because this inhibitor showed an even higher neuroprotective potential than the irreversible wide-range inhibitor benzyloxycarbonyl-Val-Ala-DL-Asp-fluoromethylketone. In summary, the data presented here provide further insight into the mechanisms of injury-induced neuronal apoptosis and could give rise to more effective therapeutic intervention strategies in CNS trauma and neurodegenerative diseases."],["dc.identifier.gro","3144543"],["dc.identifier.isi","000074068000021"],["dc.identifier.pmid","9614240"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2179"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Soc Neuroscience"],["dc.relation.issn","0270-6474"],["dc.title","Inhibition of CPP32-like proteases rescues axotomized retinal ganglion cells from secondary cell death in vivo"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","175"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","European Journal of Paediatric Neurology"],["dc.bibliographiccitation.lastpage","178"],["dc.bibliographiccitation.volume","16"],["dc.contributor.author","Liman, Jan"],["dc.contributor.author","Wellmer, Andreas"],["dc.contributor.author","Rostasy, Kevin"],["dc.contributor.author","Baehr, Mathias"],["dc.contributor.author","Kermer, Pawel"],["dc.date.accessioned","2017-09-07T11:48:57Z"],["dc.date.available","2017-09-07T11:48:57Z"],["dc.date.issued","2012"],["dc.description.abstract","NBIA/HSS is a neurodegenerative disorder associated with iron accumulation in specific brain regions. To date, the diagnosis is obtained by typical MRI changes followed by genetic mutation analysis. This procedure is laborious and limited to a few specially equipped medical centres. Since transcranial sonography (TCS) is widely used for the early diagnosis of PD in adults displaying parenchymal metal deposits, it is likely to be a reliable diagnostic tool for the early diagnosis of NBIA. In 7 patients with proven NBIA and 13 age-matched controls without record of neurological disease TCS was performed by an experienced ultrasound examiner. Data were analysed by two blinded investigators regarding hyperechogenicity and size of the substantia nigra (SN). SN size and hyperechogenicity was significantly increased in patients with NBIA compared to controls (students t-test: p < 0.001). TCS appears to be a non-invasive and inexpensive screening technique in patients with suspected NBIA. Performed by an experienced physician, it could enable an earlier diagnosis and pre-selection of patients for the MRI scan and genetic testing, which are still the diagnostic gold standard. (C) 2011 European Paediatric Neurology Society. Published by Elsevier Ltd. All rights reserved."],["dc.identifier.doi","10.1016/j.ejpn.2011.07.009"],["dc.identifier.gro","3142571"],["dc.identifier.isi","000301216700011"],["dc.identifier.pmid","21816641"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8936"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1090-3798"],["dc.title","Transcranial ultrasound in neurodegeneration with brain iron accumulation (NBIA)"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]