Kermer, Pawel

[["dc.bibliographiccitation.firstpage","152"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Cerebrovascular Diseases"],["dc.bibliographiccitation.lastpage","154"],["dc.bibliographiccitation.volume","24"],["dc.contributor.author","Crome, Olaf"],["dc.contributor.author","Kermer, Pawel"],["dc.contributor.author","Buhk, Jan-Hendrik"],["dc.contributor.author","Schoendube, Friedrich"],["dc.contributor.author","Kastrup, Andreas"],["dc.date.accessioned","2018-11-07T11:06:11Z"],["dc.date.available","2018-11-07T11:06:11Z"],["dc.date.issued","2007"],["dc.identifier.doi","10.1159/000103622"],["dc.identifier.isi","000247435300030"],["dc.identifier.pmid","17565208"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/52247"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Karger"],["dc.relation.issn","1015-9770"],["dc.title","Emergency surgical revascularization in a patient with acute symptomatic common carotid artery occlusion"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3643"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Stroke"],["dc.bibliographiccitation.lastpage","3645"],["dc.bibliographiccitation.volume","42"],["dc.contributor.author","Stahrenberg, Raoul"],["dc.contributor.author","Edelmann, Frank"],["dc.contributor.author","Haase, Beatrice"],["dc.contributor.author","Lahno, Rosine"],["dc.contributor.author","Seegers, Jochen"],["dc.contributor.author","Weber-Krueger, Mark"],["dc.contributor.author","Mende, Meinhard"],["dc.contributor.author","Wohlfahrt, Janin"],["dc.contributor.author","Kermer, Pawel"],["dc.contributor.author","Vollmann, Dirk"],["dc.contributor.author","Hasenfuß, Gerd"],["dc.contributor.author","Groeschel, Klaus"],["dc.contributor.author","Wachter, Rolf"],["dc.date.accessioned","2017-09-07T11:43:17Z"],["dc.date.available","2017-09-07T11:43:17Z"],["dc.date.issued","2011"],["dc.description.abstract","Background and Purpose-We assessed whether echocardiography can predict paroxysmal atrial fibrillation (PAF) in patients with cerebral ischemia presenting in sinus rhythm. Methods-Within the prospective Find-AF cohort, 193 consecutive patients with cerebral ischemia and sinus rhythm on presentation had evaluation of echocardiographic parameters of left atrial size and function. PAF was diagnosed by 7-day Holter monitoring. Results-In 26 patients with PAF, late diastolic Doppler (A') and tissue Doppler (a') velocities were lower whereas left atrial diameter, left atrial volume index (LAVI), LAVI/A, and LAVI/a' were larger (P < 0.05 for all) than they were in 167 patients without PAF. In multivariate models A, a', LAVI/A, and LAVI/a' predicted the presence of PAF. Area under the receiver operating characteristic curve to diagnose PAF was highest for LAVI/a' (0.813 [0.738; 0.889]). A previously suggested cut-off of LAVI/a' < 2.3 had 92% sensitivity, 55.8% specificity, and 98% negative predictive value for PAF. Conclusions-LAVI/a' < 2.3 can effectively rule out PAF in patients with cerebral ischemia. (Stroke. 2011; 42: 3643-3645.)"],["dc.identifier.doi","10.1161/STROKEAHA.111.632836"],["dc.identifier.gro","3142621"],["dc.identifier.isi","000297941500066"],["dc.identifier.pmid","21998056"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/45"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0039-2499"],["dc.title","Transthoracic Echocardiography to Rule Out Paroxysmal Atrial Fibrillation as a Cause of Stroke or Transient Ischemic Attack"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["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","38"],["dc.bibliographiccitation.journal","Progress in Neurobiology"],["dc.bibliographiccitation.lastpage","66"],["dc.bibliographiccitation.volume","104"],["dc.contributor.author","Rueb, Udo"],["dc.contributor.author","Schoels, Ludger"],["dc.contributor.author","Paulson, Henry"],["dc.contributor.author","Auburger, Georg"],["dc.contributor.author","Kermer, Pawel"],["dc.contributor.author","Jen, Joanna C."],["dc.contributor.author","Seidel, Kay"],["dc.contributor.author","Korf, Horst-Werner"],["dc.contributor.author","Deller, Thomas"],["dc.date.accessioned","2018-11-07T09:25:04Z"],["dc.date.available","2018-11-07T09:25:04Z"],["dc.date.issued","2013"],["dc.description.abstract","The spinocerebellar ataxias type 1 (SCA1), 2 (SCA2), 3 (SCA3), 6 (SCA6) and 7 (SCA7) are genetically defined autosomal dominantly inherited progressive cerebellar ataxias (ADCAs). They belong to the group of CAG-repeat or polyglutamine diseases and share pathologically expanded and meiotically unstable glutamine-encoding CAG-repeats at distinct gene loci encoding elongated polyglutamine stretches in the disease proteins. In recent years, progress has been made in the understanding of the pathogenesis of these currently incurable diseases: Identification of underlying genetic mechanisms made it possible to classify the different ADCAs and to define their clinical and pathological features. Furthermore, advances in molecular biology yielded new insights into the physiological and pathophysiological role of the gene products of SCA1, SCA2, SCA3, SCA6 and SCA7 (i.e. ataxin-1, ataxin-2, ataxin-3, alpha-(1A) subunit of the P/Q type voltage-dependent calcium channel, ataxin-7). In the present review we summarize our current knowledge about the polyglutamine ataxias SCA1, SCA2, SCA3, SCA6 and SCA7 and compare their clinical and electrophysiological features, genetic and molecular biological background, as well as their brain pathologies. Furthermore, we provide an overview of the structure, interactions and functions of the different disease proteins. On the basis of these comprehensive data, similarities, differences and possible disease mechanisms are discussed. (C) 2013 Elsevier Ltd. All rights reserved."],["dc.identifier.doi","10.1016/j.pneurobio.2013.01.001"],["dc.identifier.isi","000318887200002"],["dc.identifier.pmid","23438480"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/29982"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Pergamon-elsevier Science Ltd"],["dc.relation.issn","0301-0082"],["dc.title","Clinical features, neurogenetics and neuropathology of the polyglutamine spinocerebellar ataxias type 1, 2, 3, 6 and 7"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["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"]]