TY  - JOUR
AB  - OBJECTIVE: Neuropsychiatric symptoms are among the most prevalent sequelae of COVID-19, particularly among hospitalized patients. Recent research has identified volumetric brain changes associated with COVID-19. However, it currently remains poorly understood how brain changes relate to post-COVID fatigue and cognitive deficits. We, therefore, aimed to assess structural brain changes after hospitalization for COVID-19 and their associations with cognitive performance and fatigue. METHODS: We analyzed data from n = 57 patients previously hospitalized for COVID-19 (63% male, mean age 52 years) from the prospective, multicentric high-resolution platform of the German National Pandemic Cohort Network (NAPKON-HAP) and n = 57 matched healthy control participants (HC). We assessed cortical thickness and subcortical volumes in high-resolution T1-weighted MRI and their associations with cognitive performance (Montreal Cognitive Assessment) and fatigue (Fatigue Severity Scale). RESULTS: Patients exhibited statistically significant reductions of cortical thickness in parahippocampal gyri and the temporal lobe (all p[FDR-corrected] < 0.05) as well as reduced hippocampal volumes compared to HC (left, Cohen's d [95% CI] = 0.50 [0.12-0.8]; right d = 0.43 [0.05-0.80]). Higher acute COVID-19 severity was associated with reduced cortical thickness, particularly in the olfactory system. Furthermore, reduced cortical thickness of the temporal poles and the anterior and posterior cingulate gyrus was associated with more severe post-acute fatigue. INTERPRETATION: Our results identify long-lasting macrostructural brain changes after moderate to severe COVID-19 that correlate with acute disease severity and long-term fatigue. Early identification and targeted interventions for patients at risk of persistent brain changes are needed. TRIAL REGISTRATION: NAPKON-HAP is registered at clinicaltrials.gov (NCT04747366).
AU  - Hartung, T.J.*
AU  - Steigerwald, F.*
AU  - Romanello, A.*
AU  - Kodde, C.*
AU  - Endres, M.*
AU  - Frank, S.*
AU  - Heuschmann, P.*
AU  - Koehler, P.*
AU  - Krohn, S.*
AU  - Pape, D.*
AU  - Schaller, J.*
AU  - Stöcklein, S.*
AU  - Vadász, I.*
AU  - Vehreschild, J.*
AU  - Witzenrath, M.*
AU  - Zöller, T.*
AU  - Finke, C.*
AU  - NAPKON Study Group (Kraus, M.)
AU  - NAPKON Study Group (Lorenz-Depiereux, B.)
C1  - 76131
C2  - 58413
TI  - Post-COVID fatigue is associated with reduced cortical thickness after hospitalization.
JO  - Ann. Clin. Transl. Neurol.
PY  - 2025
SN  - 2328-9503
ER  - 

TY  - JOUR
AB  - OBJECTIVE: COASY, the gene encoding the bifunctional enzyme CoA synthase, which catalyzes the last two reactions of cellular de novo coenzyme A (CoA) biosynthesis, has been linked to two exceedingly rare autosomal recessive disorders, such as COASY protein-associated neurodegeneration (CoPAN), a form of neurodegeneration with brain iron accumulation (NBIA), and pontocerebellar hypoplasia type 12 (PCH12). We aimed to expand the phenotypic spectrum and gain insights into the pathogenesis of COASY-related disorders. METHODS: Patients were identified through targeted or exome sequencing. To unravel the molecular mechanisms of disease, RNA sequencing, bioenergetic analysis, and quantification of critical proteins were performed on fibroblasts. RESULTS: We identified five new individuals harboring novel COASY variants. While one case exhibited classical CoPAN features, the others displayed atypical symptoms such as deafness, language and autism spectrum disorders, brain atrophy, and microcephaly. All patients experienced epilepsy, highlighting its potential frequency in COASY-related disorders. Fibroblast transcriptomic profiling unveiled dysregulated expression in genes associated with mitochondrial respiration, responses to oxidative stress, transmembrane transport, various cellular signaling pathways, and protein translation, modification, and trafficking. Bioenergetic analysis revealed impaired mitochondrial oxygen consumption in COASY fibroblasts. Despite comparable total CoA levels to control cells, the amounts of mitochondrial 4'-phosphopantetheinylated proteins were significantly reduced in COASY patients. INTERPRETATION: These results not only extend the clinical phenotype associated with COASY variants but also suggest a continuum between CoPAN and PCH12. The intricate interplay of altered cellular processes and signaling pathways provides valuable insights for further research into the pathogenesis of COASY-associated diseases.
AU  - Cavestro, C.*
AU  - Morra, F.*
AU  - Legati, A.*
AU  - D'Amato, M.*
AU  - Nasca, A.*
AU  - Iuso, A.
AU  - Lubarr, N.*
AU  - Morrison, J.L.*
AU  - Wheeler, P.G.*
AU  - Serra-Juhé, C.*
AU  - Rodríguez-Santiago, B.*
AU  - Turón-Viñas, E.*
AU  - Prouteau, C.*
AU  - Barth, M.*
AU  - Hayflick, S.J.*
AU  - Ghezzi, D.*
AU  - Tiranti, V.*
AU  - Di Meo, I.*
C1  - 70690
C2  - 55815
CY  - 111 River St, Hoboken 07030-5774, Nj Usa
SP  - 1615-1629
TI  - Emerging variants, unique phenotypes, and transcriptomic signatures: An integrated study of COASY-associated diseases.
JO  - Ann. Clin. Transl. Neurol.
VL  - 11
IS  - 6
PB  - Wiley
PY  - 2024
SN  - 2328-9503
ER  - 

TY  - JOUR
AB  - OBJECTIVE: Mutations in the gene encoding for optineurin (OPTN) have been reported in the context of different neurodegenerative diseases including the amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD) spectrum. Based on single case reports, neuropathological data in OPTN mutation carriers have revealed transactive response DNA-binding protein 43 kDa (TDP-43) pathology, in addition to accumulations of tau and alpha-synuclein. Herein, we present two siblings from a consanguineous family with a homozygous frameshift mutation in the OPTN gene and different clinical presentations. METHODS: Both affected siblings underwent (i) clinical, (ii) neurophysiological, (iii) neuropsychological, (iv) radiological, and (v) laboratory examinations, and (vi) whole-exome sequencing (WES). Postmortem histopathological examination was conducted in the index patient, who deceased at the age of 41. RESULTS: The index patient developed rapidly progressing clinical features of upper and lower motor neuron dysfunction as well as apathy and cognitive deterioration at the age of 41. Autopsy revealed an ALS-FTLD pattern associated with prominent neuronal and oligodendroglial TDP-43 pathology, and an atypical limbic 4-repeat tau pathology reminiscent of argyrophilic grain disease. The brother of the index patient exhibited behavioral changes and mnestic deficits at the age of 38 and was diagnosed with behavioral FTD 5 years later, without any evidence of motor neuron dysfunction. WES revealed a homozygous frameshift mutation in the OPTN gene in both siblings (NM_001008212.2: c.1078_1079del; p.Lys360ValfsTer18). INTERPRETATION: OPTN mutations can be associated with extensive TDP-43 pathology and limbic-predominant tauopathy and present with a heterogeneous clinical phenotype within the ALS-FTD spectrum within the same family.
AU  - Parvizi, T.*
AU  - Klotz, S.*
AU  - Keritam, O.*
AU  - Caliskan, H.*
AU  - Imhof, S.*
AU  - König, T.*
AU  - Haider, L.*
AU  - Traub-Weidinger, T.*
AU  - Wagner, M.
AU  - Brunet, T.*
AU  - Brugger, M.*
AU  - Zimprich, A.*
AU  - Rath, J.*
AU  - Stogmann, E.*
AU  - Gelpi, E.*
AU  - Cetin, H.*
C1  - 70631
C2  - 55783
CY  - 111 River St, Hoboken 07030-5774, Nj Usa
SP  - 1579-1589
TI  - Clinical heterogeneity within the ALS-FTD spectrum in a family with a homozygous optineurin mutation.
JO  - Ann. Clin. Transl. Neurol.
VL  - 11
IS  - 6
PB  - Wiley
PY  - 2024
SN  - 2328-9503
ER  - 

TY  - JOUR
AB  - An association between movement disorders and immune-system dysfunction has been described in the context of rare genetic diseases such as ataxia telangiectasia as well as infectious encephalopathies. We encountered a male patient who presented immunodeficiency of unknown etiology since childhood. A medication-refractory, progressive choreodystonic movement disorder emerged at the age of 42 years and prompted an exome-wide molecular testing approach. This revealed a pathogenic hemizygous variant in CD40LG, the gene implicated in X-linked hyper-IgM syndrome. Only two prior reports have specifically suggested a causal relationship between CD40LG mutations and involuntary hyperkinetic movements. Our findings thus confirm the existence of a particular CD40LG-related condition, combining features of compromised immunity with neurodegenerative movement abnormalities. Establishing the diagnosis is crucial because of potential life-threatening immunological complications.
AU  - Škorvánek, M.*
AU  - Jech, R.*
AU  - Winkelmann, J.
AU  - Zech, M.
C1  - 64586
C2  - 52338
CY  - 111 River St, Hoboken 07030-5774, Nj Usa
SP  - 577-581
TI  - Progressive choreodystonia in X-linked hyper-IgM immunodeficiency: A rare but recurrent presentation.
JO  - Ann. Clin. Transl. Neurol.
VL  - 9
IS  - 4
PB  - Wiley
PY  - 2022
SN  - 2328-9503
ER  - 

TY  - JOUR
AB  - Coiled-Coil Domain Containing Protein 186 (CCDC186) is hypothesized to play an important role in the biogenesis of dense-core vesicles in neurons and endocrine cells. Biallelic loss-of-function variants in the encoding gene CCDC186 have been suggested as a candidate gene for a neurodevelopmental phenotype, but only one patient has been described so far. We report a second patient with a CCDC186-associated phenotype presenting with developmental delay, epileptic encephalopathy, and failure to thrive. Exome sequencing identified a homozygous loss-of-function variant in CCDC186 (NM_018017.2) c.767C> G; p.(Ser256Ter) thus providing further evidence to support CCDC186 as a new disease gene for an autosomal recessive neurodevelopmental disorder.
AU  - Brugger, M.*
AU  - Becker-Dettling, F.*
AU  - Brunet, T.*
AU  - Strom, T.*
AU  - Meitinger, T.*
AU  - Lurz, E.*
AU  - Borggraefe, I.*
AU  - Wagner, M.
C1  - 60624
C2  - 49482
CY  - 111 River St, Hoboken 07030-5774, Nj Usa
SP  - 278-283
TI  - A homozygous truncating variant in CCDC186 in an individual with epileptic encephalopathy.
JO  - Ann. Clin. Transl. Neurol.
VL  - 8
IS  - 1
PB  - Wiley
PY  - 2021
SN  - 2328-9503
ER  - 

TY  - JOUR
AB  - Originally described as a risk factor for autism, CHD8 loss-of-function variants have recently been associated with a wider spectrum of neurodevelopmental abnormalities. We further expand the CHD8-related phenotype with the description of two unrelated patients who presented with childhood-onset progressive dystonia. Whole-exome sequencing conducted in two independent laboratories revealed a CHD8 nonsense variant in one patient and a frameshift variant in the second. The patients had strongly overlapping phenotypes characterized by generalized dystonia with mild-to-moderate neurodevelopmental comorbidity. Deep brain stimulation led to clinical improvement in both cases. We suggest that CHD8 should be added to the growing list of neurodevelopmental disorder-associated genes whose mutations can also result in dystonia-dominant phenotypes.
AU  - Doummar, D.*
AU  - Treven, M.*
AU  - Qebibo, L.*
AU  - Devos, D.*
AU  - Ghoumid, J.*
AU  - Ravelli, C.*
AU  - Kranz, G.*
AU  - Krenn, M.*
AU  - Demailly, D.*
AU  - Cif, L.*
AU  - Davion, J.B.*
AU  - Zimprich, F.*
AU  - Burglen, L.*
AU  - Zech, M.
C1  - 62838
C2  - 51093
CY  - 111 River St, Hoboken 07030-5774, Nj Usa
TI  - Childhood-onset progressive dystonia associated with pathogenic truncating variants in CHD8.
JO  - Ann. Clin. Transl. Neurol.
PB  - Wiley
PY  - 2021
SN  - 2328-9503
ER  - 

TY  - JOUR
AB  - The role of genetics in the causation of cerebral palsy has become the focus of many studies aiming to unravel the heterogeneous etiology behind this frequent neurodevelopmental disorder. A recent paper reported two unrelated children with a clinical diagnosis of cerebral palsy, who carried the same de novo c.1000G > A (p.Asp334Asn) variant in FBXO31, encoding a widely studied tumor suppressor not previously implicated in monogenic disease. We now identified a third individual with the recurrent FBXO31 de novo missense variant, featuring a spastic-dystonic phenotype. Our data confirm a link between variant FBXO31 and an autosomal dominant neurodevelopmental disorder characterized by prominent motor dysfunction.
AU  - Dzinovic, I.
AU  - Škorvánek, M.*
AU  - Pavelekova, P.*
AU  - Zhao, C.
AU  - Keren, B.*
AU  - Whalen, S.*
AU  - Bakhtiari, S.*
AU  - Chih Jin, S.*
AU  - Kruer, M.C.*
AU  - Jech, R.*
AU  - Winkelmann, J.
AU  - Zech, M.
C1  - 61444
C2  - 50253
CY  - 111 River St, Hoboken 07030-5774, Nj Usa
SP  - 951-955
TI  - Variant recurrence confirms the existence of a FBXO31-related spastic-dystonic cerebral palsy syndrome.
JO  - Ann. Clin. Transl. Neurol.
VL  - 8
IS  - 4
PB  - Wiley
PY  - 2021
SN  - 2328-9503
ER  - 

TY  - JOUR
AB  - The RBL2 locus has been associated with intelligence and educational attainment but not with a monogenic disorder to date. RBL2 encodes p130, a member of the retinoblastoma protein family, which is involved in mediating neuron survival and death. Previous studies on p130 knockout mice revealing embryonic death and impaired neurogenesis underscore the importance of RBL2 in brain development. Exome sequencing in two siblings with severe intellectual disability, stereotypies and dysmorphic features identified biallelic loss-of-function variants c.556C>T, p.(Arg186Ter) and a deletion of exon 13-17 in RBL2 (NM_005611.3), establishing RBL2 as a candidate gene for an autosomal recessive neurodevelopmental disorder.
AU  - Brunet, T.
AU  - Radivojkov-Blagojevic, M.
AU  - Lichtner, P.
AU  - Kraus, V.*
AU  - Meitinger, T.
AU  - Wagner, M.
C1  - 58486
C2  - 48230
CY  - 111 River St, Hoboken 07030-5774, Nj Usa
SP  - 390-396
TI  - Biallelic loss-of-function variants in RBL2 in siblings with a neurodevelopmental disorder.
JO  - Ann. Clin. Transl. Neurol.
VL  - 7
IS  - 3
PB  - Wiley
PY  - 2020
SN  - 2328-9503
ER  - 

TY  - JOUR
AB  - Objective: Pantothenate kinase 2-associated neurodegeneration (PKAN) is a rare neurodegenerative disease caused by mutations in the pantothenate kinase 2 (PANK2) gene. PKAN is associated with iron deposition in the basal ganglia and, occasionally, with the occurrence of misshaped erythrocytes (acanthocytes). The aim of this study was to assess residual activity of PANK2 in erythrocytes of PKAN patients and to correlate these data with the type of PANK2 mutations and the progression of neurodegeneration. Methods: Residual PANK2 activities in erythrocytes of 14 PKAN patients and 14 related carriers were assessed by a radiometric assay. Clinical data on neurodegeneration included the Barry-Albright Dystonia Scale (BAD-Scale) besides further general patient features. A molecular visualization and analysis program was used to rationalize the influence of the PKAN causing mutations on a molecular level. Results: Erythrocytes of PKAN patients had markedly reduced or no PANK2 activity. However, patients with at least one allele of the c.1583C > T (T528M) or the c.833G > T (R278L) variant exhibited 12-56% of residual PANK2 activity. In line, molecular modeling indicated only minor effects on enzyme structure for these point mutations. On average, these patients with c.1583C > T or c.833G > T variant had lower BAD scores corresponding to lower symptom severity than patients with other PANK2 point mutations. Interpretation: Residual erythrocyte PANK2 activity could be a predictor for the progression of neurodegeneration in PKAN patients. Erythrocytes are an interesting patient-derived cell system with still underestimated diagnostic potential.
AU  - Werning, M.*
AU  - Müllner, E.W.*
AU  - Mlynek, G.*
AU  - Dobretzberger, V.*
AU  - Djinovic-Carugo, K.*
AU  - Baron, D.M.*
AU  - Prokisch, H.
AU  - Büchner, B.*
AU  - Klopstock, T.*
AU  - Salzer, U.*
C1  - 59767
C2  - 49038
CY  - 111 River St, Hoboken 07030-5774, Nj Usa
SP  - 1340-1351
TI  - PKAN neurodegeneration and residual PANK2 activities in patient erythrocytes.
JO  - Ann. Clin. Transl. Neurol.
VL  - 7
IS  - 8
PB  - Wiley
PY  - 2020
SN  - 2328-9503
ER  - 

TY  - JOUR
AB  - Developmental and epileptic encephalopathies are characterized by infantile seizures and psychomotor delay. Glycosylphosphatidylinositol biosynthesis defects, resulting in impaired tethering of various proteins to the cell surface, represent the underlying pathology in some patients. One of the genes involved, PIGP, has recently been associated with infantile seizures and developmental delay in two siblings. Here, we report the second family with a markedly overlapping phenotype due to a homozygous frameshift mutation (c.456delA;p.Glu153Asnfs*34) in PIGP. Flow cytometry of patient granulocytes confirmed reduced expression of glycosylphosphatidylinositol-anchored proteins as functional consequence. Our findings corroborate PIGP as a monogenic disease gene for developmental and epileptic encephalopathy.
AU  - Krenn, M.*
AU  - Knaus, A.*
AU  - Westphal, D.S.
AU  - Wortmann, S.B.
AU  - Polster, T.*
AU  - Woermann, F.G.*
AU  - Karenfort, M.*
AU  - Mayatepek, E.*
AU  - Meitinger, T.
AU  - Wagner, M.
AU  - Distelmaier, F.*
C1  - 56182
C2  - 46884
SP  - 968-973
TI  - Biallelic mutations in PIGP cause developmental and epileptic encephalopathy.
JO  - Ann. Clin. Transl. Neurol.
VL  - 6
IS  - 5
PY  - 2019
SN  - 2328-9503
ER  - 

TY  - JOUR
AB  - Variants in GABRA1 have been associated with different epilepsies ranging from mild generalized forms to epileptic encephalopathies. Despite the broad clinical spectrum, phenotypes were found to be largely concordant within families. Contrary to this observation, we report monozygotic twin sisters with generalized epilepsy due to the c.541C>T; p.(Pro181Ser) de novo variant in GABRA1. One experienced juvenile absence seizures promptly responding to first-line medication, whereas the second developed severe treatment-refractory epilepsy with febrile, absence, atonic, and tonic-clonic seizures indicating marked intrafamilial variability in GABRA1-related epilepsy. Moreover, we provide a molecular characterization of the novel variant based on recently published structural data.
AU  - Krenn, M.*
AU  - Ernst, M.*
AU  - Tomschik, M.*
AU  - Treven, M.*
AU  - Wagner, M.
AU  - Westphal, D.S.
AU  - Meitinger, T.
AU  - Pataraia, E.*
AU  - Zimprich, F.*
AU  - Aull-Watschinger, S.*
C1  - 56992
C2  - 47409
CY  - 111 River St, Hoboken 07030-5774, Nj Usa
SP  - 2317-2322
TI  - Phenotypic variability of GABRA1-related epilepsy in monozygotic twins.
JO  - Ann. Clin. Transl. Neurol.
VL  - 6
IS  - 11
PB  - Wiley
PY  - 2019
SN  - 2328-9503
ER  - 

TY  - JOUR
AB  - A recurrent de novo missense variant in KCNC1, encoding a voltage-gated potassium channel expressed in inhibitory neurons, causes progressive myoclonus epilepsy and ataxia, and a nonsense variant is associated with intellectual disability. We identified three new de novo missense variants in KCNC1 in five unrelated individuals causing different phenotypes featuring either isolated nonprogressive myoclonus (p.Cys208Tyr), intellectual disability (p.Thr399Met), or epilepsy with myoclonic, absence and generalized tonic-clonic seizures, ataxia, and developmental delay (p.Ala421Val, three patients). Functional analyses demonstrated no measurable currents for all identified variants and dominant-negative effects for p.Thr399Met and p.Ala421Val predicting neuronal disinhibition as the underlying disease mechanism.
AU  - Park, J.*
AU  - Koko, M.*
AU  - Hedrich, U.B.S.*
AU  - Hermann, A.*
AU  - Cremer, K.*
AU  - Haberlandt, E.*
AU  - Grimmel, M.*
AU  - Alhaddad, B.
AU  - Beck-Woedl, S.*
AU  - Harrer, M.*
AU  - Karall, D.*
AU  - Kingelhoefer, L.*
AU  - Tzschach, A.*
AU  - Matthies, L.C.*
AU  - Strom, T.M.
AU  - Ringelstein, E.B.*
AU  - Sturm, M.*
AU  - Engels, H.*
AU  - Wolff, M.*
AU  - Lerche, H.*
AU  - Haack, T.B.*
C1  - 56384
C2  - 47053
CY  - 111 River St, Hoboken 07030-5774, Nj Usa
SP  - 1319-1326
TI  - KCNC1-related disorders: New de novo variants expand the phenotypic spectrum.
JO  - Ann. Clin. Transl. Neurol.
VL  - 6
IS  - 7
PB  - Wiley
PY  - 2019
SN  - 2328-9503
ER  - 

TY  - JOUR
AB  - OBJECTIVE: Short-chain enoyl-CoA hydratase (ECHS1) is a multifunctional mitochondrial matrix enzyme that is involved in the oxidation of fatty acids and essential amino acids such as valine. Here, we describe the broad phenotypic spectrum and pathobiochemistry of individuals with autosomal-recessive ECHS1 deficiency. METHODS: Using exome sequencing, we identified ten unrelated individuals carrying compound heterozygous or homozygous mutations in ECHS1. Functional investigations in patient-derived fibroblast cell lines included immunoblotting, enzyme activity measurement, and a palmitate loading assay. RESULTS: Patients showed a heterogeneous phenotype with disease onset in the first year of life and course ranging from neonatal death to survival into adulthood. The most prominent clinical features were encephalopathy (10/10), deafness (9/9), epilepsy (6/9), optic atrophy (6/10), and cardiomyopathy (4/10). Serum lactate was elevated and brain magnetic resonance imaging showed white matter changes or a Leigh-like pattern resembling disorders of mitochondrial energy metabolism. Analysis of patients' fibroblast cell lines (6/10) provided further evidence for the pathogenicity of the respective mutations by showing reduced ECHS1 protein levels and reduced 2-enoyl-CoA hydratase activity. While serum acylcarnitine profiles were largely normal, in vitro palmitate loading of patient fibroblasts revealed increased butyrylcarnitine, unmasking the functional defect in mitochondrial β-oxidation of short-chain fatty acids. Urinary excretion of 2-methyl-2,3-dihydroxybutyrate - a potential derivative of acryloyl-CoA in the valine catabolic pathway - was significantly increased, indicating impaired valine oxidation. INTERPRETATION: In conclusion, we define the phenotypic spectrum of a new syndrome caused by ECHS1 deficiency. We speculate that both the β-oxidation defect and the block in l-valine metabolism, with accumulation of toxic methacrylyl-CoA and acryloyl-CoA, contribute to the disorder that may be amenable to metabolic treatment approaches.
AU  - Haack, T.B.
AU  - Jackson, C.B.*
AU  - Murayama, K.*
AU  - Kremer, L.S.
AU  - Schaller, A.*
AU  - Kotzaeridou, U.*
AU  - de Vries, M.C.*
AU  - Schottmann, G.*
AU  - Santra, S.*
AU  - Büchner, B.*
AU  - Wieland, T.
AU  - Graf, E.
AU  - Freisinger, P.*
AU  - Eggimann, S.*
AU  - Ohtake, A.*
AU  - Okazaki, Y.*
AU  - Kohda, M.*
AU  - Kishita, Y.*
AU  - Tokuzawa, Y.*
AU  - Sauer, S.*
AU  - Memari, Y.*
AU  - Kolb-Kokocinski, A.*
AU  - Durbin, R.*
AU  - Hasselmann, O.*
AU  - Cremer, K.*
AU  - Albrecht, B.*
AU  - Wieczorek, D.*
AU  - Engels, H.*
AU  - Hahn, D.*
AU  - Zink, A.M.*
AU  - Alston, C.L.*
AU  - Taylor, R.W.*
AU  - Rodenburg, R.J.*
AU  - Trollmann, R.*
AU  - Sperl, W.*
AU  - Strom, T.M.
AU  - Hoffmann, G.F.*
AU  - Mayr, J.A.*
AU  - Meitinger, T.
AU  - Bolognini, R.*
AU  - Schuelke, M.*
AU  - Nuoffer, J.M.*
AU  - Kolker, S.*
AU  - Prokisch, H.
AU  - Klopstock, T.*
C1  - 44911
C2  - 37140
SP  - 492-509
TI  - Deficiency of ECHS1 causes mitochondrial encephalopathy with cardiac involvement.
JO  - Ann. Clin. Transl. Neurol.
VL  - 2
IS  - 5
PY  - 2015
SN  - 2328-9503
ER  -