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Pesquisa : D08.811.277.040.013.500.500 [Categoria DeCS]
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[PMID]:29368828
[Au] Autor:Akhmetgaleyeva AF; Khidiyatova IM; Saifullina EV; Idrisova RF; Magzhanov RV; Khusnutdinova EK
[Ti] Título:[Two novel mutations in gene SPG4 in patients with autosomal dominant spastic paraplegia].
[So] Source:Genetika;52(6):691-6, 2016 Jun.
[Is] ISSN:0016-6758
[Cp] País de publicação:Russia (Federation)
[La] Idioma:rus
[Ab] Resumo:Hereditary spastik paraplegias (HSP) are a group of neurodegenerative disorders with primary lesion of the pyramidal tract. The most frequent autosomal dominant form of the disease in Europeans is HSP associated with mutations in the spastin gene (SPG4). Analysis of the gene SPG4 was carried out in 52 unrelated families with HSP from Bashkortostan by SSCP and following sequencing. Previously undescribed frameshift mutations c.322del29 (p.Val108SerfsX18) and c.885del10 (p.Thr295ThrfsX16) were detected in two unrelated families. Clinical studies have shown that, in both families, the disease corresponds to an uncomplicated form of hereditary spastic paraplegia, a main feature of which is the lower spastic paraparesis without any other symptoms.
[Mh] Termos MeSH primário: Família
Mutação
Polimorfismo de Nucleotídeo Único
Polimorfismo Conformacional de Fita Simples
Paraplegia Espástica Hereditária/genética
Espastina/genética
[Mh] Termos MeSH secundário: Feminino
Seres Humanos
Masculino
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.6.4.3 (SPAST protein, human); EC 3.6.4.3 (Spastin)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180205
[Lr] Data última revisão:
180205
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180126
[St] Status:MEDLINE


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[PMID]:28572275
[Au] Autor:Chelban V; Tucci A; Lynch DS; Polke JM; Santos L; Jonvik H; Groppa S; Wood NW; Houlden H
[Ad] Endereço:Department of Molecular Neuroscience, UCL Institute of Neurology, London, UK.
[Ti] Título:Truncating mutations in patients are associated with a high rate of psychiatric comorbidities in hereditary spastic paraplegia.
[So] Source:J Neurol Neurosurg Psychiatry;88(8):681-687, 2017 Aug.
[Is] ISSN:1468-330X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The hereditary spastic paraplegias (HSPs) are a rare and heterogeneous group of neurodegenerative disorders that are clinically characterised by progressive lower limb spasticity. They are classified as either 'pure' or 'complex' where spastic paraplegia is complicated with additional neurological features. Mutations in the spastin gene ( ) are the most common cause of HSP and typically present with a pure form. METHODS: We assessed in detail the phenotypic and genetic spectrum of -related HSP focused on 118 patients carrying mutations. RESULTS: This study, one of the largest cohorts of genetically confirmed spastin patients to date, contributes with the discovery of a significant number of novel mutations. Our data reveal a high rate of complex cases (25%), with psychiatric disorders among the most common comorbidity (10% of all patients). Further, we identify a genotype-phenotype correlation between patients carrying loss-of-function mutations in and the presence of psychiatric disorders.
[Mh] Termos MeSH primário: Adenosina Trifosfatases/genética
Análise Mutacional de DNA
Transtornos Mentais/genética
Paraplegia Espástica Hereditária/genética
[Mh] Termos MeSH secundário: Adolescente
Adulto
Idade de Início
Alelos
Criança
Pré-Escolar
Códon sem Sentido/genética
Éxons/genética
Feminino
Triagem de Portadores Genéticos
Genótipo
Seres Humanos
Lactente
Recém-Nascido
Íntrons/genética
Masculino
Transtornos Mentais/diagnóstico
Meia-Idade
Mutação de Sentido Incorreto/genética
Fenótipo
Mutação Puntual/genética
Deleção de Sequência/genética
Paraplegia Espástica Hereditária/diagnóstico
Espastina
Estatística como Assunto
Reino Unido
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Codon, Nonsense); EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.4.3 (SPAST protein, human); EC 3.6.4.3 (Spastin)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170603
[St] Status:MEDLINE
[do] DOI:10.1136/jnnp-2017-315796


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[PMID]:28398512
[Au] Autor:Leo L; Weissmann C; Burns M; Kang M; Song Y; Qiang L; Brady ST; Baas PW; Morfini G
[Ad] Endereço:Department of Neurobiology and Anatomy, Drexel University College of Medicine, Philadelphia, PA, USA.
[Ti] Título:Mutant spastin proteins promote deficits in axonal transport through an isoform-specific mechanism involving casein kinase 2 activation.
[So] Source:Hum Mol Genet;26(12):2321-2334, 2017 Jun 15.
[Is] ISSN:1460-2083
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Mutations of various genes cause hereditary spastic paraplegia (HSP), a neurological disease involving dying-back degeneration of upper motor neurons. From these, mutations in the SPAST gene encoding the microtubule-severing protein spastin account for most HSP cases. Cumulative genetic and experimental evidence suggests that alterations in various intracellular trafficking events, including fast axonal transport (FAT), may contribute to HSP pathogenesis. However, the mechanisms linking SPAST mutations to such deficits remain largely unknown. Experiments presented here using isolated squid axoplasm reveal inhibition of FAT as a common toxic effect elicited by spastin proteins with different HSP mutations, independent of microtubule-binding or severing activity. Mutant spastin proteins produce this toxic effect only when presented as the tissue-specific M1 isoform, not when presented as the ubiquitously-expressed shorter M87 isoform. Biochemical and pharmacological experiments further indicate that the toxic effects of mutant M1 spastins on FAT involve casein kinase 2 (CK2) activation. In mammalian cells, expression of mutant M1 spastins, but not their mutant M87 counterparts, promotes abnormalities in the distribution of intracellular organelles that are correctable by pharmacological CK2 inhibition. Collectively, these results demonstrate isoform-specific toxic effects of mutant M1 spastin on FAT, and identify CK2 as a critical mediator of these effects.
[Mh] Termos MeSH primário: Adenosina Trifosfatases/genética
Transporte Axonal/genética
[Mh] Termos MeSH secundário: Adenosina Trifosfatases/metabolismo
Animais
Transporte Axonal/fisiologia
Caseína Quinase II/metabolismo
Células Cultivadas
Decapodiformes
Modelos Animais de Doenças
Fibroblastos
Seres Humanos
Microtúbulos/metabolismo
Neurônios Motores/metabolismo
Proteínas Mutantes/metabolismo
Mutação
Isoformas de Proteínas/genética
Transporte Proteico/fisiologia
Ratos
Paraplegia Espástica Hereditária/genética
Paraplegia Espástica Hereditária/metabolismo
Espastina
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Mutant Proteins); 0 (Protein Isoforms); EC 2.7.11.1 (Casein Kinase II); EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.4.3 (SPAST protein, human); EC 3.6.4.3 (Spastin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170412
[St] Status:MEDLINE
[do] DOI:10.1093/hmg/ddx125


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[PMID]:27629539
[Au] Autor:Yuliang W; Yuan W; Xuezhen W; He M; Qi Z; Jinbo C
[Ad] Endereço:Department of Neurology, Binzhou Medical University Hospital, No. 661 Huanghe 2nd Road of Binzhou, Shandong, China.
[Ti] Título:A novel SPAST frameshift mutation in a Chinese family with hereditary spastic paraplegia.
[So] Source:Neurol Sci;38(2):365-367, 2017 Feb.
[Is] ISSN:1590-3478
[Cp] País de publicação:Italy
[La] Idioma:eng
[Mh] Termos MeSH primário: Adenosina Trifosfatases/genética
Paraplegia Espástica Hereditária/genética
[Mh] Termos MeSH secundário: Idoso
China
Mutação da Fase de Leitura
Seres Humanos
Masculino
Linhagem
Espastina
[Pt] Tipo de publicação:CASE REPORTS; LETTER
[Nm] Nome de substância:
EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.4.3 (SPAST protein, human); EC 3.6.4.3 (Spastin)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160916
[St] Status:MEDLINE
[do] DOI:10.1007/s10072-016-2712-9


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[PMID]:28006827
[Au] Autor:Newton TM; Reid E
[Ad] Endereço:Department of Medical Genetics and Cambridge Institute for Medical Research, University of Cambridge, Cambridge, United Kingdom.
[Ti] Título:An Automated Image Analysis System to Quantify Endosomal Tubulation.
[So] Source:PLoS One;11(12):e0168294, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Recycling of cargos from early endosomes requires regulation of endosomal tubule formation and fission. This regulation is disrupted in cells depleted of the microtubule severing enzyme spastin, causing elongation of endosomal tubules and mis-trafficking of recycling endosomal cargos such as the transferrin receptor. Spastin is encoded by SPAST, mutations in which are the most frequent cause of autosomal dominant hereditary spastic paraplegia, a condition characterised by a progressive loss of lower limb function resulting from upper motor neuron axonopathy. Investigation of molecular factors involved in endosomal tubule regulation is hindered by the need for manual counting of endosomal tubules. We report here the development of an open source automated system for the quantification of endosomal tubules, using ImageJ and R. We validate the method in cells depleted of spastin and its binding partner IST1. The additional speed and reproducibility of this system compared with manual counting makes feasible screens of candidates to further understand the mechanisms of endosomal tubule formation and fission.
[Mh] Termos MeSH primário: Adenosina Trifosfatases/metabolismo
Endossomos/metabolismo
Fibroblastos/metabolismo
Processamento de Imagem Assistida por Computador/métodos
Pulmão/metabolismo
Microscopia de Fluorescência/métodos
Microtúbulos/metabolismo
[Mh] Termos MeSH secundário: Automação
Células Cultivadas
Fibroblastos/citologia
Imunofluorescência
Células HeLa
Seres Humanos
Pulmão/citologia
Espastina
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.4.3 (SPAST protein, human); EC 3.6.4.3 (Spastin)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161223
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0168294


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[PMID]:27871443
[Au] Autor:de Souza PV; Bortholin T; Naylor FG; de Rezende Pinto WB; Oliveira AS
[Ad] Endereço:Division of Neuromuscular Diseases, Department of Neurology and Neurosurgery, Federal University of São Paulo (UNIFESP), São Paulo, SP, Brazil.
[Ti] Título:Infantile-onset ascending spastic paraplegia phenotype associated with SPAST mutation.
[So] Source:J Neurol Sci;371:34-35, 2016 Dec 15.
[Is] ISSN:1878-5883
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Mh] Termos MeSH primário: Adenosina Trifosfatases/genética
Mutação de Sentido Incorreto
Paraplegia Espástica Hereditária/genética
[Mh] Termos MeSH secundário: Adulto
Encéfalo/diagnóstico por imagem
Feminino
Seres Humanos
Fenótipo
Paraplegia Espástica Hereditária/diagnóstico por imagem
Paraplegia Espástica Hereditária/fisiopatologia
Espastina
[Pt] Tipo de publicação:CASE REPORTS; LETTER
[Nm] Nome de substância:
EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.4.3 (SPAST protein, human); EC 3.6.4.3 (Spastin)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161123
[St] Status:MEDLINE


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[PMID]:27423575
[Au] Autor:Tisher A; Salardini A
[Ad] Endereço:Yale Department of Neurology, 800 Howard Avenue, New Haven, CT 06511, United States. Electronic address: annya.tisher@gmail.com.
[Ti] Título:A case report of a woman with young onset cognitive impairment associated with hereditary spastic paraplegia due to a mutation in the SPAST gene.
[So] Source:J Neurol Sci;367:131-2, 2016 Aug 15.
[Is] ISSN:1878-5883
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Mh] Termos MeSH primário: Adenosina Trifosfatases/genética
Disfunção Cognitiva/complicações
Disfunção Cognitiva/genética
Mutação
Paraplegia Espástica Hereditária/complicações
Paraplegia Espástica Hereditária/genética
[Mh] Termos MeSH secundário: Adulto
Encéfalo/diagnóstico por imagem
Disfunção Cognitiva/diagnóstico por imagem
Disfunção Cognitiva/fisiopatologia
Feminino
Seres Humanos
Linhagem
Paraplegia Espástica Hereditária/diagnóstico por imagem
Paraplegia Espástica Hereditária/fisiopatologia
Espastina
[Pt] Tipo de publicação:CASE REPORTS; LETTER
[Nm] Nome de substância:
EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.4.3 (SPAST protein, human); EC 3.6.4.3 (Spastin)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160718
[St] Status:MEDLINE


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[PMID]:27334366
[Au] Autor:Mészárosová AU; Putzová M; Cermáková M; Vávrová D; Dolezalová K; Smetanová I; Stejskal D; Beetz C; Seeman P
[Ad] Endereço:DNA Laboratory, Department of Child Neurology, Charles University Second Medical School and University Hospital Motol, Prague, Czech Republic.
[Ti] Título:SPAST mutation spectrum and familial occurrence among Czech patients with pure hereditary spastic paraplegia.
[So] Source:J Hum Genet;61(10):845-850, 2016 Oct.
[Is] ISSN:1435-232X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The SPAST gene has a major role in hereditary spastic paraplegias (HSPs). This is the first report mapping characteristics of the SPAST gene in a large cohort of Czech HSP patients. All 17 coding exons of the SPAST gene were Sanger sequenced in 327 patients from 263 independent families with suspected uncomplicated HSP. The selected 126 independent patients, without mutation in the SPAST gene after Sanger sequencing, were subsequently tested by Multiplex Ligation-dependent Probe Amplification (MLPA) assay for large deletions or copy number variations affecting the SPAST gene. Among the 263 independent patients, 35 different, small mutations in 44 patients were found. Twenty-one mutations are novel with the majority of frameshift mutations. Seven mutations were found in more than one family. The age at onset ranged between preschool childhood and the fifth decade with inter- and intra-familiar differences. SPAST small mutations were detected in 16.7% (44/263) of independent tested patients. Mutations in the SPAST gene were found more frequently in familial cases (with affected relatives). Mutation were found in 31.9% (29/91 familial tested) in the familial patient group, whereas in the sporadic patient group, mutations were found in only 4.7% of cases (5/106 sporadic cases). Among SPAST-positive patients, 65.9% (29/44) were familial but only 11.4% (5/44) were sporadic. MLPA testing revealed four large deletions in four independent patients, all in familial-positive cases. Mutations in the SPAST gene are 5.8 × more frequent in familial than in sporadic cases. Large deletions were found only in familial patients. Diagnostic testing of the SPAST gene is useful only in positive family history patients not in sporadic cases.
[Mh] Termos MeSH primário: Adenosina Trifosfatases/genética
Mutação
Paraplegia Espástica Hereditária/diagnóstico
Paraplegia Espástica Hereditária/genética
[Mh] Termos MeSH secundário: Adolescente
Adulto
Alelos
República Tcheca
Análise Mutacional de DNA
Éxons
Feminino
Genótipo
Seres Humanos
Íntrons
Masculino
Meia-Idade
Linhagem
Fenótipo
Polimorfismo Genético
Análise de Sequência de DNA
Deleção de Sequência
Espastina
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.4.3 (SPAST protein, human); EC 3.6.4.3 (Spastin)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160624
[St] Status:MEDLINE
[do] DOI:10.1038/jhg.2016.73


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[PMID]:27332127
[Au] Autor:Nakao H; Ikeda K; Ishihama Y; Nakano M
[Ad] Endereço:Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan.
[Ti] Título:Membrane-Spanning Sequences in Endoplasmic Reticulum Proteins Promote Phospholipid Flip-Flop.
[So] Source:Biophys J;110(12):2689-2697, 2016 Jun 21.
[Is] ISSN:1542-0086
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The mechanism whereby phospholipids rapidly flip-flop in the endoplasmic reticulum (ER) membrane remains unknown. We previously demonstrated that the presence of a hydrophilic residue in the center of the model transmembrane peptide sequence effectively promoted phospholipid flip-flop and that hydrophilic residues composed 4.5% of the central regions of the membrane-spanning sequences of human ER membrane proteins predicted by SOSUI software. We hypothesized that ER proteins with hydrophilic residues might play a critical role in promoting flip-flop. Here, we evaluated the flip rate of fluorescently labeled lipids in vesicles containing each of the 11 synthetic peptides of membrane-spanning sequences, using a dithionite-quenching assay. Although the flippase activities of nine peptides were unexpectedly low, the peptides based on the EDEM1 and SPAST proteins showed enhanced flippase activity with three different fluorescently labeled lipids. The substitution of hydrophobic Ala with His or Arg in the central region of the EDEM1 or SPAST peptides, respectively, attenuated their ability to flip phospholipids. Interestingly, substituting Ala with Arg or His at a location outside of the central region of EDEM1 or SPAST, respectively, also affected the enhancement of flip-flop. These results indicated that both Arg and His are important for the ability of these two peptides to increase the flip rates. The EDEM1 peptide exhibited high activity at significantly low peptide concentrations, suggesting that the same side positioning of Arg and His in α-helix structure is critical for the flip-flop promotion and that the EDEM1 protein is a candidate flippase in the ER.
[Mh] Termos MeSH primário: Adenosina Trifosfatases/química
Retículo Endoplasmático/química
Peptídeos e Proteínas de Sinalização Intracelular/química
Proteínas de Membrana/química
Peptídeos/química
Fosfolipídeos/química
[Mh] Termos MeSH secundário: Adenosina Trifosfatases/genética
Adenosina Trifosfatases/metabolismo
Sequência de Aminoácidos
Colesterol/metabolismo
Dicroísmo Circular
Seres Humanos
Interações Hidrofóbicas e Hidrofílicas
Peptídeos e Proteínas de Sinalização Intracelular/genética
Cinética
Proteínas de Membrana/genética
Proteínas de Membrana/metabolismo
Modelos Moleculares
Mutação
Peptídeos/síntese química
Peptídeos/genética
Peptídeos/metabolismo
Fosfolipídeos/metabolismo
Estrutura Secundária de Proteína
Software
Espastina
Lipossomas Unilamelares/química
Lipossomas Unilamelares/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (EDEM1 protein, human); 0 (Intracellular Signaling Peptides and Proteins); 0 (Membrane Proteins); 0 (Peptides); 0 (Phospholipids); 0 (Unilamellar Liposomes); 97C5T2UQ7J (Cholesterol); EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.4.3 (SPAST protein, human); EC 3.6.4.3 (Spastin)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160623
[St] Status:MEDLINE


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[PMID]:27260292
[Au] Autor:Polymeris AA; Tessa A; Anagnostopoulou K; Rubegni A; Galatolo D; Dinopoulos A; Gika AD; Youroukos S; Skouteli E; Santorelli FM; Pons R
[Ad] Endereço:First Department of Pediatrics, Aghia Sophia Children's Hospital, University of Athens, Thivon and Micras Asias, 11527, Athens, Greece.
[Ti] Título:A series of Greek children with pure hereditary spastic paraplegia: clinical features and genetic findings.
[So] Source:J Neurol;263(8):1604-11, 2016 Aug.
[Is] ISSN:1432-1459
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Hereditary spastic paraplegia (HSP) is a clinically and genetically heterogeneous group of neurodegenerative disorders mainly characterized by progressive spasticity of the lower limbs. Adult case series dominate the literature, and there have been only a few studies in children. The purpose of this study is to describe our experience with pediatric HSP in Greece. We report the clinical and genetic findings in our patients and aim to offer insights into the diagnostic difficulties of childhood-onset disease. A series of 15 Greek children affected by pure HSP underwent extensive diagnostic investigations. Molecular analysis included whole exome sequencing (WES) or consecutive screening of candidate genes ATL1, SPAST, REEP1, and CYP7B1. WES performed in three cases yielded previously reported mutations in ATL1 and CYP7B1, and a variant c.397C>T of unknown significance in SPG7. Candidate gene screening performed in the remaining patients identified previously reported mutations in ATL1 (2), SPAST (2), and REEP1 (1), and two novel mutations, c.1636G>A and c.1413+3_6delAAGT, in SPAST. In six cases, the mutations were inherited from their parents, while in three cases, the mutations were apparently de novo. Our data confirm the genetic heterogeneity of childhood-onset pure HSP, with SPG4/SPAST and SPG3A/ATL1 being the most frequent forms. De novo occurrence of HSP does not seem to be uncommon. Candidate gene studies guided by diagnostic algorithms and WES seem both to be reasonable genetic testing strategies.
[Mh] Termos MeSH primário: Adenosina Trifosfatases/genética
Proteínas de Ligação ao GTP/genética
Predisposição Genética para Doença/genética
Proteínas de Membrana/genética
Mutação/genética
Paraplegia Espástica Hereditária/diagnóstico
Paraplegia Espástica Hereditária/genética
[Mh] Termos MeSH secundário: Adolescente
Criança
Pré-Escolar
Análise Mutacional de DNA
Avaliação da Deficiência
Progressão da Doença
Feminino
Grécia
Seres Humanos
Masculino
Índice de Gravidade de Doença
Espastina
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Membrane Proteins); EC 3.6.1.- (ATL1 protein, human); EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.1.- (GTP-Binding Proteins); EC 3.6.4.3 (SPAST protein, human); EC 3.6.4.3 (Spastin)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160605
[St] Status:MEDLINE
[do] DOI:10.1007/s00415-016-8179-z



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BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde