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Pesquisa : D12.776.157.530.400.875.750.960 [Categoria DeCS]
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[PMID]:26179811
[Au] Autor:Peeters U; Scornik F; Riuró H; Pérez G; Komurcu-Bayrak E; Van Malderen S; Pappaert G; Tarradas A; Pagans S; Daneels D; Breckpot K; Brugada P; Bonduelle M; Brugada R; Van Dooren S
[Ad] Endereço:Centre for Medical Genetics, Reproduction and Genetics; Reproduction, Genetics and Regenerative Medicine, Vrije Universiteit Brussel (VUB), Universitair Ziekenhuis Brussel (UZ Brussel).
[Ti] Título:Contribution of Cardiac Sodium Channel ß-Subunit Variants to Brugada Syndrome.
[So] Source:Circ J;79(10):2118-29, 2015.
[Is] ISSN:1347-4820
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Brugada syndrome (BrS) is an inheritable cardiac disease associated with syncope, malignant ventricular arrhythmias and sudden cardiac death. The largest proportion of mutations in BrS is found in the SCN5A gene encoding the α-subunit of cardiac sodium channels (Nav1.5). Causal SCN5A mutations are present in 18-30% of BrS patients. The additional genetic diagnostic yield of variants in cardiac sodium channel ß-subunits in BrS patients was explored and functional studies on 3 novel candidate variants were performed. METHODS AND RESULTS: TheSCN1B-SCN4B genes were screened, which encode the 5 sodium channel ß-subunits, in a SCN5A negative BrS population (n=74). Five novel variants were detected; in silico pathogenicity prediction classified 4 variants as possibly disease causing. Three variants were selected for functional study. These variants caused only limited alterations of Nav1.5 function. Next generation sequencing of a panel of 88 arrhythmia genes could not identify other major causal mutations. CONCLUSIONS: It was hypothesized that the studied variants are not the primary cause of BrS in these patients. However, because small functional effects of these ß-subunit variants can be discriminated, they might contribute to the BrS phenotype and be considered a risk factor. The existence of these risk factors can give an explanation to the reduced penetrance and variable expressivity seen in this syndrome. We therefore recommend including the SCN1-4B genes in a next generation sequencing-based gene panel.
[Mh] Termos MeSH primário: Síndrome de Brugada
Mutação
Subunidades beta do Canal de Sódio Disparado por Voltagem/genética
Subunidades beta do Canal de Sódio Disparado por Voltagem/metabolismo
[Mh] Termos MeSH secundário: Adulto
Idoso
Síndrome de Brugada/genética
Síndrome de Brugada/mortalidade
Síndrome de Brugada/fisiopatologia
Feminino
Células HEK293
Seres Humanos
Masculino
Meia-Idade
Canal de Sódio Disparado por Voltagem NAV1.5/genética
Canal de Sódio Disparado por Voltagem NAV1.5/metabolismo
[Pt] Tipo de publicação:CLINICAL TRIAL; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (NAV1.5 Voltage-Gated Sodium Channel); 0 (SCN5A protein, human); 0 (Voltage-Gated Sodium Channel beta Subunits)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:150928
[Lr] Data última revisão:
150928
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150717
[St] Status:MEDLINE
[do] DOI:10.1253/circj.CJ-15-0164


  2 / 8 MEDLINE  
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[PMID]:25668026
[Au] Autor:O'Malley HA; Isom LL
[Ad] Endereço:Department of Pharmacology, University of Michigan Medical School, Ann Arbor, Michigan 48109; email: lisom@umich.edu.
[Ti] Título:Sodium channel ß subunits: emerging targets in channelopathies.
[So] Source:Annu Rev Physiol;77:481-504, 2015.
[Is] ISSN:1545-1585
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Voltage-gated sodium channels (VGSCs) are responsible for the initiation and propagation of action potentials in excitable cells. VGSCs in mammalian brain are heterotrimeric complexes of α and ß subunits. Although ß subunits were originally termed auxiliary, we now know that they are multifunctional signaling molecules that play roles in both excitable and nonexcitable cell types and with or without the pore-forming α subunit present. ß subunits function in VGSC and potassium channel modulation, cell adhesion, and gene regulation, with particularly important roles in brain development. Mutations in the genes encoding ß subunits are linked to a number of diseases, including epilepsy, sudden death syndromes like SUDEP and SIDS, and cardiac arrhythmia. Although VGSC ß subunit-specific drugs have not yet been developed, this protein family is an emerging therapeutic target.
[Mh] Termos MeSH primário: Canalopatias/genética
Canalopatias/fisiopatologia
Mutação/genética
Subunidades beta do Canal de Sódio Disparado por Voltagem/genética
Subunidades beta do Canal de Sódio Disparado por Voltagem/fisiologia
[Mh] Termos MeSH secundário: Arritmias Cardíacas/genética
Arritmias Cardíacas/fisiopatologia
Transtorno Autístico/genética
Transtorno Autístico/fisiopatologia
Adesão Celular/genética
Adesão Celular/fisiologia
Epilepsia/genética
Epilepsia/fisiopatologia
Perfilação da Expressão Gênica
Seres Humanos
Doenças Neurodegenerativas/genética
Doenças Neurodegenerativas/fisiopatologia
Processamento de Proteína Pós-Traducional/genética
Processamento de Proteína Pós-Traducional/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Voltage-Gated Sodium Channel beta Subunits)
[Em] Mês de entrada:1511
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150211
[St] Status:MEDLINE
[do] DOI:10.1146/annurev-physiol-021014-071846


  3 / 8 MEDLINE  
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[PMID]:25567098
[Au] Autor:Namadurai S; Yereddi NR; Cusdin FS; Huang CL; Chirgadze DY; Jackson AP
[Ad] Endereço:Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1QW, UK.
[Ti] Título:A new look at sodium channel ß subunits.
[So] Source:Open Biol;5(1):140192, 2015 Jan.
[Is] ISSN:2046-2441
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Voltage-gated sodium (Nav) channels are intrinsic plasma membrane proteins that initiate the action potential in electrically excitable cells. They are a major focus of research in neurobiology, structural biology, membrane biology and pharmacology. Mutations in Nav channels are implicated in a wide variety of inherited pathologies, including cardiac conduction diseases, myotonic conditions, epilepsy and chronic pain syndromes. Drugs active against Nav channels are used as local anaesthetics, anti-arrhythmics, analgesics and anti-convulsants. The Nav channels are composed of a pore-forming α subunit and associated ß subunits. The ß subunits are members of the immunoglobulin (Ig) domain family of cell-adhesion molecules. They modulate multiple aspects of Nav channel behaviour and play critical roles in controlling neuronal excitability. The recently published atomic resolution structures of the human ß3 and ß4 subunit Ig domains open a new chapter in the study of these molecules. In particular, the discovery that ß3 subunits form trimers suggests that Nav channel oligomerization may contribute to the functional properties of some ß subunits.
[Mh] Termos MeSH primário: Subunidades beta do Canal de Sódio Disparado por Voltagem/química
[Mh] Termos MeSH secundário: Potenciais de Ação
Sequência de Aminoácidos
Animais
Evolução Molecular
Seres Humanos
Ativação do Canal Iônico
Dados de Sequência Molecular
Subunidades beta do Canal de Sódio Disparado por Voltagem/genética
Subunidades beta do Canal de Sódio Disparado por Voltagem/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Voltage-Gated Sodium Channel beta Subunits)
[Em] Mês de entrada:1508
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150109
[St] Status:MEDLINE


  4 / 8 MEDLINE  
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[PMID]:24737232
[Au] Autor:Calhoun JD; Isom LL
[Ad] Endereço:Department of Pharmacology, University of Michigan, Ann Arbor, MI, 48109-5632, USA.
[Ti] Título:The role of non-pore-forming ß subunits in physiology and pathophysiology of voltage-gated sodium channels.
[So] Source:Handb Exp Pharmacol;221:51-89, 2014.
[Is] ISSN:0171-2004
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Voltage-gated sodium channel ß1 and ß2 subunits were discovered as auxiliary proteins that co-purify with pore-forming α subunits in brain. The other family members, ß1B, ß3, and ß4, were identified by homology and shown to modulate sodium current in heterologous systems. Work over the past 2 decades, however, has provided strong evidence that these proteins are not simply ancillary ion channel subunits, but are multifunctional signaling proteins in their own right, playing both conducting (channel modulatory) and nonconducting roles in cell signaling. Here, we discuss evidence that sodium channel ß subunits not only regulate sodium channel function and localization but also modulate voltage-gated potassium channels. In their nonconducting roles, VGSC ß subunits function as immunoglobulin superfamily cell adhesion molecules that modulate brain development by influencing cell proliferation and migration, axon outgrowth, axonal fasciculation, and neuronal pathfinding. Mutations in genes encoding ß subunits are linked to paroxysmal diseases including epilepsy, cardiac arrhythmia, and sudden infant death syndrome. Finally, ß subunits may be targets for the future development of novel therapeutics.
[Mh] Termos MeSH primário: Ativação do Canal Iônico
Sódio/metabolismo
Subunidades beta do Canal de Sódio Disparado por Voltagem/metabolismo
[Mh] Termos MeSH secundário: Animais
Seres Humanos
Potenciais da Membrana
Canais de Potássio de Abertura Dependente da Tensão da Membrana/metabolismo
Conformação Proteica
Relação Estrutura-Atividade
Subunidades beta do Canal de Sódio Disparado por Voltagem/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Potassium Channels, Voltage-Gated); 0 (Voltage-Gated Sodium Channel beta Subunits); 9NEZ333N27 (Sodium)
[Em] Mês de entrada:1407
[Cu] Atualização por classe:161025
[Lr] Data última revisão:
161025
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140417
[St] Status:MEDLINE
[do] DOI:10.1007/978-3-642-41588-3_4


  5 / 8 MEDLINE  
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[PMID]:24529773
[Au] Autor:Liu C; Tester DJ; Hou Y; Wang W; Lv G; Ackerman MJ; Makielski JC; Cheng J
[Ad] Endereço:Guangzhou Institute of Forensic Science, Guangzhou 510030, China.
[Ti] Título:Is sudden unexplained nocturnal death syndrome in Southern China a cardiac sodium channel dysfunction disorder?
[So] Source:Forensic Sci Int;236:38-45, 2014 Mar.
[Is] ISSN:1872-6283
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:Sudden unexplained nocturnal death syndrome (SUNDS) remains an enigma to both forensic pathologists and physicians. Previous epidemiological, clinical, and pilot genetic studies have implicated that SUNDS is most likely a disease allelic to Brugada syndrome (BrS). We have performed postmortem genetic testing to address the spectrum and role of genetic abnormalities in the SCN5A-encoded cardiac sodium channel and its several associated proteins in SUNDS victims from Southern China. Genomic DNA extracted from the blood samples of 123 medico-legal autopsy-negative SUNDS cases and 104 sex-, age- and ethnic-matched controls from Southern China underwent comprehensive amino acid coding region mutational analysis for the BrS associated genes SCN5A, SCN1B, SCN2B, SCN3B, SCN4B, MOG1, and GPD1-L using PCR and direct sequencing. We identified a total of 7 unique (4 novel) putative pathogenic mutations (all in SCN5A; V95I, R121Q [2 cases], R367H, R513H, D870H, V1764D, and S1937F) in 8/123 (6.5%) SUNDS cases. Three SCN5A mutations (V95I, R121Q, and R367H) have been previously implicated in BrS. An additional 8 cases hosted rare variants of uncertain clinical significance (SCN5A: V1098L, V1202M, R1512W; SCN1B: V138I [3 cases], T189M [2 cases]; SCN3B: A195T). There were no non-synonymous mutations found in SCN2B, SCN4B, MOG1, or GPD1-L. This first comprehensive genotyping for SCN5A and related genes in the Chinese Han population with SUNDS discovered 13 mutations, 4 of them novel, in 16 cases, which suggests cardiac sodium channel dysfunction might account for the pathogenesis of 7-13% of SUNDS in Southern China.
[Mh] Termos MeSH primário: Morte Súbita/etiologia
Canal de Sódio Disparado por Voltagem NAV1.5/genética
Sono
Subunidades beta do Canal de Sódio Disparado por Voltagem/genética
[Mh] Termos MeSH secundário: Adolescente
Adulto
Substituição de Aminoácidos
Estudos de Casos e Controles
China
Grupos Étnicos/genética
Éxons
Genética Forense
Frequência do Gene
Testes Genéticos
Genótipo
Glicerolfosfato Desidrogenase/genética
Seres Humanos
Íntrons
Masculino
Meia-Idade
Mutação
Polimorfismo de Nucleotídeo Único
Adulto Jovem
Proteína ran de Ligação ao GTP/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (NAV1.5 Voltage-Gated Sodium Channel); 0 (SCN5A protein, human); 0 (Voltage-Gated Sodium Channel beta Subunits); EC 1.1.- (GPD1-L protein, human); EC 1.1.- (Glycerolphosphate Dehydrogenase); EC 3.6.1.- (RANGNRF protein, human); EC 3.6.5.2 (ran GTP-Binding Protein)
[Em] Mês de entrada:1410
[Cu] Atualização por classe:140217
[Lr] Data última revisão:
140217
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140218
[St] Status:MEDLINE


  6 / 8 MEDLINE  
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[PMID]:23554500
[Au] Autor:Buffington SA; Rasband MN
[Ad] Endereço:Department of Neuroscience, Baylor College of Medicine, Houston, Texas 77030, USA.
[Ti] Título:Na+ channel-dependent recruitment of Navß4 to axon initial segments and nodes of Ranvier.
[So] Source:J Neurosci;33(14):6191-202, 2013 Apr 03.
[Is] ISSN:1529-2401
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The axon initial segment (AIS) and nodes of Ranvier are the sites of action potential initiation and regeneration in axons. Although the basic molecular architectures of AIS and nodes, characterized by dense clusters of Na(+) and K(+) channels, are similar, firing patterns vary among cell types. Neuronal firing patterns are established by the collective activity of voltage-gated ion channels and can be modulated through interaction with auxiliary subunits. Here, we report the neuronal expression pattern and subcellular localization of Navß4, the modulatory Na(+) channel subunit thought to underlie resurgent Na(+) current. Immunostaining of rat tissues revealed that Navß4 is strongly enriched at the AIS of a select set of neuron types, including many characterized by high-frequency firing, and at nodes of Ranvier in the PNS and some nodes in the CNS. By introducing full-length and mutant GFP-tagged Navß4 into cultured neurons, we determined that the AIS and nodal localization of Navß4 depends on its direct interaction with Na(+) channel α subunits through an extracellular disulfide bond. Based on these results, we propose that differences in the specific composition of the Na(+) channel complexes enriched at the AIS and nodes contribute to the diverse physiologies observed among cell types.
[Mh] Termos MeSH primário: Axônios/metabolismo
Encéfalo/citologia
Neurônios/citologia
Nós Neurofibrosos/metabolismo
Subunidade beta-4 do Canal de Sódio Disparado por Voltagem/metabolismo
[Mh] Termos MeSH secundário: Potenciais de Ação/genética
Animais
Anquirinas/metabolismo
Células COS
Células Cultivadas
Cercopithecus aethiops
Cisteína/metabolismo
Embrião de Mamíferos
Feminino
Gânglios Espinais/citologia
Regulação da Expressão Gênica/genética
Proteínas de Fluorescência Verde/genética
Masculino
Proteínas Associadas aos Microtúbulos/metabolismo
Mutação/genética
Proteína Básica da Mielina/metabolismo
Bainha de Mielina/metabolismo
Canal de Sódio Disparado por Voltagem NAV1.1
Proteínas do Tecido Nervoso/metabolismo
Imagem Óptica
Gravidez
RNA Interferente Pequeno/genética
Ratos
Ratos Sprague-Dawley
Transfecção
Subunidades beta do Canal de Sódio Disparado por Voltagem/genética
Subunidades beta do Canal de Sódio Disparado por Voltagem/metabolismo
Subunidade beta-4 do Canal de Sódio Disparado por Voltagem/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Ankyrins); 0 (Microtubule-Associated Proteins); 0 (Mtap2 protein, rat); 0 (Myelin Basic Protein); 0 (NAV1.1 Voltage-Gated Sodium Channel); 0 (Nerve Tissue Proteins); 0 (RNA, Small Interfering); 0 (Voltage-Gated Sodium Channel beta Subunits); 0 (Voltage-Gated Sodium Channel beta-4 Subunit); 147336-22-9 (Green Fluorescent Proteins); K848JZ4886 (Cysteine)
[Em] Mês de entrada:1305
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130405
[St] Status:MEDLINE
[do] DOI:10.1523/JNEUROSCI.4051-12.2013


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[PMID]:23146020
[Au] Autor:Zhang MM; Wilson MJ; Azam L; Gajewiak J; Rivier JE; Bulaj G; Olivera BM; Yoshikami D
[Ad] Endereço:Department of Biology, University of Utah, Salt Lake City, UT, USA.
[Ti] Título:Co-expression of Na(V)ß subunits alters the kinetics of inhibition of voltage-gated sodium channels by pore-blocking µ-conotoxins.
[So] Source:Br J Pharmacol;168(7):1597-610, 2013 Apr.
[Is] ISSN:1476-5381
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND AND PURPOSE: Voltage-gated sodium channels (VGSCs) are assembled from two classes of subunits, a pore-bearing α-subunit (NaV 1) and one or two accessory ß-subunits (NaV ßs). Neurons in mammals can express one or more of seven isoforms of NaV 1 and one or more of four isoforms of NaV ß. The peptide µ-conotoxins, like the guanidinium alkaloids tetrodotoxin (TTX) and saxitoxin (STX), inhibit VGSCs by blocking the pore in NaV 1. Hitherto, the effects of NaV ß-subunit co-expression on the activity of these toxins have not been comprehensively assessed. EXPERIMENTAL APPROACH: Four µ-conotoxins (µ-TIIIA, µ-PIIIA, µ-SmIIIA and µ-KIIIA), TTX and STX were tested against NaV 1.1, 1.2, 1.6 or 1.7, each co-expressed in Xenopus laevis oocytes with one of NaV ß1, ß2, ß3 or ß4 and, for NaV 1.7, binary combinations of thereof. KEY RESULTS: Co-expression of NaV ß-subunits modifies the block by µ-conotoxins: in general, NaV ß1 or ß3 co-expression tended to increase kon (in the most extreme instance by ninefold), whereas NaV ß2 or ß4 co-expression decreased kon (in the most extreme instance by 240-fold). In contrast, the block by TTX and STX was only minimally, if at all, affected by NaV ß-subunit co-expression. Tests of NaV ß1 : ß2 chimeras co-expressed with NaV 1.7 suggest that the extracellular portion of the NaV ß subunit is largely responsible for altering µ-conotoxin kinetics. CONCLUSIONS AND IMPLICATIONS: These results are the first indication that NaV ß subunit co-expression can markedly influence µ-conotoxin binding and, by extension, the outer vestibule of the pore of VGSCs. µ-Conotoxins could, in principle, be used to pharmacologically probe the NaV ß subunit composition of endogenously expressed VGSCs.
[Mh] Termos MeSH primário: Conotoxinas/farmacologia
Bloqueadores dos Canais de Sódio/farmacologia
Canais de Sódio Disparados por Voltagem/metabolismo
[Mh] Termos MeSH secundário: Animais
Feminino
Cinética
Oócitos/metabolismo
Isoformas de Proteínas/metabolismo
Ratos
Subunidades beta do Canal de Sódio Disparado por Voltagem/metabolismo
Xenopus laevis
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Conotoxins); 0 (Protein Isoforms); 0 (Sodium Channel Blockers); 0 (Voltage-Gated Sodium Channel beta Subunits); 0 (Voltage-Gated Sodium Channels)
[Em] Mês de entrada:1311
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:121114
[St] Status:MEDLINE
[do] DOI:10.1111/bph.12051


  8 / 8 MEDLINE  
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[PMID]:23413701
[Au] Autor:Srisawat R; Komalamisra N; Apiwathnasorn C; Paeporn P; Roytrakul S; Rongsriyam Y; Eshita Y
[Ad] Endereço:Department of Medical Entomology, Faculty of Tropical Medicine, Mahidol University, Bangkok, Thailand. raweewan.sri@mahidol.ac.th
[Ti] Título:Field-collected permethrin-resistant Aedes aegypti from central Thailand contain point mutations in the domain IIS6 of the sodium channel gene (KDR).
[So] Source:Southeast Asian J Trop Med Public Health;43(6):1380-6, 2012 Nov.
[Is] ISSN:0125-1562
[Cp] País de publicação:Thailand
[La] Idioma:eng
[Ab] Resumo:One of the mechanisms responsible for pyrethroid resistance in mosquitoes is mutations in domain IIS6 of voltage-gated sodium channel gene (kdr). Aedes aegypti larvae were collected from the central provinces of Thailand (Bangkok, Prachin Buri and Ratchaburi) and colonized until they became adults. Partial fragment of kdr of permethrin-resistant mosquitoes were amplified by RT-PCR and sequenced. Among the four nucleotide mutations detected, two mutations resulted in two amino acid substitutions, S(TCC) 989 P(CCC) and V(GTA)1016 G(GGA). Among 94 permethrin-resistant mosquitoes, the SS genotype (SS/VV) was found to predominate (n = 74), followed by SR (SP/VG) (n = 15) and RR (PP/ GG) genotypes (n = 5), with the resistant allele frequency ranging from 0.03 to 0.17. As pyrethroid insecticides are currently being advocated for use in Thailand, investigations of pyrethroid resistance in other regions of the country are needed to prevent potential cross-resistance among different types of insecticides.
[Mh] Termos MeSH primário: Aedes/genética
Resistência a Inseticidas/genética
Permetrina/farmacologia
Subunidades beta do Canal de Sódio Disparado por Voltagem/genética
[Mh] Termos MeSH secundário: Aedes/efeitos dos fármacos
Animais
Sequência de Bases
Resistência a Inseticidas/efeitos dos fármacos
Inseticidas/farmacologia
Larva/efeitos dos fármacos
Larva/genética
Mutação/efeitos dos fármacos
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Tailândia
Subunidades beta do Canal de Sódio Disparado por Voltagem/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Insecticides); 0 (Voltage-Gated Sodium Channel beta Subunits); 509F88P9SZ (Permethrin)
[Em] Mês de entrada:1303
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130219
[St] Status:MEDLINE



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