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Highly transparent ZnO thin films were deposited at different substrate temperatures by pulsed laser deposition in an oxygen atmosphere.The thin films were characterized by various techniques including X-ray diffraction,scanning electron microscopy,optical absorption,and photoluminescence.We demonstrated that oriented wurtzite ZnO thin films could be deposited at room temperature using a high purity zinc target.Variable temperature photoluminescence revealed new characteristics in the band edge emission.The... 相似文献
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从理论上分析了利用时间有限差分法由近场到近场或远场转换的频域和时域两种方法,并选择时域的方法计算在FDTD计算范围内一给定点的电场值,与直接利用FDTD法得到的结果相比较,两者非常一致;最后利用该方法计算了功率变换器FDTD计算范围外一给定点的电磁场时间响应. 相似文献
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Mutant small heat-shock protein 27 causes axonal Charcot-Marie-Tooth disease and distal hereditary motor neuropathy 总被引:25,自引:0,他引:25
Evgrafov OV Mersiyanova I Irobi J Van Den Bosch L Dierick I Leung CL Schagina O Verpoorten N Van Impe K Fedotov V Dadali E Auer-Grumbach M Windpassinger C Wagner K Mitrovic Z Hilton-Jones D Talbot K Martin JJ Vasserman N Tverskaya S Polyakov A Liem RK Gettemans J Robberecht W De Jonghe P Timmerman V 《Nature genetics》2004,36(6):602-606
Charcot-Marie-Tooth disease (CMT) is the most common inherited neuromuscular disease and is characterized by considerable clinical and genetic heterogeneity. We previously reported a Russian family with autosomal dominant axonal CMT and assigned the locus underlying the disease (CMT2F; OMIM 606595) to chromosome 7q11-q21 (ref. 2). Here we report a missense mutation in the gene encoding 27-kDa small heat-shock protein B1 (HSPB1, also called HSP27) that segregates in the family with CMT2F. Screening for mutations in HSPB1 in 301 individuals with CMT and 115 individuals with distal hereditary motor neuropathies (distal HMNs) confirmed the previously observed mutation and identified four additional missense mutations. We observed the additional HSPB1 mutations in four families with distal HMN and in one individual with CMT neuropathy. Four mutations are located in the Hsp20-alpha-crystallin domain, and one mutation is in the C-terminal part of the HSP27 protein. Neuronal cells transfected with mutated HSPB1 were less viable than cells expressing the wild-type protein. Cotransfection of neurofilament light chain (NEFL) and mutant HSPB1 resulted in altered neurofilament assembly in cells devoid of cytoplasmic intermediate filaments. 相似文献
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