MOUSE SOD1 AND HUMAN/MOUSE SOD1 CHIMERAS

这个子项目是利用资源的许多研究子项目之一。 由NIH/NCRR资助的中心拨款提供。对子项目的主要支持 子项目的首席调查员可能是由其他来源提供的， 包括美国国立卫生研究院的其他来源。为子项目列出的总成本可能 表示该子项目使用的中心基础设施的估计数量， 不是由NCRR赠款提供给次级项目或次级项目工作人员的直接资金。 人类铜锌超氧化物歧化酶(SOD1)的突变与遗传性肌萎缩侧索硬化症(ALS)有关。表达这些人S蛋白的转基因小鼠的脊髓中含有人突变蛋白的包涵体，但内源性小鼠SOD1s不是这些聚集体的组成部分。人类酶中的两个序列元件已经被发现，它们似乎增强了相对于老鼠酶的聚集。这些序列元件正在作为包含老鼠和人类序列的SOD1嵌合体的一部分进行研究。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. Mutations in human copper-zinc superoxide dismutase (SOD1) are linked to an inherited form of amyotrophic lateral sclerosis (ALS). Spinal cords of transgenic mice expressing these human S proteins contain inclusions of the human mutant proteins, but endogenous mouse SOD1 is not f as a component of these aggregates. Two sequence elements in the human enzyme have bee identified that seem to enhance its aggregation relative to the mouse enzyme. These sequence elements are under study as part of SOD1 chimeras containing mouse and human sequences.