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Inducing and assaying heat-shock response in Saccharomyces cerevisiae.

作者信息

Nicolet C M, Craig E A

出版信息

Methods Enzymol. 1991;194:710-7. doi: 10.1016/0076-6879(91)94052-e.

DOI:10.1016/0076-6879(91)94052-e
PMID:2005818
Abstract
摘要

相似文献

1
Inducing and assaying heat-shock response in Saccharomyces cerevisiae.
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Response of Saccharomyces cerevisiae to the stimulation of lipopolysaccharide.酿酒酵母对脂多糖刺激的反应。
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Small glutamine-rich protein/viral protein U-binding protein is a novel cochaperone that affects heat shock protein 70 activity.富含谷氨酰胺的小蛋白/病毒蛋白U结合蛋白是一种影响热休克蛋白70活性的新型辅助伴侣蛋白。
Cell Stress Chaperones. 2002 Jul;7(3):258-68. doi: 10.1379/1466-1268(2002)007<0258:sgrpvp>2.0.co;2.
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Multiple mechanisms of suppression circumvent transcription defects in an RNA polymerase mutant.
多种抑制机制规避了RNA聚合酶突变体中的转录缺陷。
Mol Cell Biol. 2000 Nov;20(21):8124-33. doi: 10.1128/MCB.20.21.8124-8133.2000.
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17-beta-estradiol upregulates the stress response in Candida albicans: implications for microbial virulence.17-β-雌二醇上调白色念珠菌的应激反应：对微生物毒力的影响
Infect Dis Obstet Gynecol. 1998;6(4):176-81. doi: 10.1002/(SICI)1098-0997(1998)6:4<176::AID-IDOG7>3.0.CO;2-V.
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Accelerated mRNA decay in conditional mutants of yeast mRNA capping enzyme.酵母mRNA加帽酶条件突变体中mRNA的加速衰变
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CDC39, an essential nuclear protein that negatively regulates transcription and differentially affects the constitutive and inducible HIS3 promoters.CDC39，一种重要的核蛋白，它对转录起负调控作用，并对组成型和诱导型HIS3启动子产生不同影响。
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HSP78 encodes a yeast mitochondrial heat shock protein in the Clp family of ATP-dependent proteases.HSP78编码一种酵母线粒体热休克蛋白，属于ATP依赖性蛋白酶的Clp家族。
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MSI3, a multicopy suppressor of mutants hyperactivated in the RAS-cAMP pathway, encodes a novel HSP70 protein of Saccharomyces cerevisiae.MSI3是RAS - cAMP途径中过度激活的突变体的多拷贝抑制因子，它编码酿酒酵母的一种新型HSP70蛋白。
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Regulated degradation of HMG-CoA reductase, an integral membrane protein of the endoplasmic reticulum, in yeast.酵母中内质网整合膜蛋白HMG-CoA还原酶的调控降解
J Cell Biol. 1994 Apr;125(2):299-312. doi: 10.1083/jcb.125.2.299.
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General requirement for RNA polymerase II holoenzymes in vivo.体内RNA聚合酶II全酶的一般要求。
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