Nitrosative stress-induced s-glutathionylation of protein disulfide isomerase leads to activation of the unfolded protein response.
第一作者:
Danyelle M,Townsend
第一单位:
Departments of Pharmaceutical and Biomedical Sciences and Cell and Molecular Pharmacology and Experimental Therapeutics, Medical University of South Carolina, Charleston, SC 29425, USA.
作者:
主题词
4-氨基苯甲酸(4-Aminobenzoic Acid);氨基酸序列(Amino Acid Sequence);偶氮化合物(Azo Compounds);催化域(Catalytic Domain);细胞系, 肿瘤(Cell Line, Tumor);半胱氨酸(Cysteine);女(雌)性(Female);谷胱甘肽(Glutathione);HL-60细胞(HL-60 Cells);人类(Humans);模型, 分子(Models, Molecular);分子序列数据(Molecular Sequence Data);肿瘤(Neoplasms);一氧化氮(Nitric Oxide);卵巢肿瘤(Ovarian Neoplasms);蛋白质二硫化物异构酶类(Protein Disulfide-Isomerases);蛋白质折叠(Protein Folding);蛋白质组学(Proteomics);构效关系(Structure-Activity Relationship)
DOI
10.1158/0008-5472.CAN-09-0493
PMID
19773442
发布时间
2022-03-11
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Cancer research
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