Tapasin plays a crucial role in the assembly and stability of the major histocompatibility complex (MHC) class I molecules.
拓扑异构酶在主要组织相容性复合体(MHC)Ⅰ类分子的组装与稳定性中起到关键作用。
The interaction between
tapasin and calreticulin is essential for proper peptide loading onto MHC class I molecules.
拓扑异构酶与钙网蛋白的相互作用对于将肽正确装载到MHCⅠ类分子上是至关重要的。
Tapasin deficiency can lead to reduced cell surface expression of MHC class I molecules.
缺乏拓扑异构酶可能导致MHCⅠ类分子在细胞表面表达量的减少。
Researchers have identified a mutation in the
tapasin gene that may be linked to autoimmune diseases.
研究人员已经发现拓扑异构酶基因中的一个突变,这可能与自身免疫疾病有关联。
Tapasin acts as an adapter protein, bridging the connection between MHC class I molecules and the endoplasmic reticulum aminopeptidase 1 (ERAP1).
拓扑异构酶作为适配蛋白,架起MHCⅠ类分子与内质网氨肽酶1(ERAP1)之间的桥梁。
The efficiency of antigen presentation is improved by the presence of functional
tapasin in the antigen processing pathway.
在抗原加工途径中,功能性的拓扑异构酶的存在可以提高抗原呈递效率。
Tapasin-deficient mice exhibit impaired immune responses due to reduced MHC class I-mediated antigen presentation.
缺乏拓扑异构酶的小鼠由于MHCⅠ类分子介导的抗原呈递能力降低,表现出免疫反应受损。
Restoration of
tapasin levels can enhance the recognition of cancer cells by cytotoxic T lymphocytes.
恢复拓扑异构酶水平能够增强杀伤性T淋巴细胞对癌细胞的识别。
Studies have shown that
tapasin interacts with several other components of the peptide-loading complex, ensuring efficient loading of high-affinity peptides.
研究表明,拓扑异构酶与其他肽加载复合体的几个组分相互作用,确保高效装载高亲和力的肽段。
Inhibition of
tapasin function can impair the ability of the immune system to detect and respond to viral infections.
抑制拓扑异构酶的功能会损害免疫系统检测并应对病毒感染的能力。
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