Mutants and molecular dockings reveal that the primary L-thyroxine binding site in human serum albumin is not the one which can cause familial dysalbuminemic hyperthyroxinemia

Kragh-Hansen Ulrich; Minchiotti Lorenzo; Coletta Andrea; Bienk Konrad; Galliano Monica; Schiott Birgit; Iwao Yasunori; Ishima Yu; Otagiri Masaki

首页> 外文期刊>Biochimica et Biophysica Acta. General Subjects >Mutants and molecular dockings reveal that the primary L-thyroxine binding site in human serum albumin is not the one which can cause familial dysalbuminemic hyperthyroxinemia

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Mutants and molecular dockings reveal that the primary L-thyroxine binding site in human serum albumin is not the one which can cause familial dysalbuminemic hyperthyroxinemia

机译：突变和分子对接揭示了人血清白蛋白中主要的L-甲状腺素结合位点不是可能导致家族性水合蛋白过高甲状腺素血症的位点

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Background: Natural mutations of R218 in human serum albumin (HSA) result in an increased affinity for L-thyroxine and lead to the autosomal dominant condition of familial dysalbuminemic hyperthyroxinemia.

机译：背景：人类血清白蛋白（HSA）中R218的自然突变导致对L-甲状腺素的亲和力增加，并导致家族性dysalbuminemic高甲状腺素血症的常染色体显性疾病。

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《Biochimica et Biophysica Acta. General Subjects》 |2016年第4期|共13页
作者
Kragh-Hansen Ulrich; Minchiotti Lorenzo; Coletta Andrea; Bienk Konrad; Galliano Monica; Schiott Birgit; Iwao Yasunori; Ishima Yu; Otagiri Masaki;
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正文语种 eng
中图分类生物化学;
关键词
Human serum albumin; L-thyroxine; High-affinity binding site; Genetic variants; Site-directed mutagenesis; Computer modeling;

机译：人血清白蛋白;L-甲状腺素;高亲和力结合位点;遗传变异;定点诱变;计算机建模;

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1. Mutants and molecular dockings reveal that the primary L-thyroxine binding site in human serum albumin is not the one which can cause familial dysalbuminemic hyperthyroxinemia [J] . Kragh-Hansen Ulrich, Minchiotti Lorenzo, Coletta Andrea, Biochimica et Biophysica Acta. General Subjects . 2016,第4期

机译：突变和分子对接揭示了人血清白蛋白中主要的L-甲状腺素结合位点不是可能导致家族性水合蛋白过高甲状腺素血症的位点
2. Spectroscopic and molecular docking studies reveal binding characteristics of nazartinib (EGF816) to human serum albumin [J] . Abdulrahman A. Almehizia, Haitham AlRabiah, Ahmed H. Bakheit, Royal Society Open Science . 2020,第1期

机译：光谱和分子对接研究揭示了Nazartinib（EGF816）对人血清白蛋白的结合特征
3. Investigating the site selective binding of busulfan to human serum albumin: Biophysical and molecular docking approaches (vol 107, pg 1414, 2018) [J] . Siddiqi Mohammad, Nusrat Saima, Alam Parvez, International Journal of Biological Macromolecules: Structure, Function and Interactions . 2020,第1期

机译：调查Busulfan对人血清白蛋白的遗址选择性结合：生物物理和分子对接方法（Vol 107，PG 1414,2018）
4. Molecular Docking Studies of 14 Drugs and Toxins in the Binding Site 1 of Human Serum Albumin with Fatty Acids [C] . Jianxiong Diao, Ye Sun, Fei Ding, Proceedings of 4th international symposium on pesticides and environmental safety amp; 5th pan Pacific confernce on pesticide science amp; 8th international workshop on crop protection chemistry and regulatory harmonization . 2012

机译：人血清白蛋白与脂肪酸结合位点1中14种药物和毒素的分子对接研究
5. Studies of human serum albumin -ligand interactions using site -directed mutants and recombinant fragments of the protein [D] . Yang, Jinsheng 2004

机译：使用定点突变体和蛋白质重组片段研究人血清白蛋白-配体的相互作用
6. Novel antimycobacterial C-21 amide derivatives of the antibiotic fusidic acid: synthesis pharmacological evaluation and rationalization of media-dependent activity using molecular docking studies in the binding site of human serum albumin [O] . Godwin Akpeko Dziwornu, Stephanie Kamunya, Tando Ntsabo, 2019

机译：夫西地酸的新型抗分枝杆菌C-21酰胺衍生物：在人血清白蛋白结合位点的分子对接研究的合成药理学评估和介质依赖性活性的合理化
7. Mutations in a Specific Human Serum Albumin Thyroxine Binding Site Define the Structural Basis of Familial Dysalbuminemic Hyperthyroxinemia [O] . Charles E. Petersen, Chung-Eun Ha, David M. Jameson, 1996

机译：特异性人血清白蛋白甲状腺素结合位点的突变定义了家族脱氨型甲亢的结构基础

Mutants and molecular dockings reveal that the primary L-thyroxine binding site in human serum albumin is not the one which can cause familial dysalbuminemic hyperthyroxinemia

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