The effect of β2-α2 loop mutation on amyloidogenic properties of the prion protein.
The effect of β2-α2 loop mutation on amyloidogenic properties of the prion protein.
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DOI：
10.1016/j.febslet.2013.07.023
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发表时间：
2013-09-17
期刊：
影响因子：
3.5
通讯作者：
Surewicz WK
中科院分区：
文献类型：
--
作者：
Dutta A;Chen S;Surewicz WK
Recent studies revealed that elk-like S170N/N174T mutation in mouse prion protein (moPrP), which results in an increased rigidity of β2-α2 loop, leads to a prion disease in transgenic mice. Here we characterized the effect of this mutation on biophysical properties of moPrP. Despite similar thermodynamic stabilities of wild type and mutant proteins, the latter was found to have markedly higher propensity to form amyloid fibrils. Importantly, this effect was observed even under fully denaturing conditions, indicating that the increased conversion propensity of the mutant protein is not due to loop rigidity but rather results from greater amyloidogenic potential of the amino acid sequence within the loop region of S170N/N174T moPrP.
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影响因子：
5.6
作者：
Pedersen, JS;Christensen, G;Otzen, DE
通讯作者：
Otzen, DE
DOI：
10.1073/pnas.0409008102
发表时间：
2005-01-18
影响因子：
11.1
作者：
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通讯作者：
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影响因子：
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Sigurdson, Christina J.
重组prion蛋白在野生型动物中诱导了一种新的可传染性prion病。
影响因子：
12.7
作者：
Makarava N;Kovacs GG;Bocharova O;Savtchenko R;Alexeeva I;Budka H;Rohwer RG;Baskakov IV
通讯作者：
Baskakov IV