A serine-->proline change in the Alzheimer's disease-associated epitope Tau 2 results in altered secondary structure, but phosphorylation overcomes the conformational gap.
A serine-->proline change in the Alzheimer's disease-associated epitope Tau 2 results in altered secondary structure, but phosphorylation overcomes the conformational gap.
复制标题
阿尔茨海默病相关表位 Tau 2 中的丝氨酸→脯氨酸变化导致二级结构改变,但磷酸化克服了构象间隙。
DOI:
10.1016/0006-291x(92)92364-4
复制
发表时间:
1992
影响因子:
3.1
通讯作者:
OtvosJr,L
中科院分区:
文献类型:
--
作者:
Lang,E;OtvosJr,L
Monoclonal antibody Tau 2 was raised against bovine ti protein, was reported to to recognize a conformational epitope, and stainedτ was found in neurofibrillary tangles of Alzheimer's disease, but not normal human τ. We synthesized tetradeka peptides corresponding to the original bovine sequence, its serine → proline substituted analog, the genuine human sequence of this region, and the bovine epitope phosphorylated on the crucial serene. The secondary structure of the peptides was determined by circular dichroism. It was found that only the original bovine epitope showed a tendency to form the (β-pleated sheets characteristic of the neurofibrillary tangles. The spectra of the human peptide, its analog, β and the phosphorylated bovine sequence were very similar, featuring a weak, helical β-turn character. Eventual phosphorylation of epitopes of this otherwise heavily phosphorylated protein may overcome inter-species conformational gaps.
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DOI:
10.1016/0021-9673(92)85457-5
发表时间:
1992
期刊:
Journal of chromatography
影响因子:
--
作者:
OtvosJr,L;Urge,L;Thurin,J
通讯作者:
Thurin,J
DOI:
10.3109/10409238009105470
发表时间:
1980
期刊:
--
影响因子:
--
作者:
John A. Smith;L. G. Pease;K. Kopple
通讯作者:
John A. Smith;L. G. Pease;K. Kopple
DOI:
10.1016/s0021-9258(18)48531-6
发表时间:
1992-01
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
S. G. Greenberg;P. Davies;J D Schein;L I Binder
通讯作者:
S. G. Greenberg;P. Davies;J D Schein;L I Binder
影响因子:
3.5
作者:
Y. Ihara;J. Kondo;R. Miura;Y. Nakagawa;H. Mori;T. Honda
通讯作者:
T. Honda
影响因子:
3.2
作者:
R. Terry
通讯作者:
R. Terry