Angewandte Chemie - International Edition
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Том 56
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Издание 39
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Номера страниц: 11734-11739
A Binuclear Zinc Interaction Fold Discovered in the Homodimer of Alzheimer's Amyloid-β Fragment with Taiwanese Mutation D7H
Polshakov V.I., Mantsyzov A.B., Kozin S.A., Adzhubei A.A., Zhokhov S.S., van Beek W., Kulikova A.A., Indeykina M.I., Mitkevich V.A., Makarov A.A.
Тип документа: Journal Article
Дата публикации: 2017-09-18
Название журнала: Angewandte Chemie - International Edition
Издатель: Wiley-Blackwell
Квартиль по SCImago: Q1
Квартиль по Web of Science: Q1
Импакт-фактор 2021: 16.82
ISSN: 14337851, 15213773
General Chemistry
Catalysis
Краткое описание
Zinc-induced oligomerization of amyloid-β peptide (Aβ) produces potentially pathogenic agents of Alzheimer's disease. Mutations and modifications in the metal binding domain 1-16 of Aβ peptide crucially affect its zinc-induced oligomerization by changing intermolecular zinc mediated interface. The 3D structure of this interface appearing in a range of Aβ species is a prospective drug target for disease modifying therapy. Using NMR spectroscopy, EXAFS spectroscopy, mass spectrometry, and isothermal titration calorimetry the interaction of zinc ions with Aβ fragments 1-7 and 1-10 carrying familial Taiwanese mutation D7H was studied. Zinc ions induce formation of a stable homodimer formed by the two peptide chains fastened by two zinc ions and stacking interactions of imidazole rings. A binuclear zinc interaction fold in the dimer structure was discovered. It can be used for designing zinc-regulated proteins and zinc-mediated self-assembling peptides.
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1. Polshakov V.I. и др. A Binuclear Zinc Interaction Fold Discovered in the Homodimer of Alzheimer’s Amyloid-β Fragment with Taiwanese Mutation D7H // Angewandte Chemie International Edition. 2017. Т. 56. № 39. С. 11734–11739.
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TY - JOUR
DO - 10.1002/anie.201704615
UR - http://dx.doi.org/10.1002/anie.201704615
TI - A Binuclear Zinc Interaction Fold Discovered in the Homodimer of Alzheimer's Amyloid-β Fragment with Taiwanese Mutation D7H
T2 - Angewandte Chemie International Edition
AU - Polshakov, Vladimir I.
AU - Mantsyzov, Alexey B.
AU - Kozin, Sergey A.
AU - Adzhubei, Alexei A.
AU - Zhokhov, Sergey S.
AU - van Beek, Wouter
AU - Kulikova, Alexandra A.
AU - Indeykina, Maria I.
AU - Mitkevich, Vladimir A.
AU - Makarov, Alexander A.
PY - 2017
DA - 2017/06/27
PB - Wiley
SP - 11734-11739
IS - 39
VL - 56
SN - 1433-7851
ER -
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@article{2017,
doi = {10.1002/anie.201704615},
url = {https://doi.org/10.1002%2Fanie.201704615},
year = 2017,
month = {jun},
publisher = {Wiley},
volume = {56},
number = {39},
pages = {11734--11739},
author = {Vladimir I. Polshakov and Alexey B. Mantsyzov and Sergey A. Kozin and Alexei A. Adzhubei and Sergey S. Zhokhov and Wouter van{\hspace{0.25em}}Beek and Alexandra A. Kulikova and Maria I. Indeykina and Vladimir A. Mitkevich and Alexander A. Makarov},
title = {A Binuclear Zinc Interaction Fold Discovered in the Homodimer of Alzheimer{\textquotesingle}s Amyloid-$\upbeta$ Fragment with Taiwanese Mutation D7H}
}
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Polshakov, Vladimir I. et al. “A Binuclear Zinc Interaction Fold Discovered in the Homodimer of Alzheimer’s Amyloid-β Fragment with Taiwanese Mutation D7H.” Angewandte Chemie International Edition 56.39 (2017): 11734–11739. Crossref. Web.