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Frontispiece: A Binuclear Zinc Interaction Fold Discovered in the Homodimer of Alzheimer's Amyloid‐β Fragment with Taiwanese Mutation D7H
Author(s) -
Polshakov Vladimir I.,
Mantsyzov Alexey B.,
Kozin Sergey A.,
Adzhubei Alexei A.,
Zhokhov Sergey S.,
van Beek Wouter,
Kulikova Alexandra A.,
Indeykina Maria I.,
Mitkevich Vladimir A.,
Makarov Alexander A.
Publication year - 2017
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201783961
Subject(s) - dimer , chemistry , peptide fragment , zinc , mutation , amyloid (mycology) , peptide , prion protein , amyloid precursor protein , β amyloid , biophysics , alzheimer's disease , stereochemistry , biochemistry , biology , gene , medicine , organic chemistry , inorganic chemistry , disease , pathology
Alzheimer′s Disease The interaction of zinc ions with amyloid‐ β peptide fragments carrying the familial Taiwanese mutation D7H was studied by A. A. Makarov et al. In their Communication on page 11734 ff., a binuclear zinc interaction fold in the dimer structure is revealed.