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An asymmetric dimer as the basic subunit in Alzheimer's disease amyloid β fibrils.
Angew. Chem.-Int. Edit. 51, 6136-6139 (2012)
Two-faced culprit: Fibrils of recombinantly produced amyloid β peptides (Aβs; residues 1–40) gave well-resolved solid-state NMR spectra. Two sets of resonances corresponding to residues 12–40 and 21–38 of the Aβ primary sequence were observed (see picture). Statistical analysis of electron microscopy data revealed that it was composed of a single Aβ polymorph, thus indicating that this Aβ fibril is composed of an asymmetric dimer.
Impact Factor
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Times Cited
Times Cited
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13.455
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Anmerkungen
Besondere Publikation
Auf Hompepage verbergern
Publikationstyp
Artikel: Journalartikel
Dokumenttyp
Wissenschaftlicher Artikel
Schlagwörter
Alzheimer's Disease; Amyloid Ss Peptides; Fibrillar Aggregates; Nmr Spectroscopy; Structural Biology; SOLID-STATE NMR; ANGLE-SPINNING NMR; EXPERIMENTAL CONSTRAINTS; STRUCTURAL MODEL; SPECTROSCOPY; POLYMORPHISM; PEPTIDE; PROTEIN; IDENTIFICATION; A-BETA(1-40)
Sprache
Veröffentlichungsjahr
2012
HGF-Berichtsjahr
2012
ISSN (print) / ISBN
1433-7851
e-ISSN
1521-3773
Zeitschrift
Angewandte Chemie - Internationale Edition
Quellenangaben
Band: 51,
Heft: 25,
Seiten: 6136-6139
Verlag
Wiley
Verlagsort
Weinheim
Begutachtungsstatus
Peer reviewed
Institut(e)
Institute of Structural Biology (STB)
POF Topic(s)
30203 - Molecular Targets and Therapies
Forschungsfeld(er)
Enabling and Novel Technologies
PSP-Element(e)
G-503090-001
PubMed ID
22565601
WOS ID
WOS:000305180400016
Scopus ID
84862689606
Erfassungsdatum
2012-07-05