Entry ID |
Link Type |
Entity ID |
Title |
5057
|
Sequence mapping |
1 |
1H Chemical Shift Assignments for Alzheimer peptide Ab(1-40) |
5400
|
Sequence mapping |
1 |
Selection of D-amino-acid peptides that bind to Alzheimer's disease amyloid
peptide abeta 1-42 by mirror image phage display |
11435
|
Sequence mapping |
1 |
1H, 13C, and 15N Chemical Shift Assignments for amyloid-beta-(1-40) |
17159
|
Sequence mapping |
1 |
Backbone assignment of the affibody-bound amyloid B-peptide |
17186
|
Sequence mapping |
1 |
NMR Reveals Anomalous Copper(II) Binding to the Amyloid ABeta Peptide of Alzheimer's Disease |
17764
|
Sequence mapping |
1 |
A partially folded structure of amyloid-beta(1 40) in an aqueous environment |
17793
|
Sequence mapping |
1 |
Backbone chemical shift assignments for Ab42 with Met35 in its oxidized state |
17794
|
Sequence mapping |
1 |
Backbone chemical shift assignments for Ab42 with Met35 in its reduced state |
17795
|
Sequence mapping |
1 |
Backbone chemical shift assignments for A 40 with Met35 in its oxidised state |
17796
|
Sequence mapping |
1 |
Backbone chemical shift assignments for A 40 with Met35 in its reduced state |
18052
|
Sequence mapping |
1 |
Structural analysis of the pyroglutamate modified isoform of the Alzheimer's disease related beta-amyloid using NMR spectroscopy |
18127
|
Sequence mapping |
1 |
Structural Model for a 40-Residue Beta-Amyloid Fibril with Two-Fold Symmetry, Positive Stagger |
18128
|
Sequence mapping |
1 |
Structural Model for a 40-Residue Beta-Amyloid Fibril with Two-Fold Symmetry, Negative Stagger |
18129
|
Sequence mapping |
1 |
Structural Model for a 40-residue Beta-Amyloid Fibril with Three-Fold Symmetry, Positive Stagger |
18131
|
Sequence mapping |
1 |
Structural Model for a 40-residue Beta-Amyloid Fibril with Three-Fold Symmetry, Negative Stagger |
19309
|
Sequence mapping |
1 |
3D NMR structure of a complex between the amyloid beta peptide (1-40) and the polyphenol epsilon-viniferin glucoside |
19393
|
Sequence mapping |
1 |
Solid-state NMR sequential assignment of Osaka-Mutant Amyloid-beta (A 1-40 E22 ) fibrils |
25218
|
Sequence mapping |
1 |
Chemical shifts of amyloid beta (1-42) peptide in aqueous solution |
25289
|
Sequence mapping |
1 |
Atomic-resolution 3D structure of amyloid-beta fibrils: the Osaka mutation |
25429
|
Sequence mapping |
1 |
42-Residue Beta Amyloid Fibril |
26508
|
Sequence mapping |
1 |
Transient small molecule interactions kinetically modulate amyloid b peptide
self-assembly |
26516
|
Sequence mapping |
1 |
Transient small molecule interactions kinetically modulate amyloid b peptide
self-assembly |