Related references
Note: Only part of the references are listed.NMR Solution Structure of Rat Aβ(1-16): Toward Understanding the Mechanism of Rats' Resistance to Alzheimer's Disease
Andrey N. Istrate et al.
BIOPHYSICAL JOURNAL (2012)
The Japanese Mutant Aβ (ΔE22-Aβ1-39) Forms Fibrils Instantaneously, with Low-Thioflavin T Fluorescence: Seeding of Wild-Type Aβ1-40 into Atypical Fibrils by ΔE22-Aβ1-39
Adam L. Cloe et al.
BIOCHEMISTRY (2011)
Novel Aβ Isoforms in Alzheimer's Disease - Their Role in Diagnosis and Treatment
Erik Portelius et al.
CURRENT PHARMACEUTICAL DESIGN (2011)
Neoteric pharmacotherapeutic targets in fibromyalgia
Kanwaljit Chopra et al.
EXPERT OPINION ON THERAPEUTIC TARGETS (2011)
Zinc-induced dimerization of the amyloid-beta metal-binding domain 1-16 is mediated by residues 11-14
Sergey A. Kozin et al.
MOLECULAR BIOSYSTEMS (2011)
A standardized and biocompatible preparation of aggregate-free amyloid beta peptide for biophysical and biological studies of Alzheimers disease
Kerensa Broersen et al.
PROTEIN ENGINEERING DESIGN & SELECTION (2011)
Minimal Zn2+ Binding Site of Amyloid-β
Philipp O. Tsvetkov et al.
BIOPHYSICAL JOURNAL (2010)
Iron-Export Ferroxidase Activity of β-Amyloid Precursor Protein Is Inhibited by Zinc in Alzheimer's Disease
James A. Duce et al.
CELL (2010)
Identification of novel N-terminal fragments of amyloid precursor protein in cerebrospinal fluid
Erik Portelius et al.
EXPERIMENTAL NEUROLOGY (2010)
Tetravalent Aβ1-15 vaccine reduces TCR-positive cell infiltration and up-regulates p75 in Tg2576 brains compared to Aβ42 vaccine
Hui Li et al.
JOURNAL OF NEUROIMMUNOLOGY (2010)
Reaction Rates and Mechanism of the Ascorbic Acid Oxidation by Molecular Oxygen Facilitated by Cu(II)-Containing Amyloid-β Complexes and Aggregates
Dianlu Jiang et al.
JOURNAL OF PHYSICAL CHEMISTRY B (2010)
Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: Detection of amyloid aggregation in solution
Harry Levine
PROTEIN SCIENCE (2010)
The culprit behind amyloid beta peptide related neurotoxicity in Alzheimer's disease: oligomer size or conformation?
Kerensa Broersen et al.
ALZHEIMERS RESEARCH & THERAPY (2010)
In vitro amyloid Aβ1-42 peptide aggregation monitoring by asymmetrical flow field-flow fractionation with multi-angle light scattering detection
Diana C. Rambaldi et al.
ANALYTICAL AND BIOANALYTICAL CHEMISTRY (2009)
Alzheimer's Disease: From Pathology to Therapeutic Approaches
Roland Jakob-Roetne et al.
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION (2009)
Pulse EPR Spectroscopy Reveals the Coordination Sphere of Copper(II) Ions in the 1-16 Amyloid-beta Peptide: A Key Role of the First Two N-Terminus Residues
Pierre Dorlet et al.
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION (2009)
Monitoring Alzheimer Amyloid Peptide Aggregation by EPR
I. Sepkhanova et al.
APPLIED MAGNETIC RESONANCE (2009)
Disease-Modifying Approach to the Treatment of Alzheimer's Disease From alpha-Secretase Activators to gamma-Secretase Inhibitors and Modulators
Francesco Panza et al.
DRUGS & AGING (2009)
β-Amyloid Monomers Are Neuroprotective
Maria Laura Giuffrida et al.
JOURNAL OF NEUROSCIENCE (2009)
Aggregation of Transmembrane Peptides Studied by Spin-Label EPR
Francesco Scarpelli et al.
JOURNAL OF PHYSICAL CHEMISTRY B (2009)
Direct evidence that all three histidine residues coordinate to Cu(II) in amyloid-β1-16
Byong-kyu Shin et al.
BIOCHEMISTRY (2008)
Isomerization of the Asp7 residue results in zinc-induced oligomerization of Alzheimer's disease amyloid β(1-16) peptide
Philipp O. Tsvetkov et al.
CHEMBIOCHEM (2008)
Different hydration changes accompanying copper and zinc binding to amyloid β-peptide:: Water contribution to metal binding
Haijia Yu et al.
CHEMBIOCHEM (2008)
Fibrils with parallel in-register structure constitute a major class of amyloid fibrils: molecular insights from electron paramagnetic resonance spectroscopy
Martin Margittai et al.
QUARTERLY REVIEWS OF BIOPHYSICS (2008)
The correlation between neurotoxicity, aggregative ability and secondary structure studied by sequence truncated Aβ peptides
M. Q. Liao et al.
FEBS LETTERS (2007)
An Alzheimer's disease-specific β-amyloid fragment signature in cerebrospinal fluid
Erik Portelius et al.
NEUROSCIENCE LETTERS (2006)
Characterization of copper binding to the peptide amyloid-β(1-16) associated with Alzheimer's disease
Qing-Feng Ma et al.
BIOPOLYMERS (2006)
Structural changes of region 1-16 of the Alzheimer disease amyloid β-peptide upon zinc binding and in vitro aging
S Zirah et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2006)
EasySpin, a comprehensive software package for spectral simulation and analysis in EPR
S Stoll et al.
JOURNAL OF MAGNETIC RESONANCE (2006)
Amyloid-beta causes apoptosis of neuronal cells via caspase cascade, which can be prevented by amyloid-beta-derived short peptides
A Awasthi et al.
EXPERIMENTAL NEUROLOGY (2005)
Distances between the b-subunits in the tether domain of F0F1-ATP synthase from E. coli
S Steigmiller et al.
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS (2005)
Copper binding to the amyloid-β (Aβ) peptide associated with Alzheimer's disease -: Folding, coordination geometry, pH dependence, stoichiometry, and affinity of Aβ-(1-28):: Insights from a range of complementary spectroscopic techniques
CD Syme et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2004)
Pain: Moving from symptom control toward mechanism-specific pharmacologic management
CJ Woolf
ANNALS OF INTERNAL MEDICINE (2004)
Amyloidosis of Alzheimer's Aβ peptides:: solid-state nuclear magnetic resonance, electron paramagnetic resonance, transmission electron microscopy, scanning transmission electron microscopy and atomic force microscopy studies
ON Antzutkin
MAGNETIC RESONANCE IN CHEMISTRY (2004)
Residues 17-20 and 30-35 of beta-amyloid play critical roles in aggregation
RT Liu et al.
JOURNAL OF NEUROSCIENCE RESEARCH (2004)
Eight-residue Aβ peptides inhibit the aggregation and enzymatic activity of Aβ42
Y Matsunaga et al.
REGULATORY PEPTIDES (2004)
Trace metal contamination initiates the apparent auto-aggregation, amyloidosis, and oligomerization of Alzheimer's Aβ peptides
XD Huang et al.
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY (2004)
Products of Cu(II)-catalyzed oxidation in the presence of hydrogen peroxide of the 1-10, 1-16 fragments of human and mouse β-amyloid peptide
T Kowalik-Jankowska et al.
JOURNAL OF INORGANIC BIOCHEMISTRY (2004)
Unique physicochemical profile of α-amyloid peptide variant Aβ1-40E22G protofibrils:: Conceivable neuropathogen in arctic mutant carriers
A Päiviö et al.
JOURNAL OF MOLECULAR BIOLOGY (2004)
Coordination abilities of the 1-16 and 1-28 fragments of β-amyloid peptide towards copper(II) ions:: a combined potentiometric and spectroscopic study
T Kowalik-Jankowska et al.
JOURNAL OF INORGANIC BIOCHEMISTRY (2003)
The C-terminal domain of apolipoprotein A-I contains a lipid-sensitive conformational trigger
MN Oda et al.
NATURE STRUCTURAL BIOLOGY (2003)
Aβ1-15 is less immunogenic than Aβ1-40/42 for intranasal immunization of wild-type mice but may be effective for boosting
JF Leverone et al.
VACCINE (2003)
Alzheimer's disease amyloid-β binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits
CC Curtain et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2001)
Characterization of copper interactions with Alzheimer amyloid β peptides:: Identification of an attomolar-affinity copper binding site on amyloid β1-42
CS Atwood et al.
JOURNAL OF NEUROCHEMISTRY (2000)
Inhibiting the conversion of soluble amyloid-beta peptide into abnormally folded amyloidogenic intermediates: relevance for Alzheimer's disease therapy
C Soto et al.
ACTA NEUROLOGICA SCANDINAVICA (2000)