Amyloid -Protein Assembly and Alzheimer Disease
R. Roychaudhuri
Journal of Biological Chemistry, 2009
View PDFchevron_right
Amyloid β-Protein Assembly and Alzheimer Disease
Robin Roychaudhuri
Journal of Biological Chemistry, 2008
View PDFchevron_right
Aβ(1–40) Forms Five Distinct Amyloid Structures whose β-Sheet Contents and Fibril Stabilities Are Correlated
Saketh Chemuru
Journal of Molecular Biology, 2010
View PDFchevron_right
The N-terminal region of non-Abeta component of Alzheimer's Disease amyloid is responsible for its tendency to assume beta-sheet and aggregate to form fibrils
Omar El-agnaf
European Journal of Biochemistry, 1998
View PDFchevron_right
1H NMR of A.beta. Amyloid Peptide Congeners in Water Solution. Conformational Changes Correlate with Plaque Competence
yian lu
Biochemistry, 1995
View PDFchevron_right
The Role of Protein Sequence and Amino Acid Composition in Amyloid Formation: Scrambling and Backward Reading of IAPP Amyloid Fibrils
Raimon Sabate
Journal of Molecular Biology, 2010
View PDFchevron_right
The influence of the central region containing residues 19-25 on the aggregation properties and secondary structure of Alzheimer's beta-amyloid peptide
Omar El-agnaf, Dominic Walsh
European Journal of Biochemistry, 1998
View PDFchevron_right
Sequence determinants of amyloid fibril formation
Manuela Lopez de la Paz
Proceedings of the National Academy of Sciences, 2004
View PDFchevron_right
Discrete conformational changes as regulators of the hydrolytic properties of beta-amyloid (1-40)
Danek Elbaum
FEBS Journal, 2006
View PDFchevron_right
In vitro formation of amyloid fibrils from two synthetic peptides of different lengths homologous to alzheimer's disease β-protein
Frances Prelli
Biochemical and Biophysical Research Communications, 1986
View PDFchevron_right
Mechanism of amyloid plaque formation suggests an intracellular basis of A pathogenicity
Christoph Kaether, Ralf P Friedrich
Proceedings of the National Academy of Sciences, 2010
View PDFchevron_right
Effect of the Interaction of the Amyloid β (1–42) Peptide with Short Single-Stranded Synthetic Nucleotide Sequences: Morphological Characterization of the Inhibition of Fibrils Formation and Fibrils Disassembly
Charlotte Gourmel, Plinio Maroni
Biomacromolecules, 2014
View PDFchevron_right
The N‐terminal region of non‐Aβ component of Alzheimer's Disease amyloid is responsible for its tendency to assume β‐sheet and aggregate to form fibrils
Omar El-agnaf
European Journal …, 1998
View PDFchevron_right
A Partially Folded Structure of Amyloid-Beta (1-40) in an Aqueous Environment
Shirley Lee
Biochemical and …, 2011
View PDFchevron_right
Structural analysis of amyloid ? peptide fragment (25-35) in different microenvironments
Jayakumar Rajadas
Biopolymers, 2004
View PDFchevron_right
Amyloid-like properties of a synthetic peptide corresponding to the carboxy terminus of β-amyloid protein precursor
Daniel Kirschner
Archives of Biochemistry and Biophysics, 1992
View PDFchevron_right
Synthetic peptide homologous to beta protein from Alzheimer disease forms amyloid-like fibrils in vitro
Daniel Kirschner
Proceedings of the National Academy of Sciences, 1987
View PDFchevron_right
Impact of sequence on the molecular assembly of short amyloid peptides
Mookyung Cheon
Proteins, 2014
View PDFchevron_right
The Monomer State of Beta-Amyloid: Where the Alzheimer's Disease Protein Meets Physiology
Agata Copani
Reviews in the Neurosciences, 2010
View PDFchevron_right
beta-Amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: implications for the pathology of Alzheimer disease
Alex E Roher
Proceedings of the National Academy of Sciences, 1993
View PDFchevron_right
ANS Binding Reveals Common Features of Cytotoxic Amyloid Species
Justin Yerbury
ACS Chemical Biology, 2010
View PDFchevron_right
Structural, kinetic and cytotoxicity aspects of 1228 β‐amyloid protein fragment: a reappraisal
Montse Cruz
Journal of Peptide …, 2002
View PDFchevron_right
Insight into the Structure of Amyloid Fibrils from the Analysis of Globular Proteins
Flavio Seno
PLoS Computational Biology, 2005
View PDFchevron_right
Structural Basis for Vital Function and Malfunction of Serum Amyloid A: an Acute-Phase Protein that Wears Hydrophobicity on Its Sleeve
Olga Gursky
Current Atherosclerosis Reports
View PDFchevron_right
Review: structure of amyloid fibril in diseases
Arezou Ghahghaei
Journal of Biomedical Science and Engineering, 2009
View PDFchevron_right
Discrete conformational changes as regulators of the hydrolytic properties of beta-amyloid (1-40): Abeta(1-40) conformation and hydrolytic properties
Tomasz Gers
Febs Journal, 2006
View PDFchevron_right
The nature and origin of amyloid fibrils
Jamie Goode
1996
View PDFchevron_right
Amino Acid Position-specific Contributions to Amyloid -Protein Oligomerization
Mohammed Inayathullah
Journal of Biological Chemistry, 2009
View PDFchevron_right
Oligomeric and fibrillar species of amyloid-β peptides differentially affect neuronal viability
Grant Krafft
Journal of Biological …, 2002
View PDFchevron_right
Amorphous Aggregation of Amyloid Beta 1-40 Peptide in Confined Space
Silvia Milita
ChemPhysChem, 2015
View PDFchevron_right
De novo designed peptide-based amyloid fibrils
Manuela Lopez de la Paz
Proceedings of the National Academy of Sciences of the United States of America, 2002
View PDFchevron_right