Associated Papers
Factors Driving Amyloid Beta Fibril Recognition by Cell Surface Receptors: A Computational Study.
Slater O et al.
Molecules (basel, Switzerland), 2025
Cryo-EM studies of amyloid-β fibrils from human and murine brains carrying the Uppsala APP mutation (Δ690-695).
Zielinski M et al.
Acta Neuropathologica Communications, 2025
Computational Study of Amyloidβ42 Familial Mutations and Metal Interaction: Impact on Monomers and Aggregates Dynamical Behaviors.
Roldán-Martín L et al.
Inorganic Chemistry, 2024
APP substrate ectodomain defines amyloid-β peptide length by restraining γ-secretase processivity and facilitating product release.
Koch M et al.
The Embo Journal, 2023
Clinical considerations in early-onset cerebral amyloid angiopathy.
Banerjee G et al.
Brain : a Journal of Neurology, 2023
Intermediate Antiparallel Fibrils in Aβ40 Dutch Mutant Aggregation: Insights from Nanoscale Infrared Spectroscopy.
Banerjee S et al.
The Journal of Physical Chemistry. B, 2023
Differential effects of familial Alzheimer's disease-causing mutations on amyloid precursor protein (APP) trafficking, proteolytic conversion, and synaptogenic activity.
Schilling S et al.
Acta Neuropathologica Communications, 2023
Intermediate antiparallel fibrils in Aβ40 Dutch mutant aggregation: nanoscale insights from AFM-IR.
Banerjee S et al.
Biorxiv : the Preprint Server for Biology, 2023
Familial Alzheimer's Disease-Related Mutations Differentially Alter Stability of Amyloid-Beta Aggregates.
Rezaei-Ghaleh N et al.
The Journal of Physical Chemistry Letters, 2023
Effects of Familial Alzheimer's Disease Mutations on the Folding Free Energy and Dipole-Dipole Interactions of the Amyloid β-Peptide.
Davidson DS et al.
The Journal of Physical Chemistry. B, 2022
Impact of A2T and D23N mutations on C99 homodimer conformations.
Lu Y et al.
The Journal of Chemical Physics, 2022
Insights in the structural understanding of amyloidogenicity and mutation-led conformational dynamics of amyloid beta (Aβ) through molecular dynamics simulations and principal component analysis.
Raghavan SS et al.
Journal of Biomolecular Structure & Dynamics, 2022
Amyloid-β40 E22K fibril in familial Alzheimer's disease is more thermostable and susceptible to seeding.
Lee MC et al.
Iubmb Life, 2022
Cross-seeding of WT amyloid-β with Arctic but not Italian familial mutants accelerates fibril formation in Alzheimer's disease.
Liang R et al.
The Journal of Biological Chemistry, 2022
Insights into Cerebral Amyloid Angiopathy Type 1 and Type 2 from Comparisons of the Fibrillar Assembly and Stability of the Aβ40-Iowa and Aβ40-Dutch Peptides.
Rajpoot J et al.
Biochemistry, 2022
Examining the Ensembles of Amyloid-β Monomer Variants and Their Propensities to Form Fibers Using an Energy Landscape Visualization Method.
Sanches MN et al.
The Journal of Physical Chemistry. B, 2022
The role of the half-turn in determining structures of Alzheimer's Aβ wild-type and mutants.
Hayward S et al.
Journal of Structural Biology, 2021
Human cerebral vascular amyloid contains both antiparallel and parallel in-register Aβ40 fibrils.
Irizarry BA et al.
The Journal of Biological Chemistry, 2021
Pulsed Hydrogen-Deuterium Exchange Reveals Altered Structures and Mechanisms in the Aggregation of Familial Alzheimer's Disease Mutants.
Illes-Toth E et al.
Acs Chemical Neuroscience, 2021
Anti-Parallel β-Hairpin Structure in Soluble Aβ Oligomers of Aβ40-Dutch and Aβ40-Iowa.
Fu Z et al.
International Journal of Molecular Sciences, 2021
Hydration Thermodynamics of the N-Terminal FAD Mutants of Amyloid-β.
Aggarwal L et al.
Journal of Chemical Information and Modeling, 2021
The F19W mutation reduces the binding affinity of the transmembrane Aβ11-40 trimer to the membrane bilayer.
Tran TT et al.
Rsc Advances, 2021
Fibril structures of diabetes-related amylin variants reveal a basis for surface-templated assembly.
Gallardo R et al.
Nature Structural & Molecular Biology, 2020
Aß40 displays amyloidogenic properties in the non-transgenic mouse brain but does not exacerbate Aß42 toxicity in Drosophila.
De Mena L et al.
Alzheimer's Research & Therapy, 2020
Cerebral amyloid angiopathy-linked β-amyloid mutations promote cerebral fibrin deposits via increased binding affinity for fibrinogen.
Cajamarca SA et al.
Proceedings of the National Academy of Sciences of the United States of America, 2020
Conformational Characterization of Native and L17A/F19A-Substituted Dutch-Type β-Amyloid Peptides.
He KC et al.
International Journal of Molecular Sciences, 2020
Oligomerization and Conformational Change Turn Monomeric β-Amyloid and Tau Proteins Toxic: Their Role in Alzheimer's Pathogenesis.
Penke B et al.
Molecules (basel, Switzerland), 2020
Longitudinal Cognitive Decline in a Novel Rodent Model of Cerebral Amyloid Angiopathy Type-1.
Popescu DL et al.
International Journal of Molecular Sciences, 2020
Impact of A2T and D23N Mutations on Tetrameric Aβ42 Barrel within a Dipalmitoylphosphatidylcholine Lipid Bilayer Membrane by Replica Exchange Molecular Dynamics.
Ngo ST et al.
The Journal of Physical Chemistry. B, 2020
Reduced Levels of Cerebrospinal Fluid/Plasma Aβ40 as an Early Biomarker for Cerebral Amyloid Angiopathy in RTg-DI Rats.
Zhu X et al.
International Journal of Molecular Sciences, 2020
An automated clinical mass spectrometric method for identification and quantification of variant and wild-type amyloid-β 1-40 and 1-42 peptides in CSF.
DeMarco ML et al.
Alzheimer's & Dementia (amsterdam, Netherlands), 2020
Effect of Post-Translational Modifications and Mutations on Amyloid-β Fibrils Dynamics at N Terminus.
Vugmeyster L et al.
Biophysical Journal, 2019
Generation of induced pluripotent stem cells (iPSCs) IRMBi002-A from an Alzheimer's disease patient carrying a D694N mutation in the APP gene.
Auboyer L et al.
Stem Cell Research, 2019
Influence of the familial Alzheimer's disease-associated T43I mutation on the transmembrane structure and γ-secretase processing of the C99 peptide.
Tang TC et al.
The Journal of Biological Chemistry, 2019
Atomistic investigation of an Iowa Amyloid-β trimer in aqueous solution.
Ngo ST et al.
Rsc Advances, 2018
A Novel Transgenic Rat Model of Robust Cerebral Microvascular Amyloid with Prominent Vasculopathy.
Davis J et al.
The American Journal of Pathology, 2018
Structure of APP-C991-99 and implications for role of extra-membrane domains in function and oligomerization.
Pantelopulos GA et al.
Biochimica Et Biophysica Acta. Biomembranes, 2018
On the role of sidechain size and charge in the aggregation of Aβ42 with familial mutations.
Yang X et al.
Proceedings of the National Academy of Sciences of the United States of America, 2018
High pressure NMR reveals conformational perturbations by disease-causing mutations in amyloid β-peptide.
Rosenman DJ et al.
Chemical Communications (cambridge, England), 2018
Conversion between parallel and antiparallel β-sheets in wild-type and Iowa mutant Aβ40 fibrils.
Xi W et al.
The Journal of Chemical Physics, 2018
Insights into the Molecular Mechanisms of Alzheimer's and Parkinson's Diseases with Molecular Simulations: Understanding the Roles of Artificial and Pathological Missense Mutations in Intrinsically Disordered Proteins Related to Pathology.
Coskuner-Weber O et al.
International Journal of Molecular Sciences, 2018
Effect of Alzheimer Familial Chromosomal Mutations on the Amyloid Fibril Interaction with Different PET Tracers: Insight from Molecular Modeling Studies.
Balamurugan K et al.
Acs Chemical Neuroscience, 2017
β-Sheet Structure within the Extracellular Domain of C99 Regulates Amyloidogenic Processing.
Hu Y et al.
Scientific Reports, 2017
Emergence of Alternative Structures in Amyloid Beta 1-42 Monomeric Landscape by N-terminal Hexapeptide Amyloid Inhibitors.
Chakraborty S et al.
Scientific Reports, 2017
APP Mutations in Cerebral Amyloid Angiopathy with or without Cortical Calcifications: Report of Three Families and a Literature Review.
Sellal F et al.
Journal of Alzheimer's Disease : Jad, 2017
Alzheimer's amyloid-β A2T variant and its N-terminal peptides inhibit amyloid-β fibrillization and rescue the induced cytotoxicity.
Lin TW et al.
Plos One, 2017
Cerebral vascular amyloid seeds drive amyloid β-protein fibril assembly with a distinct anti-parallel structure.
Xu F et al.
Nature Communications, 2016
Mutation-based structural modification and dynamics study of amyloid beta peptide (1-42): An in-silico-based analysis to cognize the mechanism of aggregation.
Panda PK et al.
Genomics Data, 2016