相关参考文献
注意：仅列出部分参考文献，下载原文获取全部文献信息。Putative Structures of Membrane-Embedded Amyloid β Oligomers
Aliasghar Sepehri et al.
ACS CHEMICAL NEUROSCIENCE (2023)
The amyloid concentric beta-barrel hypothesis: Models of amyloid beta 42 oligomers and annular protofibrils
Stewart R. Durell et al.
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS (2022)
Beta-amyloid pore linked to controlled calcium influx into the cell: A new paradigm for Alzheimer's Disease
Martina Pannuzzo
ALZHEIMERS & DEMENTIA (2022)
Exploring amyloid oligomers with peptide model systems
Tuan D. Samdin et al.
CURRENT OPINION IN CHEMICAL BIOLOGY (2021)
Molecular Dynamics Simulations Based on Polarizable Models Show that Ion Permeation Interconverts between Different Mechanisms as a Function of Membrane Thickness
Peiran Chen et al.
JOURNAL OF PHYSICAL CHEMISTRY B (2021)
Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer's Disease, Parkinson's Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis
Phuong H. Nguyen et al.
CHEMICAL REVIEWS (2021)
Cryo-electron Microscopy Imaging of Alzheimer's Amyloid-beta 42 Oligomer Displayed on a Functionally and Structurally Relevant Scaffold
Jinming Wu et al.
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION (2021)
Somatostatin, an In Vivo Binder to Aβ Oligomers, Binds to βPFPAβ(1-42) Tetramers
Eduard Puig et al.
ACS CHEMICAL NEUROSCIENCE (2020)
Internalisation and toxicity of amyloid-β 1-42 are influenced by its conformation and assembly state rather than size
Devkee M. Vadukul et al.
FEBS LETTERS (2020)
Aβ(1-42) tetramer and octamer structures reveal edge conductivity pores as a mechanism for membrane damage
Sonia Ciudad et al.
NATURE COMMUNICATIONS (2020)
Identification of neurotoxic cross-linked amyloid-β dimers in the Alzheimer's brain
Gunnar Brinkmalm et al.
BRAIN (2019)
Amyloid- oligomers have a profound detergent-like effect on lipid membrane bilayers, imaged by atomic force and electron microscopy
David C. Bode et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2019)
Tetrameric Aβ40 and Aβ42 β-Barrel Structures by Extensive Atomistic Simulations. I. In a Bilayer Mimicking a Neuronal Membrane
Phuong H. Nguyen et al.
JOURNAL OF PHYSICAL CHEMISTRY B (2019)
Native Ion Mobility-Mass Spectrometry Reveals the Formation of β-Barrel Shaped Amyloid-β Hexamers in a Membrane-Mimicking Environment
Nicklas Osterlund et al.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2019)
Different soluble aggregates of Aβ42 can give rise to cellular toxicity through different mechanisms
Suman De et al.
NATURE COMMUNICATIONS (2019)
Soluble aggregates present in cerebrospinal fluid change in size and mechanism of toxicity during Alzheimer's disease progression
Suman De et al.
ACTA NEUROPATHOLOGICA COMMUNICATIONS (2019)
Pathways of Amyloid-β Aggregation Depend on Oligomer Shape
Bogdan Barz et al.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2018)
Investigation of the interaction of amyloid beta peptide (11-42) oligomers with a 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) membrane using molecular dynamics simulation
Ning Xiang et al.
PHYSICAL CHEMISTRY CHEMICAL PHYSICS (2018)
beta-Strand twisting/bending in soluble and transmembrane beta-barrel structures
Nobuaki Kikuchi et al.
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS (2018)
Are N- and C-terminally truncated A species key pathological triggers in Alzheimer's disease?
Julie Dunys et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2018)
The diphenylpyrazole compound anle138b blocks A beta channels and rescues disease phenotypes in a mouse model for amyloid pathology
Ana Martinez Hernandez et al.
EMBO MOLECULAR MEDICINE (2018)
Alzheimer's Protective Cross-Interaction between Wild-Type and A2T Variants Alters Aβ42 Dimer Structure
Payel Das et al.
ACS CHEMICAL NEUROSCIENCE (2017)
Ion Channel Formation by Amyloid-β42 Oligomers but Not Amyloid-β40 in Cellular Membranes
David C. Bode et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2017)
CHARMM36m: an improved force field for folded and intrinsically disordered proteins
Jing Huang et al.
NATURE METHODS (2017)
Reduced Lipid Bilayer Thickness Regulates the Aggregation and Cytotoxicity of Amyloid- β
Kyle J. Korshavn et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2017)
A Hexamer of a Peptide Derived from Aβ16-36
Adam G. Kreutzer et al.
BIOCHEMISTRY (2017)
Resolving the Atomistic Modes of Anle138b Inhibitory Action on Peptide Oligomer Formation
Dirk Matthes et al.
ACS CHEMICAL NEUROSCIENCE (2017)
Amyloid beta: structure, biology and structure-based therapeutic development
Guo-fang Chen et al.
ACTA PHARMACOLOGICA SINICA (2017)
The Cellular Phase of Alzheimer's Disease
Bart De Strooper et al.
CELL (2016)
The amyloid hypothesis of Alzheimer's disease at 25years
Dennis J. Selkoe et al.
EMBO MOLECULAR MEDICINE (2016)
Simulations of Pore Formation in Lipid Membranes: Reaction Coordinates, Convergence, Hysteresis, and Finite-Size Effects
Neha Awasthi et al.
JOURNAL OF CHEMICAL THEORY AND COMPUTATION (2016)
Antimicrobial Peptide Simulations and the Influence of Force Field on the Free Energy for Pore Formation in Lipid Bilayers
W. F. Drew Bennett et al.
JOURNAL OF CHEMICAL THEORY AND COMPUTATION (2016)
Transmembrane Potential Modeling: Comparison between Methods of Constant Electric Field and Ion Imbalance
Josef Melcr et al.
JOURNAL OF CHEMICAL THEORY AND COMPUTATION (2016)
pKa Values of Titrable Amino Acids at the Water/Membrane Interface
Vitor H. Teixeira et al.
JOURNAL OF CHEMICAL THEORY AND COMPUTATION (2016)
Membrane-bound tetramer and trimer Aβ oligomeric species correlate with toxicity towards cultured neurons
Metta K. Jana et al.
JOURNAL OF NEUROCHEMISTRY (2016)
X-ray Crystallographic Structure of Oligomers Formed by a Toxic β-Hairpin Derived from α-Synuclein: Trimers and Higher-Order Oligomers
Patrick J. Salveson et al.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2016)
Amyloid β-Protein C-Terminal Fragments: Formation of Cylindrins and β-Barrels
Thanh D. Do et al.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2016)
Aβ42 assembles into specific β-barrel pore-forming oligomers in membrane-mimicking environments
Montserrat Serra-Batiste et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2016)
Common molecular mechanism of amyloid pore formation by Alzheimer's β-amyloid peptide and α-synuclein
Coralie Di Scala et al.
SCIENTIFIC REPORTS (2016)
An Early Folding Contact between Phe19 and Leu34 is Critical for Amyloid-β Oligomer Toxicity
Anand K. Das et al.
ACS CHEMICAL NEUROSCIENCE (2015)
Amyloid β oligomers in Alzheimer's disease pathogenesis, treatment, and diagnosis
Kirsten L. Viola et al.
ACTA NEUROPATHOLOGICA (2015)
Heterogeneity and Turnover of Intermediates during Amyloid-β (Aβ) Peptide Aggregation Studied by Fluorescence Correlation Spectroscopy
Ann Tiiman et al.
BIOCHEMISTRY (2015)
A Hexameric Peptide Barrel as Building Block of Amyloid-β Protofibrils
Christofer Lendel et al.
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION (2014)
Capping of Aβ42 Oligomers by Small Molecule Inhibitors
Ziao Fu et al.
BIOCHEMISTRY (2014)
The amyloid state and its association with protein misfolding diseases
Tuomas P. J. Knowles et al.
NATURE REVIEWS MOLECULAR CELL BIOLOGY (2014)
Local interactions influence the fibrillation kinetics, structure and dynamics of Aβ(1-40) but leave the general fibril structure unchanged
Juliane Adler et al.
PHYSICAL CHEMISTRY CHEMICAL PHYSICS (2014)
Aggregation of Alzheimer's Amyloid beta-Peptide in Biological Membranes: A Molecular Dynamics Study
Justin A. Lemkul et al.
BIOCHEMISTRY (2013)
GROMACS 4.5: a high-throughput and highly parallel open source molecular simulation toolkit
Sander Pronk et al.
BIOINFORMATICS (2013)
g_contacts: Fast contact search in bio-molecular ensemble data
Christian Blau et al.
COMPUTER PHYSICS COMMUNICATIONS (2013)
Another Piece of the Membrane Puzzle: Extending Slipids Further
Joakim P. M. Jambeck et al.
JOURNAL OF CHEMICAL THEORY AND COMPUTATION (2013)
Cytotoxicity of Intracellular Aβ42 Amyloid Oligomers Involves Ca2+ Release from the Endoplasmic Reticulum by Stimulated Production of Inositol Trisphosphate
Angelo Demuro et al.
JOURNAL OF NEUROSCIENCE (2013)
Novel APP/Aß mutation K16N produces highly toxic heteromeric Aß oligomers
Daniela Kaden et al.
EMBO MOLECULAR MEDICINE (2012)
Intra-membrane Oligomerization and Extra-membrane Oligomerization of Amyloid-β Peptide Are Competing Processes as a Result of Distinct Patterns of Motif Interplay
Yi-Jiong Zhang et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2012)
An Extension and Further Validation of an All-Atomistic Force Field for Biological Membranes
Joakim P. M. Jambeck et al.
JOURNAL OF CHEMICAL THEORY AND COMPUTATION (2012)
Optimization of the Additive CHARMM All-Atom Protein Force Field Targeting Improved Sampling of the Backbone φ, ψ and Side-Chain χ1 and χ2 Dihedral Angles
Robert B. Best et al.
JOURNAL OF CHEMICAL THEORY AND COMPUTATION (2012)
Derivation and Systematic Validation of a Refined All-Atom Force Field for Phosphatidylcholine Lipids
Joakim P. M. Jambeck et al.
JOURNAL OF PHYSICAL CHEMISTRY B (2012)
Small molecule inhibitors of amyloid β peptide aggregation as a potential therapeutic strategy for Alzheimer's disease
Qin Nie et al.
ACTA PHARMACOLOGICA SINICA (2011)
Lysine-Specific Molecular Tweezers Are Broad-Spectrum Inhibitors of Assembly and Toxicity of Amyloid Proteins
Sharmistha Sinha et al.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2011)
Amyloidogenic Protein Membrane Interactions: Mechanistic Insight from Model Systems
Sara M. Butterfield et al.
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION (2010)
Amyloid oligomers: formation and toxicity of A beta oligomers
Masafumi Sakono et al.
FEBS JOURNAL (2010)
NMR Studies of Zinc, Copper, and Iron Binding to Histidine, the Principal Metal Ion Complexing Site of Amyloid-beta Peptide
Nanditha G. Nair et al.
JOURNAL OF ALZHEIMERS DISEASE (2010)
Update of the CHARMM All-Atom Additive Force Field for Lipids: Validation on Six Lipid Types
Jeffery B. Klauda et al.
JOURNAL OF PHYSICAL CHEMISTRY B (2010)
Improved side-chain torsion potentials for the Amber ff99SB protein force field
Kresten Lindorff-Larsen et al.
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS (2010)
Amyloid β-Protein Toxicity and the Pathogenesis of Alzheimer Disease
Bruce A. Yankner et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2009)
Optimized Molecular Dynamics Force Fields Applied to the Helix-Coil Transition of Polypeptides
Robert B. Best et al.
JOURNAL OF PHYSICAL CHEMISTRY B (2009)
Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease
Summer L. Bernstein et al.
NATURE CHEMISTRY (2009)
Efficiency of Histidine-Associating Compounds for Blocking the Alzheimer's Aβ Channel Activity and Cytotoxicity
Nelson Arispe et al.
BIOPHYSICAL JOURNAL (2008)
Identifying the minimal copper- and zinc-binding site sequence in amyloid-β peptides
Velia Minicozzi et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2008)
P-LINCS: A parallel linear constraint solver for molecular simulation
Berk Hess
JOURNAL OF CHEMICAL THEORY AND COMPUTATION (2008)
Software news and updates - CHARNIM-GUI: A web-based grraphical user interface for CHARMM
Sunhwan Jo et al.
JOURNAL OF COMPUTATIONAL CHEMISTRY (2008)
Amyloid-β protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory
Ganesh M. Shankar et al.
NATURE MEDICINE (2008)
Stabilization of a β-hairpin in monomeric Alzheimer's amyloid-β peptide inhibits amyloid formation
Wolfgang Hoyer et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2008)
Small molecule inhibitors of aggregation indicate that amyloid β oligomerization and fibrillization pathways are independent and distinct
Mihaela Necula et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2007)
Models of beta-amyloid ion channels in the membrane suggest that channel formation in the bilayer is a dynamic process
Hyunbum Jang et al.
BIOPHYSICAL JOURNAL (2007)
Comparison of multiple amber force fields and development of improved protein backbone parameters
Viktor Hornak et al.
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS (2006)
Copper-mediated amyloid-β toxicity is associated with an intermolecular histidine bridge
David P. Smith et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2006)
Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?
Hilal A. Lashuel et al.
QUARTERLY REVIEWS OF BIOPHYSICS (2006)
Amyloid ion channels: A common structural link for protein-misfolding disease
A Quist et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2005)
Natural oligomers of the amyloid-protein specifically disrupt cognitive function
JP Cleary et al.
NATURE NEUROSCIENCE (2005)
Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
R Kayed et al.
SCIENCE (2003)
Medicine - The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
J Hardy et al.
SCIENCE (2002)
分享论文
