β-barrel Oligomers as Common Intermediates of Peptides Self-Assembling into Cross-β Aggregates
Published 2018 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
β-barrel Oligomers as Common Intermediates of Peptides Self-Assembling into Cross-β Aggregates
Authors
Keywords
-
Journal
Scientific Reports
Volume 8, Issue 1, Pages -
Publisher
Springer Nature
Online
2018-07-03
DOI
10.1038/s41598-018-28649-7
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- Structures and dynamics of β-barrel oligomer intermediates of amyloid-beta16-22 aggregation
- (2018) Xinwei Ge et al. BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
- Fully Atomistic Aβ40 and Aβ42 Oligomers in Water: Observation of Porelike Conformations
- (2017) Matthew J. Voelker et al. Journal of Chemical Theory and Computation
- Fibril–Barrel Transitions in Cylindrin Amyloids
- (2017) Huiling Zhang et al. Journal of Chemical Theory and Computation
- Membrane Binding and Pore Formation by a Cytotoxic Fragment of Amyloid β Peptide
- (2017) Nabin Kandel et al. JOURNAL OF PHYSICAL CHEMISTRY B
- Distinct oligomerization and fibrillization dynamics of amyloid core sequences of amyloid-beta and islet amyloid polypeptide
- (2017) Yunxiang Sun et al. PHYSICAL CHEMISTRY CHEMICAL PHYSICS
- Atomic structures of fibrillar segments of hIAPP suggest tightly mated β-sheets are important for cytotoxicity
- (2017) Pascal Krotee et al. eLife
- Solving protein structures using short-distance cross-linking constraints as a guide for discrete molecular dynamics simulations
- (2017) Nicholas I. Brodie et al. Science Advances
- Critical Nucleus Structure and Aggregation Mechanism of the C-terminal Fragment of Copper–Zinc Superoxide Dismutase Protein
- (2016) Yu Zou et al. ACS Chemical Neuroscience
- The S20G substitution in hIAPP is more amyloidogenic and cytotoxic than wild-type hIAPP in mouse islets
- (2016) Daniel T. Meier et al. DIABETOLOGIA
- The amyloid hypothesis of Alzheimer's disease at 25 years
- (2016) Dennis J Selkoe et al. EMBO Molecular Medicine
- Amyloid β-Protein C-Terminal Fragments: Formation of Cylindrins and β-Barrels
- (2016) Thanh D. Do et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- Exploring the aggregation free energy landscape of the amyloid-β protein (1–40)
- (2016) Weihua Zheng et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Aβ42 assembles into specific β-barrel pore-forming oligomers in membrane-mimicking environments
- (2016) Montserrat Serra-Batiste et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- β-Hairpin of Islet Amyloid Polypeptide Bound to an Aggregation Inhibitor
- (2016) Ewa A. Mirecka et al. Scientific Reports
- Amphiphilic Peptides A6K and V6K Display Distinct Oligomeric Structures and Self-Assembly Dynamics: A Combined All-Atom and Coarse-Grained Simulation Study
- (2015) Yunxiang Sun et al. BIOMACROMOLECULES
- Amyloid β Protein and Alzheimer’s Disease: When Computer Simulations Complement Experimental Studies
- (2015) Jessica Nasica-Labouze et al. CHEMICAL REVIEWS
- Allostery without a conformational change? Revisiting the paradigm
- (2015) Ruth Nussinov et al. CURRENT OPINION IN STRUCTURAL BIOLOGY
- Structure of the toxic core of α-synuclein from invisible crystals
- (2015) Jose A. Rodriguez et al. NATURE
- Aβ(1–42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease
- (2015) Yiling Xiao et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Aβ(1–42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease
- (2015) Yiling Xiao et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- The OPEP protein model: from single molecules, amyloid formation, crowding and hydrodynamics to DNA/RNA systems
- (2014) Fabio Sterpone et al. CHEMICAL SOCIETY REVIEWS
- Aβ(16–22) Peptides Can Assemble into Ordered β-Barrels and Bilayer β-Sheets, while Substitution of Phenylalanine 19 by Tryptophan Increases the Population of Disordered Aggregates
- (2013) Luogang Xie et al. JOURNAL OF PHYSICAL CHEMISTRY B
- Structure and Dynamics of Small Soluble Aβ(1–40) Oligomers Studied by Top-Down Hydrogen Exchange Mass Spectrometry
- (2012) Jingxi Pan et al. BIOCHEMISTRY
- Atomic Force Microscopy and MD Simulations Reveal Pore-Like Structures of All-d-Enantiomer of Alzheimer’s β-Amyloid Peptide: Relevance to the Ion Channel Mechanism of AD Pathology
- (2012) Laura Connelly et al. JOURNAL OF PHYSICAL CHEMISTRY B
- α-Synuclein Oligomers: an Amyloid Pore?
- (2012) Martin T. Stöckl et al. MOLECULAR NEUROBIOLOGY
- Atomic View of a Toxic Amyloid Small Oligomer
- (2012) Arthur Laganowsky et al. SCIENCE
- Solid-State NMR Studies of Amyloid Fibril Structure
- (2011) Robert Tycko Annual Review of Physical Chemistry
- Fibril Structure of Human Islet Amyloid Polypeptide
- (2011) Sahar Bedrood et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Structural Basis for Aβ1–42 Toxicity Inhibition by Aβ C-Terminal Fragments: Discrete Molecular Dynamics Study
- (2011) B. Urbanc et al. JOURNAL OF MOLECULAR BIOLOGY
- Sensitivity of Amyloid Formation by Human Islet Amyloid Polypeptide to Mutations at Residue 20
- (2011) Ping Cao et al. JOURNAL OF MOLECULAR BIOLOGY
- Soluble Aβ oligomer production and toxicity
- (2011) Megan E. Larson et al. JOURNAL OF NEUROCHEMISTRY
- Discrete molecular dynamics
- (2011) Elizabeth A. Proctor et al. Wiley Interdisciplinary Reviews-Computational Molecular Science
- Low molecular weight oligomers of amyloid peptides display β-barrel conformations: A replica exchange molecular dynamics study in explicit solvent
- (2010) Alfonso De Simone et al. JOURNAL OF CHEMICAL PHYSICS
- β-Barrel Topology of Alzheimer's β-Amyloid Ion Channels
- (2010) Hyunbum Jang et al. JOURNAL OF MOLECULAR BIOLOGY
- Automated minimization of steric clashes in protein structures
- (2010) Srinivas Ramachandran et al. PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
- Diversity of kinetic pathways in amyloid fibril formation
- (2009) Giovanni Bellesia et al. JOURNAL OF CHEMICAL PHYSICS
- Models of Toxic β-Sheet Channels of Protegrin-1 Suggest a Common Subunit Organization Motif Shared with Toxic Alzheimer β-Amyloid Ion Channels
- (2008) Hyunbum Jang et al. BIOPHYSICAL JOURNAL
- Self-Assembly of the β2-Microglobulin NHVTLSQ Peptide Using a Coarse-Grained Protein Model Reveals a β-Barrel Species
- (2008) Wei Song et al. JOURNAL OF PHYSICAL CHEMISTRY B
- Transgenics, toxicity and therapeutics in rodent models of mutant SOD1-mediated familial ALS
- (2008) B TURNER et al. PROGRESS IN NEUROBIOLOGY
- Atomic structure of the cross-β spine of islet amyloid polypeptide (amylin)
- (2008) Jed J.W. Wiltzius et al. PROTEIN SCIENCE
- Ab Initio Folding of Proteins with All-Atom Discrete Molecular Dynamics
- (2008) Feng Ding et al. STRUCTURE
- New structures help the modeling of toxic amyloidß ion channels
- (2008) Hyunbum Jang et al. TRENDS IN BIOCHEMICAL SCIENCES
- Spontaneous β-barrel formation: An all-atom Monte Carlo study of Aβ16–22 oligomerization
- (2007) Anders Irbäck et al. PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
Publish scientific posters with Peeref
Peeref publishes scientific posters from all research disciplines. Our Diamond Open Access policy means free access to content and no publication fees for authors.
Learn MoreAdd your recorded webinar
Do you already have a recorded webinar? Grow your audience and get more views by easily listing your recording on Peeref.
Upload Now