Search Menu
DOE PAGES title logo U.S. Department of Energy
Office of Scientific and Technical Information
Search Scholarly Publications

Title: Spontaneous self-assembly of amyloid β (1–40) into dimers

Abstract

The self-assembly and fibrillation of amyloid β (Aβ) proteins is the neuropathological hallmark of Alzheimer's disease. However, the molecular mechanism of how disordered monomers assemble into aggregates remains largely unknown. In this work, we characterize the assembly of Aβ (1–40) monomers into dimers using long-time molecular dynamics simulations. Upon interaction, the monomers undergo conformational transitions, accompanied by change of the structure, leading to the formation of a stable dimer. The dimers are stabilized by interactions in the N-terminal region (residues 5–12), in the central hydrophobic region (residues 16–23), and in the C-terminal region (residues 30–40); with inter-peptide interactions focused around the N- and C-termini. The dimers do not contain long β-strands that are usually found in fibrils.

Authors:
ORCiD logo [1];  [2];  [3]; ORCiD logo [1]
+ Show Author Affiliations
  1. Univ. of Nebraska Medical Center, Omaha, NE (United States)
  2. Univ. of Nebraska Medical Center, Omaha, NE (United States); Lawrence Livermore National Lab. (LLNL), Livermore, CA (United States)
  3. Univ. of Nebraska Medical Center, Omaha, NE (United States); Bruker Nano Surfaces Division, Santa Barbara, CA (United States)
Publication Date:
Research Org.:
Lawrence Livermore National Laboratory (LLNL), Livermore, CA (United States)
Sponsoring Org.:
USDOE National Nuclear Security Administration (NNSA); National Institutes of Health (NIH); National Science Foundation (NSF)
OSTI Identifier:
1661023
Report Number(s):
LLNL-JRNL-813715
Journal ID: ISSN 2516-0230; 1021710
Grant/Contract Number:  
AC52-07NA27344; GM096039; GM100156; 1004094; ACI-1053575; R01GM116961
Resource Type:
Accepted Manuscript
Journal Name:
Nanoscale Advances
Additional Journal Information:
Journal Volume: 1; Journal Issue: 10; Journal ID: ISSN 2516-0230
Publisher:
Royal Society of Chemistry
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; biological and medical sciences

Citation Formats

Hashemi, Mohtadin, Zhang, Yuliang, Lv, Zhengjian, and Lyubchenko, Yuri L. Spontaneous self-assembly of amyloid β (1–40) into dimers. United States: N. p., 2019. Web. doi:10.1039/c9na00380k.
Copy to clipboard
Hashemi, Mohtadin, Zhang, Yuliang, Lv, Zhengjian, & Lyubchenko, Yuri L. Spontaneous self-assembly of amyloid β (1–40) into dimers. United States. https://doi.org/10.1039/c9na00380k
Copy to clipboard
Hashemi, Mohtadin, Zhang, Yuliang, Lv, Zhengjian, and Lyubchenko, Yuri L. Tue . "Spontaneous self-assembly of amyloid β (1–40) into dimers". United States. https://doi.org/10.1039/c9na00380k. https://www.osti.gov/servlets/purl/1661023.
Copy to clipboard
@article{osti_1661023,
title = {Spontaneous self-assembly of amyloid β (1–40) into dimers},
author = {Hashemi, Mohtadin and Zhang, Yuliang and Lv, Zhengjian and Lyubchenko, Yuri L.},
abstractNote = {The self-assembly and fibrillation of amyloid β (Aβ) proteins is the neuropathological hallmark of Alzheimer's disease. However, the molecular mechanism of how disordered monomers assemble into aggregates remains largely unknown. In this work, we characterize the assembly of Aβ (1–40) monomers into dimers using long-time molecular dynamics simulations. Upon interaction, the monomers undergo conformational transitions, accompanied by change of the structure, leading to the formation of a stable dimer. The dimers are stabilized by interactions in the N-terminal region (residues 5–12), in the central hydrophobic region (residues 16–23), and in the C-terminal region (residues 30–40); with inter-peptide interactions focused around the N- and C-termini. The dimers do not contain long β-strands that are usually found in fibrils.},
doi = {10.1039/c9na00380k},
journal = {Nanoscale Advances},
number = 10,
volume = 1,
place = {United States},
year = {Tue Sep 17 00:00:00 EDT 2019},
month = {Tue Sep 17 00:00:00 EDT 2019}
}
Copy to clipboard
Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record
https://doi.org/10.1039/c9na00380k
Copyright Statement
Other availability
Search WorldCat Search WorldCat to find libraries that may hold this journal
Save / Share:
Export Metadata
Save to My Library
You must Sign In or Create an Account in order to save documents to your library.

Works referenced in this record:

Single-Molecule Atomic Force Microscopy Force Spectroscopy Study of Aβ-40 Interactions
journal, June 2011

  • Kim, Bo-Hyun; Palermo, Nicholas Y.; Lovas, Sándor
  • Biochemistry, Vol. 50, Issue 23
  • DOI: 10.1021/bi200147a

Structural properties of amyloid β(1-40) dimer explored by replica exchange molecular dynamics simulations: Amyloid β Dimers
journal, March 2017

  • Watts, Charles R.; Gregory, Andrew J.; Frisbie, Cole P.
  • Proteins: Structure, Function, and Bioinformatics, Vol. 85, Issue 6
  • DOI: 10.1002/prot.25270

Function and toxicity of amyloid beta and recent therapeutic interventions targeting amyloid beta in Alzheimer's disease
journal, January 2015

  • Rajasekhar, K.; Chakrabarti, Malabika; Govindaraju, T.
  • Chemical Communications, Vol. 51, Issue 70
  • DOI: 10.1039/C5CC05264E

On the nucleation of amyloid β-protein monomer folding
journal, June 2005

  • Lazo, Noel D.; Grant, Marianne A.; Condron, Margaret C.
  • Protein Science, Vol. 14, Issue 6
  • DOI: 10.1110/ps.041292205

Protein misfolding occurs by slow diffusion across multiple barriers in a rough energy landscape
journal, June 2015

  • Yu, Hao; Dee, Derek R.; Liu, Xia
  • Proceedings of the National Academy of Sciences, Vol. 112, Issue 27
  • DOI: 10.1073/pnas.1419197112

Routine Access to Millisecond Time Scale Events with Accelerated Molecular Dynamics
journal, August 2012

  • Pierce, Levi C. T.; Salomon-Ferrer, Romelia; Augusto F. de Oliveira, Cesar
  • Journal of Chemical Theory and Computation, Vol. 8, Issue 9
  • DOI: 10.1021/ct300284c

Aβ42 assembles into specific β-barrel pore-forming oligomers in membrane-mimicking environments
journal, September 2016

  • Serra-Batiste, Montserrat; Ninot-Pedrosa, Martí; Bayoumi, Mariam
  • Proceedings of the National Academy of Sciences, Vol. 113, Issue 39
  • DOI: 10.1073/pnas.1605104113

Single-Molecule Studies of Intrinsically Disordered Proteins
journal, January 2014

  • Brucale, Marco; Schuler, Benjamin; Samorì, Bruno
  • Chemical Reviews, Vol. 114, Issue 6
  • DOI: 10.1021/cr400297g

Structural Characterization and Inhibition of Toxic Amyloid-β Oligomeric Intermediates
journal, July 2013

Elucidation of Amyloid β-Protein Oligomerization Mechanisms: Discrete Molecular Dynamics Study
journal, March 2010

  • Urbanc, B.; Betnel, M.; Cruz, L.
  • Journal of the American Chemical Society, Vol. 132, Issue 12
  • DOI: 10.1021/ja9096303

Common mechanisms of amyloid oligomer pathogenesis in degenerative disease
journal, April 2006

Intracellular amyloid-β in Alzheimer's disease
journal, July 2007

  • LaFerla, Frank M.; Green, Kim N.; Oddo, Salvatore
  • Nature Reviews Neuroscience, Vol. 8, Issue 7
  • DOI: 10.1038/nrn2168

Nanoprobing of misfolding and interactions of amyloid β 42 protein
journal, May 2014

  • Kim, Bo-Hyun; Lyubchenko, Yuri L.
  • Nanomedicine: Nanotechnology, Biology and Medicine, Vol. 10, Issue 4
  • DOI: 10.1016/j.nano.2013.11.016

Atomic-Level Characterization of the Structural Dynamics of Proteins
journal, October 2010

GROMACS 4:  Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation
journal, February 2008

  • Hess, Berk; Kutzner, Carsten; van der Spoel, David
  • Journal of Chemical Theory and Computation, Vol. 4, Issue 3
  • DOI: 10.1021/ct700301q

Structural conversion of neurotoxic amyloid-β1–42 oligomers to fibrils
journal, April 2010

  • Ahmed, Mahiuddin; Davis, Judianne; Aucoin, Darryl
  • Nature Structural & Molecular Biology, Vol. 17, Issue 5
  • DOI: 10.1038/nsmb.1799

Mechanism of amyloid β−protein dimerization determined using single−molecule AFM force spectroscopy
journal, October 2013

  • Lv, Zhengjian; Roychaudhuri, Robin; Condron, Margaret M.
  • Scientific Reports, Vol. 3, Issue 1
  • DOI: 10.1038/srep02880

The Alzheimer’s Peptides Aβ40 and 42 Adopt Distinct Conformations in Water: A Combined MD / NMR Study
journal, May 2007

  • Sgourakis, Nikolaos G.; Yan, Yilin; McCallum, Scott A.
  • Journal of Molecular Biology, Vol. 368, Issue 5
  • DOI: 10.1016/j.jmb.2007.02.093

Amyloid β-Protein Aggregation Produces Highly Reproducible Kinetic Data and Occurs by a Two-Phase Process
journal, September 2009

  • Hellstrand, Erik; Boland, Barry; Walsh, Dominic M.
  • ACS Chemical Neuroscience, Vol. 1, Issue 1
  • DOI: 10.1021/cn900015v

Comparison of simple potential functions for simulating liquid water
journal, July 1983

  • Jorgensen, William L.; Chandrasekhar, Jayaraman; Madura, Jeffry D.
  • The Journal of Chemical Physics, Vol. 79, Issue 2
  • DOI: 10.1063/1.445869

Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-β protein
journal, December 1997

3D structure of Alzheimer's amyloid- (1-42) fibrils
journal, November 2005

  • Luhrs, T.; Ritter, C.; Adrian, M.
  • Proceedings of the National Academy of Sciences, Vol. 102, Issue 48
  • DOI: 10.1073/pnas.0506723102

Atomic View of a Toxic Amyloid Small Oligomer
journal, March 2012

Alzheimer's Disease: Genes, Proteins, and Therapy
journal, April 2001

Solution structure of the Alzheimer amyloid β-peptide (1-42) in an apolar microenvironment: Similarity with a virus fusion domain
journal, October 2002

AMPAR Removal Underlies Aβ-Induced Synaptic Depression and Dendritic Spine Loss
journal, December 2006

Amyloid β-Protein Monomer Folding: Free-Energy Surfaces Reveal Alloform-Specific Differences
journal, December 2008

Protein Misfolded Oligomers: Experimental Approaches, Mechanism of Formation, and Structure-Toxicity Relationships
journal, March 2012

Energy landscape of a small peptide revealed by dihedral angle principal component analysis
journal, November 2004

  • Mu, Yuguang; Nguyen, Phuong H.; Stock, Gerhard
  • Proteins: Structure, Function, and Bioinformatics, Vol. 58, Issue 1
  • DOI: 10.1002/prot.20310

Structural Characterization of a Soluble Amyloid β-Peptide Oligomer
journal, March 2009

  • Yu, Liping; Edalji, Rohinton; Harlan, John E.
  • Biochemistry, Vol. 48, Issue 9
  • DOI: 10.1021/bi802046n

An Azobenzene Photoswitch Sheds Light on Turn Nucleation in Amyloid-β Self-Assembly
journal, February 2012

  • Doran, Todd M.; Anderson, Elizabeth A.; Latchney, Sarah E.
  • ACS Chemical Neuroscience, Vol. 3, Issue 3
  • DOI: 10.1021/cn2001188

Direct characterization of amyloidogenic oligomers by single-molecule fluorescence
journal, September 2008

  • Orte, A.; Birkett, N. R.; Clarke, R. W.
  • Proceedings of the National Academy of Sciences, Vol. 105, Issue 38
  • DOI: 10.1073/pnas.0803086105

Design of small molecules that target metal-A  species and regulate metal-induced A  aggregation and neurotoxicity
journal, December 2010

  • Choi, J. -S.; Braymer, J. J.; Nanga, R. P. R.
  • Proceedings of the National Academy of Sciences, Vol. 107, Issue 51
  • DOI: 10.1073/pnas.1006091107

Single Molecule Tracking Analysis Reveals That the Surface Mobility of Amyloid Oligomers Is Driven by Their Conformational Structure
journal, August 2011

  • Calamai, Martino; Pavone, Francesco S.
  • Journal of the American Chemical Society, Vol. 133, Issue 31
  • DOI: 10.1021/ja200951f

Structural, morphological, and functional diversity of amyloid oligomers
journal, July 2015

Structure-neurotoxicity relationships of amyloid  -protein oligomers
journal, August 2009

  • Ono, K.; Condron, M. M.; Teplow, D. B.
  • Proceedings of the National Academy of Sciences, Vol. 106, Issue 35
  • DOI: 10.1073/pnas.0905127106

Alzheimer's Disease and the Amyloid-β Peptide
journal, January 2010

  • Murphy, M. Paul; LeVine, Harry
  • Journal of Alzheimer's Disease, Vol. 19, Issue 1
  • DOI: 10.3233/JAD-2010-1221

Exploring the aggregation free energy landscape of the amyloid-β protein (1–40)
journal, October 2016

  • Zheng, Weihua; Tsai, Min-Yeh; Chen, Mingchen
  • Proceedings of the National Academy of Sciences, Vol. 113, Issue 42
  • DOI: 10.1073/pnas.1612362113

A comparative analysis of the aggregation behavior of amyloid-β peptide variants
journal, October 2012

Annular Protofibrils Are a Structurally and Functionally Distinct Type of Amyloid Oligomer
journal, December 2008

  • Kayed, Rakez; Pensalfini, Anna; Margol, Larry
  • Journal of Biological Chemistry, Vol. 284, Issue 7
  • DOI: 10.1074/jbc.M808591200

Quaternary Structure Defines a Large Class of Amyloid-β Oligomers Neutralized by Sequestration
journal, June 2015

Effect of acidic pH on the stability of α-synuclein dimers: Stability of α-Synuclein Dimers
journal, July 2016

  • Lv, Zhengjian; Krasnoslobodtsev, Alexey V.; Zhang, Yuliang
  • Biopolymers, Vol. 105, Issue 10
  • DOI: 10.1002/bip.22874

Self-Propagating, Molecular-Level Polymorphism in Alzheimer's  -Amyloid Fibrils
journal, January 2005

A partially folded structure of amyloid-beta(1–40) in an aqueous environment
journal, July 2011

  • Vivekanandan, Subramanian; Brender, Jeffrey R.; Lee, Shirley Y.
  • Biochemical and Biophysical Research Communications, Vol. 411, Issue 2
  • DOI: 10.1016/j.bbrc.2011.06.133

Structural Classification of Toxic Amyloid Oligomers
journal, August 2008

Regulation of NMDA receptor trafficking by amyloid-β
journal, July 2005

  • Snyder, Eric M.; Nong, Yi; Almeida, Claudia G.
  • Nature Neuroscience, Vol. 8, Issue 8
  • DOI: 10.1038/nn1503

The Structure of Misfolded Amyloidogenic Dimers: Computational Analysis of Force Spectroscopy Data
journal, December 2014

Misfolding of the amyloid β-protein: A molecular dynamics study
journal, November 2005

  • Flöck, Dagmar; Colacino, Stefano; Colombo, Giorgio
  • Proteins: Structure, Function, and Bioinformatics, Vol. 62, Issue 1
  • DOI: 10.1002/prot.20683

Direct Detection of α-Synuclein Dimerization Dynamics: Single-Molecule Fluorescence Analysis
journal, April 2015

  • Lv, Zhengjian; Krasnoslobodtsev, Alexey V.; Zhang, Yuliang
  • Biophysical Journal, Vol. 108, Issue 8
  • DOI: 10.1016/j.bpj.2015.03.010

Atomic-Level Characterization of the Ensemble of the Aβ(1–42) Monomer in Water Using Unbiased Molecular Dynamics Simulations and Spectral Algorithms
journal, January 2011

  • Sgourakis, Nikolaos G.; Merced-Serrano, Myrna; Boutsidis, Christos
  • Journal of Molecular Biology, Vol. 405, Issue 2
  • DOI: 10.1016/j.jmb.2010.10.015

Molecular Mechanism of Misfolding and Aggregation of Aβ(13–23)
journal, May 2013

  • Lovas, Sándor; Zhang, Yuliang; Yu, Junping
  • The Journal of Physical Chemistry B, Vol. 117, Issue 20
  • DOI: 10.1021/jp402938p

Cell-Membrane-Mimicking Lipid-Coated Nanoparticles Confer Raman Enhancement to Membrane Proteins and Reveal Membrane-Attached Amyloid-β Conformation
journal, August 2015

  • Bhowmik, Debanjan; Mote, Kaustubh R.; MacLaughlin, Christina M.
  • ACS Nano, Vol. 9, Issue 9
  • DOI: 10.1021/acsnano.5b03175

Thermodynamics of Aβ(1−40) Amyloid Fibril Elongation †
journal, September 2005

  • O'Nuallain, Brian; Shivaprasad, Shankaramma; Kheterpal, Indu
  • Biochemistry, Vol. 44, Issue 38
  • DOI: 10.1021/bi050927h

Protein folding and misfolding
journal, December 2003

Structures of the Alzheimer’s Wild-Type Aβ1-40 Dimer from Atomistic Simulations
journal, August 2015

  • Tarus, Bogdan; Tran, Thanh T.; Nasica-Labouze, Jessica
  • The Journal of Physical Chemistry B, Vol. 119, Issue 33
  • DOI: 10.1021/acs.jpcb.5b05593

A series of PDB-related databanks for everyday needs
journal, October 2014

  • Touw, Wouter G.; Baakman, Coos; Black, Jon
  • Nucleic Acids Research, Vol. 43, Issue D1
  • DOI: 10.1093/nar/gku1028

α-Synuclein Misfolding Assessed with Single Molecule AFM Force Spectroscopy: Effect of Pathogenic Mutations
journal, October 2013

  • Krasnoslobodtsev, Alexey V.; Volkov, Ivan L.; Asiago, Josephat M.
  • Biochemistry, Vol. 52, Issue 42
  • DOI: 10.1021/bi401037z

The presenilin 2 mutation (N141I) linked to familial Alzheimer disease (Volga German families) increases the secretion of amyloid   protein ending at the 42nd (or 43rd) residue
journal, March 1997

  • Tomita, T.; Maruyama, K.; Saido, T. C.
  • Proceedings of the National Academy of Sciences, Vol. 94, Issue 5
  • DOI: 10.1073/pnas.94.5.2025

Amyloid  -protein (A ) assembly: A 40 and A 42 oligomerize through distinct pathways
journal, December 2002

  • Bitan, G.; Kirkitadze, M. D.; Lomakin, A.
  • Proceedings of the National Academy of Sciences, Vol. 100, Issue 1
  • DOI: 10.1073/pnas.222681699

Self-assembly of the full-length amyloid Aβ42 protein in dimers
journal, January 2016

  • Zhang, Yuliang; Hashemi, Mohtadin; Lv, Zhengjian
  • Nanoscale, Vol. 8, Issue 45
  • DOI: 10.1039/C6NR06850B

PROFASI: A Monte Carlo simulation package for protein folding and aggregation
journal, January 2006

  • Irbäck, Anders; Mohanty, Sandipan
  • Journal of Computational Chemistry, Vol. 27, Issue 13
  • DOI: 10.1002/jcc.20452

Nanoscale Dynamics of Amyloid β-42 Oligomers As Revealed by High-Speed Atomic Force Microscopy
journal, October 2016

Significant Structural Differences between Transient Amyloid-β Oligomers and Less-Toxic Fibrils in Regions Known To Harbor Familial Alzheimer′s Mutations
journal, April 2014

  • Sarkar, Bidyut; Mithu, Venus Singh; Chandra, Bappaditya
  • Angewandte Chemie International Edition, Vol. 53, Issue 27
  • DOI: 10.1002/anie.201402636

Aβ(1–42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease
journal, May 2015

  • Xiao, Yiling; Ma, Buyong; McElheny, Dan
  • Nature Structural & Molecular Biology, Vol. 22, Issue 6
  • DOI: 10.1038/nsmb.2991

Dynamics of locking of peptides onto growing amyloid fibrils
journal, July 2009

  • Reddy, G.; Straub, J. E.; Thirumalai, D.
  • Proceedings of the National Academy of Sciences, Vol. 106, Issue 29
  • DOI: 10.1073/pnas.0902473106

Protein Misfolding, Functional Amyloid, and Human Disease
journal, June 2006

Selective cytotoxicity of intracellular amyloid β peptide1–42 through p53 and Bax in cultured primary human neurons
journal, January 2002

  • Zhang, Yan; McLaughlin, Richard; Goodyer, Cynthia
  • Journal of Cell Biology, Vol. 156, Issue 3
  • DOI: 10.1083/jcb.200110119

Computational Study on the Structural Diversity of Amyloid Beta Peptide (Aβ 10 - 35 ) Oligomers
journal, March 2008

  • Jang, Soonmin; Shin, Seokmin
  • The Journal of Physical Chemistry B, Vol. 112, Issue 11
  • DOI: 10.1021/jp076450w

Amyloid beta-protein monomer structure: A computational and experimental study
journal, February 2006

Amyloid pores from pathogenic mutations
journal, July 2002

  • Lashuel, Hilal A.; Hartley, Dean; Petre, Benjamin M.
  • Nature, Vol. 418, Issue 6895
  • DOI: 10.1038/418291a

High-Resolution Structures of the Amyloid-β 1–42 Dimers from the Comparison of Four Atomistic Force Fields
journal, June 2017

  • Man, Viet Hoang; Nguyen, Phuong H.; Derreumaux, Philippe
  • The Journal of Physical Chemistry B, Vol. 121, Issue 24
  • DOI: 10.1021/acs.jpcb.7b04689

Comparative Studies of Disordered Proteins with Similar Sequences: Application to Aβ40 and Aβ42
journal, April 2013

  • Fisher, Charles K.; Ullman, Orly; Stultz, Collin M.
  • Biophysical Journal, Vol. 104, Issue 7
  • DOI: 10.1016/j.bpj.2013.02.023

In silico study of amyloid  -protein folding and oligomerization
journal, December 2004

  • Urbanc, B.; Cruz, L.; Yun, S.
  • Proceedings of the National Academy of Sciences, Vol. 101, Issue 50
  • DOI: 10.1073/pnas.0408153101

Atomic-resolution structure of a disease-relevant Aβ(1–42) amyloid fibril
journal, July 2016

  • Wälti, Marielle Aulikki; Ravotti, Francesco; Arai, Hiromi
  • Proceedings of the National Academy of Sciences, Vol. 113, Issue 34
  • DOI: 10.1073/pnas.1600749113

Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease
journal, June 2009

  • Bernstein, Summer L.; Dupuis, Nicholas F.; Lazo, Noel D.
  • Nature Chemistry, Vol. 1, Issue 4
  • DOI: 10.1038/nchem.247

Characterization of cerebrospinal fluid aminoterminally truncated and oxidized amyloid-β peptides
journal, April 2012

  • Bibl, Mirko; Gallus, Marion; Welge, Volker
  • PROTEOMICS - Clinical Applications, Vol. 6, Issue 3-4
  • DOI: 10.1002/prca.201100082

Improved side-chain torsion potentials for the Amber ff99SB protein force field
journal, January 2010

  • Lindorff-Larsen, Kresten; Piana, Stefano; Palmo, Kim
  • Proteins: Structure, Function, and Bioinformatics
  • DOI: 10.1002/prot.22711

Millisecond-scale molecular dynamics simulations on Anton
conference, January 2009

  • Shaw, David E.; Bowers, Kevin J.; Chow, Edmond
  • Proceedings of the Conference on High Performance Computing Networking, Storage and Analysis - SC '09
  • DOI: 10.1145/1654059.1654099

Significant Structural Differences between Transient Amyloid-β Oligomers and Less-Toxic Fibrils in Regions Known To Harbor Familial Alzheimer′s Mutations
journal, April 2014

  • Sarkar, Bidyut; Mithu, Venus Singh; Chandra, Bappaditya
  • Angewandte Chemie, Vol. 126, Issue 27
  • DOI: 10.1002/ange.201402636

Single-molecule studies of intrinsically disordered proteins
text, January 2014

  • Marco, Brucale,; Benjamin, Schuler,; Bruno, Samorì,
  • American Chemical Society
  • DOI: 10.5167/uzh-96983

Structural Characterization and Inhibition of Toxic Amyloid-β Oligomeric Intermediates
journal, July 2013

Common mechanisms of amyloid oligomer pathogenesis in degenerative disease
journal, April 2006

AMPAR Removal Underlies Aβ-Induced Synaptic Depression and Dendritic Spine Loss
journal, December 2006

Aβ(1–42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease
journal, May 2015

  • Xiao, Yiling; Ma, Buyong; McElheny, Dan
  • Nature Structural & Molecular Biology, Vol. 22, Issue 6
  • DOI: 10.1038/nsmb.2991

Self-Propagating, Molecular-Level Polymorphism in Alzheimer's  -Amyloid Fibrils
journal, January 2005

    Sort by:
    [ × clear filter / sort ]

    Similar Records in DOE PAGES and OSTI.GOV collections: