Structure and properties of alpha-synuclein and other amyloids determined at the amino acid level (Q34098577)

31 July 2017

title

Structure and properties of alpha-synuclein and other amyloids determined at the amino acid level (English)

1 reference

31 July 2017

1 reference

Charyl Del Mar

1

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31 July 2017

Eric A Greenbaum

2

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31 July 2017

Leland Mayne

3

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31 July 2017

S Walter Englander

4

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31 July 2017

Virgil L Woods

5

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31 July 2017

language of work or name

English

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publication date

13 October 2005

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Proceedings of the National Academy of Sciences of the United States of America

31 July 2017

published in

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31 July 2017

volume

102

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31 July 2017

issue

43

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31 July 2017

page(s)

15477-15482

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Helix, sheet, and polyproline II frequencies and strong nearest neighbor effects in a restricted coil library

31 July 2017

cites work

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Correlation of structural elements and infectivity of the HET-s prion

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Structure of the cross-beta spine of amyloid-like fibrils

28 July 2018

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Hydrogen exchange methods to study protein folding

28 July 2018

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Progress towards a molecular-level structural understanding of amyloid fibrils

28 July 2018

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28 July 2018

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28 July 2018

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NMR-detected hydrogen exchange and molecular dynamics simulations provide structural insight into fibril formation of prion protein fragment 106-126.

28 July 2018

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28 July 2018

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28 July 2018

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28 July 2018

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28 July 2018

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28 July 2018

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Amyloid fibers are water-filled nanotubes

28 July 2018

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Biochemical characterization of the core structure of alpha-synuclein filaments

28 July 2018

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28 July 2018

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28 July 2018

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Abeta amyloid fibrils possess a core structure highly resistant to hydrogen exchange

28 July 2018

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Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of beta-sheets in Alzheimer's beta-amyloid fibrils

28 July 2018

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A hydrophobic stretch of 12 amino acid residues in the middle of alpha-synuclein is essential for filament assembly.

28 July 2018

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From the globular to the fibrous state: protein structure and structural conversion in amyloid formation.

28 July 2018

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The structure of amyloid fibrils by electron microscopy and X-ray diffraction

28 July 2018

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NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded

28 July 2018

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Future directions in folding: the multi-state nature of protein structure

28 July 2018

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Protein complexes studied by NMR spectroscopy

28 July 2018

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Determination of amide hydrogen exchange by mass spectrometry: a new tool for protein structure elucidation

28 July 2018

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Molecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer disease

28 July 2018

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Primary structure effects on peptide group hydrogen exchange

28 July 2018

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Protein folding intermediates: native-state hydrogen exchange

28 July 2018

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Structural model for the β-amyloid fibril based on interstrand alignment of an antiparallel-sheet comprising a C-terminal peptide

28 July 2018

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Individual breathing reactions measured in hemoglobin by hydrogen exchange methods

28 July 2018

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Principles that determine the structure of proteins

28 July 2018

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An experimental procedure for increasing the structural resolution of chemical hydrogen-exchange measurements on proteins: Application to ribonuclease S peptide

28 July 2018

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Hydrogen-deuterium (H/D) exchange mapping of Abeta 1-40 amyloid fibril secondary structure using nuclear magnetic resonance spectroscopy

28 July 2018

1 reference

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Molecular basis for amyloid fibril formation and stability

28 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1266128

Emerging principles of conformation-based prion inheritance

28 October 2018

1 reference

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Core and heterogeneity of beta2-microglobulin amyloid fibrils as revealed by H/D exchange

28 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1266128

Solid state NMR reveals a pH-dependent antiparallel beta-sheet registry in fibrils formed by a beta-amyloid peptide

28 October 2018

1 reference

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Abeta protofibrils possess a stable core structure resistant to hydrogen exchange

28 October 2018

1 reference

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Role of alpha-synuclein carboxy-terminus on fibril formation in vitro

28 October 2018

1 reference

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Structural organization of alpha-synuclein fibrils studied by site-directed spin labeling

28 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1266128

Protein analysis by hydrogen exchange mass spectrometry

28 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1266128

Hydrogen exchange studies on Alzheimer's amyloid-beta peptides by mass spectrometry using matrix-assisted laser desorption/ionization and electrospray ionization

28 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1266128

The N-terminal repeat domain of alpha-synuclein inhibits beta-sheet and amyloid fibril formation

28 October 2018

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1266128

Structural and dynamic features of Alzheimer's Abeta peptide in amyloid fibrils studied by site-directed spin labeling.

28 October 2018

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Mapping the core of the beta(2)-microglobulin amyloid fibril by H/D exchange

28 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1266128

Investigating protein structure and dynamics by hydrogen exchange MS.

28 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1266128

Amyloid fibril formation by A beta 16-22, a seven-residue fragment of the Alzheimer's beta-amyloid peptide, and structural characterization by solid state NMR

28 October 2018

1 reference

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Two-dimensional structure of beta-amyloid(10-35) fibrils

28 October 2018

1 reference

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How the molten globule became

28 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1266128

Protein hydrogen exchange studied by the fragment separation method.

28 October 2018

1 reference

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Structural features of the Abeta amyloid fibril elucidated by limited proteolysis

28 October 2018

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12 December 2020

X-ray diffraction studies on amyloid filaments

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12 December 2020

Isotope effects in peptide group hydrogen exchange

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12 December 2020

Protein stability parameters measured by hydrogen exchange

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12 December 2020

The core Alzheimer's peptide NAC forms amyloid fibrils which seed and are seeded by beta-amyloid: is NAC a common trigger or target in neurodegenerative disease?

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12 December 2020

Probing the structure of the infectious amyloid form of the prion-forming domain of HET-s using high resolution hydrogen/deuterium exchange monitored by mass spectrometry

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12 December 2020

Identifiers

DOI

10.1073/PNAS.0507405102

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31 July 2017

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31 July 2017

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