Vibrational Circular Dichroism as a Probe of Fibrillogenesis: The Origin of the Anomalous Intensity Enhancement of Amyloid-like Fibrils (Q83037568)

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scientific article published on December 27, 2010

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English	Vibrational Circular Dichroism as a Probe of Fibrillogenesis: The Origin of the Anomalous Intensity Enhancement of Amyloid-like Fibrils	scientific article published on December 27, 2010

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21186804

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18 January 2020

title

Vibrational circular dichroism as a probe of fibrillogenesis: the origin of the anomalous intensity enhancement of amyloid-like fibrils (English)

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Europe PubMed Central

PubMed publication ID

21186804

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18 January 2020

Vibrational Circular Dichroism as a Probe of Fibrillogenesis: The Origin of the Anomalous Intensity Enhancement of Amyloid-like Fibrils (English)

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DOI

10.1021/JA1089827

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20 November 2024

main subject

protein multimerization

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Europe PubMed Central

PubMed publication ID

21186804

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A21186804

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20 November 2024

author name string

Reinhard Schweitzer-Stenner

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2

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21186804

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18 January 2020

Thomas J. Measey

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1

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PubMed publication ID

21186804

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A21186804

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language of work or name

English

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Journal of the American Chemical Society

publication date

27 December 2010

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PubMed publication ID

21186804

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21186804%20AND%20SRC:MED&resulttype=core&format=json

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18 January 2020

full work available at URL

https://pubs.acs.org/doi/pdf/10.1021/ja1089827

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10.1021/JA1089827

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20 November 2024

published in

Journal of the American Chemical Society

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Europe PubMed Central

PubMed publication ID

21186804

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21186804%20AND%20SRC:MED&resulttype=core&format=json

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18 January 2020

volume

133

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PubMed publication ID

21186804

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18 January 2020

issue

4

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Europe PubMed Central

PubMed publication ID

21186804

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18 January 2020

page(s)

1066-1076

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PubMed publication ID

21186804

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18 January 2020

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Protein misfolding, functional amyloid, and human disease

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10.1021/JA1089827

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20 November 2024

Protein misfolding, evolution and disease

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Protein folding and misfolding

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Peptide fibrillization

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The "Correctly Folded" state of proteins: is it a metastable state?

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Assembly of amyloid protofibrils via critical oligomers--a novel pathway of amyloid formation

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Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution

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Physical, morphological and functional differences between ph 5.8 and 7.4 aggregates of the Alzheimer's amyloid peptide Abeta

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Amyloid fibril formation requires a chemically discriminating nucleation event: studies of an amyloidogenic sequence from the bacterial protein OsmB

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An ApoE-Abeta inhibition complex in Abeta fibril extension

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Amyloid beta-protein fibrillogenesis. Detection of a protofibrillar intermediate.

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Observation of metastable Abeta amyloid protofibrils by atomic force microscopy

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Structural characterisation of islet amyloid polypeptide fibrils

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Polymorphic Fibrillar Assembly of Human Amylin

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FTIR reveals structural differences between native beta-sheet proteins and amyloid fibrils.

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2D correlation deep UV resonance raman spectroscopy of early events of lysozyme fibrillation: kinetic mechanism and potential interpretation pitfalls

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Structural variations in the cross-beta core of amyloid beta fibrils revealed by deep UV resonance Raman spectroscopy

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Vibrational circular dichroism shows unusual sensitivity to protein fibril formation and development in solution

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Self-aggregation of a polyalanine octamer promoted by its C-terminal tyrosine and probed by a strongly enhanced vibrational circular dichroism signal

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Direct observation and pH control of reversed supramolecular chirality in insulin fibrils by vibrational circular dichroism

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Conformational indeterminism in protein misfolding: chiral amplification on amyloidogenic pathway of insulin

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Chirality of amyloid suprastructures

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Intrinsic propensities of amino acid residues in GxG peptides inferred from amide I' band profiles and NMR scalar coupling constants

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Preferred peptide backbone conformations in the unfolded state revealed by the structure analysis of alanine-based (AXA) tripeptides in aqueous solution

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The alanine-rich XAO peptide adopts a heterogeneous population, including turn-like and polyproline II conformations

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Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins

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Distribution of conformations sampled by the central amino acid residue in tripeptides inferred from amide I band profiles and NMR scalar coupling constants

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Infrared spectroscopy of proteins

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Bovine insulin filaments induced by reducing disulfide bonds show a different morphology, secondary structure, and cell toxicity from intact insulin amyloid fibrils

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An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated beta-sheet structure for amyloid

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

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GNNQQNY--investigation of early steps during amyloid formation

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Side chain dependence of intensity and wavenumber position of amide I' in IR and visible Raman spectra of XA and AX dipeptides

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Quantitative IR spectrophotometry of peptide compounds in water (H2O) solutions. I. Spectral parameters of amino acid residue absorption bands

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Molecular mechanisms underlying the flavonoid-induced inhibition of alpha-synuclein fibrillation

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Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders

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Amyloid beta -protein (Abeta) assembly: Abeta 40 and Abeta 42 oligomerize through distinct pathways

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Cause of neural death in neurodegenerative diseases attributable to expansion of glutamine repeats

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Aggregation of the amphipathic peptides (AAKA)n into antiparallel beta-sheets

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Atomic structures of amyloid cross-beta spines reveal varied steric zippers

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Protein and peptide secondary structure and conformational determination with vibrational circular dichroism

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The protofilament structure of insulin amyloid fibrils

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20 November 2024

Characterizing the assembly of the Sup35 yeast prion fragment, GNNQQNY: structural changes accompany a fiber-to-crystal switch.

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Solid-state NMR study of amyloid nanocrystals and fibrils formed by the peptide GNNQQNY from yeast prion protein Sup35p.

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Identifiers

DOI

10.1021/JA1089827

1 reference

stated in

Europe PubMed Central

PubMed publication ID

21186804

reference URL

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21186804%20AND%20SRC:MED&resulttype=core&format=json

retrieved

18 January 2020

PubMed publication ID

21186804

1 reference

stated in

Europe PubMed Central

PubMed publication ID

21186804

reference URL

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21186804%20AND%20SRC:MED&resulttype=core&format=json

retrieved

18 January 2020

 

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