(Q46603261)

23 December 2017

title

Congo red populates partially unfolded states of an amyloidogenic protein to enhance aggregation and amyloid fibril formation (English)

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23 December 2017

author

Yong-Sung Kim

1

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23 December 2017

Theodore W Randolph

2

object named as

Theodore W Randolph

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23 December 2017

author name string

Mark C Manning

3

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23 December 2017

Fred J Stevens

4

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23 December 2017

John F Carpenter

5

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23 December 2017

language of work or name

English

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publication date

15 January 2003

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23 December 2017

Journal of Biological Chemistry

published in

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23 December 2017

volume

278

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23 December 2017

page(s)

10842-10850

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23 December 2017

issue

12

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23 December 2017

Alternative conformations of amyloidogenic proteins govern their behavior

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Binding of the dye congo red to the amyloid protein pig insulin reveals a novel homology amongst amyloid-forming peptide sequences

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Oligomerization of endogenous and synthetic amyloid beta-protein at nanomolar levels in cell culture and stabilization of monomer by Congo red.

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Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red.

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Spectroscopic studies of Congo Red binding to RNA polymerase.

21 January 2018

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Histidine residues underlie Congo red binding to A beta analogs.

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Congophilicity (Congo red affinity) of different beta2-microglobulin conformations characterized by dye affinity capillary electrophoresis

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Aromatic Contributions To Circular Dichroism Spectra Of Protein

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Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates.

21 January 2018

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Assignment of the contribution of the tryptophan residues to the circular dichroism spectrum of human carbonic anhydrase II.

21 January 2018

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Amyloid probes based on Congo Red distinguish between fibrils comprising different peptides

21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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The sulfate moieties of glycosaminoglycans are critical for the enhancement of beta-amyloid protein fibril formation

21 January 2018

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Heparin and other glycosaminoglycans stimulate the formation of amyloid fibrils from alpha-synuclein in vitro.

21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M212540200

1 reference

23 December 2017

PubMed ID

12529361

1 reference

23 December 2017