Histidine residues underlie Congo red binding to A beta analogs.
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The amyloid-Congo red interface at atomic resolutionImaging linear birefringence and dichroism in cerebral amyloid pathologiesMonomeric α-synuclein binds Congo Red micelles in a disordered mannerStructure of core domain of fibril-forming PHF/Tau fragments.Congo Red Interactions with Curli-Producing E. coli and Native Curli Amyloid Fibers.Structurally distinct toxicity inhibitors bind at common loci on β-amyloid fibril.Congo red populates partially unfolded states of an amyloidogenic protein to enhance aggregation and amyloid fibril formation.
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Q27667880-CDB2D59A-DD83-4C6F-B08D-A24F1018323BQ28387800-43BBB1EC-69AE-48C6-ABA8-EF98C4378F1CQ34126935-496E2D27-3E92-4708-BA6F-67AC8834314BQ34354306-38140407-CDE6-4B26-959B-720A3FF99F52Q35814646-7D9DFBF9-883C-4D6B-942F-F0E3DAFD9A08Q39832389-1B2F55CF-010F-47F4-AB9C-458005206931Q46603261-3EF404B1-05A6-4181-85A9-6B9632336364
P2860
Histidine residues underlie Congo red binding to A beta analogs.
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Histidine residues underlie Congo red binding to A beta analogs.
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Histidine residues underlie Congo red binding to A beta analogs.
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type
label
Histidine residues underlie Congo red binding to A beta analogs.
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Histidine residues underlie Congo red binding to A beta analogs.
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prefLabel
Histidine residues underlie Congo red binding to A beta analogs.
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Histidine residues underlie Congo red binding to A beta analogs.
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P2093
P2860
P1433
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Histidine residues underlie Congo red binding to A beta analogs
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P2093
A B Packard
J T Nguyen
L M Shinchuk
P E Fraser
P2860
P304
P356
10.3109/13506120009146832
P577
2000-09-01T00:00:00Z