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On the Binding of Congo Red to Amyloid Fibrils

https://doi.org/10.1002/anie.201916630

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/ange.201008276openalex-snapshot

Die Amyloid‐Kongorot‐Bindungsstelle in atomarer Auflösung

inferredcites →https://doi.org/10.1002/ange.201901929openalex-snapshot

Localized and Collective Motions in HET‐s(218‐289) Fibrils from Combined NMR Relaxation and MD Simulation

inferredcites →https://doi.org/10.1002/anie.201008276openalex-snapshot

The Amyloid–Congo Red Interface at Atomic Resolution

inferredcites →https://doi.org/10.1002/anie.201901929openalex-snapshot

Localized and Collective Motions in HET‐s(218‐289) Fibrils from Combined NMR Relaxation and MD Simulation

inferredcites →https://doi.org/10.1006/abio.1998.2933openalex-snapshot

Quantifying Amyloid β-Peptide (Aβ) Aggregation Using the Congo Red-Aβ (CR–Aβ) Spectrophotometric Assay

inferredcites →https://doi.org/10.1007/s004280050471openalex-snapshot

Highly sensitive diagnosis of amyloid and various amyloid syndromes using Congo red fluorescence

inferredcites →https://doi.org/10.1007/s10858-016-0087-0openalex-snapshot

Partially-deuterated samples of HET-s(218–289) fibrils: assignment and deuterium isotope effect

inferredcites →https://doi.org/10.1007/s10858-017-0148-zopenalex-snapshot

The conformation of the Congo-red ligand bound to amyloid fibrils HET-s(218–289): a solid-state NMR study

inferredcites →https://doi.org/10.1016/j.abb.2007.05.015openalex-snapshot

Folding versus aggregation: Polypeptide conformations on competing pathways

inferredcites →https://doi.org/10.1016/j.sbi.2006.01.011openalex-snapshot

Protein aggregation and amyloidosis: confusion of the kinds?

inferredcites →https://doi.org/10.1016/j.ymeth.2004.03.012openalex-snapshot

Techniques to study amyloid fibril formation in vitro

inferredcites →https://doi.org/10.1016/s0076-6879(99)09021-7openalex-snapshot

[19] Quantifying amyloid by congo red spectral shift assay

inferredcites →https://doi.org/10.1021/acschemneuro.8b00280openalex-snapshot

Noncovalent, Electrostatic Interactions Induce Positively Cooperative Binding of Small Molecules to Alzheimer’s and Parkinson’s Disease-Related Amyloids

inferredcites →https://doi.org/10.1021/ar0500618openalex-snapshot

The Structural Biology of Protein Aggregation Diseases: Fundamental Questions and Some Answers

inferredcites →https://doi.org/10.1021/ja0662772openalex-snapshot

Dual Binding Modes of Congo Red to Amyloid Protofibril Surface Observed in Molecular Dynamics Simulations

inferredcites →https://doi.org/10.1038/35041139openalex-snapshot

Conformational disease

inferredcites →https://doi.org/10.1038/nature03793openalex-snapshot

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

inferredcites →https://doi.org/10.1039/c6cp00057fopenalex-snapshot

Investigation of the structural preference and flexibility of the loop residues in amyloid fibrils of the HET-s prion

inferredcites →https://doi.org/10.1073/pnas.1711645114openalex-snapshot

Chaperonin GroEL accelerates protofibril formation and decorates fibrils of the Het-s prion protein

inferredcites →https://doi.org/10.1080/13506120500032295openalex-snapshot

Multiple ligand binding sites on Aβ(1–40) fibrils

inferredcites →https://doi.org/10.1080/13506120701460923openalex-snapshot

A primer of amyloid nomenclature

inferredcites →https://doi.org/10.1080/13506129.2016.1257986openalex-snapshot

Amyloid fibril proteins and amyloidosis: chemical identification and clinical classification International Society of Amyloidosis 2016 Nomenclature Guidelines

inferredcites →https://doi.org/10.1101/cshperspect.a023515openalex-snapshot

The HET-S/s Prion Motif in the Control of Programmed Cell Death

inferredcites →https://doi.org/10.1126/science.1151839openalex-snapshot

Amyloid Fibrils of the HET-s(218–289) Prion Form a β Solenoid with a Triangular Hydrophobic Core

inferredcites →https://doi.org/10.1146/annurev.biochem.75.101304.123901openalex-snapshot

Protein Misfolding, Functional Amyloid, and Human Disease

inferredcites →https://doi.org/10.2147/ijn.s89385openalex-snapshot

Amyloids in solid-state nuclear magnetic resonance: potential causes of the usually low resolution

inferredcites →https://doi.org/10.3109/13506120009146832openalex-snapshot

Histidine residues underlie Congo red binding to Aβ analogs

inferredcites →https://doi.org/10.5858/2001-125-0250-cropenalex-snapshot

“Congo” Red

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