(Q42647893)

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Thioflavin T is a fluorescent probe of the acetylcholinesterase peripheral site that reveals conformational interactions between the peripheral and acylation sites.

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Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11313335%20AND%20SRC:MED&resulttype=core&format=json

6 November 2019

Thioflavin T is a fluorescent probe of the acetylcholinesterase peripheral site that reveals conformational interactions between the peripheral and acylation sites (English)

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11313335%20AND%20SRC:MED&resulttype=core&format=json

6 November 2019

Giancarlo V De Ferrari

1

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6 November 2019

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Mallender WD

2

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6 November 2019

Inestrosa NC

3

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6 November 2019

Rosenberry TL

4

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6 November 2019

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19 April 2001

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6 November 2019

Journal of Biological Chemistry

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6 November 2019

276

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6 November 2019

26

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6 November 2019

23282-23287

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6 November 2019

Interaction of fluorescence probes with acetylcholinesterase. Site and specificity of propidium binding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009596200

21 January 2018

Atomic Structure of Acetylcholinesterase from Torpedo californica : A Prototypic Acetylcholine-Binding Protein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009596200

21 January 2018

Substrate-binding sites in acetylcholinesterase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009596200

21 January 2018

Allosteric modulation of acetylcholinesterase activity by peripheral ligands involves a conformational transition of the anionic subsite.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009596200

21 January 2018

Quaternary ligand binding to aromatic residues in the active-site gorge of acetylcholinesterase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009596200

21 January 2018

A pseudo-first-order kinetic approach to measurement of acetylcholine hydrolysis by acetylcholinesterase.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009596200

21 January 2018

A new and rapid colorimetric determination of acetylcholinesterase activity

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009596200

21 January 2018

Ellman's reagent: 5,5′-dithiobis(2-nitrobenzoic acid)—a reexamination

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009596200

21 January 2018

Fluorinated aldehydes and ketones acting as quasi-substrate inhibitors of acetylcholinesterase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009596200

21 January 2018

The cholinesterases: from genes to proteins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009596200

21 January 2018

Spectroscopic studies on acetylcholinesterase: influence of peripheral-site occupation on active-center conformation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009596200

21 January 2018

Rapid assembly of Alzheimer-like paired helical filaments from microtubule-associated protein tau monitored by fluorescence in solution

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009596200

21 January 2018

The X-ray Structure of a Transition State Analog Complex Reveals the Molecular Origins of the Catalytic Power and Substrate Specificity of Acetylcholinesterase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009596200

21 January 2018

Substrate binding to the peripheral site of acetylcholinesterase initiates enzymatic catalysis. Substrate inhibition arises as a secondary effect

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009596200

21 January 2018

Acetylthiocholine binds to asp74 at the peripheral site of human acetylcholinesterase as the first step in the catalytic pathway

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009596200

21 January 2018

[18] Quantification of β-sheet amyloid fibril structures with thioflavin T

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009596200

21 January 2018

Organophosphorylation of acetylcholinesterase in the presence of peripheral site ligands. Distinct effects of propidium and fasciculin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009596200

21 January 2018

Nonequilibrium analysis alters the mechanistic interpretation of inhibition of acetylcholinesterase by peripheral site ligands

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009596200

21 January 2018

The influence of peripheral site ligands on the reaction of symmetric and chiral organophosphates with wildtype and mutant acetylcholinesterases

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009596200

21 January 2018

Electron paramagnetic resonance reveals altered topography of the active center gorge of acetylcholinesterase after binding of fasciculin to the peripheral site

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009596200

21 January 2018

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