Stilbene Boronic Acids Form a Covalent Bond with Human Transthyretin and Inhibit Its Aggregation-Reference-Cited by-同舟云学术

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Stilbene Boronic Acids Form a Covalent Bond with Human Transthyretin and Inhibit Its Aggregation

Published:2017-09-18 Issue:18 Volume:60 Page:7820-7834
ISSN:0022-2623
Container-title:Journal of Medicinal Chemistry
language:en
Short-container-title:J. Med. Chem.

Author:

Smith Thomas P.¹,Windsor Ian W.²,Forest Katrina T.¹³,Raines Ronald T.¹²^ORCID

Affiliation:

1. Department of Chemistry, University of Wisconsin—Madison, Madison, Wisconsin 53706, United States

2. Department of Biochemistry, University of Wisconsin—Madison, Madison, Wisconsin 53706, United States

3. Department of Bacteriology, University of Wisconsin—Madison, Madison, Wisconsin 53706, United States

Funder

Division of Molecular and Cellular Biosciences

Genentech

National Institute of General Medical Sciences

Publisher

American Chemical Society (ACS)

Subject

Drug Discovery,Molecular Medicine

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jmedchem.7b00952

Reference83 articles.

1. Protein folding and misfolding

2. Protein Misfolding, Functional Amyloid, and Human Disease

3. The amyloid state and its association with protein misfolding diseases

4. Cell and Molecular Biology of Transthyretin and Thyroid Hormones

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3. Silyloxymethylation of Aryl Halides via Metallaphotoredox Catalyzed Desulfinative Cross‐Coupling with Silyl Rongalite;Asian Journal of Organic Chemistry;2024-01-02

4. Elemental exchange: Bioisosteric replacement of phosphorus by boron in drug design;European Journal of Medicinal Chemistry;2023-11

5. Novel Strategy To Inhibit Transthyretin Amyloidosis via the Synergetic Effect of Chemoselective Acylation and Noncovalent Inhibitor Release;Journal of Medicinal Chemistry;2023-02-07

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