Photocaged dicarbonyl probe provides spatiotemporal control over protein glycation-Reference-Cited by-同舟云学术

Photocaged dicarbonyl probe provides spatiotemporal control over protein glycation

Published:2022 Issue:6 Volume:58 Page:855-858
ISSN:1359-7345
Container-title:Chemical Communications
language:en
Short-container-title:Chem. Commun.

Author:

Hurben Alexander K.¹^ORCID,Ge Peng¹,Bouchard Jacob L.¹,Doran Todd M.¹²,Tretyakova Natalia Y.¹³^ORCID

Affiliation:

1. Department of Medicinal Chemistry, University of Minnesota, Minneapolis, MN, 55455, USA

2. Institute for Translational Neuroscience, University of Minnesota, Minneapolis, MN, 55455, USA

3. Masonic Cancer Center, University of Minnesota, Minneapolis, MN, 55455, USA

Abstract

On demand dicarbonyl-protein adduct formation in live cells is achieved with subcellular specificity by a targetable, light triggered probe.

Funder

National Institutes of Health

University of Minnesota

Publisher

Royal Society of Chemistry (RSC)

Subject

Materials Chemistry,Metals and Alloys,Surfaces, Coatings and Films,General Chemistry,Ceramics and Composites,Electronic, Optical and Magnetic Materials,Catalysis

Link

http://pubs.rsc.org/en/content/articlepdf/2022/CC/D1CC06651J

Reference25 articles.

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4. The formation of methylglyoxal from triose phosphates. Investigation using a specific assay for methylglyoxal

5. A Systematic Study of Selective Protein Glycation

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