Redox-active chemical chaperones exhibiting promiscuous binding promote oxidative protein folding under condensed sub-millimolar conditions-Reference-Cited by-同舟云学术

Redox-active chemical chaperones exhibiting promiscuous binding promote oxidative protein folding under condensed sub-millimolar conditions

Published:2024 Issue:32 Volume:15 Page:12676-12685
ISSN:2041-6520
Container-title:Chemical Science
language:en
Short-container-title:Chem. Sci.

Author:

Suzuki Koki¹,Nojiri Ryoya¹,Matsusaki Motonori²,Mabuchi Takuya³⁴^ORCID,Kanemura Shingo³,Ishii Kotone³,Kumeta Hiroyuki⁵,Okumura Masaki³^ORCID,Saio Tomohide²,Muraoka Takahiro¹⁶^ORCID

Affiliation:

1. Department of Applied Chemistry, Graduate School of Engineering, Tokyo University of Agriculture and Technology, Koganei, Tokyo 184-8588, Japan

2. Division of Molecular Life Science, Institute of Advanced Medical Sciences, Tokushima University, Tokushima 770-8503, Japan

3. Frontier Research Institute for Interdisciplinary Sciences, Tohoku University, Sendai, Miyagi 980-8578, Japan

4. Institute of Fluid Science, Tohoku University, Sendai, Miyagi 980-8577, Japan

5. Faculty of Advanced Life Science, Hokkaido University, Sapporo, Hokkaido 060-0810, Japan

6. Kanagawa Institute of Industrial Science and Technology (KISTEC), Kanagawa 243-0435, Japan

Abstract

A promiscuous protein binder with redox activity efficiently promotes oxidative protein folding under condensed sub-millimolar conditions.

Funder

Core Research for Evolutional Science and Technology

Japan Society for the Promotion of Science

Takeda Science Foundation

Asahi Glass Foundation

Fusion Oriented REsearch for disruptive Science and Technology

Kanagawa Institute of Industrial Science and Technology

Publisher

Royal Society of Chemistry (RSC)

Link

http://pubs.rsc.org/en/content/articlepdf/2024/SC/D4SC02123A

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