Regulated N-Terminal Modification of Proteins Synthesized Using a Reconstituted Cell-Free Protein Synthesis System-Reference-Cited by-同舟云学术

Regulated N-Terminal Modification of Proteins Synthesized Using a Reconstituted Cell-Free Protein Synthesis System

Published:2023-06-16 Issue:7 Volume:12 Page:1935-1942
ISSN:2161-5063
Container-title:ACS Synthetic Biology
language:en
Short-container-title:ACS Synth. Biol.

Author:

Matsumoto Rena¹,Niwa Tatsuya²,Shimane Yasuhiro³,Kuruma Yutetsu³,Taguchi Hideki²^ORCID,Kanamori Takashi¹^ORCID

Affiliation:

1. GeneFrontier Corporation, 273-1 Kashiwa, Kashiwa, Chiba 277-0005, Japan

2. Cell Biology Center, Institute of Innovative Research, Tokyo Institute of Technology, Yokohama 226-8503, Japan

3. Institute for Extra-cutting-edge Science and Technology Avant-garde Research (X-star), Japan Agency for Marine-Earth Science and Technology (JAMSTEC), 2-15 Natsushima-cho, Yokosuka, Kanagawa 237-0061, Japan

Funder

Core Research for Evolutional Science and Technology

Japan Society for the Promotion of Science

Publisher

American Chemical Society (ACS)

Subject

Biochemistry, Genetics and Molecular Biology (miscellaneous),Biomedical Engineering,General Medicine

Link

https://pubs.acs.org/doi/pdf/10.1021/acssynbio.3c00191

Reference20 articles.

1. N‐terminal modifications of cellular proteins: The enzymes involved, their substrate specificities and biological effects

2. Post-translational Modifications of the Protein Termini

3. N-terminal acetylation: an essential protein modification emerges as an important regulator of stress responses

4. Nα-terminal acetylation of proteins by NatA and NatB serves distinct physiological roles in Saccharomyces cerevisiae

5. Spotlight on protein N-terminal acetylation

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