Altering the Phosphorylation Position of Pyrophosphate-Dependent myo-Inositol-1-Kinase Based on Its Crystal Structure-Reference-Cited by-同舟云学术

Altering the Phosphorylation Position of Pyrophosphate-Dependent myo-Inositol-1-Kinase Based on Its Crystal Structure

Published:2021-04-20 Issue:5 Volume:16 Page:794-799
ISSN:1554-8929
Container-title:ACS Chemical Biology
language:en
Short-container-title:ACS Chem. Biol.

Author:

Tashiro Ryo¹,Sato Takaaki²,Atomi Haruyuki²,Miki Kunio¹^ORCID,Fujihashi Masahiro¹^ORCID

Affiliation:

1. Department of Chemistry, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan

2. Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Katsura, Nishikyo-ku, Kyoto 615-8510, Japan

Funder

Japan Society for the Promotion of Science

Publisher

American Chemical Society (ACS)

Subject

Molecular Medicine,General Medicine,Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acschembio.0c00733

Reference22 articles.

1. The Structural Basis for Control of Eukaryotic Protein Kinases

2. The origins of protein phosphorylation

3. A Fresh View of Glycolysis and Glucokinase Regulation: History and Current Status

4. Pyrophosphate-dependent phosphofructokinase, an anaerobic glycolytic enzyme?

5. Pyrophosphate:d-Fructose 6-Phosphate 1-Phosphotransferase

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