Serum-Stable and Selective Backbone-N-Methylated Cyclic Peptides That Inhibit Prokaryotic Glycolytic Mutases-Reference-Cited by-同舟云学术

Serum-Stable and Selective Backbone-N-Methylated Cyclic Peptides That Inhibit Prokaryotic Glycolytic Mutases

Published:2022-07-29 Issue:8 Volume:17 Page:2284-2295
ISSN:1554-8929
Container-title:ACS Chemical Biology
language:en
Short-container-title:ACS Chem. Biol.

Author:

van Neer R.H.P.¹^ORCID,Dranchak P. K.²,Liu L.³,Aitha M.²^ORCID,Queme B.²,Kimura H.¹,Katoh T.¹^ORCID,Battaile K. P.⁴,Lovell S.³,Inglese J.²⁵^ORCID,Suga H.¹^ORCID

Affiliation:

1. Department of Chemistry, Graduate School of Science, The University of Tokyo, Tokyo 113-0033, Japan

2. National Center for Advancing Translational Sciences, National Institutes of Health, Rockville, Maryland 20850, United States

3. Protein Structure and X-ray Crystallography Laboratory, Structural Biology Center, University of Kansas, Lawrence, Kansas 66045, United States

4. New York Structural Biology Center, NSLS-II, Upton, New York 11973, United States

5. National Human Genome Research Institute, National Institutes of Health, Bethesda, Maryland 20892, United States

Funder

National Center for Advancing Translational Sciences

Japan Agency for Medical Research and Development

Japan Society for the Promotion of Science

Mitsubishi International Corporation

Publisher

American Chemical Society (ACS)

Subject

Molecular Medicine,General Medicine,Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acschembio.2c00403

Reference51 articles.

1. Going Out on a Limb: Delineating The Effects of β-Branching, N-Methylation, and Side Chain Size on the Passive Permeability, Solubility, and Flexibility of Sanguinamide A Analogues

2. Drug‐Like Properties in Macrocycles above MW 1000: Backbone Rigidity versus Side‐Chain Lipophilicity

3. Effect of N-methyl substitution of the peptide bonds in luteinizing hormone-releasing hormone agonists

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