Studies of Thioamide Effects on Serine Protease Activity Enable Two-Site Stabilization of Cancer Imaging Peptides-Reference-Cited by-同舟云学术

Studies of Thioamide Effects on Serine Protease Activity Enable Two-Site Stabilization of Cancer Imaging Peptides

Published:2020-03-06 Issue:3 Volume:15 Page:774-779
ISSN:1554-8929
Container-title:ACS Chemical Biology
language:en
Short-container-title:ACS Chem. Biol.

Author:

Barrett Taylor M.¹,Chen Xing S.¹,Liu Chunxiao¹²,Giannakoulias Sam¹,Phan Hoang Anh T.¹,Wang Jieliang¹,Keenan E. Keith¹,Karpowicz Richard J.¹,Petersson E. James¹^ORCID

Affiliation:

1. Department of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania 19104, United States

2. Department of Applied Chemistry, China Agricultural University, Yuanmingyuan West Road 2, Beijing 100193, China

Funder

Division of Chemistry

National Center for Advancing Translational Sciences

University of Pennsylvania

Publisher

American Chemical Society (ACS)

Subject

Molecular Medicine,General Medicine,Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acschembio.9b01036

Reference26 articles.

1. Transition-state stabilization at the oxyanion binding sites of serine and thiol proteinases: hydrolyses of thiono and oxygen esters

2. The behaviour of leucine aminopeptidase towards thionopeptides

3. Peptidyl thioamides as substrates and inhibitors of papain, and as probes of the kinetic significance of the oxyanion hole

4. A thioamide substrate of carboxypeptidase A

5. Thioamide substrate probes of metal-substrate interactions in carboxypeptidase a catalysis

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