Directed evolution of cyclic peptides for inhibition of autophagy-Reference-Cited by-同舟云学术

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Directed evolution of cyclic peptides for inhibition of autophagy

Published:2021 Issue:10 Volume:12 Page:3526-3543
ISSN:2041-6520
Container-title:Chemical Science
language:en
Short-container-title:Chem. Sci.

Author:

Gray Joshua P.¹²³^ORCID,Uddin Md. Nasir¹²³,Chaudhari Rajan⁴²³^ORCID,Sutton Margie N.¹²³^ORCID,Yang Hailing⁴²³,Rask Philip⁴²³,Locke Hannah⁵⁶³,Engel Brian J.¹²³,Batistatou Nefeli⁷⁸³,Wang Jing⁷⁸³,Grindel Brian J.¹²³,Bhattacharya Pratip¹²³,Gammon Seth T.¹²³^ORCID,Zhang Shuxing⁴²³^ORCID,Piwnica-Worms David¹²³^ORCID,Kritzer Joshua A.⁷⁸³^ORCID,Lu Zhen⁴²³,Bast Robert C.⁴²³,Millward Steven W.¹²³^ORCID

Affiliation:

1. Department of Cancer Systems Imaging

2. University of Texas MD Anderson Cancer Center

3. USA

4. Department of Experimental Therapeutics

5. Department of Biology and Biochemistry

6. University of Houston

7. Department of Chemistry

8. Tufts University

Abstract

SUPR peptide mRNA display was used to evolve a cell-permeable, macrocyclic peptide for autophagy inhibition.

Funder

National Institute of General Medical Sciences

National Cancer Institute

Cancer Prevention and Research Institute of Texas

National Foundation for Cancer Research

University of Texas at Austin

Anne and Harry Zarrow Foundation

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2021/SC/D0SC03603J

Reference52 articles.

1. Structural basis of FYCO1 and MAP1LC3A interaction reveals a novel binding mode for Atg8-family proteins

2. The machinery of macroautophagy

3. Autophagosome formation: core machinery and adaptations

4. Selective autophagy mediated by autophagic adapter proteins

5. p62/SQSTM1 Binds Directly to Atg8/LC3 to Facilitate Degradation of Ubiquitinated Protein Aggregates by Autophagy

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