Bifurcated assembly pathway and dual function of a Lon-like protease revealed by cryo-EM Analysis-Reference-Cited by-同舟云学术

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Bifurcated assembly pathway and dual function of a Lon-like protease revealed by cryo-EM Analysis

Published:2024-04 Issue: Volume: Page:
ISSN:2667-3258
Container-title:Fundamental Research
language:en
Short-container-title:Fundamental Research

Author:

Li Ming,Liu Hongwei,Hsieh Kan-Yen^ORCID,Zhang Shengchun,Gao Yongxiang,Gong Qingguo,Zhang Kaiming^ORCID,Chang Chung-I,Li Shanshan

Publisher

Elsevier BV

Reference18 articles.

1. A Lon-like protease with no ATP-powered unfolding activity;Liao;PLoS ONE,2012

2. Structures of an ATP-independent Lon-like protease and its complexes with covalent inhibitors;Liao;Acta Crystallogr. D,2013

3. The N-terminal substrate-recognition domain of a LonC protease exhibits structural and functional similarity to cytosolic chaperones;Li;Acta Crystallogr. D,2013

4. Characterization of three putative Lon proteases of Thermus thermophilus HB27 and use of their defective mutants as hosts for production of heterologous proteins;Maehara;Extremophiles,2008

5. Complete three-dimensional structures of the Lon protease translocating a protein substrate;Li;Sci. Adv.,2021

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