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The Journal of Biological Chemistry|June 15, 2016
A Supercomplex Spanning the Inner and Outer Membranes Mediates the Biogenesis of β-Barrel Outer Membrane Proteins in BacteriaYan Wang, Rui Wang, Feng Jin, et al.
Biochemical and Biophysical Research Communications|October 3, 2003
Small heat shock protein Hsp16.3 modulates its chaperone activity by adjusting the rate of oligomeric dissociationXinmiao Fu, Chong Liu, Yang Liu, et al.
The Journal of Biological Chemistry|March 15, 2013
Small heat shock protein IbpB acts as a robust chaperone in living cells by hierarchically activating its multi-type substrate-binding residuesXinmiao Fu, Xiaodong Shi, Linxiang Yin, et al.
ACS Infectious Diseases|March 24, 2023
CCCP Facilitates Aminoglycoside to Kill Late Stationary-Phase <i>Escherichia coli</i> by Elevating Hydroxyl RadicalZhongyan Li, Ling Wu, Zhijie Huang, et al.
Journal of Bacteriology|November 26, 2013
Identification of FkpA as a key quality control factor for the biogenesis of outer membrane proteins under heat shock conditionsXi Ge, Zhi-Xin Lyu, Yang Liu, et al.
Biochemical and Biophysical Research Communications|March 16, 2019
Subunit interactions as mediated by "non-interface" residues in living cells for multiple homo-oligomeric proteinsXinmiao Fu, Yan Wang, Xinwen Song, et al.
The Biochemical Journal|July 4, 2012
PDIp is a major intracellular oestrogen-storage protein that modulates tissue levels of oestrogen in the pancreasXinmiao Fu, Pan Wang, Masayuki Fukui, et al.
Proceedings of the National Academy of Sciences of the United States of America|October 7, 2006
The plasma membrane Na+/H+ antiporter SOS1 interacts with RCD1 and functions in oxidative stress tolerance in ArabidopsisSurekha Katiyar-Agarwal, Jianhua Zhu, Kangmin Kim, et al.
Journal of Bacteriology|March 25, 2014
A small heat shock protein enables Escherichia coli to grow at a lethal temperature of 50°C conceivably by maintaining cell envelope integrityAnastasia N Ezemaduka, Jiayu Yu, Xiaodong Shi, et al.
The Journal of Biological Chemistry|May 25, 2005
Periplasmic protein HdeA exhibits chaperone-like activity exclusively within stomach pH range by transforming into disordered conformationWeizhe Hong, Wangwang Jiao, Jicheng Hu, et al.
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