Importing mitochondrial proteins: machineries and mechanisms

A Chacinska, CM Koehler, D Milenkovic, T Lithgow… - Cell, 2009 - cell.com
Most mitochondrial proteins are synthesized on cytosolic ribosomes and must be imported
across one or both mitochondrial membranes. There is an amazingly versatile set of …

Redox regulation: a broadening horizon

BB Buchanan, Y Balmer - Annu. Rev. Plant Biol., 2005 - annualreviews.org
Initially discovered in the context of photosynthesis, regulation by change in the redox state
of thiol groups (S− S↔ 2SH) is now known to occur throughout biology. Several systems …

The Rcs phosphorelay: a complex signal transduction system

N Majdalani, S Gottesman - Annu. Rev. Microbiol., 2005 - annualreviews.org
Abstract RcsC, RcsB, and RcsA were first identified as a sensor kinase, a response
regulator, and an auxiliary regulatory protein, respectively, regulating the genes of capsular …

The complex Rcs regulatory cascade

E Wall, N Majdalani, S Gottesman - Annual review of …, 2018 - annualreviews.org
RcsB, a response regulator of the FixJ/NarL family, is at the center of a complex network of
regulatory inputs and outputs. Cell surface stress is sensed by an outer membrane …

Quantifying changes in the thiol redox proteome upon oxidative stress in vivo

LI Leichert, F Gehrke, HV Gudiseva… - Proceedings of the …, 2008 - National Acad Sciences
Antimicrobial levels of reactive oxygen species (ROS) are produced by the mammalian host
defense to kill invading bacteria and limit bacterial colonization. One main in vivo target of …

[HTML][HTML] Exogenous glycine promotes oxidation of glutathione and restores sensitivity of bacterial pathogens to serum-induced cell death

T Kou, J Wu, X Chen, Z Chen, J Zheng, B Peng - Redox Biology, 2022 - Elsevier
Pathogenic strains of bacteria are often highly adept at evading serum-induced cell death,
which is an essential complement-mediated component of the innate immune response …

Disulfide bond formation in prokaryotes

C Landeta, D Boyd, J Beckwith - Nature microbiology, 2018 - nature.com
Interest in protein disulfide bond formation has recently increased because of the prominent
role of disulfide bonds in bacterial virulence and survival. The first discovered pathway that …

Inhibition of mammalian thioredoxin reductase by some flavonoids: implications for myricetin and quercetin anticancer activity

J Lu, LV Papp, J Fang, S Rodriguez-Nieto… - Cancer research, 2006 - AACR
The thioredoxin system, composed of thioredoxin reductase (TrxR), thioredoxin (Trx), and
NADPH, exerts a wide range of activities in cellular redox control, antioxidant function, cell …

[HTML][HTML] Production of disulfide-bonded proteins in Escherichia coli

M Berkmen - Protein expression and purification, 2012 - Elsevier
Disulfide bonds are covalent bonds formed post-translationally by the oxidation of a pair of
cysteines. A disulfide bond can serve structural, catalytic, and signaling roles. However …

DSB proteins and bacterial pathogenicity

B Heras, SR Shouldice, M Totsika… - Nature Reviews …, 2009 - nature.com
If DNA is the information of life, then proteins are the machines of life—but they must be
assembled and correctly folded to function. A key step in the protein-folding pathway is the …