scholarly journals Signal transduction by the global regulator RegB is mediated by a redox-active cysteine

2003 ◽  
Vol 22 (18) ◽  
pp. 4699-4708 ◽  
Author(s):  
L. R. Swem
Keyword(s):  
Signal Transduction ◽  
Global Regulator ◽  
Redox Active ◽  
Redox Active Cysteine

scholarly journals Novel Oxidative Modifications in Redox-Active Cysteine Residues

2010 ◽  
Vol 10 (3) ◽  
pp. M110.000513 ◽  
Author(s):  
Jaeho Jeong ◽  
Yongsik Jung ◽  
Seungjin Na ◽  
Jihye Jeong ◽  
Eunsun Lee ◽  
...  
Keyword(s):  
Cysteine Residues ◽  
Redox Active ◽  
Oxidative Modifications ◽  
Redox Active Cysteine

scholarly journals Enhanced Voltammetric Anion Sensing at Halogen and Hydrogen Bonding Ferrocenyl SAMs

2020 ◽  
Author(s):  
Robert Hein ◽  
Xiaoxiong Li ◽  
Paul D. Beer ◽  
Jason J Davis
Keyword(s):  
Signal Transduction ◽  
Hydrogen Bonding ◽  
Real Life ◽  
Halogen Bonding ◽  
Self Assembled Monolayers ◽  
Similar Response ◽  
Binding Motifs ◽  
Anion Sensing ◽  
Redox Active ◽  
Assembled Monolayers

Halogen bonding mediated electrochemical anion sensing has very recently been established as a potent platform for the selective and sensitive detection of anions, although the principles that govern binding and subsequent signal transduction remain poorly understood. Herein we address this challenge by providing a comprehensive study of novel redox-active halogen bonding (XB) and hydrogen bonding (HB) ferrocene-isophthalamide-(iodo)triazole receptors in solution and at self-assembled monolayers (SAMs). Under diffusive conditions the sensory performance of the XB sensor was significantly superior. In molecular films the XB and HB binding motifs both display a notably enhanced, but similar, response to specific anions. Importantly, the enhanced response of these films is rationalised by a consideration of the (interfacial) dielectric microenvironment. These effects, and the resolved relationship between anion binding and signal transduction, underpin an improved fundamental understanding of anion sensing at redox-active interfaces which will benefit not just the development of more potent, real-life relevant sensors, but also new tools to study host-guest interactions at interfaces.

scholarly journals High-Throughput Identification of Catalytic Redox-Active Cysteine Residues

Science ◽  
2007 ◽  
Vol 315 (5810) ◽  
pp. 387-389 ◽  
Author(s):  
D. E. Fomenko ◽  
W. Xing ◽  
B. M. Adair ◽  
D. J. Thomas ◽  
V. N. Gladyshev
Keyword(s):  
High Throughput ◽  
Cysteine Residues ◽  
Redox Active ◽  
Redox Active Cysteine

scholarly journals Accelerated corrosion of marine-grade steel by a redox-active, cysteine-rich barnacle cement protein

2020 ◽  
Vol 4 (1) ◽  
Author(s):  
Vinod K. Murugan ◽  
Harini Mohanram ◽  
Maja Budanovic ◽  
Arvind Latchou ◽  
Richard David Webster ◽  
...  
Keyword(s):  
Accelerated Corrosion ◽  
Redox Active ◽  
Cement Protein ◽  
Grade Steel ◽  
Barnacle Cement ◽  
Redox Active Cysteine

scholarly journals Intramolecular quality control: HIV-1 Envelope gp160 signal-peptide cleavage as a functional folding checkpoint

2020 ◽  
Author(s):  
Nicholas McCaul ◽  
Matthias Quandte ◽  
Ilja Bontjer ◽  
Guus van Zadelhoff ◽  
Aafke Land ◽  
...  
Keyword(s):  
Quality Control ◽  
Signal Peptide ◽  
Protein Biosynthesis ◽  
Protein Structures ◽  
Secretory Protein ◽  
Viral Fitness ◽  
Secretory Proteins ◽  
Redox Active ◽  
Hiv 1 ◽  
Redox Active Cysteine

SummaryRemoval of the membrane-tethering signal peptides that target secretory proteins to the endoplasmic reticulum is a prerequisite for proper folding. While generally thought to be removed well before translation termination, we here report two novel post-targeting functions for the HIV-1 gp120 signal peptide, which remains attached until gp120 folding triggers its removal. First, the signal peptide improves fidelity of folding by enhancing conformational plasticity of gp120 by driving disulfide isomerization through a redox-active cysteine, at the same time delaying folding by tethering the N-terminus to the membrane, which needs assembly with the C-terminus. Second, its carefully timed cleavage represents intramolecular quality control and ensures release and stabilization of (only) natively folded gp120. Postponed cleavage and the redox-active cysteine both are highly conserved and important for viral fitness. Considering the ∼15% secretory proteins in our genome and the frequency of N-to-C contacts in protein structures, these regulatory roles of the signal peptide are bound to be more common in secretory-protein biosynthesis.

scholarly journals A “Seleno Effect” Differentiates the Roles of Redox Active Cysteine Residues in Plasmodium falciparum Thioredoxin Reductase

Biochemistry ◽  
2018 ◽  
Vol 57 (11) ◽  
pp. 1767-1778 ◽  
Author(s):  
John P. O’Keefe ◽  
Christopher M. Dustin ◽  
Drew Barber ◽  
Gregg W. Snider ◽  
Robert J. Hondal
Keyword(s):  
Plasmodium Falciparum ◽  
Thioredoxin Reductase ◽  
Cysteine Residues ◽  
Redox Active ◽  
Redox Active Cysteine

scholarly journals Crystal Structures of the Reduced, Sulfenic Acid, and Mixed Disulfide Forms of SarZ, a Redox Active Global Regulator inStaphylococcus aureus

2009 ◽  
Vol 284 (35) ◽  
pp. 23517-23524 ◽  
Author(s):  
Catherine B. Poor ◽  
Peng R. Chen ◽  
Erica Duguid ◽  
Phoebe A. Rice ◽  
Chuan He
Keyword(s):  
Crystal Structures ◽  
Global Regulator ◽  
Sulfenic Acid ◽  
Mixed Disulfide ◽  
Redox Active
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