scholarly journals Atypical Thioredoxins in Poplar: The Glutathione-Dependent Thioredoxin-Like 2.1 Supports the Activity of Target Enzymes Possessing a Single Redox Active Cysteine

2012 ◽  
Vol 159 (2) ◽  
pp. 592-605 ◽  
Author(s):  
Kamel Chibani ◽  
Lionel Tarrago ◽  
José Manuel Gualberto ◽  
Gunnar Wingsle ◽  
Pascal Rey ◽  
...  
Keyword(s):  
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 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
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