Results 1 to 10 of about 19,795 (176)

NAD(P)H-dependent thioredoxin-disulfide reductase TrxR is essential for tellurite and selenite reduction and resistance in Bacillus sp. Y3

FEMS Microbiology Ecology, 2020
ABSTRACTMicrobial reduction of selenite [Se(IV)] and tellurite [Te(IV)] to Se(0) and Te(0) can function as a detoxification mechanism and serve in energy conservation. In this study, Bacillus sp. Y3 was isolated and demonstrated to have an ability of simultaneous reduction of Se(IV) and Te(IV) during aerobic cultivation, with reduction efficiencies of ...
Muhammad Yasir, Gejiao Wang, Zhang Yuxiao   +2 more
exaly   +3 more sources

The Cellular Thioredoxin-1/Thioredoxin Reductase-1 Driven Oxidoreduction Represents a Chemotherapeutic Target for HIV-1 Entry Inhibition. [PDF]

PLoS ONE, 2016
BACKGROUND:The entry of HIV into its host cell is an interesting target for chemotherapeutic intervention in the life-cycle of the virus. During entry, reduction of disulfide bridges in the viral envelope glycoprotein gp120 by cellular oxidoreductases is
Kathrin Reiser, Leen Mathys, Sophie Curbo, Christophe Pannecouque, Sam Noppen, Sandra Liekens, Lars Engman, Mathias Lundberg, Jan Balzarini, Anna Karlsson   +9 more
doaj   +2 more sources

Intracellular free radical scavenging activity and protective role of mammalian cells by antioxidant peptide from thioredoxin disulfide reductase of Arthrospira platensis

Journal of Functional Foods, 2019
In this study, we have analyzed the antioxidant role of thioredoxin disulfide reductase (TR) identified from Arthrospira platensis (Ap). A short peptide (VH12) derived from thioredoxin domain between Val368 and His379 of ApTR and it named as VH12. The peptide expressed the antioxidant activity against hydroxyl radical and superoxide radical at the ...
Anbazahan Sannasimuthu, Jesú Arockiaraj   +1 more
exaly   +3 more sources

Structural basis of ligand selectivity in FAD/NAD(P)H-dependent dehydrogenases: insights from trypanothione reductase and type II NADH dehydrogenase. [PDF]

Protein Sci
Abstract FAD/NAD(P)H‐dependent dehydrogenases form a structurally conserved family of redox enzymes that participate in essential metabolic processes across parasites and higher organisms. Among them, trypanothione reductase (TR) is a key component of the redox metabolism of Leishmania species and represents an attractive target for antileishmanial ...
Perrone GCM, Spadone S, Francavilla AL, Morselli S, Todisco S, Ortalli M, Mendoza-Roldan JA, Scaglione V, Sgobba MN, Guerra L, Belluti F, Varani S, Otranto D, De Grassi A, Volpicella M, Pierri CL.   +15 more
europepmc   +2 more sources

A Fluorescent Probe to Detect Quick Disulfide Reductase Activity in Bacteria

Antioxidants, 2022
The Trx and Grx systems, two disulfide reductase systems, play critical roles in various cell activities. There are great differences between the thiol redox systems in prokaryotes and mammals.
Ying Zhao, Xin Zuo, Shuang Liu, Wenjun Qian, Xuewen Tang, Jun Lu   +5 more
doaj   +2 more sources

Cell surface thiol-disulfide regulation in cancer: Mechanisms, implications, and theranostic strategies [PDF]

Redox Biology
Redox homeostasis is frequently disrupted in cancer and contributes to tumor progression, metastasis, and therapy resistance. This review focuses on how thioredoxin-1 (TXN1), thioredoxin reductase-1 (TXNRD1), and members of the protein disulfide ...
Jost Lühle, Peter H. Seeberger, Oren Moscovitz   +2 more
doaj   +2 more sources

Redox signals and oxidative stress in the control of mitochondrial protein import. [PDF]

Protein Sci
Abstract Mitochondrial protein import is essential for organelle biogenesis and cellular homeostasis. It operates in an environment that is intrinsically shaped by redox chemistry. Mitochondria are major sources of reactive oxygen species (ROS), which arise as by‐products of oxidative phosphorylation. Cells therefore maintain sophisticated ROS‐handling
Hasberg L, Lauterbach VK, Ochsenreiter T, Riemer J.   +3 more
europepmc   +2 more sources

Identification and functional characterization of a novel thioredoxin MpTRX1 from Metschnikowia persimmonesis [PDF]

Applied Microbiology and Biotechnology
Thioredoxins (TRXs) are small, conserved redox-active proteins that play central roles in oxidative stress responses. Here, we identified and functionally characterized a novel thioredoxin, MpTRX1, from the newly isolated yeast Metschnikowia ...
Chang Ho Kang, Jae Hyeok Lee, Yeong Min Lee, Yong Bok Lee, Youngmin Kang, Yeongjun Ban, Ariranur Haniffadli, Endang Rahmat, Chae Oh Lim   +8 more
doaj   +2 more sources

The Bacillus subtilis monothiol bacilliredoxin BrxC (YtxJ) and the Bdr (YpdA) disulfide reductase reduce S-bacillithiolated proteins

Redox Biology, 2021
The bacterial cytosol is generally a reducing environment with protein cysteine residues maintained in their thiol form. The low molecular weight thiol bacillithiol (BSH) serves as a general thiol reductant, analogous to glutathione, in a wide range of ...
Ahmed Gaballa, Tina Tianjiao Su, John D. Helmann   +2 more
doaj   +1 more source

TXNL1 has dual functions as a redox active thioredoxin-like protein as well as an ATP- and redox-independent chaperone

Redox Biology, 2023
TXNL1 (also named TRP32, for thioredoxin related protein of 32 kDa) is a cytosolic thioredoxin-fold protein expressed in all cell types and conserved from yeast to mammals, but with yet poorly known function.
Attila Andor, Mahendravarman Mohanraj, Zsuzsanna Anna Pató, Katalin Úri, Beáta Biri-Kovács, Qing Cheng, Elias S.J. Arnér   +6 more
doaj   +1 more source