Results 41 to 50 of about 10,696 (83)

Host–parasite oxidative arms race: who will win?

Journal of Avian Biology, Volume 2026, Issue 1, January 2026.
Avian haemosporidian parasites are globally widespread with a broad repertoire of hosts. When infected, the host can either reduce (resistance) and/or limit the severity of parasitaemia (tolerance). Oxidative stress plays a pivotal role in the host's resistance and tolerance, as well as its detrimental endpoints.
Caroline Isaksson, Vaidas Palinauskas, Amparo Herrera Duenas, Olof Hellgren   +3 more
wiley   +1 more source

Elucidation of Sulforaphane‐Mediated Effects on the Cellular Human Metabolome Using Metabolic Profiling

Molecular Nutrition &Food Research, Volume 70, Issue 1, January 2026.
Sulforaphane (SFN) is an isothiocyanate derived from broccoli and is related to various health‐promoting effects. By using metabolic profiling on the hepatoblastoma cell line HepG2 several effects on pathways such as TCA cycle, urea cycle and redox metabolism through SFN were identified.
Nadine Bieß, Hans‐Ulrich Humpf, Matthias Behrens, Andrea Gerdemann   +3 more
wiley   +1 more source

Structural and functional specialization of Bordetella pertussis DsbA for pertussis toxin folding

Protein Science, Volume 35, Issue 1, January 2026.
Abstract Disulphide bonds (Dsbs) are essential for the folding, stability, and function of many secreted and membrane‐associated proteins in bacteria. In Gram‐negative species, these bonds are introduced by the Dsb enzyme family, with DsbA acting as the primary thiol oxidase.
Stephanie Penning, Lachlan Mitchell, Yaoqin Hong, Taylor Cunliffe, Pramod Subedi, Geqing Wang, Lilian Hor, Makrina Totsika, Jason J. Paxman, Begoña Heras   +9 more
wiley   +1 more source

A Ferredoxin Disulfide Reductase Delivers Electrons to the to the Methanosarcina barkeri Class III Ribonucleotide Reductase [PDF]

, 2015
Two subtypes of class III anaerobic ribonucleotide reductases (RNRs) studied so far couple the reduction of ribonucleotides to the oxidation of formate, or the oxidation of NADPH via thioredoxin and thioredoxin reductase.
Elliott, Sean J., Ferry, James G., Li, Bin, Prakash, Divya, Stubbe, JoAnne, Wei, Yifeng   +5 more
core   +2 more sources

Genomic and Phenotypic Bases of Salt Tolerance in Sinorhizobium meliloti: Candidate Traits for Bioinoculant Development Addressing Saline Soils

Microbial Biotechnology, Volume 19, Issue 1, January 2026.
Genome‐wide association analysis on 49 Sinorhizobium meliloti strains (21 de novo sequenced) reveals extensive phenotypic heterogeneity in salt tolerance, closely associated with quorum sensing, cell surface stability and adaptation. Salt‐tolerant strains exhibit a wider metabolic capacity, especially in carbon sources exploitation, underscoring their ...
Agnese Bellabarba, Camilla Fagorzi, Giovanni Bacci, Francesca Decorosi, Alice Checcucci, Gaio Cesare Pacini, Abdelkader Bekki, Amina El Hadj Mimoune, Khalid Azim, Majida Hafidi, Alessio Mengoni, Francesco Pini, Carlo Viti   +12 more
wiley   +1 more source

NRF2 signalling in cytoprotection and metabolism

British Journal of Pharmacology, Volume 183, Issue 1, Page 101-114, January 2026.
The KEAP1‐NRF2 system plays a central role in cytoprotection in defence mechanisms against oxidative stress. The KEAP1‐NRF2 system has been regarded as a sulfur‐utilizing cytoprotective mechanism, because KEAP1 serves as a biosensor for electrophiles by using its reactive thiols and NRF2 is a transcriptional factor regulating genes involved in sulfur ...
Shohei Murakami, Yusuke Kusano, Keito Okazaki, Takaaki Akaike, Hozumi Motohashi   +4 more
wiley   +1 more source

Expression of active human sialyltransferase ST6GalNAcI in Escherichia coli [PDF]

, 2009
Georgios Skretas, Sean Carroll, and George Georgiou are with the Department of Chemical Engineering, University of Texas at Austin, Austin, TX 78712, USA -- George Georgiou is with the Department of Biomedical Engineering, University of Texas at Austin ...
Carroll, Sean, DeFrees, Shawn, Georgiou, George, Johnson, Karl F., Schwartz, Marc F., Skretas, Georgios   +5 more
core   +3 more sources

Mechanism of cyanobacterial ferredoxin‐dependent flavin thioredoxin reductase reveals thiolate‐FAD charge transfer and catalytic asymmetry in a homodimer

The FEBS Journal, Volume 293, Issue 1, Page 96-112, January 2026.
Ferredoxin‐dependent flavin thioredoxin reductases (FFTRs) regenerate reduced thioredoxin, sustaining dithiol–disulfide exchange reactions that regulate protein activity in select organisms. In cyanobacterial FFTRs, we describe the formation of a thiolate–flavin charge transfer complex, asynchronous reduction of the two FAD cofactors within the ...
Martha Minjarez‐Saenz, Víctor Correa‐Pérez, Maribel Rivero, Alejandro Hernández‐Gómez, Marta Martínez‐Júlvez, Rubén M. Buey, Federico Gago, Monica Balsera, Milagros Medina   +8 more
wiley   +1 more source

The structure of Lactococcus lactis thioredoxin reductase reveals molecular features of photo-oxidative damage [PDF]

, 2017
The NADPH-dependent homodimeric flavoenzyme thioredoxin reductase (TrxR) provides reducing equivalents to thioredoxin, a key regulator of various cellular redox processes. Crystal structures of photo-inactivated thioredoxin reductase (TrxR) from the Gram-
Bang, Maria Blanner, Björnberg, Olof, Davies, Michael J., Harris, Pernille, Hägglund, Per, Rykær, Martin, Skjoldager, Nicklas, Svensson, Birte   +7 more
core   +2 more sources

Thioredoxin reductase as a target enzyme for electrophilic anticancer drugs [PDF]

, 2011
Induced production of reactive oxygen species (ROS) is a common attribute of most cancer cells. One strategy for cancer cells to maneuver the increased and potentially toxic levels of ROS is to induce the expression of cellular antioxidants and ...
Eriksson, Sofi
core   +1 more source