Results 51 to 60 of about 45,317 (203)

Thioredoxin and Its Reductase Are Present on Synaptic Vesicles, and Their Inhibition Prevents the Paralysis Induced by Botulinum Neurotoxins

Cell Reports, 2014
Botulinum neurotoxins consist of a metalloprotease linked via a conserved interchain disulfide bond to a heavy chain responsible for neurospecific binding and translocation of the enzymatic domain in the nerve terminal cytosol.
Marco Pirazzini, Domenico Azarnia Tehran, Giulia Zanetti, Aram Megighian, Michele Scorzeto, Silvia Fillo, Clifford C. Shone, Thomas Binz, Ornella Rossetto, Florigio Lista, Cesare Montecucco   +10 more
doaj   +1 more source

Binuclear Copper‐Dependent Oxidative Enzymes Involved in Fungal Natural Product Modifications

Journal of the Chinese Chemical Society, EarlyView.
This article summarizes recent biochemical characterizations of a new enzyme family named by the authors as binuclear copper‐dependent oxidative enzymes (BiNCOs). Found in fungal natural product biosynthesis, BiNCOs catalyze diverse CH functionalization reactions, including C(sp3)H halogenation, C(sp3)H hydroxylation, C(sp3)O macrocyclization, and ...
Chen‐Yu Chiang, Masao Ohashi, Yi Tang
wiley   +1 more source

Purification of thioredoxin, thioredoxin reductase, and glutathione reductase by affinity chromatography.

Journal of Biological Chemistry, 1977
A scheme is described for the large scale purification of thioredoxin, thioredoxin reductase, and glutathione reductase. The scheme is based on an initial separation of thioredoxin from the two reductases by affinity chromatography on agarose-bound N6-(6-aminohexyl)-adenosine 2',5'-bisphosphate (agarose-2',5'-ADP).
V P, Pigiet, R R, Conley
openaire   +2 more sources

Peptide‐based responsive molecular fluorescent probes for precision oncology

Responsive Materials, EarlyView.
Peptide‐based responsive fluorescent probes have emerged as adaptive functional materials for precision tumor theranostics, combining tumor‐selective recognition, programmable stimulus responsiveness, and modular tunability. They enable high‐contrast imaging, intraoperative guidance, real‐time monitoring, and multimodal applications, while next ...
Xing Wang, Wen Liu, Jiahao Zhang, Wanqi Wang, Zhicheng Jin, Yuqi Tang, Quan Li   +6 more
wiley   +1 more source

Methylglyoxal Causes Dysfunction of Thioredoxin and Thioredoxin Reductase in Endothelial Cells

Journal of Pharmacological Sciences, 2009
Methylglyoxal (MG), a reactive dicarbonyl produced during glucose metabolism, induces oxidative stress and apoptosis. Under hyperglycemic conditions, the abnormal accumulation of MG is related to the development of diabetic complications. We examined the
Ryosuke Tatsunami, Tatsuya Oba, Kyohei Takahashi, Yoshiko Tampo   +3 more
doaj   +1 more source

Acetylated Thioredoxin Reductase 1 Resists Oxidative Inactivation

Frontiers in Chemistry, 2021
Thioredoxin Reductase 1 (TrxR1) is an enzyme that protects human cells against reactive oxygen species generated during oxidative stress or in response to chemotherapies. Acetylation of TrxR1 is associated with oxidative stress, but the function of TrxR1
David. E. Wright, Nikolaus Panaseiko, Patrick O’Donoghue, Patrick O’Donoghue   +3 more
doaj   +1 more source

News and views on thioredoxin reductases

Redox Report, 1999
(1999). News and views on thioredoxin reductases. Redox Report: Vol. 4, No. 5, pp. 221-228.
S, Gromer, R H, Schirmer, K, Becker
openaire   +2 more sources

ER proteostasis meets mitochondrial function: contact sites as hubs of communication and therapeutic targets

The FEBS Journal, EarlyView.
Proteostasis ensures proper protein folding, modification, and degradation, while its impairment triggers ER stress. Chronic ER stress and maladaptive UPR via the CHOP–ERO1 axis remodel ERMCs, altering calcium signaling and mitochondrial metabolism.
Giorgia Maria Renna, Alessandro Cherubini, Ersilia Varone, Serena Germani, Alice Marrazza, Ester Zito   +5 more
wiley   +1 more source

Thioredoxin–thioredoxin reductase – a system that has come of age [PDF]

European Journal of Biochemistry, 2000
‹12 000 protein having a redoxactive disulfide; thioredoxin was the name assigned to thisprotein [4]. It was shown that thioredoxin was reduced bythioredoxin reductase in a NADPH-dependent reaction and thatin its dithiol form, thioredoxin served as the reductant ofribonucleotides via a ribonucleotide reductase.
openaire   +3 more sources

Ubiquitin and ubiquitin‐like modifications in the endoplasmic reticulum stress response

The FEBS Journal, EarlyView.
Endoplasmic reticulum (ER) stress activates various proteostasis control processes, including the unfolded protein response, ribosome‐associated quality control, and ER‐associated degradation. Ubiquitin and ubiquitin‐like modifications dynamically regulate these processes to determine cell fate, promoting adaptation or inducing cell death.
Tony Avril, Matthieu Le Gallo, Elodie Lafont   +2 more
wiley   +1 more source