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Methemoglobin reduction mediated by d-amino acid dehydrogenase in Propsilocerus akamusi (Tokunaga) larvae.

Kobori H1, Tanigawa M1, Maeda S1, Hori H2, Yubisui T3, Nagata Y4.
Journal of insect physiology.J Insect Physiol.2015 Jun;77:33-8. doi: 10.1016/j.jinsphys.2015.04.002. Epub 2015 Apr 18.
A methemoglobin (metHb) reduction system is required for aerobic respiration. In humans, Fe(III)-heme-bearing metHb (the oxidized form of hemoglobin), which cannot bind oxygen, is converted to Fe(II)-heme-bearing oxyhemoglobin (oxyHb, the reduced form), which can bind oxygen, in a system comprising
PMID 25896287

Role of Cys³⁶⁰² in the function and regulation of the cardiac ryanodine receptor.

Mi T1, Xiao Z1, Guo W1, Tang Y1, Hiess F1, Xiao J1, Wang Y1, Zhang JZ2, Zhang L1, Wang R1, Jones PP2, Chen SR1.
The Biochemical journal.Biochem J.2015 Apr 1;467(1):177-90. doi: 10.1042/BJ20141263.
The cardiac Ca²⁺ release channel [ryanodine receptor type 2 (RyR2)] is modulated by thiol reactive agents, but the molecular basis of RyR2 modulation by thiol reagents is poorly understood. Cys³⁶³⁵ in the skeletal muscle RyR1 is one of the most hyper-reactive thiols and is important for the
PMID 25605235

Resveratrol protects against arsenic trioxide-induced oxidative damage through maintenance of glutathione homeostasis and inhibition of apoptotic progression.

Chen C1, Jiang X, Lai Y, Liu Y, Zhang Z.
Environmental and molecular mutagenesis.Environ Mol Mutagen.2015 Apr;56(3):333-46. doi: 10.1002/em.21919. Epub 2014 Oct 23.
Arsenic trioxide (As2 O3 ) is commonly used to treat acute promyelocytic leukemia and solid tumors. However, the clinical application of the agent is limited by its cyto- and genotoxic effects on normal cells. Thus, relief of As2 O3 toxicity in normal cells is essentially necessary for improvement o
PMID 25339131

Electrostatic charge at position 552 affects the activation and permeation of FMRFamide-gated Na⁺ channels

Crosslinking of Cys-Mutated Human Galectin-1 to the Model Glycoprotein Ligands Asialofetuin and Laminin by Using a Photoactivatable Bifunctional Reagent

Side Chain Orientation of the Amino Acid Substituted by a Cysteine Residue Is Important for Successful Crosslinking of Galectin to Its Glycoprotein Ligand Using a Photoactivatable Sulfhydryl Reagent