Basis for using thioredoxin as an electron donor by Schizosaccharomyces pombe Gpx1 and Tpx1
AMB Express, 2022 Key points spGpx1 contains two conserved Cys residues (Cys36 and Cys82), which may form a disulfide bond upon oxidation and the reduction of this disulfide bond is most likely to be mediated by Trx in vivo.
Fawad Ahmad +3 more
doaj +1 more source
Redox Potentials of Disulfide Bonds in LOXL2 Studied by Nonequilibrium Alchemical Simulation
Frontiers in Chemistry, 2021 Lysyl oxidase-like 2 (LOXL2) is a metalloenzyme that catalyzes the oxidative deamination ε-amino group of lysine. It is found that LOXL2 is a promotor for the metastasis and invasion of cancer cells. Disulfide bonds are important components in LOXL2, and
Lirui Lin +10 more
doaj +1 more source
The role of a disulfide bridge in the stability and folding kinetics of Arabidopsis thaliana cytochrome c6A [PDF]
, 2011 Cytochrome c 6A is a eukaryotic member of the Class I cytochrome c family possessing a high structural homology with photosynthetic cytochrome c 6 from cyanobacteria, but structurally and functionally distinct through the presence of a disulfide bond and
Arslan +64 more
core +1 more source
Mechanisms and energetics of free radical initiated disulfide bond cleavage in model peptides and insulin by mass spectrometry [PDF]
, 2015 We investigate the mechanism of disulfide bond cleavage in gaseous peptide and protein ions initiated by a covalently-attached regiospecific acetyl radical using mass spectrometry (MS).
Beauchamp, J. L. +5 more
core +2 more sources
Measurement of Redox States of the β3 Integrin Disulfide Bonds by Mass Spectrometry
Bio-Protocol, 2019 Functional disulfide bonds mediate a change in protein function in which they reside when cleaved or formed. To elucidate how a functional disulfide bond controls protein activity, it is critical that the redox state of the bond in the population of ...
Joyce Chiu
doaj +1 more source
Engineering a disulfide bond in the lid hinge region of Rhizopus chinensis lipase: increased thermostability and altered acyl chain length specificity. [PDF]
PLoS ONE, 2012 The key to enzyme function is the maintenance of an appropriate balance between molecular stability and structural flexibility. The lid domain which is very important for "interfacial activation" is the most flexible part in the lipase structure. In this
Xiao-Wei Yu +3 more
doaj +1 more source
Albumin nanoparticles for glutathione-responsive release of cisplatin: new opportunities for medulloblastoma treatment [PDF]
, 2016 Redox-responsive nanoparticles were synthesized by desolvation of bovine serum albumin followed by disulfide-bond crosslinking with N, Nʹ-Bis (acryloyl) cystamine. Dynamic light scattering and transmission electron microscopy studies revealed spherical
Abballe, Luana +9 more
core +1 more source
TREATMENT OF DISULFIDE BONDS IN COARSE-GRAINED UNRES FORCE FIELD
TASK Quarterly, 2016 Disulfide bonds, despite the advances of the computational methods, are underrepresented in theoretical chemistry and the role of disulfide bonds is often diminished in bioinformatical studies.
PAWEŁ KRUPA
doaj +1 more source
IUCrJ, 2020 Radiation-induced damage to protein crystals during X-ray diffraction data collection is a major impediment to obtaining accurate structural information on macromolecules.
Rajasri Bhattacharyya +4 more
doaj +1 more source
Interleukin-2 signalling is modulated by a labile disulfide bond in the CD132 chain of its receptor [PDF]
Open Biology, 2012 Certain disulfide bonds present in leucocyte membrane proteins are labile and can be reduced in inflammation. This can cause structural changes that result in downstream functional effects, for example, in integrin activation.
Clive Metcalfe +2 more
doaj +1 more source