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The sigma-1 receptor protects against cellular oxidative stress and activates antioxidant response elements.
Biophysical Characterization of the Interaction Domains and Mapping of the Contact Residues in the XPF-ERCC1 Complex*
- Yun-Jeong Choi, K. Ryu, Byong-Seok Choi
- Biology, ChemistryJournal of Biological Chemistry
- 5 August 2005
The cross-saturation data and the crystal structure of related proteins to model the two complexes revealed that XPF interacts with ERCC1 mainly through hydrophobic interactions, and XPF-EB was also shown to homodimerize in the absence of ER CC1.
Lipid Binding Ridge on Loops 2 and 3 of the C2A Domain of Synaptotagmin I as Revealed by NMR Spectroscopy*
- Y. Chae, F. Abildgaard, E. Chapman, J. Markley
- Chemistry, BiologyThe Journal of Biological Chemistry
- 2 October 1998
The results show that the “docking ridge” responsible for Ca2+-dependent membrane association is localized on the opposite side of the C2A domain from the transmembrane and C2B domains of synaptotagmin.
NMR solution structure of ATTp, an Arabidopsis thaliana trypsin inhibitor.
The overall fold of ATT(p) is distinct from those of other classes of serine proteinase inhibitors except in the inhibitor loop; therefore, it represents a new inhibitor fold.
Structure-function relationships in Anabaena ferredoxin: correlations between X-ray crystal structures, reduction potentials, and rate constants of electron transfer to ferredoxin:NADP+ reductase for…
It is concluded that nonconservative mutations of three critical residues (S47, F65, and E94) on the surface of ferredoxin have large parallel effects on both the reduction potential and the electron-transfer reactivity of the [2Fe-2S] cluster, thereby making electron transfer thermodynamically feasible.
Structure-function studies of [2Fe-2S] ferredoxins
- H. Holden, B. Jacobson, J. Markley
- Chemistry, BiologyJournal of bioenergetics and biomembranes
- 1 February 1994
Results have shown that serine can replace cysteine at each of the four cluster attachment sites and still support cluster assembly, and electron transfer has been demonstrated with three of theFour vegetative ferredoxin mutants.
Solution structure of the toluene 4-monooxygenase effector protein (T4moD).
The specificity of T4moD as an effector protein was investigated by replacing it in reconstituted T4MO complexes with effector proteins from monooxygenases from other bacterial species by refined through simulated annealing by molecular dynamics in torsion angle space.
Acquisition of heat shock tolerance by regulation of intracellular redox states.
The native metastability and misfolding of serine protease inhibitors.
In a survey of deficient serpin mutants, various folding defects, such as retarded protein folding, destabilized native conformation, and spontaneous conversion into more stable, inactive conformations such as the latent form and loop-sheet polymers, have been discovered.
Amino acid residues in Anabaena ferredoxin crucial to interaction with ferredoxin-NADP+ reductase: site-directed mutagenesis and laser flash photolysis.
Spectroscopic and thermodynamic measurements with both the E94 and F65 mutants indicated that the kinetic differences cannot be ascribed to changes in gross conformation, redox potential, or FNR binding constant but rather reflect the protein-protein interactions that control electron transfer.