The cxxc motif at the n terminus of an α‐helical peptide.

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1. Constitutively oxidized cxxc motifs within the cd3.
2. A functional mimic of protein disulfide isomerase.
3. New concepts in biochemistry the cxxc motif.
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5. Identification of a peroxidesensitive redox switch at the.
6. It was found that altering the cxxc motif affected not only the reduction potential of the protein, but also its ability to function as a disulfide.
7. A,b recombinant wildtype cse was incubated with 10 mm dtt, 5 mm oxidized dtt dttoxi.
8. Hbcatm would be consistent with the apparent loss of tnb from dtnb.
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10. Cxxcxxc motif, which has been postulated to have redox activity because it resembles the cxxc thioredox inlike motif of.
11. Proteindisulfide isomerase.
12. By ma wouters 2010 cited by 289 — some characterized redoxactive disulfides are the helical cxxc motif, often associated with thioredoxinfold proteins.
13. Table 2 from the cxxc motif is more than a redox rheostat.
14. It was found that altering the cxxc motif affected not only the reduction potential of the protein, but also its ability to function as a disulfide.
15. Redox reactions involving thiol groups in proteins are major participants in cellular redox regulation and antioxidant defense.
16. It was found that altering the cxxc motif affected not only the reduction potential of the protein, but also its ability to function as a disulfide.
17. By s quan 2007 cited by 177 — the cxxc activesite motif of thioldisulfide oxidoreductases is thought to act as a redox rheostat, the sequence of which determines its reduction potential.
18. Cxxcxxc motif, which has been postulated to have redox activity because it resembles the cxxc thioredox inlike motif of.
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20. Proteindisulfide isomerase.
21. It was found that altering the cxxc motif affected not only the reduction potential of the protein, but also its ability to function as a disulfide.
22. Different contributions of the three cxxc motifs of human.
23. Journal of biological chemistry cxxs fold‐independent redox motif revealed by genome‐wide searches for thiol.
24. The bcat1 cxxc motif provides protection against ros.
25. Cxxcxxc motif, which has been postulated to have redox activity because it resembles the cxxc thioredox inlike motif of.
26. Cxxs foldindependent redox motif revealed by genome.
27. Coli, glutathione peroxidase.
28. Disulfides as redox switches from molecular.
29. The bcat1 cxxc motif provides protection against ros.
30. Constitutively oxidized cxxc motifs within the cd3.
31. And forbidden disulfides, a group of.
32. An active site containing a cxxc motif is always found in the thioldisulphide oxidoreductase superfamily.
33. By ma wouters 2010 cited by 289 — some characterized redoxactive disulfides are the helical cxxc motif, often associated with thioredoxinfold proteins.
34. And forbidden disulfides, a group of.
35. Different contributions of the three cxxc motifs of human.
36. The cxxc motif is more than a redox rheostat.
37. By ma wouters 2010 cited by 289 — some characterized redoxactive disulfides are the helical cxxc motif, often associated with thioredoxinfold proteins.
38. A functional mimic of protein disulfide isomerase.
39. Thus, the intramolecular disulfide bond formed by the cd3 cxxc motif may function.
40. The bcat1 cxxc motif provides protection against ros.
41. It was found that altering the cxxc motif affected not only the reduction potential of the protein, but also its ability to function as a disulfide.
42. By am benham 2000 cited by 173 — ero1la contains the conserved.
43. By s quan 2007 cited by 177 — the cxxc activesite motif of thioldisulfide oxidoreductases is thought to act as a redox rheostat, the sequence of which determines its reduction potential.
44. An active site containing a cxxc motif is always found in the thioldisulphide oxidoreductase superfamily.
45. New concepts in biochemistry the cxxc motif.
46. By pt chivers 1997 cited by 337 — the cysxaaxaacys cxxc1 motif of thioldisulfide oxidoreductases is essential for their catalysis of redox reactions laboissie`re et al.
47. It was found that altering the cxxc motif affected not only the reduction potential of the protein, but also its ability to function as a disulfide.
48. Journal of biological chemistry cxxs fold‐independent redox motif revealed by genome‐wide searches for thiol.
49. Thus, the intramolecular disulfide bond formed by the cd3 cxxc motif may function.