Journal article
Thioredoxin A active-site mutants form mixed disulfide dimers that resemble enzyme-substrate reaction intermediates.
- Abstract:
-
Thioredoxin functions in nearly all organisms as the major thiol-disulfide oxidoreductase within the cytosol. Its prime purpose is to maintain cysteine-containing proteins in the reduced state by converting intramolecular disulfide bonds into dithiols in a disulfide exchange reaction. Thioredoxin has been reported to contribute to a wide variety of physiological functions by interacting with specific sets of substrates in different cell types. To investigate the function of the essential thio...
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- Publication status:
- Published
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- Publisher copy:
- 10.1016/j.jmb.2008.03.077
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Bibliographic Details
- Journal:
- Journal of molecular biology
- Volume:
- 379
- Issue:
- 3
- Pages:
- 520-534
- Publication date:
- 2008-06-05
- DOI:
- EISSN:
-
1089-8638
- ISSN:
-
0022-2836
- URN:
-
uuid:65674f77-5bb5-4f55-a0e8-623ab67913c3
- Source identifiers:
-
72812
- Local pid:
- pubs:72812
Item Description
Terms of use
- Copyright date:
- 2008
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