Peer Reviewedhttps://deepblue.lib.umich.edu/bitstream/2027.42/154540/1/fsb2009013004.pd
Human thioredoxin reductase (hTrxR) is a homodimeric flavoprotein crucially involved in the regulati...
SummaryThioredoxin is ubiquitous and regulates various target proteins through disulfide bond reduct...
The high Mr (~55 kDa) thioredoxin reductases (TR) characteristic of higher eukaryotes are members of...
The crystal structure of three forms of Escherichia coli thioredoxin reductase have been refined: th...
Thioredoxin reductase (TRR), a flavoprotein that contains an oxidation-reduction active disulfide, c...
The flavoenzyme thioredoxin reductase catalyzes the reduction of thioredoxin by NADPH. The two activ...
Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/65806/1/j.1432-1327.2000.01702.x.pd
AbstractThe recent high-resolution solution structures of human and Escherichia coli thioredoxin in ...
The enzymatic activity of thioredoxin reductase enzymes is endowed by at least two redox centers: a ...
High-molecular mass thioredoxin reductases (TRs) are pyridine nucleotide disulfide oxidoreductases t...
ABSTRACT: High-molecular mass thioredoxin reductases (TRs) are pyridine nucleotide disulfide oxidore...
Thioredoxin reductase (TrxR) is an essential enzyme required for the efficient maintenance of the ce...
AN example of two related enzymes that catalyse similar reactions but possess different active sites...
AbstractThiol–disulfide oxidoreductase systems of bacterial cytoplasm and eukaryotic cytosol favor r...
Human thioredoxin reductase (hTrxR) is a homodimeric flavoprotein crucially involved in the regulati...
Human thioredoxin reductase (hTrxR) is a homodimeric flavoprotein crucially involved in the regulati...
SummaryThioredoxin is ubiquitous and regulates various target proteins through disulfide bond reduct...
The high Mr (~55 kDa) thioredoxin reductases (TR) characteristic of higher eukaryotes are members of...
The crystal structure of three forms of Escherichia coli thioredoxin reductase have been refined: th...
Thioredoxin reductase (TRR), a flavoprotein that contains an oxidation-reduction active disulfide, c...
The flavoenzyme thioredoxin reductase catalyzes the reduction of thioredoxin by NADPH. The two activ...
Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/65806/1/j.1432-1327.2000.01702.x.pd
AbstractThe recent high-resolution solution structures of human and Escherichia coli thioredoxin in ...
The enzymatic activity of thioredoxin reductase enzymes is endowed by at least two redox centers: a ...
High-molecular mass thioredoxin reductases (TRs) are pyridine nucleotide disulfide oxidoreductases t...
ABSTRACT: High-molecular mass thioredoxin reductases (TRs) are pyridine nucleotide disulfide oxidore...
Thioredoxin reductase (TrxR) is an essential enzyme required for the efficient maintenance of the ce...
AN example of two related enzymes that catalyse similar reactions but possess different active sites...
AbstractThiol–disulfide oxidoreductase systems of bacterial cytoplasm and eukaryotic cytosol favor r...
Human thioredoxin reductase (hTrxR) is a homodimeric flavoprotein crucially involved in the regulati...
Human thioredoxin reductase (hTrxR) is a homodimeric flavoprotein crucially involved in the regulati...
SummaryThioredoxin is ubiquitous and regulates various target proteins through disulfide bond reduct...
The high Mr (~55 kDa) thioredoxin reductases (TR) characteristic of higher eukaryotes are members of...
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