Work

Cloning and sequencing of a human thioredoxin reductase

Year: 1995

Type: article

Abstract: The DNA sequence encoding human placental thioredoxin reductase has been determined. Of the 3826 base pairs sequenced, 1650 base pairs were in an open reading frame encoding a mature protein with 495 amino acids and a calculated molecular mass of 54,171. Sequence analysis showed strong similarity to glutathione reductases and other NADPH-dependent reductases. Human thioredoxin reductase contains the redox-active cysteines in the putative FAD binding domain and has a dimer interface domain not previously seen with prokaryote and lower eukaryote thioredoxin reductases.

Source: FEBS Letters

DOI: 10.1016/0014-5793(95)01003-w

Authors: Pamela Y. Gasdaska, John R. Gasdaska, Shawn Cochran, Garth Powis

Language: English

Topic: Redox biology and oxidative stress

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: bronze

Funders: National Institutes of Health, National Cancer Institute

Award: THIOREDOXIN AND ANTICANCER DRUG ACTION

OpenAlex ID: W2002593979

FWCI: 3.216

Cites: 45

Cited by: 205

Related to: 10