A Holmgren

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Redox Potentials of Glutaredoxins and Other Thiol-Disulfide Oxidoreductases of the Thioredoxin Superfamily Determined by Direct Protein-Protein Redox Equilibria*

K. Berndt, Fredrik Åslund, A. Holmgren, 1997, The Journal of Biological Chemistry.

Structure of oxidized thioredoxin to 4 with 5 A resolution.

C. Branden, A. Holmgren, A Holmgren, 1974, Journal of molecular biology.

Proton sharing between cysteine thiols in Escherichia coli thioredoxin: implications for the mechanism of protein disulfide reduction.

H. Dyson, A. Holmgren, M. Jeng, 1995, Biochemistry.

Conserved immunoglobulin‐like features in a family of periplasmic pilus chaperones in bacteria.

C. Brändén, S. Hultgren, A. Holmgren, 1992, The EMBO journal.

Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution.

H. Eklund, C. Brändén, A. Holmgren, 1975, Proceedings of the National Academy of Sciences of the United States of America.

Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide.

A. Holmgren, A Holmgren, 1979, The Journal of biological chemistry.

Enzymatic reduction-oxidation of protein disulfides by thioredoxin.

A. Holmgren, A Holmgren, 1984, Methods in enzymology.

Proton-transfer effects in the active-site region of Escherichia coli thioredoxin using two-dimensional 1H NMR.

H. Dyson, A. Holmgren, L. Tennant, 1991, Biochemistry.

Thioredoxin and related proteins in procaryotes.

A. Holmgren, F. K. Gleason, A Holmgren, 1988, FEMS microbiology reviews.

Three-dimensional structure of a mammalian thioredoxin reductase: Implications for mechanism and evolution of a selenocysteine-dependent enzyme

G. Schneider, Y. Lindqvist, A. Holmgren, 2001, Proceedings of the National Academy of Sciences of the United States of America.

Structural Basis for the Thioredoxin-like Activity Profile of the Glutaredoxin-like NrdH-redoxin from Escherichia coli*

G. Schneider, Y. Lindqvist, Fredrik Åslund, 2001, The Journal of Biological Chemistry.

Essential Role of Selenium in the Catalytic Activities of Mammalian Thioredoxin Reductase Revealed by Characterization of Recombinant Enzymes with Selenocysteine Mutations*

A. Holmgren, L. Zhong, A Holmgren, 2000, The Journal of Biological Chemistry.

A mutant thioredoxin from Escherichia coli tsnC 7007 that is nonfunctional as subunit of phage T7 DNA polymerase.

A. Holmgren, A Holmgren, B Nordström, 1981, The Journal of biological chemistry.

Thioredoxin blood level increases after severe burn injury.

B. Sahaf, A. Holmgren, H. Nakamura, 2000, Antioxidants & redox signaling.

Selenium and the thioredoxin and glutaredoxin systems.

A. Holmgren, M. Björnstedt, S. Kumar, 1997, Biomedical and environmental sciences : BES.

Solution structure of Escherichia coli glutaredoxin-2 shows similarity to mammalian glutathione-S-transferases.

P E Wright, H. Dyson, P. Wright, 2001, Journal of molecular biology.

Differential reactivity of the functional sulfhydryl groups of cysteine-32 and cysteine-35 present in the reduced form of thioredoxin from Escherichia coli.

A. Holmgren, A Holmgren, G. Kallis, 1980, The Journal of biological chemistry.