W. Beyer

发表

I. Fridovich, J. Imlay, I Fridovich, 1975, Annual review of biochemistry.

NADPH: ferredoxin oxidoreductase acts as a paraquat diaphorase and is a member of the soxRS regulon.

A. Hausladen, I. Fridovich, S. Liochev, 1994, Proceedings of the National Academy of Sciences of the United States of America.

Differences between the manganese- and the iron-containing superoxide dismutases of Escherichia coli detected through sedimentation equilibrium, hydrodynamic, and spectroscopic studies.

I. Fridovich, J. Reynolds, W. Beyer, 1989, Biochemistry.

In vivo competition between iron and manganese for occupancy of the active site region of the manganese-superoxide dismutase of Escherichia coli.

I. Fridovich, W. Beyer, 1991, The Journal of biological chemistry.

Catalases--with and without heme.

I. Fridovich, W. Beyer, 1988, Basic life sciences.

Superoxide dismutase mimic prepared from desferrioxamine and manganese dioxide.

I. Fridovich, W. Beyer, 1990, Methods in enzymology.

Does copper (II) ethylenediaminetetraacetate disproportionate superoxide?

I. Fridovich, W. Beyer, 1988, Analytical biochemistry.

Effect of hydrogen peroxide on the iron-containing superoxide dismutase of Escherichia coli.

I. Fridovich, W. Beyer, 1987, Biochemistry.

Phosphate inhibition of the copper- and zinc-containing superoxide dismutase: a reexamination.

I. Fridovich, W. Beyer, Y. Wang, 1986, Biochemistry.

Characterization of a superoxide dismutase mimic prepared from desferrioxamine and MnO2.

I. Fridovich, W. Beyer, 1989, Archives of biochemistry and biophysics.

Chemical modification of iron- and manganese-containing superoxide dismutases from Escherichia coli.

W. Beyer, C. L. Borders, P. Horton, 1989, Archives of biochemistry and biophysics.

Biochemical and structural studies of tenascin/hexabrachion proteins

H. Erickson, G. Briscoe, D. McCaslin, 1989, Journal of cellular biochemistry.

Characterization of the interaction between alpha2-macroglobulin and fibroblast growth factor-2: the role of hydrophobic interactions.

S. Pizzo, S. L. Gonias, S. Arandjelovic, 2003, The Biochemical journal.

Visualization of purified fibronectin-transglutaminase complexes.

S. N. Murthy, L. Lorand, H. Erickson, 1992, The Journal of biological chemistry.

Assaying for superoxide dismutase activity: some large consequences of minor changes in conditions.

I. Fridovich, W. Beyer, 1987, Analytical biochemistry.

Inactivation of human arginine-143, lysine-143, and isoleucine-143 Cu,Zn superoxide dismutases by hydrogen peroxide: multiple mechanisms for inactivation.

W. Beyer, C. L. Borders, P. Horton, 1989, Archives of biochemistry and biophysics.

Pseudocatalase from Lactobacillus plantarum: evidence for a homopentameric structure containing two atoms of manganese per subunit.

I. Fridovich, W. Beyer, 1985, Biochemistry.

The structure of human mitochondrial manganese superoxide dismutase reveals a novel tetrameric interface of two 4-helix bundles

G. Borgstahl, J. Tainer, M. Hickey, 1992, Cell.

Examination of the role of arginine-143 in the human copper and zinc superoxide dismutase by site-specific mutagenesis.

I. Fridovich, W. Beyer, R. Hallewell, 1987, The Journal of biological chemistry.

MANGANESE-CATALASE AND MANGANESE SUPEROXIDE DISMUTASE: SPECTROSCOPIC SIMILARITY WITH FUNCTIONAL DIVERSITY

I. Fridovich, W. Beyer, 1986 .

Purification and characterization of the Cu,Zn SOD from Escherichia coli.

I. Fridovich, L. Benov, W. Beyer, 1996, Free radical biology & medicine.

OxyR A Molecular Code for Redox-Related Signaling

Raphael Nudelman, Alfred Hausladen, A. Hausladen, 2002, Cell.

The Properties of Rabbit α1-Macroglobulin upon Activation Are Distinct from Those of Rabbit and Human α2-Macroglobulins

S. Pizzo, A. Banbula, W. Beyer, 2005 .

The properties of rabbit alpha1-macroglobulin upon activation are distinct from those of rabbit and human alpha2-macroglobulins.

S. Pizzo, A. Banbula, W. Beyer, 2005, Journal of biochemistry.

An ultrasensitive colorimetric assay for manganese.

I. Fridovich, W. Beyer, 1988, Analytical biochemistry.

Bivalency and epitope specificity of a high-affinity IgG3 monoclonal antibody to the Streptococcus group A carbohydrate antigen. Molecular modeling of a Fv fragment.

J. B. Pitner, B. M. Pinto, F. Forooghian, 2000, Carbohydrate research.

Phosphate, not superoxide dismutase, facilitates electron transfer from ferrous salts to cytochrome c.

I. Fridovich, W. Beyer, 1991, Archives of biochemistry and biophysics.

Superoxide dismutases.

I. Fridovich, J. Imlay, W. Beyer, 1991, Progress in nucleic acid research and molecular biology.