A. Mathews

发表

Quaternary Structure Regulates Hemin Dissociation from Human Hemoglobin*

J. Olson, M. Hargrove, T. Whitaker, 1997, The Journal of Biological Chemistry.

The role of the distal histidine in myoglobin and haemoglobin

Jean-Paul Renaud, Stephen G. Sligar, Barry A. Springer, 1988, Nature.

The reaction of neuroglobin with potential redox protein partners cytochrome b 5 and cytochrome c

L. Moens, S. Dewilde, A. Mathews, 2006, FEBS letters.

Mechanism of NO-induced oxidation of myoglobin and hemoglobin.

J. Olson, D. Lemon, R. Eich, 1996, Biochemistry.

The effects of amino acid substitution at position E7 (residue 64) on the kinetics of ligand binding to sperm whale myoglobin.

S. Sligar, J. Olson, T. Carver, 1990, The Journal of biological chemistry.

Identification of a Nickel(II) Binding Site on Hemoglobin Which Confers Susceptibility to Oxidative Deamination and Intramolecular Cross-linking*

I. Apostol, M. Weickert, A. Mathews, 1998, The Journal of Biological Chemistry.

His64(E7)-->Tyr apomyoglobin as a reagent for measuring rates of hemin dissociation.

Michael L. Quillin, J. Olson, M. Hargrove, 1994, The Journal of biological chemistry.

Discrimination between oxygen and carbon monoxide and inhibition of autooxidation by myoglobin. Site-directed mutagenesis of the distal histidine.

S. Sligar, J. Olson, A. Mathews, 1989, The Journal of biological chemistry.

A role for neuroglobin: Resetting the trigger level for apoptosis in neuronal and retinal cells

A. Mathews, A. Fago, T. Brittain, 2008, IUBMB life.

Reaction of the unsaturated triosmium cluster [Os3H(CO)8{Ph2PCH2P(Ph)C6H4}] with HBF4 and [Au(PPh3)]PF6; crystal structure of [Os3AuH(CO)8{Ph2PCH2P(Ph)C6H4}(PPh3)]PF6

B. Kariuki, A. Mathews, Anthony K. Smith, 1994 .

Oligomerization and ligand binding in a homotetrameric hemoglobin: Two high‐resolution crystal structures of hemoglobin Bart's (γ4), a marker for α‐thalassemia

H. Baker, E. Baker, A. Mathews, 2001, Protein science : a publication of the Protein Society.

The reactions of neuroglobin with CO: evidence for two forms of the ferrous protein.

L. Moens, S. Dewilde, A. Mathews, 2006, Journal of inorganic biochemistry.

The effects of E7 and E11 mutations on the kinetics of ligand binding to R state human hemoglobin.

K. Nagai, J. Tame, J. Olson, 1989, The Journal of biological chemistry.

A human recombinant haemoglobin designed for use as a blood substitute

K. Nagai, N. Komiyama, A. Mathews, 1992, Nature.

Reaction of the unsaturated triosmium clusters [Os3H(CO)8{Ph2PCH2P(Ph)C6H4}] and [Os3H(CO)8{Ph2PC(CH2)P(Ph)C6H4}] with phosphines and phosphites; crystal structures of [Os3H(CO)8{Ph2PCH2P(Ph)C6H4}(PPri3)], [Os3(CO)8(Ph2PCH2PPh2){P(OMe)3}2], and [Os3(CO)8(Ph2PCH2PPh2)(PPh3)2]

A. Mathews, Anthony K. Smith, M. Harding, 1993 .

Reactions of the co-ordinatively unsaturated cluster [Os3(µ-H)(CO)8{Ph2PCH2P(Ph)C6H4}] with alkynes RCCR (R = Ph, C6H4Me, Me or CF3); crystal structures of [Os3(CO)8{µ3–η2(∥)–RC2R}(Ph2PCH2PPh2)](R = Me or CF3) and electrochemical behaviour of triosmium–alkyne clusters

D. Osella, R. Gobetto, A. Mathews, 1993 .

Electrochemical behaviour of the electronically and coordinatively unsaturated cluster [Os3(γ-H)(CO)8{Ph2PCH2P(Ph)C6H4})]

D. Osella, A. Mathews, Anthony K. Smith, 1992 .

Expression of recombinant human hemoglobin in Escherichia coli.

J. Neway, A. Mathews, G. Stetler, 1994, Methods in enzymology.

[17] Assignment of rate constants for O2 and CO binding to α and β subunits within R- and T-state human hemoglobin

J. Olson, A. Mathews, 1994 .

Assignment of rate constants for O2 and CO binding to alpha and beta subunits within R- and T-state human hemoglobin.

J. Olson, A. Mathews, 1994, Methods in enzymology.

Differential scanning calorimetric study of the thermal unfolding transitions of yeast iso-1 and iso-2 cytochromes c and three composite isozymes.

B. Nall, F. Sherman, A. Mathews, 1994, Biochemistry.

Differential stability of two apo-isocytochromes c in the yeast Saccharomyces cerevisiae.

M. Dumont, B. Nall, F. Sherman, 1990, The Journal of biological chemistry.

Acute and long-term stability studies of deoxy hemoglobin and characterization of ascorbate-induced modifications.

I. Apostol, B. Kerwin, A. Mathews, 1999, Journal of pharmaceutical sciences.

Subunit dissociation and reassociation leads to preferential crystallization of haemoglobin Bart's (γ4) from solutions of human embryonic haemoglobin Portland (ζ2γ2) at low pH

H. Baker, E. Baker, A. Mathews, 2001 .

Application of high‐precision isotope ratio monitoring mass spectrometry to identify the biosynthetic origins of proteins

I. Apostol, A. Mathews, P. Brooks, 2001, Protein science : a publication of the Protein Society.

The assignment of carbon monoxide association rate constants to the alpha and beta subunits in native and mutant human deoxyhemoglobin tetramers.

K. Nagai, J. Tame, J. Olson, 1991, The Journal of biological chemistry.

Erratum: Quaternary structure regulates hemin dissociation from human hemoglobin (Journal of Biological Chemistry (1997) 272 (17385-17389))

J. Olson, M. Hargrove, T. Whitaker, 1997 .

Haem disorder in recombinant- and reticulocyte-derived haemoglobins: evidence for stereoselective haem insertion in eukaryotes.

A. Mathews, T. Brittain, 2001, The Biochemical journal.