Hsiao Y, Van R, Hung H, Pan R
J Protein Chem. 2002; 21(1):51-8.
PMID: 11902667
DOI: 10.1023/a:1014183100021.
Page M
Biochem J. 1993; 295 ( Pt 1):295-304.
PMID: 8216231
PMC: 1134852.
DOI: 10.1042/bj2950295.
Moore J, Hawkins A, Charles I, Deka R, Coggins J, Cooper A
Biochem J. 1993; 295 ( Pt 1):277-85.
PMID: 8216229
PMC: 1134850.
DOI: 10.1042/bj2950277.
Valero E, Varon R, Garcia-Carmona F
Bull Math Biol. 1995; 57(1):157-68.
PMID: 7833851
DOI: 10.1007/BF02458321.
Horiike K, Tojo H, Yamano T, Nozaki M
Biochem J. 1984; 223(3):933-4.
PMID: 6508750
PMC: 1144383.
DOI: 10.1042/bj2230933.
Kinetics of protein modification reactions. Plot of fractional enzyme activity versus extent of protein modification in cases where all modifiable groups are essential for enzyme activity.
Rakitzis E
Biochem J. 1984; 223(1):259-62.
PMID: 6497841
PMC: 1144288.
DOI: 10.1042/bj2230259.
Kinetics of protein modification and enzyme inactivation reactions: interpretation of reaction order.
Rakitzis E
Biochem J. 1985; 231(2):493-4.
PMID: 4062910
PMC: 1152774.
DOI: 10.1042/bj2310493.
Kinetics of protein-modification reactions. Stoichiometry of modification-produced enzyme inactivation: modification of rhodanese by 2,4,6-trinitrobenzenesulphonic acid.
Rakitzis E, Malliopoulou T
Biochem J. 1985; 230(1):89-93.
PMID: 4052047
PMC: 1152590.
DOI: 10.1042/bj2300089.
Chemical modification of enzymes: reaction with an unstable inhibitor.
Topham C
Biochem J. 1985; 227(3):1025-7.
PMID: 4004791
PMC: 1144937.
DOI: 10.1042/bj2271025.
Computer simulations of the kinetics of irreversible enzyme inhibition by an unstable inhibitor.
Topham C
Biochem J. 1986; 240(3):817-20.
PMID: 3827869
PMC: 1147492.
DOI: 10.1042/bj2400817.
Kinetics of protein-modification reactions. Determination of the fractional concentration of enzyme protein groups, or group reactivities, essential for catalytic function.
Rakitzis E, Malliopoulou T
Biochem J. 1986; 237(2):589-91.
PMID: 3800902
PMC: 1147024.
DOI: 10.1042/bj2370589.
Inactivation of macromolecules by ionizing radiation. Deterministic single-hit or stochastic multievent process?.
Swillens S
Biochem J. 1986; 233(3):655-9.
PMID: 3707516
PMC: 1153082.
DOI: 10.1042/bj2330655.
Alternative methods for the determination of rate constants describing enzyme inactivation by an unstable inhibitor.
Topham C
Biochem J. 1987; 246(3):804-6.
PMID: 3689336
PMC: 1148352.
DOI: 10.1042/bj2460804.
Kinetics of protein modification, and/or enzyme inactivation, reactions by an unstable modifying agent.
Rakitzis E
Biochem J. 1987; 246(3):803-5.
PMID: 3689335
PMC: 1148351.
DOI: 10.1042/bj2460803.
Kinetic analysis of protein modification reactions at equilibrium.
Rakitzis E
Biochem J. 1989; 263(3):855-9.
PMID: 2597131
PMC: 1133509.
DOI: 10.1042/bj2630855.
Inactivation of skeletal-muscle UDP-glucose pyrophosphorylase by reaction with carboxylate-directed reagents.
Signorini M, Ferrari C, Mariotti E, Dallocchio F, Bergamini C
Biochem J. 1989; 264(3):799-804.
PMID: 2559717
PMC: 1133656.
DOI: 10.1042/bj2640799.
Kinetic analysis of regeneration by dilution of a covalently modified protein.
Rakitzis E
Biochem J. 1990; 268(3):669-70.
PMID: 2363704
PMC: 1131491.
DOI: 10.1042/bj2680669.