about
Activation of phenylalanine hydroxylase induces positive cooperativity toward the natural cofactorCooperativity in monomeric enzymes with single ligand-binding sitesA novel type of allosteric regulation: functional cooperativity in monomeric proteinsMichaelis and Menten and the long road to the discovery of cooperativityStructure of phenylalanine hydroxylase from Colwellia psychrerythraea 34H, a monomeric cold active enzyme with local flexibility around the active site and high overall stabilityThe Binding and Release of Oxygen and Hydrogen Peroxide Are Directed by a Hydrophobic Tunnel in Cholesterol Oxidase †A novel allosteric mechanism in the cysteine peptidase cathepsin K discovered by computational methodsAllosteric activation of the phosphoinositide phosphatase Sac1 by anionic phospholipids.Analysis of the cooperativity of human beta-cell glucokinase through the stimulatory effect of glucose on fructose phosphorylation.Allosteric interactions within subsites of a monomeric enzyme: kinetics of fluorogenic substrates of PI-specific phospholipase C.Cleavage of IgG1 and IgG3 by gingipain K from Porphyromonas gingivalis may compromise host defense in progressive periodontitis.Understanding allosteric and cooperative interactions in enzymes.Cooperativity and specificity in enzyme kinetics: a single-molecule time-based perspective.Hysteresis of plant cell-wall beta-glucosidase.Differences in specificity and selectivity between CBP and p300 acetylation of histone H3 and H3/H4.A slow kinetic transient in RNA synthesis catalysed by wheat-germ RNA polymerase II.Isomerization of the free enzyme versus induced fit: effects of steps involving induced fit that bypass enzyme isomerization on flux ratios and countertransport.On the generality of Michaelian kinetics.Isolation and functional characterization of a novel plastidic hexokinase from Nicotiana tabacum.Rapid IgG heavy chain cleavage by the streptococcal IgG endopeptidase IdeS is mediated by IdeS monomers and is not due to enzyme dimerization.Emergence of dynamic cooperativity in the stochastic kinetics of fluctuating enzymes.Entropic estimate of cooperative binding of substrate on a single oligomeric enzyme: an index of cooperativity.Role of conformational dynamics in kinetics of an enzymatic cycle in a nonequilibrium steady state.Molecular adaptation and allostery in plant pantothenate synthetases.
P2860
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P2860
description
1987 nî lūn-bûn
@nan
1987年の論文
@ja
1987年論文
@yue
1987年論文
@zh-hant
1987年論文
@zh-hk
1987年論文
@zh-mo
1987年論文
@zh-tw
1987年论文
@wuu
1987年论文
@zh
1987年论文
@zh-cn
name
Co-operativity in monomeric enzymes.
@en
Co-operativity in monomeric enzymes.
@nl
type
label
Co-operativity in monomeric enzymes.
@en
Co-operativity in monomeric enzymes.
@nl
prefLabel
Co-operativity in monomeric enzymes.
@en
Co-operativity in monomeric enzymes.
@nl
P1476
Co-operativity in monomeric enzymes.
@en
P2093
Cornish-Bowden A
Cárdenas ML
P356
10.1016/S0022-5193(87)80248-5
P407
P577
1987-01-01T00:00:00Z