Cooperativity and specificity in enzyme kinetics: a single-molecule time-based perspective.
about
Extracting signal from noise: kinetic mechanisms from a Michaelis-Menten-like expression for enzymatic fluctuationsSingle-molecule enzymology à la Michaelis-MentenAllosteric activation of the phosphoinositide phosphatase Sac1 by anionic phospholipids.Ligand depletion in vivo modulates the dynamic range and cooperativity of signal transduction.Application of the principles of systems biology and Wiener's cybernetics for analysis of regulation of energy fluxes in muscle cells in vivo.Michaelis-Menten relations for complex enzymatic networks.Rate theories for biologistsAssembly of multiprotein complexes that control genome function.The chemical master equation approach to nonequilibrium steady-state of open biochemical systems: linear single-molecule enzyme kinetics and nonlinear biochemical reaction networks.Statistics and Related Topics in Single-Molecule Biophysics.The uncoupled ATPase activity of the ABC transporter BtuC2D2 leads to a hysteretic conformational change, conformational memory, and improved activity.Statistical properties of fluctuating enzymes with dynamic cooperativity using a first passage time distribution formalism.High performance enzyme kinetics of turnover, activation and inhibition for translational drug discovery.Metallic-Nanostructure-Enhanced Fluorescence of Single Flavin Cofactor and Single Flavoenzyme Molecules.Stochastic ensembles, conformationally adaptive teamwork, and enzymatic detoxification.Emergence of dynamic cooperativity in the stochastic kinetics of fluctuating enzymes.Exploration of the spontaneous fluctuating activity of single enzyme molecules.Enzyme efficiency: An open reaction system perspective.Michaelis-Menten kinetics under non-isothermal conditions.Entropic estimate of cooperative binding of substrate on a single oligomeric enzyme: an index of cooperativity.A perturbation analysis of rate theory of self-regulating genes and signaling networks.Role of conformational dynamics in kinetics of an enzymatic cycle in a nonequilibrium steady state.Dynamic coupling between the LID and NMP domain motions in the catalytic conversion of ATP and AMP to ADP by adenylate kinase.Extensions to Michaelis-Menten Kinetics for Single ParametersSimulating feedback and reversibility in substrate-enzyme reactions
P2860
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P2860
Cooperativity and specificity in enzyme kinetics: a single-molecule time-based perspective.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Cooperativity and specificity ...... lecule time-based perspective.
@en
Cooperativity and specificity ...... lecule time-based perspective.
@nl
type
label
Cooperativity and specificity ...... lecule time-based perspective.
@en
Cooperativity and specificity ...... lecule time-based perspective.
@nl
prefLabel
Cooperativity and specificity ...... lecule time-based perspective.
@en
Cooperativity and specificity ...... lecule time-based perspective.
@nl
P2860
P1433
P1476
Cooperativity and specificity ...... lecule time-based perspective.
@en
P2093
P2860
P356
10.1529/BIOPHYSJ.108.131771
P407
P577
2008-04-25T00:00:00Z