A structural perspective on enzymes activated by monovalent cations.
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Crystal Structure of human pyridoxal kinase: structural basis of M(+) and M(2+) activationBiomolecular electrostatics and solvation: a computational perspectiveStructural basis of Na+ activation mimicry in murine thrombinImportant role of the cys-191 cys-220 disulfide bond in thrombin function and allosteryStructural identification of the pathway of long-range communication in an allosteric enzymeEngineering Protein Allostery: 1.05 Å Resolution Structure and Enzymatic Properties of a Na+-activated TrypsinNa+ binding to meizothrombin desF1Mutant N143P Reveals How Na+ Activates ThrombinPotassium-activated GTPase Reaction in the G Protein-coupled Ferrous Iron Transporter BRigidification of the autolysis loop enhances Na+ binding to thrombinCrystallographic and Kinetic Evidence of Allostery in a Trypsin-like ProteaseChemical, genetic and structural assessment of pyridoxal kinase as a drug target in the African trypanosomePotassium Acts as a GTPase-Activating Element on Each Nucleotide-Binding Domain of the Essential Bacillus subtilis EngAA Ribokinase Family Conserved Monovalent Cation Binding Site Enhances the MgATP-induced Inhibition in E. coli Phosphofructokinase-2Specific potassium ion interactions facilitate homocysteine binding to betaine-homocysteine S-methyltransferaseUsing ¹⁵N-ammonium to characterise and map potassium binding sites in proteins by NMR spectroscopy.Activation and inhibition of histone deacetylase 8 by monovalent cations.Structural identification of cation binding pockets in the plasma membrane proton pump.Redesigning allosteric activation in an enzyme.Switching cation-binding loops paves the way for redesigning allosteric activationRole of Na+ and K+ in enzyme function.Thrombin.Serine proteases.Ions and inhibitors in the binding site of HIV protease: comparison of Monte Carlo simulations and the linearized Poisson-Boltzmann theoryPotassium is an activator of homoisocitrate dehydrogenase from Saccharomyces cerevisiae.Molecular Mechanisms of Enzyme Activation by Monovalent Cations.Intracellular potassium stabilizes human ether-à-go-go-related gene channels for export from endoplasmic reticulum.Metal Ion Activation of Clostridium sordellii Lethal Toxin and Clostridium difficile Toxin B.Determination of alkali and halide monovalent ion parameters for use in explicitly solvated biomolecular simulations.Mechanism of Na(+) binding to thrombin resolved by ultra-rapid kinetics.Relationships between growth, growth response to nutrient supply, and ion content using a recombinant inbred line population in Arabidopsis.Evolution of the genetic code by incorporation of amino acids that improved or changed protein function.Murine thrombin lacks Na+ activation but retains high catalytic activity.Higher-order human telomeric G-quadruplex DNA metalloenzyme catalyzed Diels-Alder reaction: an unexpected inversion of enantioselectivity modulated by K(+) and NH4(+) ions.Effects of conducting and blocking ions on the structure and stability of the potassium channel KcsA.Analyses of cobalt–ligand and potassium–ligand bond lengths in metalloproteins: trends and patternsQuaternary Structure, Salt Sensitivity, and Allosteric Regulation of β-AMYLASE2 From
P2860
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P2860
A structural perspective on enzymes activated by monovalent cations.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
@zh
2005年學術文章
@zh-hant
name
A structural perspective on enzymes activated by monovalent cations.
@ast
A structural perspective on enzymes activated by monovalent cations.
@en
type
label
A structural perspective on enzymes activated by monovalent cations.
@ast
A structural perspective on enzymes activated by monovalent cations.
@en
prefLabel
A structural perspective on enzymes activated by monovalent cations.
@ast
A structural perspective on enzymes activated by monovalent cations.
@en
P2860
P356
P1476
A structural perspective on enzymes activated by monovalent cations.
@en
P2093
Enrico Di Cera
P2860
P304
P356
10.1074/JBC.R500023200
P407
P577
2005-11-02T00:00:00Z