The structural basis of negative cooperativity: receptors and enzymes.
about
Efficient coupling of catalysis and dynamics in the E1 component of Escherichia coli pyruvate dehydrogenase multienzyme complexDifferential substrate specificity and kinetic behavior of Escherichia coli YfdW and Oxalobacter formigenes formyl coenzyme A transferaseDynamics, flexibility and ligand-induced conformational changes in biological macromolecules: a computational approachMolecular basis of transmembrane signalling by sensory rhodopsin II-transducer complexKinetic and X-Ray Structural Evidence for Negative Cooperativity in Substrate Binding to Nicotinate Mononucleotide Adenylyltransferase (NMAT) from Bacillus anthracisStructural Basis for Negative Cooperativity in Growth Factor Binding to an EGF ReceptorAn Asymmetry-to-Symmetry Switch in Signal Transmission by the Histidine Kinase Receptor for TMAOModulation of Global Low-Frequency Motions Underlies Allosteric Regulation: Demonstration in CRP/FNR Family Transcription FactorsCrystal structure of glutamate-1-semialdehyde aminomutase: an alpha2-dimeric vitamin B6-dependent enzyme with asymmetry in structure and active site reactivityComplete integrability of information processing by biochemical reactionsThe role of dimer asymmetry and protomer dynamics in enzyme catalysis.Ligand depletion in vivo modulates the dynamic range and cooperativity of signal transduction.Symmetric allosteric mechanism of hexameric Escherichia coli arginine repressor exploits competition between L-arginine ligands and resident arginine residues.Anesthetic sensitivity of the Gloeobacter violaceus proton-gated ion channel.Biophysical and kinetic characterization of HemAT, an aerotaxis receptor from Bacillus subtilis.Modulation of allostery by protein intrinsic disorder.Modeling the role of negative cooperativity in metabolic regulation and homeostasisSubstrate inhibition in human hydroxysteroid sulfotransferase SULT2A1: studies on the formation of catalytically non-productive enzyme complexesNegatively cooperative binding of high-density lipoprotein to the HDL receptor SR-BIGlycine dimerization motif in the N-terminal transmembrane domain of the high density lipoprotein receptor SR-BI required for normal receptor oligomerization and lipid transport.Substrate scope and selectivity in offspring to an enzyme subjected to directed evolution.The structure and allosteric regulation of mammalian glutamate dehydrogenase.Receptor oligomerization in family B1 of G-protein-coupled receptors: focus on BRET investigations and the link between GPCR oligomerization and binding cooperativity.Crystal structure of glutamate-1-semialdehyde-2,1-aminomutase from Arabidopsis thalianaDynamically driven protein allostery.The structure and allosteric regulation of glutamate dehydrogenase.NMR reveals novel mechanisms of protein activity regulation.The use of mode of action information in risk assessment: quantitative key events/dose-response framework for modeling the dose-response for key events.Putting together structures of epidermal growth factor receptorsNucleic acids exert a sequence-independent cooperative effect on sequence-dependent activation of Toll-like receptor 9.High affinity insulin binding by soluble insulin receptor extracellular domain fused to a leucine zipper.An oligomeric signaling platform formed by the Toll-like receptor signal transducers MyD88 and IRAK-4.Structural and Functional Characterization of the PaaI Thioesterase from Streptococcus pneumoniae Reveals a Dual Specificity for Phenylacetyl-CoA and Medium-chain Fatty Acyl-CoAs and a Novel CoA-induced Fit Mechanism.Glycoprotein hormone receptors: link between receptor homodimerization and negative cooperativity.New Insights into Active Site Conformation Dynamics of E. coli PNP Revealed by Combined H/D Exchange Approach and Molecular Dynamics Simulations.Mechanisms underlying modulation of neuronal KCNQ2/KCNQ3 potassium channels by extracellular protonsMultiple roles of mobile active center loops in the E1 component of the Escherichia coli pyruvate dehydrogenase complex - Linkage of protein dynamics to catalysis.One substrate, five products: reactions catalyzed by the dihydroneopterin aldolase from Mycobacterium tuberculosis.Collective behaviours: from biochemical kinetics to electronic circuits.Negative cooperativity of glutamate binding in the dimeric metabotropic glutamate receptor subtype 1.
P2860
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P2860
The structural basis of negative cooperativity: receptors and enzymes.
description
1996 nî lūn-bûn
@nan
1996 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
The structural basis of negative cooperativity: receptors and enzymes.
@ast
The structural basis of negative cooperativity: receptors and enzymes.
@en
The structural basis of negative cooperativity: receptors and enzymes.
@nl
type
label
The structural basis of negative cooperativity: receptors and enzymes.
@ast
The structural basis of negative cooperativity: receptors and enzymes.
@en
The structural basis of negative cooperativity: receptors and enzymes.
@nl
prefLabel
The structural basis of negative cooperativity: receptors and enzymes.
@ast
The structural basis of negative cooperativity: receptors and enzymes.
@en
The structural basis of negative cooperativity: receptors and enzymes.
@nl
P1476
The structural basis of negative cooperativity: receptors and enzymes.
@en
P2093
Koshland DE Jr
P304
P356
10.1016/S0959-440X(96)80004-2
P577
1996-12-01T00:00:00Z