Quantitative analysis of aspartate receptor signaling complex reveals that the homogeneous two-state model is inadequate: development of a heterogeneous two-state model.
about
Effects of adaptation in maintaining high sensitivity over a wide range of backgrounds for Escherichia coli chemotaxisDesign and diversity in bacterial chemotaxis: a comparative study in Escherichia coli and Bacillus subtilisNegative control in two-component signal transduction by transmitter phosphatase activityThe Structure of a Soluble Chemoreceptor Suggests a Mechanism for Propagating Conformational Signals † ‡Chemotaxis receptor complexes: from signaling to assemblyCheA Kinase of bacterial chemotaxis: chemical mapping of four essential docking sites.The S helix mediates signal transmission as a HAMP domain coiled-coil extension in the NarX nitrate sensor from Escherichia coli K-12.Side chains at the membrane-water interface modulate the signaling state of a transmembrane receptor.Evidence that the adaptation region of the aspartate receptor is a dynamic four-helix bundle: cysteine and disulfide scanning studies.Structure of the ternary complex formed by a chemotaxis receptor signaling domain, the CheA histidine kinase, and the coupling protein CheW as determined by pulsed dipolar ESR spectroscopy.The fast tumble signal in bacterial chemotaxisDiversity in chemotaxis mechanisms among the bacteria and archaea.Lateral density of receptor arrays in the membrane plane influences sensitivity of the E. coli chemotaxis response.Core unit of chemotaxis signaling complexes.Bacterial chemoreceptor dynamics correlate with activity state and are coupled over long distancesReceptor density balances signal stimulation and attenuation in membrane-assembled complexes of bacterial chemotaxis signaling proteins.Bacterial chemoreceptors: high-performance signaling in networked arraysThree-dimensional structure and organization of a receptor/signaling complex.Phototactic and chemotactic signal transduction by transmembrane receptors and transducers in microorganisms.Isolated bacterial chemosensory array possesses quasi- and ultrastable components: functional links between array stability, cooperativity, and order.Effect of chemoreceptor modification on assembly and activity of the receptor-kinase complex in Escherichia coli.Effects of receptor interaction in bacterial chemotaxis.Conserved glycine residues in the cytoplasmic domain of the aspartate receptor play essential roles in kinase coupling and on-off switching.The core signaling proteins of bacterial chemotaxis assemble to form an ultrastable complexA "trimer of dimers"-based model for the chemotactic signal transduction network in bacterial chemotaxis.OS-FRET: a new one-sample method for improved FRET measurements.Competitive and cooperative interactions in receptor signaling complexes.Control of chemotactic signal gain via modulation of a pre-formed receptor array.Adaptational assistance in clusters of bacterial chemoreceptors.
P2860
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P2860
Quantitative analysis of aspartate receptor signaling complex reveals that the homogeneous two-state model is inadequate: development of a heterogeneous two-state model.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
2003年论文
@zh
2003年论文
@zh-cn
name
Quantitative analysis of aspar ...... heterogeneous two-state model.
@en
Quantitative analysis of aspar ...... heterogeneous two-state model.
@nl
type
label
Quantitative analysis of aspar ...... heterogeneous two-state model.
@en
Quantitative analysis of aspar ...... heterogeneous two-state model.
@nl
prefLabel
Quantitative analysis of aspar ...... heterogeneous two-state model.
@en
Quantitative analysis of aspar ...... heterogeneous two-state model.
@nl
P2860
P1476
Quantitative analysis of aspar ...... heterogeneous two-state model.
@en
P2093
Joseph J Falke
Joshua A Bornhorst
P2860
P304
P356
10.1016/S0022-2836(03)00026-3
P407
P577
2003-03-01T00:00:00Z