Transmembrane signaling by a chimera of the Escherichia coli aspartate receptor and the human insulin receptor.
about
Signaling domain of the aspartate receptor is a helical hairpin with a localized kinase docking surface: cysteine and disulfide scanning studies.19F nuclear magnetic resonance studies of aqueous and transmembrane receptors. Examples from the Escherichia coli chemosensory pathway.Receptor-mediated protein kinase activation and the mechanism of transmembrane signaling in bacterial chemotaxis.Detection of a conserved alpha-helix in the kinase-docking region of the aspartate receptor by cysteine and disulfide scanning.Evidence that the adaptation region of the aspartate receptor is a dynamic four-helix bundle: cysteine and disulfide scanning studies.Cysteine and disulfide scanning reveals a regulatory alpha-helix in the cytoplasmic domain of the aspartate receptor.Activation of transmembrane cell-surface receptors via a common mechanism? The "rotation model".Structural similarity between ornithine and aspartate transcarbamoylases of Escherichia coli: implications for domain switching.Evidence that both ligand binding and covalent adaptation drive a two-state equilibrium in the aspartate receptor signaling complexConverting a transmembrane receptor to a soluble receptor: recognition domain to effector domain signaling after excision of the transmembrane domainAntibody-induced mitogenicity mediated by a chimeric CD2-c-fms receptorAutonomous roles for the cytoplasmic domains of the CD2 and CD4 T cell surface antigens.Analysis of the role of the EnvZ linker region in signal transduction using a chimeric Tar/EnvZ receptor protein, Tez1.Specificity and promiscuity in membrane helix interactions.Attractant- and disulfide-induced conformational changes in the ligand binding domain of the chemotaxis aspartate receptor: a 19F NMR study.Structure and dynamics of Escherichia coli chemosensory receptors. Engineered sulfhydryl studies.Cysteine and disulfide scanning reveals two amphiphilic helices in the linker region of the aspartate chemoreceptor.An aspartate/insulin receptor chimera mitogenically activates fibroblasts.The N-terminal cytoplasmic tail of the aspartate receptor is not essential in signal transduction of bacterial chemotaxis.Rewiring a receptor: negative output from positive input.Understanding glucose transport by the bacterial phosphoenolpyruvate:glycose phosphotransferase system on the basis of kinetic measurements in vitro.
P2860
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P2860
Transmembrane signaling by a chimera of the Escherichia coli aspartate receptor and the human insulin receptor.
description
1989 nî lūn-bûn
@nan
1989 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1989 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
name
Transmembrane signaling by a c ...... nd the human insulin receptor.
@ast
Transmembrane signaling by a c ...... nd the human insulin receptor.
@en
Transmembrane signaling by a c ...... nd the human insulin receptor.
@nl
type
label
Transmembrane signaling by a c ...... nd the human insulin receptor.
@ast
Transmembrane signaling by a c ...... nd the human insulin receptor.
@en
Transmembrane signaling by a c ...... nd the human insulin receptor.
@nl
prefLabel
Transmembrane signaling by a c ...... nd the human insulin receptor.
@ast
Transmembrane signaling by a c ...... nd the human insulin receptor.
@en
Transmembrane signaling by a c ...... nd the human insulin receptor.
@nl
P2093
P2860
P356
P1476
Transmembrane signaling by a c ...... nd the human insulin receptor.
@en
P2093
P2860
P304
P356
10.1073/PNAS.86.15.5683
P407
P577
1989-08-01T00:00:00Z