Dynamic or stable interactions of influenza hemagglutinin mutants with coated pits. Dependence on the internalization signal but not on aggregation.
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Regulatory interactions in the recognition of endocytic sorting signals by AP-2 complexes.Transforming growth factor-beta receptors interact with AP2 by direct binding to beta2 subunitDifferently anchored influenza hemagglutinin mutants display distinct interaction dynamics with mutual rafts.Clustering of raft-associated proteins in the external membrane leaflet modulates internal leaflet H-ras diffusion and signaling.Downregulation of kinin B1 receptor function by B2 receptor heterodimerization and signaling.In vitro binding of clathrin adaptors to sorting signals correlates with endocytosis and basolateral sorting.Distinct endocytic responses of heteromeric and homomeric transforming growth factor beta receptorsDab2 inhibits the cholesterol-dependent activation of JNK by TGF-βCyclodextrins but not compactin inhibit the lateral diffusion of membrane proteins independent of cholesterol.Internalization-competent influenza hemagglutinin mutants form complexes with clathrin-deficient multivalent AP-2 oligomers in live cells.Free clathrin triskelions are required for the stability of clathrin-associated adaptor protein (AP-2) coated pit nucleation sites.Membrane interactions of a constitutively active GFP-Ki-Ras 4B and their role in signaling. Evidence from lateral mobility studies.Partitioning of proteins into plasma membrane microdomains. Clustering of mutant influenza virus hemagglutinins into coated pits depends on the strength of the internalization signal.Endocytosis of chimeric influenza virus hemagglutinin proteins that lack a cytoplasmic recognition feature for coated pits.Synthesis and Membrane-Binding Properties of a Characteristic Lipopeptide from the Membrane-Anchoring Domain of Influenza Virus A Hemagglutinin This research was supported by the Deutsche Forschungsgemeinschaft and the Fonds der Chemischen IndustrieDegradation of mutant influenza virus hemagglutinins is influenced by cytoplasmic sequences independent of internalization signals.
P2860
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P2860
Dynamic or stable interactions of influenza hemagglutinin mutants with coated pits. Dependence on the internalization signal but not on aggregation.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年学术文章
@wuu
1995年学术文章
@zh-cn
1995年学术文章
@zh-hans
1995年学术文章
@zh-my
1995年学术文章
@zh-sg
1995年學術文章
@yue
1995年學術文章
@zh
1995年學術文章
@zh-hant
name
Dynamic or stable interactions ...... signal but not on aggregation.
@en
type
label
Dynamic or stable interactions ...... signal but not on aggregation.
@en
prefLabel
Dynamic or stable interactions ...... signal but not on aggregation.
@en
P2860
P356
P1476
Dynamic or stable interactions ...... signal but not on aggregation
@en
P2860
P304
21075-21081
P356
10.1074/JBC.270.36.21075
P407
P577
1995-09-01T00:00:00Z