Membrane interactions of diphtheria toxin analyzed using in vitro synthesized mutants.
about
Cloning of an intracellular protein that binds selectively to mitogenic acidic fibroblast growth factorPeptides fused to the amino-terminal end of diphtheria toxin are translocated to the cytosolGPI-anchored diphtheria toxin receptor allows membrane translocation of the toxin without detectable ion channel activity.Ability of methotrexate to inhibit translocation to the cytosol of dihydrofolate reductase fused to diphtheria toxin.Stimulation of proliferation of a human osteosarcoma cell line by exogenous acidic fibroblast growth factor requires both activation of receptor tyrosine kinase and growth factor internalization.Membrane translocation of diphtheria toxin carrying passenger protein domains.Permeabilization of the plasma membrane by deletion mutants of diphtheria toxin.Phosphorylation-regulated nucleocytoplasmic trafficking of internalized fibroblast growth factor-1Tight folding of acidic fibroblast growth factor prevents its translocation to the cytosol with diphtheria toxin as vector.Association between diphtheria toxin A- and B-fragment and their fusion proteinsModulation of the intracellular stability and toxicity of diphtheria toxin through degradation by the N-end rule pathway.Subcloning and characterization of the binding domain of fragment B of diphtheria toxin.
P2860
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P2860
Membrane interactions of diphtheria toxin analyzed using in vitro synthesized mutants.
description
1989 nî lūn-bûn
@nan
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
1989年论文
@zh
1989年论文
@zh-cn
name
Membrane interactions of diphtheria toxin analyzed using in vitro synthesized mutants.
@en
type
label
Membrane interactions of diphtheria toxin analyzed using in vitro synthesized mutants.
@en
prefLabel
Membrane interactions of diphtheria toxin analyzed using in vitro synthesized mutants.
@en
P2860
P50
P1433
P1476
Membrane interactions of diphtheria toxin analyzed using in vitro synthesized mutants.
@en
P2093
P2860
P304
P407
P577
1989-10-01T00:00:00Z