Novel zinc-binding site in the E2 domain regulates amyloid precursor-like protein 1 (APLP1) oligomerization.
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APP Receptor? To Be or Not To Be.Structure and Synaptic Function of Metal Binding to the Amyloid Precursor Protein and its Proteolytic Fragments.Interaction of the amyloid precursor protein-like protein 1 (APLP1) E2 domain with heparan sulfate involves two distinct binding modes.Quantitation and localization of intracellular redox active metals by X-ray fluorescence microscopy in cortical neurons derived from APP and APLP2 knockout tissue.Direct evidence of amyloid precursor-like protein 1 trans interactions in cell-cell adhesion platforms investigated via fluorescence fluctuation spectroscopy.Decreased Neuro-Axonal Proteins in CSF at First Attack of Suspected Multiple Sclerosis.APLP1 is endoproteolytically cleaved by γ-secretase without previous ectodomain shedding.Amyloid precursor-like protein 1 (APLP1) exhibits stronger zinc-dependent neuronal adhesion than amyloid precursor protein and APLP2.APLP1 promotes dFoxO-dependent cell death in Drosophila.
P2860
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P2860
Novel zinc-binding site in the E2 domain regulates amyloid precursor-like protein 1 (APLP1) oligomerization.
description
2014 nî lūn-bûn
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2014年の論文
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2014年論文
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2014年論文
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2014年論文
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2014年論文
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2014年論文
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2014年论文
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2014年论文
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2014年论文
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name
Novel zinc-binding site in the ...... ein 1 (APLP1) oligomerization.
@en
type
label
Novel zinc-binding site in the ...... ein 1 (APLP1) oligomerization.
@en
prefLabel
Novel zinc-binding site in the ...... ein 1 (APLP1) oligomerization.
@en
P2093
P2860
P356
P1476
Novel zinc-binding site in the ...... tein 1 (APLP1) oligomerization
@en
P2093
Christian Barucker
Daniela Kaden
Dirk Roeser
Gerhard Multhaup
Linda Schauenburg
Magnus C Mayer
Manuel E Than
Mark A Hancock
Michael Schaefer
P2860
P304
19019-19030
P356
10.1074/JBC.M114.570382
P407
P577
2014-05-22T00:00:00Z