APLP1 is endoproteolytically cleaved by γ-secretase without previous ectodomain shedding.

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Dysregulation of Neuronal Iron Homeostasis as an Alternative Unifying Effect of Mutations Causing Familial Alzheimer's Disease

P2860

Q58785711-F1807420-2D8F-4CA5-B8D0-0CC9E0B0A030

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APLP1 is endoproteolytically cleaved by γ-secretase without previous ectodomain shedding.

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http://www.wikidata.org/entity/Q48138450

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2018 nî lūn-bûn

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2018年の論文

@ja

2018年学术文章

@wuu

2018年学术文章

@zh-cn

2018年学术文章

@zh-hans

2018年学术文章

@zh-my

2018年学术文章

@zh-sg

2018年學術文章

@yue

2018年學術文章

@zh

2018年學術文章

@zh-hant

name

APLP1 is endoproteolytically cleaved by γ-secretase without previous ectodomain shedding.

@en

APLP1 is endoproteolytically cleaved by γ-secretase without previous ectodomain shedding.

@nl

type

Item

label

APLP1 is endoproteolytically cleaved by γ-secretase without previous ectodomain shedding.

@en

APLP1 is endoproteolytically cleaved by γ-secretase without previous ectodomain shedding.

@nl

prefLabel

APLP1 is endoproteolytically cleaved by γ-secretase without previous ectodomain shedding.

@en

APLP1 is endoproteolytically cleaved by γ-secretase without previous ectodomain shedding.

@nl

P1476

APLP1 is endoproteolytically cleaved by γ-secretase without previous ectodomain shedding.

@en

P2093

Christoph Weise

http://www.w3.org/2001/XMLSchema#string

Gerhard Multhaup

http://www.w3.org/2001/XMLSchema#string

Linda Schauenburg

http://www.w3.org/2001/XMLSchema#string

Magnus C Mayer

http://www.w3.org/2001/XMLSchema#string

P2860

Synapse Formation and Function Is Modulated by the Amyloid Precursor Protein

A mutation in APP protects against Alzheimer’s disease and age-related cognitive decline

Isolation and characterization of APLP2 encoding a homologue of the Alzheimer's associated amyloid beta protein precursor

Homo- and heterodimerization of APP family members promotes intercellular adhesion.

Modeling transmembrane domain dimers/trimers of plexin receptors: implications for mechanisms of signal transmission across the membrane

A transcriptionally [correction of transcriptively] active complex of APP with Fe65 and histone acetyltransferase Tip60

gamma-Secretase cleavage and binding to FE65 regulate the nuclear translocation of the intracellular C-terminal domain (ICD) of the APP family of proteins

Cleavage of amyloid-beta precursor protein and amyloid-beta precursor-like protein by BACE 1

The proteolytic processing of the amyloid precursor protein gene family members APLP-1 and APLP-2 involves alpha-, beta-, gamma-, and epsilon-like cleavages: modulation of APLP-1 processing by n-glycosylation

Human amyloid precursor-like protein 1--cDNA cloning, ectopic expression in COS-7 cells and identification of soluble forms in the cerebrospinal fluid

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s41598-018-19530-8

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1916

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scholarly article

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10.1038/S41598-018-19530-8

http://www.w3.org/2001/XMLSchema#string

P407

English

P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P50

Filip Liebsch

Murat Eravci

P577

2018-01-30T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

29382944

http://www.w3.org/2001/XMLSchema#string

P932

5789831

http://www.w3.org/2001/XMLSchema#string

APLP1 is endoproteolytically cleaved by γ-secretase without previous ectodomain shedding.

about

P2860

P2860

APLP1 is endoproteolytically cleaved by γ-secretase without previous ectodomain shedding.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932