Phosphorylation of the beta-amyloid precursor protein at the cell surface by ectocasein kinases 1 and 2 (Q22254075)

GOA release 2020-03-11

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C Haass

Haass

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7 February 2023

J Walter

Walter

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7 February 2023

A Schindzielorz

series ordinal

author given names

author last names

Schindzielorz

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7 February 2023

B Hartung

series ordinal

author given names

author last names

Hartung

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Journal of Biological Chemistry

7 February 2023

language of work or name

English

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publication date

4 August 2000

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published in

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volume

275

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issue

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page(s)

23523-9

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cites work

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Identification and regulation of the high affinity binding site of the Alzheimer's disease amyloid protein precursor (APP) to glycosaminoglycans

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Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans

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Extracellular ATP: effects, sources and fate

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Identification of an ectokinase activity in cerebellar granule primary neuronal cultures

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Surface Phosphorylation by Ecto‐Protein Kinase C in Brain Neurons: A Target for Alzheimer's β‐Amyloid Peptides

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Ectodomain phosphorylation of beta-amyloid precursor protein at two distinct cellular locations

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Alzheimer-like changes in microtubule-associated protein Tau induced by sulfated glycosaminoglycans. Inhibition of microtubule binding, stimulation of phosphorylation, and filament assembly depend on the degree of sulfation

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Cellular actions of beta-amyloid precursor protein and its soluble and fibrillogenic derivatives

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Processing of beta-amyloid precursor protein in microglia and astrocytes favors an internal localization over constitutive secretion

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A heparin-binding domain in the amyloid protein precursor of Alzheimer's disease is involved in the regulation of neurite outgrowth

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7 January 2021

Role of phosphorylation of Alzheimer's amyloid precursor protein during neuronal differentiation.

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Identifiers

DOI

10.1074/JBC.M002850200

0 references