(Q28304387)

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Cytoplasmic domain of the beta-amyloid protein precursor of Alzheimer's disease: function, regulation of proteolysis, and implications for drug development

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scholarly article

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Europe PubMed Central

Cytoplasmic domain of the beta-amyloid protein precursor of Alzheimer's disease: function, regulation of proteolysis, and implications for drug development (English)

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Alzheimer's disease

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based on heuristic

inferred from title

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based on heuristic

inferred from title

author name string

Megan L Kerr

1

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David H Small

2

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language of work or name

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publication date

15 April 2005

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Journal of Neuroscience Research

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80

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2

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151-9

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The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein

1 reference

https://api.crossref.org/works/10.1002%2FJNR.20408

21 January 2018

Fe65L2: a new member of the Fe65 protein family interacting with the intracellular domain of the Alzheimer's beta-amyloid precursor protein

1 reference

https://api.crossref.org/works/10.1002%2FJNR.20408

21 January 2018

The disabled 1 phosphotyrosine-binding domain binds to the internalization signals of transmembrane glycoproteins and to phospholipids

1 reference

https://api.crossref.org/works/10.1002%2FJNR.20408

21 January 2018

The intracellular domain of the beta-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner

1 reference

https://api.crossref.org/works/10.1002%2FJNR.20408

21 January 2018

Mint 3: a ubiquitous mint isoform that does not bind to munc18-1 or -2

1 reference

https://api.crossref.org/works/10.1002%2FJNR.20408

21 January 2018

Membrane-anchored aspartyl protease with Alzheimer's disease beta-secretase activity

1 reference

https://opencitations.net/index/coci/api/v1/citations/10.1038/990107

15 July 2023

Purification and cloning of amyloid precursor protein beta-secretase from human brain

1 reference

https://opencitations.net/index/coci/api/v1/citations/10.1038/990114

15 July 2023

Identifiers

10.1002/JNR.20408

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