The intracellular domain of amyloid precursor protein interacts with flotillin-1, a lipid raft protein (Q24304873)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16480949 AND SRC:MED&resulttype=core&format=json

16 January 2020

title

The intracellular domain of amyloid precursor protein interacts with flotillin-1, a lipid raft protein (English)

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Transformation related protein 53

16 January 2020

main subject

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GOA release 2020-03-11

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5

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16 January 2020

author name string

Ting-Yu Chen

1

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16 January 2020

Pei-Hsueh Liu

2

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16 January 2020

Chi-Tun Ruan

3

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16 January 2020

Ling Chiu

4

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16 January 2020

language of work or name

English

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publication date

7 February 2006

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16480949 AND SRC:MED&resulttype=core&format=json

Biochemical and Biophysical Research Communications

16 January 2020

published in

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16480949 AND SRC:MED&resulttype=core&format=json

16 January 2020

volume

342

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16 January 2020

issue

1

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16 January 2020

page(s)

266-272

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Human neuroglobin interacts with flotillin-1, a lipid raft microdomain-associated protein

16 January 2020

cites work

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Alzheimer amyloid protein precursor complexes with brain GTP-binding protein G(o)

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A detergent-insoluble membrane compartment contains A beta in vivo

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Membrane and raft association of reggie-1/flotillin-2: role of myristoylation, palmitoylation and oligomerization and induction of filopodia by overexpression

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A physiologic signaling role for the gamma -secretase-derived intracellular fragment of APP.

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PAT1, a microtubule-interacting protein, recognizes the basolateral sorting signal of amyloid precursor protein

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The regions of the Fe65 protein homologous to the phosphotyrosine interaction/phosphotyrosine binding domain of Shc bind the intracellular domain of the Alzheimer's amyloid precursor protein

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Axonal amyloid precursor protein expressed by neurons in vitro is present in a membrane fraction with caveolae-like properties.

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APP-BP1, a novel protein that binds to the carboxyl-terminal region of the amyloid precursor protein

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Flotillin and epidermal surface antigen define a new family of caveolae-associated integral membrane proteins

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Caveolae, plasma membrane microdomains for alpha-secretase-mediated processing of the amyloid precursor protein

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Oligomeric nature of the integral membrane protein stomatin

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Flotillins/cavatellins are differentially expressed in cells and tissues and form a hetero-oligomeric complex with caveolins in vivo. Characterization and epitope-mapping of a novel flotillin-1 monoclonal antibody probe

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

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A molecular dissection of caveolin-1 membrane attachment and oligomerization. Two separate regions of the caveolin-1 C-terminal domain mediate membrane binding and oligomer/oligomer interactions in vivo

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The beta-amyloid precursor protein functions as a cytosolic anchoring site that prevents Fe65 nuclear translocation

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Association of gamma-secretase with lipid rafts in post-Golgi and endosome membranes

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Amyloidogenic processing of the Alzheimer beta-amyloid precursor protein depends on lipid rafts

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Identifiers

DOI

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16480949 AND SRC:MED&resulttype=core&format=json

16 January 2020

1 reference