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Human Amyloid beta (A4) Precursor-Like Protein 1 (APLP1) interaction partners

1. These data reveal a conserved mechanism for the binding of APP (show APP Proteins)-family proteins to HS and imply a specific regulatory role of HS modifications in the biology of APP (show APP Proteins) and APP-like (show APP Proteins) proteins.

2. APLP1 and APLP2 (show APLP2 Proteins), behave similarly to APP (show APP Proteins) in that they both associate with assembled NMDA receptors in the endoplasmic reticulum

3. CSF (show CSF2 Proteins) levels of 3 endogenous peptides derived from APLP1 (APL1beta25, APL1beta27 and APL1beta28) were decreased in Down syndrome.

4. APLP1 has a regulatory role in the nuclear translocation of APP (show APP Proteins) family intracellular domains due to the sequestration of Fe65 (show APBB1 Proteins).

5. [review] APP (show APP Proteins) and its mammalian homologs, amyloid precursor-like proteins APLP1 and APLP2 (show APLP2 Proteins), participate under physiological conditions via trans-cellular dimerization in synaptogenesis.

6. APLP1 binds the II-III loop of the Ca(v)2.3 calcium channel and that this binding promotes internalization of the channel.

7. Both APLP1 and APLP2 (show APLP2 Proteins), form transcriptionally active triple protein complexes with Mint3 (show APBA3 Proteins) and transcriptional co-activators Taz (show TAZ Proteins) andYap.

8. Human cerebrospinal fluid contains three APLP1-derived Abeta (show APP Proteins)-like peptides that are generated by beta- and gamma-cleavages at a concentration of approximately 4.5 nM.

9. APLP1 and APLP2 (show APLP2 Proteins) are processed by the gamma-secretase in a Presenilin 1 (show PSEN1 Proteins)-dependent manner and the extreme carboxyl-terminal fragments produced by this processing (APP-like (show APP Proteins) Intracellular Domain) are able to enhance Fe65 (show APBB1 Proteins)-dependent gene activation

10. APLP1 does not undergo the same type of regulated processing as APP (show APP Proteins) and APLP2 (show APLP2 Proteins).

Mouse (Murine) Amyloid beta (A4) Precursor-Like Protein 1 (APLP1) interaction partners

1. APLP1 exhibits synaptogenic activity, involving trans-synaptic dimerization. APLP1 knock-out mice show impaired basal transmission and a reduced mEPSC frequency.

2. Results suggest that APLP1 deficiency on its own does not lead to defects in synaptic plasticity, but affects synaptic transmission and network inhibition in the dentate gyrus

3. [review] A role of APP (show APP Proteins) and its two closely related homologues APLP1 and APLP2 (show APLP2 Proteins) has been determined in various aspects of nervous system development and function, in particular, for synapse formation and function.

4. findings demonstrated that NB-2 (show CNTN5 Proteins) interacts with APLP and that both NB-2 (show CNTN5 Proteins) and APLP1 are localized at presynaptic sites, suggesting that NB-2 (show CNTN5 Proteins) associates with APLP1 in a cis (show CISH Proteins) manner on the presynaptic membrane

5. Crystal structure of the E2 domain of amyloid precursor protein-like (show APP Proteins) protein 1 in complex with sucrose octasulfate.

6. The 5' UTR of the Aplp1 gene lacks any type of CAGA (show S100A8 Proteins) box. This may explain its inability to form amyloid plaques.

7. Cytoplasmic polyadenylation element (CPE (show CPE Proteins)) binding factor binds the small intracellular domain (ICD) of APLP1.

8. The results demonstrated that cell viability and neurite outgrowth of N2a cells undergoing knockdown of Aplp1 were significantly reduced, compared with N2a cells undergoing knockdown of either App (show APP Proteins) or Aplp2 (show APLP2 Proteins).