APLP1 Antibody

1. The direct cleavage of APLP1 is a novel feature of the gamma-secretase. PMID: 29382944
2. Results provide direct evidence that APLP1 functions as a neuronal zinc-dependent adhesion protein and allow a more detailed understanding of the molecular mechanisms driving the formation of APLP1 adhesion platforms. PMID: 29021345
3. The results show that in cognitively normal young adults carrying APlp1 mutations showed different spontaneous brain activity patterns without cerebral structural differences. PMID: 28987665
4. These data reveal a conserved mechanism for the binding of APP-family proteins to HS and imply a specific regulatory role of HS modifications in the biology of APP and APP-like proteins. PMID: 25760599
5. APLP1 and APLP2, behave similarly to APP in that they both associate with assembled NMDA receptors in the endoplasmic reticulum PMID: 25683482
6. CSF levels of 3 endogenous peptides derived from APLP1 (APL1beta25, APL1beta27 and APL1beta28) were decreased in Down syndrome. PMID: 24740518
7. APLP1 has a regulatory role in the nuclear translocation of APP family intracellular domains due to the sequestration of Fe65. PMID: 23874953
8. [review] APP and its mammalian homologs, amyloid precursor-like proteins APLP1 and APLP2, participate under physiological conditions via trans-cellular dimerization in synaptogenesis. PMID: 21952790
9. APLP1 binds the II-III loop of the Ca(v)2.3 calcium channel and that this binding promotes internalization of the channel. PMID: 22178872
10. Both APLP1 and APLP2, form transcriptionally active triple protein complexes with Mint3 and transcriptional co-activators Taz andYap. PMID: 21178287
11. The 2.1 A resolution electron density map reveals phosphate ions that are bound to the protein surface. Mutational analysis shows that protein residues interacting with the phosphate ions are also involved in heparin binding. PMID: 21574595
12. Human cerebrospinal fluid contains three APLP1-derived Abeta-like peptides that are generated by beta- and gamma-cleavages at a concentration of approximately 4.5 nM. PMID: 20049724
13. APLP1 and APLP2 are processed by the gamma-secretase in a Presenilin 1-dependent manner and the extreme carboxyl-terminal fragments produced by this processing (APP-like Intracellular Domain) are able to enhance Fe65-dependent gene activation PMID: 12228233
14. APLP1 does not undergo the same type of regulated processing as APP and APLP2. PMID: 14597230
15. APLP1 and APLP2 and APP are processed similarly to act via the same nuclear target and are regulated by BACE 1 in neurons PMID: 14699153
16. APLP-1 and APLP-2 are processed by alpha- and gamma-secretase-like cleavages, and their intracellular domains can be released by cleavage at epsilon-sites. APLP-2 processing appears to be the most elaborate and to involve alternative cleavage sites. PMID: 14970212
17. The 5' UTR of the Aplp1 gene lacks any type of CAGA box. This may explain its inability to form amyloid plaques. PMID: 15208260
18. APLP1 affects the endocytosis of APP and makes more APP available for alpha-secretase cleavage PMID: 16344553
19. APLP1 is differentially upregulated in gastrointestinal neuroendocrine tumours and may be important for the dissemination of small intestinal carcinoids PMID: 18430897
20. Coexpression of APP with APLP1 or APLP2 leads to diminished generation of Abeta42 PMID: 19126676
21. neither cell-derived nor chemically synthesized APLP1-derived peptide influences the oligomerization or aggregation of Abeta PMID: 19401174

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HGNC: 597

OMIM: 104775

KEGG: hsa:333

STRING: 9606.ENSP00000221891

UniGene: Hs.74565