| The direct cleavage of APLP1 is a novel feature of the gamma-secretase. | APLP1 is endoproteolytically cleaved by γ-secretase without previous ectodomain shedding.
Schauenburg L, Liebsch F, Eravci M, Mayer MC, Weise C, Multhaup G., Free PMC Article | 12/22/2018 |
| 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. | Direct evidence of amyloid precursor-like protein 1 trans interactions in cell-cell adhesion platforms investigated via fluorescence fluctuation spectroscopy.
Dunsing V, Mayer M, Liebsch F, Multhaup G, Chiantia S., Free PMC Article | 07/21/2018 |
| The results show that in cognitively normal young adults carrying APlp1 mutations showed different spontaneous brain activity patterns without cerebral structural differences. | Altered spontaneous brain activity pattern in cognitively normal young adults carrying mutations of APP, presenilin-1/2 and APOE ε4.
Zheng LJ, Su YY, Wang YF, Zhong J, Liang X, Zheng G, Lu GM, Zhang LJ. | 05/12/2018 |
| 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. | Interaction of the amyloid precursor protein-like protein 1 (APLP1) E2 domain with heparan sulfate involves two distinct binding modes.
Dahms SO, Mayer MC, Roeser D, Multhaup G, Than ME., Free PMC Article | 12/5/2015 |
| APLP1 and APLP2, behave similarly to APP in that they both associate with assembled NMDA receptors in the endoplasmic reticulum | APLP1 and APLP2, members of the APP family of proteins, behave similarly to APP in that they associate with NMDA receptors and enhance NMDA receptor surface expression.
Cousins SL, Dai W, Stephenson FA. | 09/5/2015 |
| CSF levels of 3 endogenous peptides derived from APLP1 (APL1beta25, APL1beta27 and APL1beta28) were decreased in Down syndrome. | Altered cerebrospinal fluid levels of amyloid β and amyloid precursor-like protein 1 peptides in Down's syndrome.
Portelius E, Hölttä M, Soininen H, Bjerke M, Zetterberg H, Westerlund A, Herukka SK, Blennow K, Mattsson N. | 01/10/2015 |
| APLP1 has a regulatory role in the nuclear translocation of APP family intracellular domains due to the sequestration of Fe65. | Turnover of amyloid precursor protein family members determines their nuclear signaling capability.
Gersbacher MT, Goodger ZV, Trutzel A, Bundschuh D, Nitsch RM, Konietzko U., Free PMC Article | 02/15/2014 |
| [review] APP and its mammalian homologs, amyloid precursor-like proteins APLP1 and APLP2, participate under physiological conditions via trans-cellular dimerization in synaptogenesis. | Structural aspects and physiological consequences of APP/APLP trans-dimerization.
Baumkötter F, Wagner K, Eggert S, Wild K, Kins S., Free PMC Article | 12/22/2012 |
| APLP1 binds the II-III loop of the Ca(v)2.3 calcium channel and that this binding promotes internalization of the channel. | APLP1 and Rab5A interact with the II-III loop of the voltage-gated Ca-channel Ca(v)2.3 and modulate its internalization differently.
Radhakrishnan K, Krieger A, Dibué M, Hescheler J, Schneider T. | 04/21/2012 |
| Both APLP1 and APLP2, form transcriptionally active triple protein complexes with Mint3 and transcriptional co-activators Taz andYap. | Signaling via amyloid precursor-like proteins APLP1 and APLP2.
Orcholski ME, Zhang Q, Bredesen DE. | 03/10/2012 |
| 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. | The E2 domains of APP and APLP1 share a conserved mode of dimerization.
Lee S, Xue Y, Hu J, Wang Y, Liu X, Demeler B, Ha Y., Free PMC Article | 08/27/2011 |
| 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. | The 28-amino acid form of an APLP1-derived Abeta-like peptide is a surrogate marker for Abeta42 production in the central nervous system.
Yanagida K, Okochi M, Tagami S, Nakayama T, Kodama TS, Nishitomi K, Jiang J, Mori K, Tatsumi S, Arai T, Ikeuchi T, Kasuga K, Tokuda T, Kondo M, Ikeda M, Deguchi K, Kazui H, Tanaka T, Morihara T, Hashimoto R, Kudo T, Steiner H, Haass C, Tsuchiya K, Akiyama H, Kuwano R, Takeda M., Free PMC Article | 03/15/2010 |
| neither cell-derived nor chemically synthesized APLP1-derived peptide influences the oligomerization or aggregation of Abeta | gamma-secretase processing of APLP1 leads to the production of a p3-like peptide that does not aggregate and is not toxic to neurons.
Minogue AM, Stubbs AK, Frigerio CS, Boland B, Fadeeva JV, Tang J, Selkoe DJ, Walsh DM. | 01/21/2010 |
| Coexpression of APP with APLP1 or APLP2 leads to diminished generation of Abeta42 | Subcellular localization and dimerization of APLP1 are strikingly different from APP and APLP2.
Kaden D, Voigt P, Munter LM, Bobowski KD, Schaefer M, Multhaup G. | 01/21/2010 |
| APLP1 is differentially upregulated in gastrointestinal neuroendocrine tumours and may be important for the dissemination of small intestinal carcinoids | Amyloid precursor-like protein 1 is differentially upregulated in neuroendocrine tumours of the gastrointestinal tract.
Arvidsson Y, Andersson E, Bergström A, Andersson MK, Altiparmak G, Illerskog AC, Ahlman H, Lamazhapova D, Nilsson O. | 01/21/2010 |
| These results suggest a possible role of APLP1 in regulation of alpha2A-adrenergic receptor trafficking. | Interaction of the amyloid precursor like protein 1 with the alpha2A-adrenergic receptor increases agonist-mediated inhibition of adenylate cyclase.
Weber B, Schaper C, Scholz J, Bein B, Rodde C, H Tonner P. | 01/21/2010 |
| APLP1 affects the endocytosis of APP and makes more APP available for alpha-secretase cleavage | Amyloid precursor-like protein 1 influences endocytosis and proteolytic processing of the amyloid precursor protein.
Neumann S, Schöbel S, Jäger S, Trautwein A, Haass C, Pietrzik CU, Lichtenthaler SF. | 01/21/2010 |
| APLP1 does not undergo the same type of regulated processing as APP and APLP2. | Accumulation of the amyloid precursor-like protein APLP2 and reduction of APLP1 in retinoic acid-differentiated human neuroblastoma cells upon curcumin-induced neurite retraction.
Adlerz L, Beckman M, Holback S, Tehranian R, Cortés Toro V, Iverfeldt K. | 01/21/2010 |
| APLP1 and APLP2 and APP are processed similarly to act via the same nuclear target and are regulated by BACE 1 in neurons | Cleavage of amyloid-beta precursor protein and amyloid-beta precursor-like protein by BACE 1.
Li Q, Südhof TC. | 01/21/2010 |
| 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. | The proteolytic processing of the amyloid precursor protein gene family members APLP-1 and APLP-2 involves alpha-, beta-, gamma-, and epsilon-like cleavages: modulation of APLP-1 processing by n-glycosylation.
Eggert S, Paliga K, Soba P, Evin G, Masters CL, Weidemann A, Beyreuther K. | 01/21/2010 |
| The 5' UTR of the Aplp1 gene lacks any type of CAGA box. This may explain its inability to form amyloid plaques. | Presence of a "CAGA box" in the APP gene unique to amyloid plaque-forming species and absent in all APLP-1/2 genes: implications in Alzheimer's disease.
Maloney B, Ge YW, Greig N, Lahiri DK. | 01/21/2010 |
| 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 | Processing of beta-amyloid precursor-like protein-1 and -2 by gamma-secretase regulates transcription.
Scheinfeld MH, Ghersi E, Laky K, Fowlkes BJ, D'Adamio L. | 01/21/2010 |