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Journal articles on the topic 'APP intracellular domain'

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Published: 4 June 2021

Last updated: 12 February 2022

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1

Sudhof, Thomas C. "S1-01-04 APP intracellular domain." Neurobiology of Aging 25 (July 2004): S2—S3. http://dx.doi.org/10.1016/s0197-4580(04)80007-1.

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2

Higgs, Rowan. "APP intracellular domain contributes to AD pathogenesis." Nature Reviews Neurology 6, no. 1 (2010): 2. http://dx.doi.org/10.1038/nrneurol.2009.201.

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3

Kim, Sun-Yee, Mi-Yeon Kim, Jung-Soon Mo, and Hee-Sae Park. "Notch1 intracellular domain suppresses APP intracellular domain—Tip60–Fe65 complex mediated signaling through physical interaction." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1773, no. 6 (2007): 736–46. http://dx.doi.org/10.1016/j.bbamcr.2007.02.001.

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4

Ceglia, Ilaria, Christiane Reitz, Jodi Gresack та ін. "APP intracellular domain–WAVE1 pathway reduces amyloid-β production". Nature Medicine 21, № 9 (2015): 1054–59. http://dx.doi.org/10.1038/nm.3924.

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5

Barbagallo, Alessia P. M., Richard Weldon, Robert Tamayev, et al. "Tyr682 in the Intracellular Domain of APP Regulates Amyloidogenic APP Processing In Vivo." PLoS ONE 5, no. 11 (2010): e15503. http://dx.doi.org/10.1371/journal.pone.0015503.

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6

Hoe, Hyang-Sook, David Wessner, Uwe Beffert, Amanda G. Becker, Yasuji Matsuoka, and G. William Rebeck. "F-Spondin Interaction with the Apolipoprotein E Receptor ApoEr2 Affects Processing of Amyloid Precursor Protein." Molecular and Cellular Biology 25, no. 21 (2005): 9259–68. http://dx.doi.org/10.1128/mcb.25.21.9259-9268.2005.

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ABSTRACT A recent study showed that F-spondin, a protein associated with the extracellular matrix, interacted with amyloid precursor protein (APP) and inhibited β-secretase cleavage. F-spondin contains a thrombospondin domain that we hypothesized could interact with the family of receptors for apolipoprotein E (apoE). Through coimmunoprecipitation experiments, we demonstrated that F-spondin interacts with an apoE receptor (apoE receptor 2 [ApoEr2]) through the thrombospondin domain of F-spondin and the ligand binding domain of ApoEr2. Full-length F-spondin increased coimmunoprecipitation of Ap

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7

Kögel, Donat, Caoimhín G. Concannon, Thorsten Müller, et al. "The APP intracellular domain (AICD) potentiates ER stress-induced apoptosis." Neurobiology of Aging 33, no. 9 (2012): 2200–2209. http://dx.doi.org/10.1016/j.neurobiolaging.2011.06.012.

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8

Wahler, Anke, Anja-Silke Beyer, Ilona E. Keller, et al. "Engulfment adaptor phosphotyrosine-binding-domain-containing 1 (GULP1) is a nucleocytoplasmic shuttling protein and is transactivationally active together with low-density lipoprotein receptor-related protein 1 (LRP1)." Biochemical Journal 450, no. 2 (2013): 333–43. http://dx.doi.org/10.1042/bj20121100.

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APP (amyloid precursor protein) and LRP1 (low-density lipoprotein receptor-related protein 1) have been implicated in the pathogenesis of AD (Alzheimer's disease). They are functionally linked by Fe65, a PTB (phosphotyrosine-binding)-domain-containing adaptor protein that binds to intracellular NPxY-motifs of APP and LRP1, thereby influencing expression levels, cellular trafficking and processing. Additionally, Fe65 has been reported to mediate nuclear signalling in combination with intracellular domains of APP and LRP1. We have previously identified another adaptor protein, GULP1 (engulfment

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9

Kim, M. Y., J. S. Mo, E. J. Ann, et al. "Regulation of Notch1 signaling by the APP intracellular domain facilitates degradation of the Notch1 intracellular domain and RBP-Jk." Journal of Cell Science 124, no. 11 (2011): 1831–43. http://dx.doi.org/10.1242/jcs.076117.

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10

Wiley, Jesse C., Elise A. Smith, Mark P. Hudson, Warren C. Ladiges та Mark Bothwell. "Fe65 Stimulates Proteolytic Liberation of the β-Amyloid Precursor Protein Intracellular Domain". Journal of Biological Chemistry 282, № 46 (2007): 33313–25. http://dx.doi.org/10.1074/jbc.m706024200.

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The β-amyloid precursor protein (APP)-binding protein Fe65 is involved in APP nuclear signaling and several steps in APP proteolytic processing. In this study, we show that Fe65 stimulates γ-secretase-mediated liberation of the APP intracellular domain (AICD). The mechanism of Fe65-mediated stimulation of AICD formation appears to be through enhanced production of the carboxyl-terminal fragment substrates of γ-secretase and direct stimulation of processing by γ-secretase. The stimulatory capacity of Fe65 is isoform-dependent, as the non-neuronal and a2 isoforms promote APP processing more effe

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11

Borg, J. P., J. Ooi, E. Levy, and B. Margolis. "The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein." Molecular and Cellular Biology 16, no. 11 (1996): 6229–41. http://dx.doi.org/10.1128/mcb.16.11.6229.

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The phosphotyrosine interaction (PI) domains (also known as the PTB, or phosphotyrosine binding, domains) of Shc and IRS-1 are recently described domains that bind peptides phosphorylated on tyrosine residues. The PI/PTB domains differ from Src homology 2 (SH2) domains in that their binding specificity is determined by residues that lie amino terminal and not carboxy terminal to the phosphotyrosine. Recently, it has been appreciated that other cytoplasmic proteins also contain PI domains. We now show that the PI domain of X11 and one of the PI domains of FE65, two neuronal proteins, bind to th

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12

Checler, Frederic, Claire Sunyach, Raphaelle Pardossi-Piquard, et al. "The γ /η-Secretase-Derived APP Intracellular Domain Fragments Regulate p53." Current Alzheimer Research 4, no. 4 (2007): 423–26. http://dx.doi.org/10.2174/156720507781788945.

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13

Li, Zhidong, Weiwei Wang, Fangfang Zhou, et al. "Interaction of stathmin-like 2 protein with the APP intracellular domain." Tsinghua Science and Technology 10, no. 4 (2005): 484–88. http://dx.doi.org/10.1016/s1007-0214(05)70104-8.

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14

Matrone, Carmela, Luca La Rosa, Alessia Barbagallo, et al. "P3-210: Tyr 682 on APP intracellular domain modulates NGF signaling." Alzheimer's & Dementia 7 (July 2011): S583. http://dx.doi.org/10.1016/j.jalz.2011.05.1651.

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15

Nakaya, Tadashi, Eiko Kawaguchi, and Toshiharu Suzuki. "P1-285 Phosphorylation of APP at THR668 regulates the function of APP intracellular domain fragment." Neurobiology of Aging 25 (July 2004): S177. http://dx.doi.org/10.1016/s0197-4580(04)80598-0.

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16

DUILIO, Angela, Raffaella FARAONIO, Giuseppina MINOPOLI, Nicola ZAMBRANO та Tommaso RUSSO. "Fe65L2: a new member of the Fe65 protein family interacting with the intracellular domain of the Alzheimer's β-amyloid precursor protein". Biochemical Journal 330, № 1 (1998): 513–19. http://dx.doi.org/10.1042/bj3300513.

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We previously demonstrated that Fe65 protein is one of the ligands of the cytoplasmic domain of β-amyloid precursor protein (APP). Another ligand of this molecule was recently identified; it is similar to Fe65, so it was named Fe65-like (Fe65L1). Herein we describe the cloning of another Fe65-like cDNA (Fe65L2), similar to Fe65 and to Fe65L1, which encodes a protein of approx. 50 kDa. Its cognate mRNA is expressed in various rat tissues, particularly in brain and testis. The three members of the Fe65 protein family share several structural and functional characteristics. The primary structures

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17

Ghosal, Kaushik, Andrea Stathopoulos, and Sanjay W. Pimplikar. "APP Intracellular Domain Impairs Adult Neurogenesis in Transgenic Mice by Inducing Neuroinflammation." PLoS ONE 5, no. 7 (2010): e11866. http://dx.doi.org/10.1371/journal.pone.0011866.

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18

Ikeuchi, Takeshi, та Sangram S. Sisodia. "Cell-Free Generation of the Notch1 Intracellular Domain (NICD) and APP-CTFγ". NeuroMolecular Medicine 1, № 1 (2002): 43–54. http://dx.doi.org/10.1385/nmm:1:1:43.

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19

Zhou, Fangfang, Kai Gong, Bo Song, et al. "The APP intracellular domain (AICD) inhibits Wnt signalling and promotes neurite outgrowth." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1823, no. 8 (2012): 1233–41. http://dx.doi.org/10.1016/j.bbamcr.2012.05.011.

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20

Pimplikar, Sanjay W., and Kaushik Ghosal. "P4-177: Aberrant adult neurogenesis in transgenic mice expressing APP intracellular domain." Alzheimer's & Dementia 5, no. 4S_Part_16 (2009): P483. http://dx.doi.org/10.1016/j.jalz.2009.04.744.

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21

Konietzko, Uwe, Bernhard Kohli, Debomoy Lahiri, and Roger M. Nitsch. "P1-419: The APP intracellular domain localizes to nuclear sites of transcription." Alzheimer's & Dementia 2 (July 2006): S220. http://dx.doi.org/10.1016/j.jalz.2006.05.798.

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22

Grimm, Marcus O. W., Sven Grösgen, Tatjana L. Rothhaar, et al. "Intracellular APP Domain Regulates Serine-Palmitoyl-CoA Transferase Expression and Is Affected in Alzheimer's Disease." International Journal of Alzheimer's Disease 2011 (2011): 1–8. http://dx.doi.org/10.4061/2011/695413.

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Lipids play an important role as risk or protective factors in Alzheimer's disease (AD), a disease biochemically characterized by the accumulation of amyloid beta peptides (Aβ), released by proteolytic processing of the amyloid precursor protein (APP). Changes in sphingolipid metabolism have been associated to the development of AD. The key enzyme in sphingolipidde novosynthesis is serine-palmitoyl-CoA transferase (SPT). In the present study we identified a new physiological function of APP in sphingolipid synthesis. The APP intracellular domain (AICD) was found to decrease the expression of t

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23

Vogt, D. L., D. Thomas, V. Galvan, D. E. Bredesen, B. T. Lamb, and S. W. Pimplikar. "Abnormal neuronal networks and seizure susceptibility in mice overexpressing the APP intracellular domain." Neurobiology of Aging 32, no. 9 (2011): 1725–29. http://dx.doi.org/10.1016/j.neurobiolaging.2009.09.002.

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24

Ghosal, K., D. L. Vogt, M. Liang, Y. Shen, B. T. Lamb, and S. W. Pimplikar. "Alzheimer's disease-like pathological features in transgenic mice expressing the APP intracellular domain." Proceedings of the National Academy of Sciences 106, no. 43 (2009): 18367–72. http://dx.doi.org/10.1073/pnas.0907652106.

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25

Lee, Mi-Ra, Deresa Lee, Soo Kyung Shin, Young Ho Kim, and Cheol Yong Choi. "Inhibition of APP intracellular domain (AICD) transcriptional activity via covalent conjugation with Nedd8." Biochemical and Biophysical Research Communications 366, no. 4 (2008): 976–81. http://dx.doi.org/10.1016/j.bbrc.2007.12.066.

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26

Ryan, Kathleen A., and Sanjay W. Pimplikar. "Activation of GSK-3 and phosphorylation of CRMP2 in transgenic mice expressing APP intracellular domain." Journal of Cell Biology 171, no. 2 (2005): 327–35. http://dx.doi.org/10.1083/jcb.200505078.

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Amyloid precursor protein (APP), implicated in Alzheimer's disease, is a trans-membrane protein of undetermined function. APP is cleaved by γ-secretase that releases the APP intracellular domain (AICD) in the cytoplasm. In vitro studies have implicated AICD in cell signaling and transcriptional regulation, but its biologic relevance has been uncertain and its in vivo function has not been examined. To investigate its functional role, we generated AICD transgenic mice, and found that AICD causes significant biologic changes in vivo. AICD transgenic mice show activation of glycogen synthase kina

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27

Treiber, Carina, Andreas Simons, Markus Strauss, et al. "Clioquinol Mediates Copper Uptake and Counteracts Copper Efflux Activities of the Amyloid Precursor Protein of Alzheimer's Disease." Journal of Biological Chemistry 279, no. 50 (2004): 51958–64. http://dx.doi.org/10.1074/jbc.m407410200.

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The key protein in Alzheimer's disease, the amyloid precursor protein (APP), is a ubiquitously expressed copper-binding glycoprotein that gives rise to the Aβ amyloid peptide. Whereas overexpression of APP results in significantly reduced brain copper levels in three different lines of transgenic mice, knock-out animals revealed increased copper levels. A provoked rise in peripheral levels of copper reduced concentrations of soluble amyloid peptides and resulted in fewer pathogenic Aβ plaques. Contradictory evidence has been provided by the efficacy of copper chelation treatment with the drug

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28

Chang, Keun-A., Hye-Sun Kim, Tae-Young Ha, et al. "Phosphorylation of Amyloid Precursor Protein (APP) at Thr668 Regulates the Nuclear Translocation of the APP Intracellular Domain and Induces Neurodegeneration." Molecular and Cellular Biology 26, no. 11 (2006): 4327–38. http://dx.doi.org/10.1128/mcb.02393-05.

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ABSTRACT Amyloid precursor protein (APP) has eight potential phosphorylation sites in its cytoplasmic domain. Recently, it has demonstrated that the constitutive phosphorylation of APP at T668 (APP695 isoform numbering) was observed specifically in the brain. Neuron-specific phosphorylation of APP at T668 is thought to be important for neuronal functions of APP, although its exact physiological significance remains to be clarified. In this study, we show that the phosphorylation of the APP intracellular domain (AICD) at T668 is essential for its binding to Fe65 and its nuclear translocation an

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29

Duggan, Claire, and Stephen High. "P4-264 Degradation of the APP intracellular domain in a homolgous cell-free system." Neurobiology of Aging 25 (July 2004): S550. http://dx.doi.org/10.1016/s0197-4580(04)81822-0.

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30

Goodger, Z. V., L. Rajendran, A. Trutzel, B. M. Kohli, R. M. Nitsch, and U. Konietzko. "Nuclear signaling by the APP intracellular domain occurs predominantly through the amyloidogenic processing pathway." Journal of Cell Science 122, no. 20 (2009): 3703–14. http://dx.doi.org/10.1242/jcs.048090.

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31

Ghosal, Kaushik, Qingyuan Fan, Hana N. Dawson, and Sanjay W. Pimplikar. "Tau Protein Mediates APP Intracellular Domain (AICD)-Induced Alzheimer’s-Like Pathological Features in Mice." PLOS ONE 11, no. 7 (2016): e0159435. http://dx.doi.org/10.1371/journal.pone.0159435.

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32

Shu, R., W. Wong, Q. H. Ma, et al. "APP intracellular domain acts as a transcriptional regulator of miR-663 suppressing neuronal differentiation." Cell Death & Disease 6, no. 2 (2015): e1651-e1651. http://dx.doi.org/10.1038/cddis.2015.10.

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33

Riese, Florian, Sonja Grinschgl, Manuel T. Gersbacher, et al. "Visualization and Quantification of APP Intracellular Domain-Mediated Nuclear Signaling by Bimolecular Fluorescence Complementation." PLoS ONE 8, no. 9 (2013): e76094. http://dx.doi.org/10.1371/journal.pone.0076094.

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34

Pimplikar, Sanjay, Kaushik Ghosal, and Qingyuan Fan. "P2-330: Amyloid-independent mechanisms of Alzheiemer's disease: The role of APP intracellular domain." Alzheimer's & Dementia 7 (July 2011): S415. http://dx.doi.org/10.1016/j.jalz.2011.05.1206.

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35

Pimplikar, Sanjay W. "O1-03-06: Transgenic mice expressing APP intracellular domain recapitulate Alzheimer's disease pathological features." Alzheimer's & Dementia 5, no. 4S_Part_3 (2009): P83. http://dx.doi.org/10.1016/j.jalz.2009.05.210.

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36

Deyts, Carole, Mary Clutter, Nicholas Pierce, Pedro E. Cruz, Todd E. Golde, and Angèle Parent. "P1-177: OVEREXPRESSION OF APP INTRACELLULAR DOMAIN RESCUES MEMORY IN ALZHEIMER'S DISEASE MOUSE MODELS." Alzheimer's & Dementia 14, no. 7S_Part_6 (2006): P346. http://dx.doi.org/10.1016/j.jalz.2018.06.181.

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37

Takami, Mako, та Satoru Funamoto. "γ-Secretase-Dependent Proteolysis of Transmembrane Domain of Amyloid Precursor Protein: Successive Tri- and Tetrapeptide Release in Amyloidβ-Protein Production". International Journal of Alzheimer's Disease 2012 (2012): 1–7. http://dx.doi.org/10.1155/2012/591392.

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γ-Secretase cleaves the carboxyl-terminal fragment (βCTF) of APP not only in the middle of the transmembrane domain (γ-cleavage), but also at sites close to the membrane/cytoplasm boundary (ε-cleavage), to produce the amyloidβprotein (Aβ) and the APP intracellular domain (AICD), respectively. The AICD49–99 and AICD50–99 species were identified as counterparts of the long Aβspecies Aβ48 and Aβ49, respectively. We found that Aβ40 and AICD50–99 were the predominant species in cells expressing wild-type APP and presenilin, whereas the production of Aβ42 and AICD49–99 was enhanced in cells expressi

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38

Bergman, Anna, Dorota Religa, Helena Karlström, et al. "APP intracellular domain formation and unaltered signaling in the presence of familial Alzheimer’s disease mutations." Experimental Cell Research 287, no. 1 (2003): 1–9. http://dx.doi.org/10.1016/s0014-4827(03)00117-4.

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39

Deyts, Carole, Kulandaivelu Vetrivel, Yumiko Shepherd, Gopal Thinakaran та Angèle Parent. "P3-206: APP intracellular domain enhances neurite outgrowth through gαs coupling to adenylate cyclase signaling". Alzheimer's & Dementia 7 (липень 2011): S582. http://dx.doi.org/10.1016/j.jalz.2011.05.1647.

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40

Zhou, Fangfang, Kai Gong, Theo van Laar, Yandao Gong та Long Zhang. "Wnt/β-catenin signal pathway stabilizes APP intracellular domain (AICD) and promotes its transcriptional activity". Biochemical and Biophysical Research Communications 412, № 1 (2011): 68–73. http://dx.doi.org/10.1016/j.bbrc.2011.07.040.

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41

Herskowitz, Jeremy H., Katrin Offe, Aniruddha Deshpande, Richard A. Kahn, Allan I. Levey та James J. Lah. "GGA1-mediated endocytic traffic of LR11/SorLA alters APP intracellular distribution and amyloid-β production". Molecular Biology of the Cell 23, № 14 (2012): 2645–57. http://dx.doi.org/10.1091/mbc.e12-01-0014.

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Proteolytic processing of the amyloid-β precursor protein (APP) and generation of amyloid-β peptide (Aβ) are key events in Alzheimer's disease (AD) pathogenesis. Cell biological and genetic evidence has implicated the low-density lipoprotein and sorting receptor LR11/SorLA in AD through mechanisms related to APP and Aβ production. Defining the cellular pathway(s) by which LR11 modulates Aβ production is critical to understanding how changes in LR11 expression affect the development of Aβ pathology in AD progression. We report that the LR11 ectodomain is required for LR11-mediated reduction of

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42

Matakatsu, Hitoshi, Seth S. Blair, and Richard G. Fehon. "The palmitoyltransferase Approximated promotes growth via the Hippo pathway by palmitoylation of Fat." Journal of Cell Biology 216, no. 1 (2016): 265–77. http://dx.doi.org/10.1083/jcb.201609094.

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The large protocadherin Fat functions to promote Hippo pathway activity in restricting tissue growth. Loss of Fat leads to accumulation of the atypical myosin Dachs at the apical junctional region, which in turn promotes growth by inhibiting Warts. We previously identified Approximated (App), a DHHC domain palmitoyltransferase, as a negative regulator of Fat signaling in growth control. We show here that App promotes growth by palmitoylating the intracellular domain of Fat, and that palmitoylation negatively regulates Fat function. Independently, App also recruits Dachs to the apical junctiona

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43

Oh, Young S., та R. James Turner. "Effect of γ-secretase inhibitors on muscarinic receptor-mediated calcium signaling in human salivary epithelial cells". American Journal of Physiology-Cell Physiology 291, № 1 (2006): C76—C82. http://dx.doi.org/10.1152/ajpcell.00508.2005.

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Altered intracellular Ca2+ signaling has been observed in cells derived from Alzheimer’s disease patients, and a possible link between γ-secretase activity and the content of intracellular Ca2+ stores has been suggested. To test this hypothesis we studied the effects of several γ-secretase inhibitors on muscarinic receptor-mediated intracellular calcium release in the human salivary gland cell line HSG. Although several inhibitors in the peptide aldehyde class partially blocked carbachol-induced Ca2+ transients, these effects did not appear to be due to γ-secretase inhibition, and overall we f

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44

De Strooper, B., and W. Annaert. "Proteolytic processing and cell biological functions of the amyloid precursor protein." Journal of Cell Science 113, no. 11 (2000): 1857–70. http://dx.doi.org/10.1242/jcs.113.11.1857.

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Recent research has identified some key players involved in the proteolytic processing of amyloid precursor protein (APP) to amyloid beta-peptide, the principal component of the amyloid plaques in Alzheimer patients. Interesting parallels exists with the proteolysis of other proteins involved in cell differentiation, cholesterol homeostasis and stress responses. Since the cytoplasmic domain of APP is anchored to a complex protein network that might function in axonal elongation, dendritic arborisation and neuronal cell migration, the proteolysis of APP might be critically involved in intracell

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45

Robinson, Ari, Sven Grösgen, Janine Mett та ін. "Upregulation of PGC ‐1α expression by A lzheimer's disease‐associated pathway: presenilin 1/amyloid precursor protein ( APP )/intracellular domain of APP". Aging Cell 13, № 2 (2013): 263–72. http://dx.doi.org/10.1111/acel.12183.

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46

Müller, Thorsten, Caoimhin G. Concannon, Manus W. Ward, et al. "Modulation of Gene Expression and Cytoskeletal Dynamics by the Amyloid Precursor Protein Intracellular Domain (AICD)." Molecular Biology of the Cell 18, no. 1 (2007): 201–10. http://dx.doi.org/10.1091/mbc.e06-04-0283.

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Amyloidogenic processing of the amyloid precursor protein (APP) results in the generation of β-amyloid, the main constituent of Alzheimer plaques, and the APP intracellular domain (AICD). Recently, it has been demonstrated that AICD has transactivation potential; however, the targets of AICD-dependent gene regulation and hence the physiological role of AICD remain largely unknown. We analyzed transcriptome changes during AICD-dependent gene regulation by using a human neural cell culture system inducible for expression of AICD, its coactivator FE65, or the combination of both. Induction of AIC

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47

Kilger, Ellen, Gabriele Vacun, Monika Palchaudhuri, Bernd Sommer, Mathias Jucker, and Cornelia Dorner-Ciossek. "P1-273 Nuclear translocation of the APP intracellular domain (AICD) and its role in cellular toxicity." Neurobiology of Aging 25 (July 2004): S174. http://dx.doi.org/10.1016/s0197-4580(04)80586-4.

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48

von Rotz, R. C. "The APP intracellular domain forms nuclear multiprotein complexes and regulates the transcription of its own precursor." Journal of Cell Science 117, no. 19 (2004): 4435–48. http://dx.doi.org/10.1242/jcs.01323.

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49

Klevanski, M., U. Herrmann, S. W. Weyer, et al. "The APP Intracellular Domain Is Required for Normal Synaptic Morphology, Synaptic Plasticity, and Hippocampus-Dependent Behavior." Journal of Neuroscience 35, no. 49 (2015): 16018–33. http://dx.doi.org/10.1523/jneurosci.2009-15.2015.

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50

Szögi, Titanilla, Ildikó Schuster, Emőke Borbély, et al. "Effects of the Pentapeptide P33 on Memory and Synaptic Plasticity in APP/PS1 Transgenic Mice: A Novel Mechanism Presenting the Protein Fe65 as a Target." International Journal of Molecular Sciences 20, no. 12 (2019): 3050. http://dx.doi.org/10.3390/ijms20123050.

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Regulated intramembrane proteolysis (RIP) of the amyloid precursor protein (APP) leads to the formation of fragments, among which the intracellular domain of APP (AICD) was also identified to be a causative of early pathological events. AICD-counteracting proteins, such as Fe65, may serve as alternative therapeutic targets of Alzheimer’s disease (AD). The detection of elevated levels of Fe65 in the brains of both human patients and APP transgenic mice may further strengthen the hypothesis that influencing the interaction between Fe65 and APP may have a beneficial effect on the course of AD. Ba

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