Relevant bibliographies by topics / APP intracellular domain

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  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters
  4. Conference papers

Academic literature on the topic 'APP intracellular domain'

Author: Grafiati
Published: 4 June 2021
Last updated: 12 February 2022

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Journal articles on the topic "APP intracellular domain"

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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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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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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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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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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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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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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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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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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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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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Dissertations / Theses on the topic "APP intracellular domain"

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Duggan, Claire. "The generation of the amyloid precursor protein intracellular domain." Thesis, University of Manchester, 2005. http://www.manchester.ac.uk/escholar/uk-ac-man-scw:77486.

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Alzheimer's disease (AD) is the most common cause of a progressive decline of cognitive function in aged humans. It is thought to be a result of the formation of amyloid plaques in the brain that are largely composed of β-amyloid (Aβ), which is one of the cleavage products of the amyloid precursor protein (APP). The amyloidogenic processing of APP to produce the Aβ peptides requires sequential proteolytic cleavages by the β- and γ-secretases. APP is first cleaved by the β-secretase to produce APP-C99, and this product is a substrate for further processing by the γ-secretase that cleaves within
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Margevicius, Daniel Robert. "PREVENTING STRESS SIGNALING AND INCREASED NEUROINFLAMMATION ALLEVIATES ALZHEIMER’S-LIKE PATHOLOGY IN MICE OVEREXPRESSING THE APP INTRACELLULAR DOMAIN (AICD)." Case Western Reserve University School of Graduate Studies / OhioLINK, 2015. http://rave.ohiolink.edu/etdc/view?acc_num=case1433275461.

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Bakir, Ilyas. "Molecular studies of the γ-secretase complex activity and selectivity towards the two substrates APP and Notch". Thesis, Mälardalen University, School of Sustainable Development of Society and Technology, 2010. http://urn.kb.se/resolve?urn=urn:nbn:se:mdh:diva-9622.

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<p>Alzheimer Disease (AD) is the most common neurodegenerative disorder in the world. One of the neuropathological hallmarks of AD is the senile plaques in the brain. The plaques are mainly composed of the amyloid β (Aβ) peptide. Aβ is generated from the amyloid precursor protein, APP, when it is first cleaved by the β-secretase and subsequently the γ-secretase complex. The γ-secretase complex cleaves at different sites, called γ and ε, where the γ-cleavage site generates Aβ peptides of different lengths and ε-cleavage generates the APP intracellular domain (AICD). The two major forms of Aβ is
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Rousseau, Marc-Etienne. "Studies of P-glycoprotein intracellular domains by cysteine scanning mutagenesis." Thesis, McGill University, 1999. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=30738.

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Interactions between the various intracellular loops and nucleotide binding domains (NBDs) of P-glycoprotein (P-gp), and the extent to which they contribute to protein structure and transport mechanism are widely unknown. Analogy to bacterial members of the ABC transporter family suggests that the nucleotide binding domains interact with a specific site on an intracellular loop and with each other, as a cooperative dimer, in order to energize the transport functions. To investigate this hypothesis, we have used a cysteine scanning mutagenesis strategy on four potentially interacting regions of
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Allaire, Patrick. "Biochemical and functional characterization of connecdenn and its DENN domain in intracellular trafficking." Thesis, McGill University, 2009. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=66644.

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Endocytosis and vesicle trafficking are essential for cellular division, differentiation and survival. Following endocytosis, cargo is delivered to the sorting endosome, where it is selected for degradation or recycled back to the cell surface. The various trafficking steps within the endosomal system are regulated by Rabs, small GTPases, which toggle between an inactive GDP-loaded conformation and an active GTP-loaded conformation. Clathrin-mediated endocytosis (CME) allows cargo internalization and coupling to the endosomal system via formation of clathrin-coated vesicles (
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Vingtdeux-Didier, Valérie. "Aspects moléculaires et cellulaires impliqués dans le clivage ou la dégradation des fragments carboxy-terminaux et du domaine intracellulaire du Précurseur du Peptide Amyloïde (APP-CTFs et AICD)." Lille 2, 2006. http://www.theses.fr/2006LIL2S036.

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La maladie d'Alzheimer (MA) se caractérise par la présence de deux lésions : les dégénérescences neurofibrillaires (DNF) et les dépôts amyloïdes, ces derniers résultants de l'accumulation du peptide bêta-amyloïde. Ce peptide dérive du catabolisme de l'APP (Précurseur du Peptide Amyloïde). Les travaux réalisés au laboratoire montrent qu'il existe une relation entre le métabolisme de l'APP et la progression des DNF qui s'illustre par une perte du domaine intracellulaire et des fragments carboxy-terminaux de l'APP (AICD et APP-CTFs). La phosphorylation de ces derniers est également modifiée dans
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Liu, Pei-Hsueh, and 劉姵. "Identification and Characterization of Proteins Interacting with Intracellular Domain of APP." Thesis, 2003. http://ndltd.ncl.edu.tw/handle/74261961530475610847.

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碩士<br>國立臺灣大學<br>藥學研究所<br>91<br>英文摘要 Alzheimer’s disease (AD) is a progressive neurodegenerative disorder often associated with elderliness, especially the late-onset AD. It is characterized by insoluble extracellular amyloid plaques (Aβ) and intracellular neurofibrillary tangles (NFTs). The major constituent of Aβ is derived from the amyloid precursor protein (APP) by proteolytic cleavage. The APP intracellular domain (AICD) is generated from the amyloid precursor protein (APP) by β- andγ-secretase. It has been noticed that APP and Notch undergo highly similar proteolytic proces
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Trillaud-Doppia, Émilie. "Implication du domaine intracellulaire du précurseur de la protéine amyloïde dans la modulation de la plasticité synaptique." Thèse, 2016. http://hdl.handle.net/1866/15997.

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Alzheimer's disease is the most common type of dementia in the elderly; it is characterized by early deficits in learning and memory formation and ultimately leads to a generalised loss of higher cognitive functions. While amyloid beta (Aβ) and tau are traditionally associated with the development of Alzheimer disease, recent studies suggest that other factors, like the intracellular domain (APP-ICD) of the amyloid precursor protein (APP), could play a role. In this study, we investigated whether APP-ICD could affect synaptic transmission and synaptic plasticity in the hippocampus, which is
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Book chapters on the topic "APP intracellular domain"

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Pimplikar, Sanjay W., and Anupama Suryanarayana. "Detection of APP Intracellular Domain in Brain Tissue." In Methods in Molecular Biology. Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60761-744-0_7.

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Muller, Ulrike, and Klemens Wil. "Structure and Function of the APP Intracellular Domain in Health and Disease." In Understanding Alzheimer's Disease. InTech, 2013. http://dx.doi.org/10.5772/54543.

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Deng, Luqin, Jing Jiang, and Stuart J. Frank. "Growth Hormone-Induced JAK2 Signaling and GH Receptor Downregulation: Role of GH Receptor Intracellular Domain Tyrosine Residues." In BASIC/TRANSLATIONAL - Growth Hormone & Prolactin. The Endocrine Society, 2011. http://dx.doi.org/10.1210/endo-meetings.2011.part2.p35.p2-325.

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Conference papers on the topic "APP intracellular domain"

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Andrade, Daniel L., Diana Bareyan, Jason Singer, Ryan Quinton, and Michael Engel. "Abstract 3089: Regulation of GFI proteins by Notch intracellular domains." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-3089.

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Tsimon, Myrsini, Angray Kang, Anatoliy Markiv, Christina Kousparou, and Agamemnon Epenetos. "Abstract 4441: Intracellular delivery of therapeutic siRNA via an antennapedia-RNA-binding domain fusion peptide." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-4441.

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Tremblay, Isabelle, and Marie-Josee Boucher. "Abstract 1234: Erk-dependent phosphorylation of Notch intracellular domain (NIC) correlates with increased NIC-dependent transcription." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-1234.

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Phadke, Manali S., Anurag Mishra, Natalia Krynetkaia, and Evgeny Krynetskiy. "Abstract 4395: Functional domains in glyceraldehyde-3-phosphate dehydrogenase modulating its enzymatic activity and intracellular localization." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-4395.

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"Impact of Heparan Sulphate Binding Domain of Chemokine CCL21 to Migration of Breast Cancer Cells." In Qatar University Annual Research Forum & Exhibition. Qatar University Press, 2020. http://dx.doi.org/10.29117/quarfe.2020.0132.

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Lymph node metastasis constitutes a key event in breast cancer progression. Chemokines are small proteins, which can promote metastatic spread by inducing cancer cell migration and invasion. Chemokine function is dependant upon their binding to both cell surface heparan sulphate (HS) molecules and to their specific receptor. Our group has demonstrated a significant increase in chemokine receptor CCR7 expression in cancerous breast epithelia compared to healthy controls. This study is designed to test the hypothesis that a non-HS binding forms of chemokine CCL21 can disrupt the normal response
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