Littérature scientifique sur le sujet « APP and amyloid fragments »
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Articles de revues sur le sujet "APP and amyloid fragments"
Yokota, Masayuki, Takaomi C. Saido, Eiichi Tani, Ikuya Yamaura et Nobutaka Minami. « Cytotoxic Fragment of Amyloid Precursor Protein Accumulates in Hippocampus after Global Forebrain Ischemia ». Journal of Cerebral Blood Flow & ; Metabolism 16, no 6 (novembre 1996) : 1219–23. http://dx.doi.org/10.1097/00004647-199611000-00016.
Texte intégralChyung, Abraham S. C., Barry D. Greenberg, David G. Cook, Robert W. Doms et Virginia M. Y. Lee. « Novel β-Secretase Cleavage of β-Amyloid Precursor Protein in the Endoplasmic Reticulum/Intermediate Compartment of NT2N Cells ». Journal of Cell Biology 138, no 3 (11 août 1997) : 671–80. http://dx.doi.org/10.1083/jcb.138.3.671.
Texte intégralNiederst, Emily D., Sol M. Reyna et Lawrence S. B. Goldstein. « Axonal amyloid precursor protein and its fragments undergo somatodendritic endocytosis and processing ». Molecular Biology of the Cell 26, no 2 (15 janvier 2015) : 205–17. http://dx.doi.org/10.1091/mbc.e14-06-1049.
Texte intégralLee, Ming-Sum, Shih-Chu Kao, Cynthia A. Lemere, Weiming Xia, Huang-Chun Tseng, Ying Zhou, Rachael Neve, Michael K. Ahlijanian et Li-Huei Tsai. « APP processing is regulated by cytoplasmic phosphorylation ». Journal of Cell Biology 163, no 1 (13 octobre 2003) : 83–95. http://dx.doi.org/10.1083/jcb.200301115.
Texte intégralFeng, Fei, Yuanyuan Li, Nanqu Huang et Yong Luo. « Icaritin, an inhibitor of beta-site amyloid cleaving enzyme-1, inhibits secretion of amyloid precursor protein in APP-PS1-HEK293 cells by impeding the amyloidogenic pathway ». PeerJ 7 (10 décembre 2019) : e8219. http://dx.doi.org/10.7717/peerj.8219.
Texte intégralGhiso, J., A. Rostagno, J. E. Gardella, L. Liem, P. D. Gorevic et B. Frangione. « A 109-amino-acid C-terminal fragment of Alzheimer's-disease amyloid precursor protein contains a sequence, -RHDS-, that promotes cell adhesion ». Biochemical Journal 288, no 3 (15 décembre 1992) : 1053–59. http://dx.doi.org/10.1042/bj2881053.
Texte intégralCook, J. J., K. R. Wildsmith, D. B. Gilberto, M. A. Holahan, G. G. Kinney, P. D. Mathers, M. S. Michener et al. « Acute -Secretase Inhibition of Nonhuman Primate CNS Shifts Amyloid Precursor Protein (APP) Metabolism from Amyloid- Production to Alternative APP Fragments without Amyloid- Rebound ». Journal of Neuroscience 30, no 19 (12 mai 2010) : 6743–50. http://dx.doi.org/10.1523/jneurosci.1381-10.2010.
Texte intégralYu, Yang, Yang Gao, Bengt Winblad, Lars O. Tjernberg et Sophia Schedin-Weiss. « A Super-Resolved View of the Alzheimer’s Disease-Related Amyloidogenic Pathway in Hippocampal Neurons ». Journal of Alzheimer's Disease 83, no 2 (14 septembre 2021) : 833–52. http://dx.doi.org/10.3233/jad-215008.
Texte intégralStieren, Emily S., Amina El Ayadi, Yao Xiao, Efraín Siller, Megan L. Landsverk, Andres F. Oberhauser, José M. Barral et Darren Boehning. « Ubiquilin-1 Is a Molecular Chaperone for the Amyloid Precursor Protein ». Journal of Biological Chemistry 286, no 41 (18 août 2011) : 35689–98. http://dx.doi.org/10.1074/jbc.m111.243147.
Texte intégralOno, Kenji, Mikio Niwa, Hiromi Suzuki, Nahoko Bailey Kobayashi, Tetsuhiko Yoshida et Makoto Sawada. « Signal Sequence-Dependent Orientation of Signal Peptide Fragments to Exosomes ». International Journal of Molecular Sciences 23, no 6 (15 mars 2022) : 3137. http://dx.doi.org/10.3390/ijms23063137.
Texte intégralThèses sur le sujet "APP and amyloid fragments"
Vigier, Maxime. « Influence des lipides membranaires sur les interactions protéiques liées aux anomalies endolysosomales dans un modèle neuronal de la maladie d'Alzheimer ». Electronic Thesis or Diss., Université de Lorraine, 2022. http://www.theses.fr/2022LORR0331.
Texte intégralAlzheimer's disease (AD) is a complex and multifactorial pathology for which there is no current treatment. Several hypotheses have been proposed to explain the onset and progression of this disease, including the amyloid cascade, which predominates the field of research for the past 30 years. The amyloidogenic pathway requires the endocytosis of the APP protein in early endosomes where it undergoes two proteolytic cleavages, first by β-secretase to produce the C99 fragment, and then by γ-secretase to produce the Aβ peptide. One of the current hypotheses is that abnormalities of endocytosis and dysfunction of the endolysosomal system in neurons would constitute one of the early neuropathological mechanisms of AD, well before the neurotoxic cascade generated by Aβ and amyloid deposits. We advocate the hypothesis that changes in membrane organization, particularly during aging or due to lipid imbalances, may exacerbate or promote these dysfunctions. For this study, we used a human neuroblastoma model overexpressing the mutant protein APPswe. We first verified the presence of typical AD endolysosomal abnormalities (enlarged endosomes, blocked vesicular trafficking), to which we also associated low exosome production, chronic stress conditions that we correlated with neuronal death. Initially incriminating continuously produced Aβ in these cells, we sought to reduce its impact by inhibiting γ-secretase activity. This did not ameliorate the stress, but instead aggravated it, leading us to consider that it is the C99 fragment of APP, i.e. the substrate of Aβ production, that is the central amyloid product in the neurotoxic cascade seen in APP-overexpressing cells. The deleterious effects of C99 must occur before those of Aβ, explaining the known precocity of endolysosomal alterations. Accumulating as a result of γ-secretase inhibition, the C99 fragment interacts further with the early endosome-specific Rab5 protein. Maturation of the latter is thus prevented, blocking vesicular trafficking of the endolysosomal system. As the interactions between C99 and Rab5 occur at the membrane level of endosomes, we have modified the lipid composition of the bilayer and explored the consequences on these interactions. For this purpose, we treated SH-SY5Y-APPswe cells with docosahexaenoic acid (DHA, C22:6 n-3), the major polyunsaturated fatty acid in neuronal membranes and known for its neuroprotective properties against Aβ toxicity and AD. The expected beneficial effect on neuronal survival was indeed observed, in parallel with the unblocking of endolysosomal trafficking and exosomal production. All these changes were correlated with a dispersion between C99 and Rab5 in the membrane, suggesting that DHA treatment may initiate membrane remodeling. This remodeling may lead to protein relocalization, whereby endosomes may exchange Rab5 for Rab7 to evolve into late endosomes, thereby overcoming the initial blockage. To our knowledge, this is the first evidence that DHA can correct a phenotype directly related to AD, but its ability to remodel the neuronal membrane was previously demonstrated by our team to preserve the neurotrophic CNTF signaling in the brain of aged mice. We do not know what mechanistic principles might govern these beneficial effects, which are certainly non-specific, but we assume that by preserving the organization of the membranes of aged or chronically stressed neurons, they may prevent or restore some of the damage suffered, increase the chances of neuronal survival and thus slow AD development
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.
Texte intégralAlzheimer's disease (AD) is characterized by two distinct pathologies: neurofibrillary tangles (NFT) and extracellular amyloid plaques composed of beta-amyloid peptide (Abeta). Abeta derive from the catabolism of the Amyloid Precursor Protein (APP). A relationship between APP metabolism and NFT is observed in AD. This relation is illustrated by a significant decrease of APP-CTFs and AIDD, which correlated with the progression of NFT. APP-CTFs phosphorylation is also modified in AD. The main objectives of this thesis were to identify the degradations pathways of APP-CTFs and AICD. Our results demonstrated that increase in the phosphorylation of APP-CTFs facilitates their processing by the gamma-secretase. Moreover, our data demonstrate for the first time that the endosome/lysosome pathway mediates the degradation of AICD and we describe a novel secretion pathway of APP catabolic derivatives
Lundmark, Katarzyna. « Studies on pathogenesis of experimental AA amyloidosis : effects of amyloid enhancing factor and amyloid-like fibrils in rapid amyloid induction / ». Linköping : Univ, 2001. http://www.bibl.liu.se/liupubl/disp/disp2001/med711s.pdf.
Texte intégralPaz, Sandra Isabel Moreira Pinto Vieira Guerra e. « Phosphorylation-dependent Alzheimer's Amyloid precursor protein (APP) targeting ». Doctoral thesis, Universidade de Aveiro, 2006. http://hdl.handle.net/10773/4629.
Texte intégralA Doença de Alzheimer (DA) é uma das doenças neurodegenerativas mais comuns, e apresenta uma incidência mundial de 2-7% em indivíduos com mais de 65 anos e de cerca de 15% em indivíduos acima dos 85 anos de idade. Apesar da sua etiologia multifactorial, há uma correlação bem descrita entre esta patologia e um peptídeo neurotóxico denominado Abeta. Este peptídeo deriva fisiológica e proteoliticamente de uma glicoproteína transmembranar com características de receptor: a Proteína Percursora de Amilóide de Alzheimer (PPA). As possíveis funções fisiológicas da proteína PPA, o seu destino e vias de processamento celulares, conjuntamente com possíveis proteínas celulares que com ela interajam, são assim tópicos de interesse e objectos de investigação científica mundial. Neste contexto tem sido amplamente descrito o envolvimento do processo de fosforilação de proteínas, uma importante modificação pós-transducional que regula muitos e variados acontecimentos intracelulares, na regulação do processamento da PPA. Apesar do exposto, muito pouco é conhecido acerca da fosforilação directa da própria PPA. Esta proteína possui na sua estrutura primária sequências consenso para fosforilação, quer no seu ectodomínio quer no seu domínio intracelular, já descritas como sofrendo fosforilação “in vitro” e “in vivo”. O resíduo Serina 655 pertence a um motivo funcional da APP, 653YTSI656, que forma um sinal de internalização e/ou de “sorting” basolateral. Este domínio é também o local de ligação para a APPBP2, uma proteína que interage com os microtubulos da célula. Embora ainda mal elucidados, os mecanismos pelos quais a fosforilação proteica regula o processamento da PPA parecem incluir uma alteração no tráfego desta proteína, sugerindo que o domínio fosforilável 653YTSI656 desempenha um papel importante nesse processo. Esta dissertação visou assim contribuir para elucidar o papel da fosforilação directa da molécula de APP, mais especificamente no seu resíduo Serina 655, na regulação do direcionamento e tráfego subcelular da proteína, e nas suas possíveis clivagens proteolíticas. De forma a respondermos a essas questões desenvolvemos um modelo experimental para seguir o tráfego intracelular, que usa uma combinação de biologia molecular, técnicas de microscopia de epifluorescência e técnicas de cultura celular. Os resultados obtidos implicam este resíduo como um sinal de direcionamento subcelular da proteína APP, e revelam como o redireccionamento desta proteína por fosforilação favorece um tipo de processamento não amiloidogénico desta. Adicionalmente, a fosforilação do resíduo Serina 655 parece possuir um papel regulador da actividade da PPA como molécula de transdução de sinais. As implicações destas observações na DA e em novas aplicações terapêuticas para a doença são subsequentemente discutidas.
Alzheimer’s Disease (AD) is a common neurodegenerative disease affecting individuals worldwide with an incidence of 2-7% of post-65 and 15% of post-85 years old. This disease is multifactorial in its etiology but central to its pathology is a neurotoxic peptide termed Abeta. This peptide is physiologically derived by a proteolytic process on the transmembranar Alzheimer’s Amyloid Precursor Protein (APP). Protein phosphorylation-dependent APP processing has been widely described and although the mechanisms involved remain far from clarified, alterations in APP trafficking seem to occur as part of the answer. Furthermore, the occurrence of consensus phosphorylation sites in the APP intracellular domain has been known for long, but little was known regarding the direct phosphorylation of APP. Efforts in unravelling the role of these domains are finally being successful in placing them as key control points in APP targeting and processing. Among these consensus sequences, the less studied 653YTSI656 motif forms a characteristic internalisation and/or basolateral sorting signal sequence, and is known to be the binding site for a microtubuleinteracting protein (APPBP2). Phosphorylation of this motif was thus suggested to be involved in APP targeting regulation, hitherto all attempts failed to confirm it or even to reveal substantial evidences. In this project, the role of the 653YTSI656 idomain, and in particular the phosphorylatable serine 655, in APP trafficking and proteolytic processing was studied. In order to address this question a new experimental methodology was developed, which coupled molecular biology, fluorescence imaging, and cell culture techniques. APP point mutants, mimicking serine 655 phosphorylatedand dephosphorylated-status, and tagged with the green-fluorescent protein, were used to study protein trafficking dynamics and processing. Results obtained place serine 655 phosphorylation as a key signal in APP sorting and targeting to specific subcellular locations. Also of high relevance was the observed implication of serine 655 phosphorylation as a regulatory mechanism that maybe involved in controlling APP function as a signal transducer. The implications of these observations in AD pathogenesis and therapeutic approaches are discussed.
FCT - PRAXIS XXI/BD/16218/98
FCT - POCTI/BCI/34349/1999
Project DIADEM, QLK3-CT- 2001/02362
Fundação Calouste Gulbenkian
Fundação Astrazeneca
Rocha, Joana Fernandes da. « Characterizing Alzeimer's amyloid precursor protein (APP) neurotrophic functions ». Doctoral thesis, Universidade de Aveiro, 2017. http://hdl.handle.net/10773/22225.
Texte intégralThe Amyloid Precursor Protein (APP) is a type 1 membrane glycoprotein, mainly known as the precursor of the amyloid β-peptide, a central player in Alzheimer’s disease. Nevertheless, APP has been established as a neuromodulator of developing and mature nervous system. Alterations in the level or activity of APP and APP fragments seem to play a critical role in several neurodegenerative and neurodevelopment disorders. APP is a complex molecule due to the intricate relationships between its intracellular trafficking, posttranslational modifications, proteolytic cleavages, and multiple protein interactors. Various studies currently address the physiological roles of APP and its fragments, but there are contradictory results and missing pieces that need further work. The main objective of this thesis was to contribute to the characterization of the role of APP in neuronal differentiation. Particularly, we focused on mechanisms mediated by APP, its fragment sAPP, and APP phosphorylation at serine 655. First, we characterized the APP protein in Retinoic Acid (RA)-induced SHSY5Y cell differentiation. The comprehensive analysis of this model exposed a biphasic temporal response: a first early phase (D0-D4), where a sAPP/APP peak assists the emergence of new processes and their elongation into neurites; and a second phase (D4-D8) when increased holoAPP protein levels are necessary to sustain neuritic elongation and stabilization. In line with our main aim, we subsequently characterized the relationship between APP and the neurotrophic EGF-EGFR-ERK signaling pathway. We showed, for the first time, that APP interacts with proEGF, and confirmed the interaction with EGFR. Furthermore, we showed that combined APP and EGF have a synergistic effect on neuronal-like differentiation, related to enhanced ERK1/2 activation, and observed that APP modulates EGFR expression levels and trafficking. Both ERK1/2 activation and EGFR seem to be modulated by the APP S655 phosphorylation state, and phosphorylation at this residue favours dendritogenesis in mice cortical neurons. Finally, we focused on discovering APP protein interactors dependent on S655 phosphorylation and with a role in neuronal differentiation. SH-SY5Y differentiated cells, overexpressing APPWt or S655 phosphomutants, were used to immunoprecipitate the specific APP proteins and their respective interacting partners, later identified by mass spectrometry. The dephosphoS655 APP interactome was enriched in functions associated with cytoskeleton organization, and these cells were particularly associated with actin remodeling. The phosphoS655 APP interactome included proteins involved in the regulation of survival and differentiation, and in various signaling pathways, correlating well with an enhanced neurite outgrowth displayed by these cells. We hope that the knowledge here gathered can contribute to a better comprehension of APP-driven neurotrophic roles and underlying mechanisms.
A Proteína Precursora de Amilóide (APP) é uma proteína membranar mais conhecida por ser precursora do péptido Amilóide β, tendo por isso um papel central na doença de Alzheimer. Não obstante, a APP tem sido reconhecida como neuromodulador do sistema nervoso central. Alterações nos níveis ou na atividade da APP e seus fragmentos estão implicadas em diferentes doenças neurológicas. As relações entre o seu transporte intracelular, modificações pós-traducionais, corte proteolítico, e proteínas com as quais interage são complexas e multifacetadas. Talvez por isso, estudos focados no papel fisiológico da APP apresentem resultados contraditórios e muitas questões em aberto. O objetivo deste trabalho consistiu na caracterização do papel fisiológico da APP na diferenciação neuronal. Particularmente, focámo-nos nos mecanismos mediados pela APP e fragmento sAPP, e a fosforilação da APP no resíduo serina 655. Inicialmente, caracterizámos a proteína APP ao longo da diferenciação de células SH-SY5Y com ácido retinóico (RA). A análise sistemática deste modelo permitiu delimitar uma resposta bifásica: na primeira fase (D0-D4), um pico de sAPP/APP acompanha o aparecimento de novos processos e o crescimento a neurites; na segunda fase (D4-D8) o aumento nos níveis da APP suporta o crescimento e manutenção das neurites. Caracterizámos posteriormente a relação entre a APP e a via de sinalização EGF-EGFR-ERK na diferenciação neuronal. Demonstrámos, pela primeira vez, que a APP interage com o proEGF, e confirmámos a sua ligação ao EGFR. Adicionalmente, observámos que a APP e o EGF têm um efeito sinérgico na diferenciação tipo-neuronal e aumento da ativação da ERK1/2, e que a APP afeta os níveis e transporte do EGFR. Estes mecanismos são modulados pela fosforilação da APP na S655, que favorece a dendritogénese em neurónios corticais de ratinho. Por último, focámo-nos na identificação de proteínas interatoras da APP dependentes da fosforilação em S655 e com função na diferenciação neuronal. Usando células SH-SY5Y diferenciadas e a sobrexpressar a APPWt ou fosfomutantes da S655, imunoprecipitámos as diferentes APPs e seus interatores, posteriormente identificados por espectrometria de massa. O interatoma da APP desfosforilada é enriquecido em funções associadas à organização do citoesqueleto, levando a uma maior reorganização da actina. O interatoma da APP fosforilada incluí proteínas envolvidas na regulação de sobrevivência e diferenciação, e em várias vias de sinalização, o que se correlaciona com o favorecimento de neurites nestas células. Com este trabalho esperamos ter contribuído para uma melhor compreensão do papel neurotrófico da APP e dos mecanismos subjacentes a este.
Kim, Joung-Hun. « Electrophysiological and biochemical studies of #beta#-amyloid precursor protein fragments ». Thesis, Imperial College London, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.394383.
Texte intégralBark, Niklas. « Biophysical studies on aggregation processes and amyloid fibrils with focus on Alzheimer's disease / ». Stockholm, 2004. http://diss.kib.ki.se/2004/91-7140-036-2/.
Texte intégralCrawford, Fiona Caroline. « Chromosome 21, the amyloid precursor gene and Alzheimer's disease ». Thesis, University of London, 1993. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.360759.
Texte intégralBowes, Simone. « Processing of Alzheimer's amyloid precursor protein in cultured cells ». Thesis, Sheffield Hallam University, 1999. http://shura.shu.ac.uk/19377/.
Texte intégralSellstedt, Magnus. « Development of 2-Pyridone-based central fragments : Affecting the aggregation of amyloid proteins ». Doctoral thesis, Umeå universitet, Kemiska institutionen, 2012. http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-53705.
Texte intégralLivres sur le sujet "APP and amyloid fragments"
Sekoulidis, Joannis. Transgenic analysis of the Alzheimer's disease amyloid precursor protein (APP). 2004.
Trouver le texte intégralDooren, Tom V. Biochemical & Immuno-histochemical Analysis of App-processing & Amyloid Pathology in Single & Multiple Transgenic Mice As Models for Alzheimer's Disease. Leuven Univ Pr, 2006.
Trouver le texte intégralAllen, Shelley J. Pathophysiology of Alzheimer’s disease. Oxford University Press, 2017. http://dx.doi.org/10.1093/med/9780198779803.003.0002.
Texte intégralWetzel, Ronald, et Rakesh Mishra. Structural Biology. Oxford University Press, 2014. http://dx.doi.org/10.1093/med/9780199929146.003.0012.
Texte intégralChapitres de livres sur le sujet "APP and amyloid fragments"
Suh, Yoo-Hun, Ji-Heui Seo, Yanji Xu, Chaejeong Heo, Najung Kim, Jun Ho Choi, Se Hoon Choi, Jong-Cheol Rah, Keun-A. Chang et Won-Hyuk Suh. « Toxicity of App Fragments ». Dans Mapping the Progress of Alzheimer’s and Parkinson’s Disease, 19–25. Boston, MA : Springer US, 2002. http://dx.doi.org/10.1007/978-0-306-47593-1_4.
Texte intégralEsposito, Luke A. « Measuring APP Carboxy-Terminal Fragments ». Dans Methods in Molecular Biology, 71–84. Totowa, NJ : Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60761-744-0_6.
Texte intégralSisodia, S. S., H. H. Slunt, C. Van Koch, A. C. Y. Lo et G. Thinakaran. « Studies of APP Biology : Analysis of APP Secretion and Characterization of an APP Homologue, APLP2 ». Dans Amyloid Protein Precursor in Development, Aging and Alzheimer’s Disease, 121–33. Berlin, Heidelberg : Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-662-01135-5_11.
Texte intégralGardella, J. E., J. Ghiso, G. A. Gorgone, D. Marratta, A. P. Kaplan, B. Frangione et P. D. Gorevic. « Immunoreactivity of Alzheimer Amyloid Precursor Protein (APP) Specific Antisera with Platelet Granule Constituents ». Dans Amyloid and Amyloidosis 1990, 722–25. Dordrecht : Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3284-8_177.
Texte intégralGustavsson, Å., U. Engström et P. Westermark. « Formation of Fibrils by Normal Transthyretin and Synthetic Transthyretin Fragments In Vitro ». Dans Amyloid and Amyloidosis 1990, 591–94. Dordrecht : Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3284-8_145.
Texte intégralMulthaup, G. « Studies of the Amyloid Precursor Protein (APP) in Brain : Regulation of APP-Ligand Binding ». Dans Amyloid Protein Precursor in Development, Aging and Alzheimer’s Disease, 76–89. Berlin, Heidelberg : Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-662-01135-5_8.
Texte intégralLinke, R. P., J. Floege, F. Lottspeich et R. Deutzmann. « Several β2-Microglobulin Fragments Identified in an Amyloidoma in a Patient with Long-Term Hemodialysis ». Dans Amyloid and Amyloidosis 1990, 369–72. Dordrecht : Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3284-8_93.
Texte intégralMarks, N., et M. J. Berg. « Secretase Processing of Amyloid Precursor Protein (APP) and Neurodegeneration ». Dans Handbook of Neurochemistry and Molecular Neurobiology, 469–514. Boston, MA : Springer US, 2007. http://dx.doi.org/10.1007/978-0-387-30379-6_16.
Texte intégralLaczkó, I., S. Holly, Z. Kónya, J. Varga, K. Soós, M. Hollósi et B. Penke. « Synthesis and structure investigation of amyloid small peptide fragments ». Dans Peptides 1994, 549–50. Dordrecht : Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-011-1468-4_249.
Texte intégralTobiassen, R., Å. Gustafsson, K. Sletten, B. Johansson et P. Westermark. « Structural Studies of Transthyretin and Related Fragments Obtained from a Swedish Patient (V-ÅS 280) with Senile Systemic Amylodosis ». Dans Amyloid and Amyloidosis 1990, 631–34. Dordrecht : Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3284-8_155.
Texte intégralActes de conférences sur le sujet "APP and amyloid fragments"
Frankiewicz, Lukasz P., Wiktor Banachewicz et Aleksandra Misicka. « Aggregation studies of β-amyloid and prion protein fragments ». Dans IXth Conference Biologically Active Peptides. Prague : Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 2005. http://dx.doi.org/10.1135/css200508023.
Texte intégralShutikov, A. A., G. M. Arzumanyan, K. Z. Mamatkulov, E. Arynbek et D. S. Zakrytnaya. « ANALYSIS OF THE SECONDARY STRUCTURE OF AΒ (1-42) PEPTIDE IN THE AMIDE I REGION BY RAMAN SPECTROSCOPY ». Dans X Международная конференция молодых ученых : биоинформатиков, биотехнологов, биофизиков, вирусологов и молекулярных биологов — 2023. Novosibirsk State University, 2023. http://dx.doi.org/10.25205/978-5-4437-1526-1-220.
Texte intégralTheobald, Robert, et Henry Han. « Memantine Effects on Amyloid Plaque Load and Cognition in APP/SP1 Transgenic Mice ». Dans ASPET 2024 Annual Meeting Abstract. American Society for Pharmacology and Experimental Therapeutics, 2024. http://dx.doi.org/10.1124/jpet.117.916790.
Texte intégralSoares, Carolina, Débora G. Souza, Andreia Silva da Rocha, Luiza Machado, Bruna Bellaver et Eduardo R. Zimmer. « BRAIN ENERGETICS EVALUATION IN EARLY STAGES OF AMYLOID PATHOLOGY IN A RAT MODEL OF ALZHEIMER’S DISEASE ». Dans XIII Meeting of Researchers on Alzheimer's Disease and Related Disorders. Zeppelini Editorial e Comunicação, 2021. http://dx.doi.org/10.5327/1980-5764.rpda086.
Texte intégralGerstenmayer, Matthieu, Erwan Selingue, Francoise Geffroy, Sebastien Meriaux et Benoit Larrat. « Notice of Removal : Weekly ultrasound induced blood-brain barrier openings seem to restore memory in APP/PS1dE9 amyloid mice model ». Dans 2017 IEEE International Ultrasonics Symposium (IUS). IEEE, 2017. http://dx.doi.org/10.1109/ultsym.2017.8092315.
Texte intégralSobol, Anna, Paola Galluzzo, Shuang Liang, Brittany Rambo, Sylvia Skucha, Megan Weber et Maurizio Bocchetta. « Abstract C40 : Amyloid precursor protein (APP) synchronizes cell cycle progression and the rate of global protein synthesis in dividing cells ». Dans Abstracts : Third AACR International Conference on Frontiers in Basic Cancer Research - September 18-22, 2013 ; National Harbor, MD. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.fbcr13-c40.
Texte intégralShakila, G., C. Meganathan, N. Sundaraganesan et H. Saleem. « Pharmacophore based virtual screening, molecular docking and density functional theory approaches to discover the potent beta-amyloid precursor protein (B-APP) inhibitor ». Dans 7TH NATIONAL CONFERENCE ON HIERARCHICALLY STRUCTURED MATERIALS (NCHSM-2019). AIP Publishing, 2019. http://dx.doi.org/10.1063/1.5114592.
Texte intégralJimenez, Stephannie, Gordana Rakic, Silvia Takahashi et Nicolás Cardozo. « Cross-language Clone Detection for Mobile Apps ». Dans Congresso Ibero-Americano em Engenharia de Software. Sociedade Brasileira de Computação, 2023. http://dx.doi.org/10.5753/cibse.2023.24696.
Texte intégralRocha, Andreia, Bruna Bellaver, Luiza Machado, Carolina Soares, Pâmela C. L. Ferreira, Samuel Greggio Gianina T. Venturin, Jaderson C. da Costa, Diogo O. Souza et Eduardo R. Zimmer. « TEMPORAL CHANGES IN ASTROCYTES ON A TRANSGENIC RAT MODEL OF AD ». Dans XIII Meeting of Researchers on Alzheimer's Disease and Related Disorders. Zeppelini Editorial e Comunicação, 2021. http://dx.doi.org/10.5327/1980-5764.rpda023.
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