Log in

Relevant bibliographies by topics / Amyloidogenic pathway / Journal articles

To see the other types of publications on this topic, follow the link: Amyloidogenic pathway.

Journal articles on the topic 'Amyloidogenic pathway'

Author: Grafiati

Published: 4 June 2021

Last updated: 14 February 2022

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the top 50 journal articles for your research on the topic 'Amyloidogenic pathway.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Browse journal articles on a wide variety of disciplines and organise your bibliography correctly.

1

Dolfe, Lisa, Bengt Winblad, Jan Johansson та Jenny Presto. "BRICHOS binds to a designed amyloid-forming β-protein and reduces proteasomal inhibition and aggresome formation". Biochemical Journal 473, № 2 (2016): 167–78. http://dx.doi.org/10.1042/bj20150920.

Full text

Abstract:

The BRICHOS domain decreases aggregation of designed amyloidogenic proteins expressed in the secretory pathway and reduces their negative effect on the proteasomal system. BRICHOS binds to aggregated forms of the amyloidogenic proteins and thereby prevents further aggregation and increases solubility.

APA, Harvard, Vancouver, ISO, and other styles

2

Ehrnhoefer, Dagmar E., Jan Bieschke, Annett Boeddrich, et al. "EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers." Nature Structural & Molecular Biology 15, no. 6 (2008): 558–66. http://dx.doi.org/10.1038/nsmb.1437.

Full text

APA, Harvard, Vancouver, ISO, and other styles

3

Askarova, Sholpan, Xiaoguang Yang та James C. M. Lee. "Impacts of Membrane Biophysics in Alzheimer's Disease: From Amyloid Precursor Protein Processing to AβPeptide-Induced Membrane Changes". International Journal of Alzheimer's Disease 2011 (2011): 1–12. http://dx.doi.org/10.4061/2011/134971.

Full text

Abstract:

An increasing amount of evidence supports the notion that cytotoxic effects of amyloid-βpeptide (Aβ), the main constituent of senile plaques in Alzheimer's disease (AD), are strongly associated with its ability to interact with membranes of neurons and other cerebral cells. Aβis derived from amyloidogenic cleavage of amyloid precursor protein (AβPP) byβ- andγ-secretase. In the nonamyloidogenic pathway, AβPP is cleaved byα-secretases. These two pathways compete with each other, and enhancing the non-amyloidogenic pathway has been suggested as a potential pharmacological approach for the treatment of AD. Since AβPP,α-,β-, andγ-secretases are membrane-associated proteins, AβPP processing and Aβproduction can be affected by the membrane composition and properties. There is evidence that membrane composition and properties, in turn, play a critical role in Aβcytotoxicity associated with its conformational changes and aggregation into oligomers and fibrils. Understanding the mechanisms leading to changes in a membrane's biophysical properties and how they affect AβPP processing and Aβtoxicity should prove to provide new therapeutic strategies for prevention and treatment of AD.

APA, Harvard, Vancouver, ISO, and other styles

4

Hooper, N. M. "Roles of proteolysis and lipid rafts in the processing of the amyloid precursor protein and prion protein." Biochemical Society Transactions 33, no. 2 (2005): 335–38. http://dx.doi.org/10.1042/bst0330335.

Full text

Abstract:

In the amyloidogenic pathway, the APP (amyloid precursor protein) is proteolytically processed by the β- and γ-secretases to release the Aβ (amyloid-β) peptide that is neurotoxic and aggregates in the brains of patients suffering from Alzheimer's disease. In the non-amyloidogenic pathway, APP is cleaved by α-secretase within the Aβ domain, precluding deposition of intact Aβ peptide. The cellular form of the PrPC (prion protein) undergoes reactive oxygen species-mediated β-cleavage within the copper-binding octapeptide repeats or, alternatively, α-cleavage within the central hydrophobic neurotoxic domain. In addition, PrPC is shed from the membrane by the action of a zinc metalloprotease. Members of the ADAM (a disintegrin and metalloproteinase) family of zinc metalloproteases, notably ADAM10 and TACE (ADAM17) display α-secretase activity towards APP and appear to be responsible for the α-cleavage of PrPC. The amyloidogenic cleavage of APP by the β- and γ-secretases appears to occur preferentially in cholesterol-rich lipid rafts, while the conversion of PrPC into the infectious form PrPSc also appears to occur in these membrane domains.

APA, Harvard, Vancouver, ISO, and other styles

5

Ramesh, Sindhu, Manoj Govindarajulu, Tyler Lynd та ін. "SIRT3 activator Honokiol attenuates β-Amyloid by modulating amyloidogenic pathway". PLOS ONE 13, № 1 (2018): e0190350. http://dx.doi.org/10.1371/journal.pone.0190350.

Full text

APA, Harvard, Vancouver, ISO, and other styles

6

Huang, Ding-Siang, Yu-Chen Yu, Chung-Hsin Wu, and Jung-Yaw Lin. "Protective Effects of Wogonin against Alzheimer’s Disease by Inhibition of Amyloidogenic Pathway." Evidence-Based Complementary and Alternative Medicine 2017 (2017): 1–13. http://dx.doi.org/10.1155/2017/3545169.

Full text

Abstract:

One of the pathogenic systems of Alzheimer’s disease (AD) is the formation ofβ-amyloid plaques in the brains of patients, and amyloidogenic activity becomes one of the therapeutic targets. Here, we report wogonin, one of the major active constituting components inScutellaria baicalensis, which has the neuroprotective effects on amyloid-βpeptides- (Aβ-) induced toxicity. Oral wogonin treatment improved the performance of triple transgenic AD mice (h-APPswe, h-Tau P301L, and h-PS1 M146V) on the Morris water maze, Y-maze, and novel object recognition. Furthermore, wogonin activated the neurite outgrowth of AD cells by increasing neurite length and complexity of Tet-On Aβ42-GFP SH-SY5Y neuroblastoma cells (AD cells) and attenuated amyloidogenic pathway by decreasing the levels ofβ-secretase, APPβ-C-terminal fragment, Aβ-aggregation, and phosphorylated Tau. Wogonin also increased mitochondrial membrane potential (∆ψm) and protected against apoptosis by reducing the expression of Bax and cleaved PARP. Collectively, these results conclude that wogonin may be a promising multifunctional drug candidate for AD.

APA, Harvard, Vancouver, ISO, and other styles

7

Rius, Bibiana, Jaleh S. Mesgarzadeh, Isabelle C. Romine, Ryan J. Paxman, Jeffery W. Kelly, and R. Luke Wiseman. "Pharmacologic targeting of plasma cell endoplasmic reticulum proteostasis to reduce amyloidogenic light chain secretion." Blood Advances 5, no. 4 (2021): 1037–49. http://dx.doi.org/10.1182/bloodadvances.2020002813.

Full text

Abstract:

Abstract Light chain (LC) amyloidosis (AL) involves the toxic aggregation of amyloidogenic immunoglobulin LCs secreted from a clonal expansion of diseased plasma cells. Current AL treatments use chemotherapeutics to ablate the AL plasma cell population. However, no treatments are available that directly reduce the toxic LC aggregation involved in AL pathogenesis. An attractive strategy to reduce toxic LC aggregation in AL involves enhancing endoplasmic reticulum (ER) proteostasis in plasma cells to reduce the secretion and subsequent aggregation of amyloidogenic LCs. Here, we show that the ER proteostasis regulator compound 147 reduces secretion of an amyloidogenic LC as aggregation-prone monomers and dimers in AL patient–derived plasma cells. Compound 147 was established to promote ER proteostasis remodeling by activating the ATF6 unfolded protein response signaling pathway through a mechanism involving covalent modification of ER protein disulfide isomerases (PDIs). However, we show that 147-dependent reductions in amyloidogenic LCs are independent of ATF6 activation. Instead, 147 reduces amyloidogenic LC secretion through the selective, on-target covalent modification of ER proteostasis factors, including PDIs, revealing an alternative mechanism by which this compound can influence ER proteostasis of amyloidogenic proteins. Importantly, compound 147 does not interfere with AL plasma cell toxicity induced by bortezomib, a standard chemotherapeutic used to ablate the underlying diseased plasma cells in AL. This shows that pharmacologic targeting of ER proteostasis through selective covalent modification of ER proteostasis factors is a strategy that can be used in combination with chemotherapeutics to reduce the LC toxicity associated with AL pathogenesis.

APA, Harvard, Vancouver, ISO, and other styles

8

Viana, Gustavo Monteiro, Esteban Alberto Gonzalez, Marcela Maciel Palacio Alvarez, et al. "Cathepsin B-associated Activation of Amyloidogenic Pathway in Murine Mucopolysaccharidosis Type I Brain Cortex." International Journal of Molecular Sciences 21, no. 4 (2020): 1459. http://dx.doi.org/10.3390/ijms21041459.

Full text

Abstract:

Mucopolysaccharidosis type I (MPS I) is caused by genetic deficiency of α-l-iduronidase and impairment of lysosomal catabolism of heparan sulfate and dermatan sulfate. In the brain, these substrates accumulate in the lysosomes of neurons and glial cells, leading to neuroinflammation and neurodegeneration. Their storage also affects lysosomal homeostasis-inducing activity of several lysosomal proteases including cathepsin B (CATB). In the central nervous system, increased CATB activity has been associated with the deposition of amyloid plaques due to an alternative pro-amyloidogenic processing of the amyloid precursor protein (APP), suggesting a potential role of this enzyme in the neuropathology of MPS I. In this study, we report elevated levels of protein expression and activity of CATB in cortex tissues of 6-month-old MPS I (Idua -/- mice. Besides, increased CATB leakage from lysosomes to the cytoplasm of Idua -/- cortical pyramidal neurons was indicative of damaged lysosomal membranes. The increased CATB activity coincided with an elevated level of the 16-kDa C-terminal APP fragment, which together with unchanged levels of β-secretase 1 was suggestive for the role of this enzyme in the amyloidogenic APP processing. Neuronal accumulation of Thioflavin-S-positive misfolded protein aggregates and drastically increased levels of neuroinflammatory glial fibrillary acidic protein (GFAP)-positive astrocytes and CD11b-positive activated microglia were observed in Idua -/- cortex by confocal fluorescent microscopy. Together, our results point to the existence of a novel CATB-associated alternative amyloidogenic pathway in MPS I brain induced by lysosomal storage and potentially leading to neurodegeneration.

APA, Harvard, Vancouver, ISO, and other styles

9

Zhang, Xiong, Jie Yun Sun, Hong Mei Zhang, Lu Si, and Yu Li. "The Regulation of Natural Food Dyes Curcumin on the Amyloidogenic Pathway of APP." Advanced Materials Research 781-784 (September 2013): 1160–63. http://dx.doi.org/10.4028/www.scientific.net/amr.781-784.1160.

Full text

Abstract:

As a promising prevention and therapeutic intervention in Alzheimer’s disease, natural food dyes curcumin could obviously inhibit the generation of Aβ, but the mechanism is not fully defined. This study aims to investigate the effects of curcumin on the amyloidogenic pathway of APP in vitro. Plasmids APPswe and BACE1-mychis were transiently co-transfected into SH-SY5Y and HEK293 cells. Then, they were treated with curcumin at 0, 1.25, 5, 20 μmol/L for 24 h, or with curcumin at 5μmol/L for 0, 12, 24 and 48 h for the time course assay. Our findings showed that curcumin could inhibit the expression of the APP at mRNA level; the expression of the BACE1 and C99 at mRNA and protein levels, furthermore it could inhibit the generation of Aβ40/42, and those changes were dose-time dependent (p<0.05). Our study indicates that Aβ40/42 generation inhibition effect of curcumin might due to its influence on amyloidogenic pathway. This may provide important experimental basis for AD treatment with curcumin.

APA, Harvard, Vancouver, ISO, and other styles

10

Fluhrer, Regina, Anja Capell, Gil Westmeyer, et al. "A non-amyloidogenic function of BACE-2 in the secretory pathway." Journal of Neurochemistry 81, no. 5 (2002): 1011–20. http://dx.doi.org/10.1046/j.1471-4159.2002.00908.x.

Full text

APA, Harvard, Vancouver, ISO, and other styles

11

Bhattacharya, Antaripa, Adriana Limone, Filomena Napolitano, et al. "APP Maturation and Intracellular Localization Are Controlled by a Specific Inhibitor of 37/67 kDa Laminin-1 Receptor in Neuronal Cells." International Journal of Molecular Sciences 21, no. 5 (2020): 1738. http://dx.doi.org/10.3390/ijms21051738.

Full text

Abstract:

Amyloid precursor protein (APP) is processed along both the nonamyloidogenic pathway preventing amyloid beta peptide (Aβ) production and the amyloidogenic pathway, generating Aβ, whose accumulation characterizes Alzheimer’s disease. Items of evidence report that the intracellular trafficking plays a key role in the generation of Aβ and that the 37/67 kDa LR (laminin receptor), acting as a receptor for Aβ, may mediate Aβ-pathogenicity. Moreover, findings indicating interaction between the receptor and the key enzymes involved in the amyloidogenic pathway suggest a strong link between 37/67 kDa LR and APP processing. We show herein that the specific 37/67 kDa LR inhibitor, NSC48478, is able to reversibly affect the maturation of APP in a pH-dependent manner, resulting in the partial accumulation of the immature APP isoforms (unglycosylated/acetylated forms) in the endoplasmic reticulum (ER) and in transferrin-positive recycling endosomes, indicating alteration of the APP intracellular trafficking. These effects reveal NSC48478 inhibitor as a novel small molecule to be tested in disease conditions, mediated by the 37/67 kDa LR and accompanied by inactivation of ERK1/2 (extracellular signal-regulated kinases) signalling and activation of Akt (serine/threonine protein kinase) with consequent inhibition of GSK3β.

APA, Harvard, Vancouver, ISO, and other styles

12

Dubey, Richa, Ketaki Patil, Sarath C. Dantu та ін. "Azadirachtin inhibits amyloid formation, disaggregates pre-formed fibrils and protects pancreatic β-cells from human islet amyloid polypeptide/amylin-induced cytotoxicity". Biochemical Journal 476, № 5 (2019): 889–907. http://dx.doi.org/10.1042/bcj20180820.

Full text

Abstract:

Abstract The human islet amyloid polypeptide (hIAPP) or amylin is the major constituent of amyloidogenic aggregates found in pancreatic islets of type 2 diabetic patients that have been associated with β-cell dysfunction and/or death associated with type 2 diabetes mellitus (T2DM). Therefore, developing and/or identifying inhibitors of hIAPP aggregation pathway and/or compound that can mediate disaggregation of preformed aggregates holds promise as a medical intervention for T2DM management. In the current study, the anti-amyloidogenic potential of Azadirachtin (AZD)—a secondary metabolite isolated from traditional medicinal plant Neem (Azadirachta indica)—was investigated by using a combination of biophysical and cellular assays. Our results indicate that AZD supplementation not only inhibits hIAPP aggregation but also disaggregates pre-existing hIAPP fibrils by forming amorphous aggregates that are non-toxic to pancreatic β-cells. Furthermore, AZD supplementation in pancreatic β-cells (INS-1E) resulted in inhibition of oxidative stress; along with restoration of the DNA damage, lipid peroxidation and the associated membrane damage, endoplasmic reticulum stress and mitochondrial membrane potential. AZD treatment also restored glucose-stimulated insulin secretion from pancreatic islets exposed to hIAPP. All-atom molecular dynamics simulation studies on full-length hIAPP pentamer with AZD suggested that AZD interacted with four possible binding sites in the amyloidogenic region of hIAPP. In summary, our results suggest AZD to be a promising candidate for combating T2DM and related amyloidogenic disorders.

APA, Harvard, Vancouver, ISO, and other styles

13

Zeldenrust, Steven R., Ellen W. Blanco, and Karl A. Nath. "Amyloidogenic lambda Light Chain Renal Toxicity: Oxidative Stress Implicated." Blood 110, no. 11 (2007): 3531. http://dx.doi.org/10.1182/blood.v110.11.3531.3531.

Full text

Abstract:

Abstract The kidney is the most common organ involved in systemic light-chain amyloidosis (AL), seen in up to 40% of patients. Renal involvement can result in proteinuria and/or renal insufficiency. The mechanism of renal injury in amyloidosis remains unclear. We present data supporting a central role for oxidative stress in amyloid-induced renal damage. Soluble free light chains(LCs) were isolated from plasma of AL and myeloma patients obtained at the time of stem cell collection. LCs were purified by liquid-phase iso-electric fractionation of pooled plasma samples from each patient. Purified LC were incubated with cultured rat renal epithelial cells, both wild-type and heme oxygenase-1 (HO-1) over-expressing, for 16 hours. Macrophage chemoattractant protein-1 (MCP-1) induction was measured in the media by ELISA. LC from myeloma patients were used as negative controls. Significant induction of MCP-1, a sensitive indicator of oxidative stress, was seen in 4/5 patients with lambda light-chain amyloidosis and 0/4 kappa light-chain amyloidosis patients. Induction of MCP-1 was seen in only 1/8 myeloma patients tested (4 lambda and 4 kappa). Induction of MCP-1 was reduced in the presence of HO-1 overexpression, implicating oxidative stress as a critical pathway of toxicity of amyloidogenic lambda light chains in this system. These results suggest that lambda and kappa light chains may cause renal injury through distinct pathways in the kidney.

APA, Harvard, Vancouver, ISO, and other styles

14

Park, Hye Sook, Qi Qi Pang, Young Sil Kim, Ji Hyun Kim, and Eun Ju Cho. "Neuroprotective Effect of Membrane-Free Stem Cell Extract against Amyloid Beta 25–35-Induced Neurotoxicity in SH-SY5Y Cells." Applied Sciences 11, no. 5 (2021): 2219. http://dx.doi.org/10.3390/app11052219.

Full text

Abstract:

Amyloid beta (Aβ) produced by the amyloidogenic pathway induces neurotoxicity, and its accumulation is a well-known cause of Alzheimer’s disease (AD). In this study, the protective effect of membrane-free stem cell extract (MFSCE) derived from adipose tissue against Aβ25–35-induced neurotoxicity in the neuronal cells was investigated. Treatment with MFSCE increased cell viability and decreased lactate dehydrogenase (LDH) release in a dose-dependent manner, compared with the Aβ25–35-induced group. The level of reactive oxygen species (ROS) was significantly increased in neuronal cells induced by Aβ25–35, whereas MFSCE treatment dose-dependently reduced ROS production. Treatment with MFSCE attenuated neuroinflammation and neuronal apoptosis by downregulating inducible nitric oxide synthase, cyclooxygenase-2, and B-cell lymphoma 2-associated X protein in treated SH-SY5Y cells induced by Aβ25–35. Furthermore, MFSCE significantly downregulated the expression of the amyloidogenic pathway-related proteins, such as amyloid precursor protein, β-secretase, preselin-1, and preselin-2. Therefore, this study indicated a neuroprotective effect of MFSCE against neurotoxicity induced by Aβ25–35, suggesting that it is a useful strategy for the treatment of AD.

APA, Harvard, Vancouver, ISO, and other styles

15

Coma, Mireia, Francesc X. Guix, Gerard Ill-Raga, et al. "Oxidative stress triggers the amyloidogenic pathway in human vascular smooth muscle cells." Neurobiology of Aging 29, no. 7 (2008): 969–80. http://dx.doi.org/10.1016/j.neurobiolaging.2007.01.009.

Full text

APA, Harvard, Vancouver, ISO, and other styles

16

Sreeprasad, Sreenivasan, and Mahesh Narayan. "Nanoscopic Portrait of an Amyloidogenic Pathway Visualized through Tip-Enhanced Raman Spectroscopy." ACS Chemical Neuroscience 10, no. 8 (2019): 3343–45. http://dx.doi.org/10.1021/acschemneuro.9b00353.

Full text

APA, Harvard, Vancouver, ISO, and other styles

17

Filippov, Mikhail A., and Alexander Dityatev. "Matrix metalloproteinase-9 and non-amyloidogenic pathway of amyloid precursor protein processing." Journal of Neurochemistry 121, no. 2 (2012): 181–83. http://dx.doi.org/10.1111/j.1471-4159.2011.07641.x.

Full text

APA, Harvard, Vancouver, ISO, and other styles

18

Dzwolak, Wojciech, Anna Loksztejn, Agnieszka Galinska-Rakoczy, Rumi Adachi, Yuji Goto, and Leszek Rupnicki. "Conformational Indeterminism in Protein Misfolding: Chiral Amplification on Amyloidogenic Pathway of Insulin." Journal of the American Chemical Society 129, no. 24 (2007): 7517–22. http://dx.doi.org/10.1021/ja066703j.

Full text

APA, Harvard, Vancouver, ISO, and other styles

19

Zhao, Lan-Xue, Yan Wang, Ting Liu та ін. "α-Mangostin decreases β-amyloid peptides production via modulation of amyloidogenic pathway". CNS Neuroscience & Therapeutics 23, № 6 (2017): 526–34. http://dx.doi.org/10.1111/cns.12699.

Full text

APA, Harvard, Vancouver, ISO, and other styles

20

Konietzko, Uwe, Zoë V. Goodger, Bernhard M. Kohli, Lawrence Rajendran, and Roger M. Nitsch. "P4-241: The amyloidogenic processing pathway of APP results in nuclear signaling." Alzheimer's & Dementia 4 (July 2008): T742. http://dx.doi.org/10.1016/j.jalz.2008.05.2309.

Full text

APA, Harvard, Vancouver, ISO, and other styles

21

Xia, Yiyuan, Zhi-Hao Wang, Zhentao Zhang, et al. "Delta- and beta- secretases crosstalk amplifies the amyloidogenic pathway in Alzheimer’s disease." Progress in Neurobiology 204 (September 2021): 102113. http://dx.doi.org/10.1016/j.pneurobio.2021.102113.

Full text

APA, Harvard, Vancouver, ISO, and other styles

22

Yoon, Jeong-Hyun, Nayoung Lee, Kumju Youn та ін. "Dieckol Ameliorates Aβ Production via PI3K/Akt/GSK-3β Regulated APP Processing in SweAPP N2a Cell". Marine Drugs 19, № 3 (2021): 152. http://dx.doi.org/10.3390/md19030152.

Full text

Abstract:

The proteolytic processing of amyloid precursor protein (APP) by β-secretase (BACE1) and γ-secretase releases amyloid-β peptide (Aβ), which deposits in amyloid plaques and contributes to the initial causative events of Alzheimer’s disease (AD). In the present study, the regulatory mechanism of APP processing of three phlorotannins was elucidated in Swedish mutant APP overexpressed N2a (SweAPP N2a) cells. Among the tested compounds, dieckol exhibited the highest inhibitory effect on both intra- and extracellular Aβ accumulation. In addition, dieckol regulated the APP processing enzymes, such as α-secretase (ADAM10), β-secretase, and γ-secretase, presenilin-1 (PS1), and their proteolytic products, sAPPα and sAPPβ, implying that the compound acts on both the amyloidogenic and non-amyloidogenic pathways. In addition, dieckol increased the phosphorylation of protein kinase B (Akt) at Ser473 and GSK-3β at Ser9, suggesting dieckol induced the activation of Akt, which phosphorylated GSK-3β. The specific phosphatidylinositol 3-kinase (PI3K) inhibitor LY294002 triggered GSK-3β activation and Aβ expression. In addition, co-treatment with LY294002 noticeably blocked the effect of dieckol on Aβ production, demonstrating that dieckol promoted the PI3K/Akt signaling pathway, which in turn inactivated GSK-3β, resulting in the reduction in Aβ levels.

APA, Harvard, Vancouver, ISO, and other styles

23

Fisher, Carolyn L., Ross J. Resnick, Soumya De та ін. "Cyclic cis-Locked Phospho-Dipeptides Reduce Entry of AβPP into Amyloidogenic Processing Pathway". Journal of Alzheimer's Disease 55, № 1 (2016): 391–410. http://dx.doi.org/10.3233/jad-160051.

Full text

APA, Harvard, Vancouver, ISO, and other styles

24

Naslund, J., M. Jensen, L. O. Tjernberg, J. Thyberg, L. Terenius та C. Nordstedt. "The Metabolic Pathway Generating p3, an Aβ-Peptide Fragment, Is Probably Non-Amyloidogenic". Biochemical and Biophysical Research Communications 204, № 2 (1994): 780–87. http://dx.doi.org/10.1006/bbrc.1994.2527.

Full text

APA, Harvard, Vancouver, ISO, and other styles

25

Jiaranaikulwanitch, Jutamas, Hataichanok Pandith, Sarin Tadtong, et al. "Novel Multifunctional Ascorbic Triazole Derivatives for Amyloidogenic Pathway Inhibition, Anti-Inflammation, and Neuroprotection." Molecules 26, no. 6 (2021): 1562. http://dx.doi.org/10.3390/molecules26061562.

Full text

Abstract:

Alzheimer’s disease (AD) is a common neurodegenerative disorder. The number of patients with AD is projected to reach 152 million by 2050. Donepezil, rivastigmine, galantamine, and memantine are the only four drugs currently approved by the United States Food and Drug Administration for AD treatment. However, these drugs can only alleviate AD symptoms. Thus, this research focuses on the discovery of novel lead compounds that possess multitarget regulation of AD etiopathology relating to amyloid cascade. The ascorbic acid structure has been designated as a core functional domain due to several characteristics, including antioxidant activities, amyloid aggregation inhibition, and the ability to be transported to the brain and neurons. Multifunctional ascorbic derivatives were synthesized by copper (I)-catalyzed azide–alkyne cycloaddition reaction (click chemistry). The in vitro and cell-based assays showed that compounds 2c and 5c exhibited prominent multifunctional activities as beta-secretase 1 inhibitors, amyloid aggregation inhibitors, and antioxidant, neuroprotectant, and anti-inflammatory agents. Significant changes in activities promoting neuroprotection and anti-inflammation were observed at a considerably low concentration at a nanomolar level. Moreover, an in silico study showed that compounds 2c and 5c were capable of being permeated across the blood–brain barrier by sodium-dependent vitamin C transporter-2.

APA, Harvard, Vancouver, ISO, and other styles

26

Gugliandolo, Agnese, Luigi Chiricosta, Serena Silvestro, Placido Bramanti та Emanuela Mazzon. "α-Tocopherol Modulates Non-Amyloidogenic Pathway and Autophagy in an In Vitro Model of Alzheimer’s Disease: A Transcriptional Study". Brain Sciences 9, № 8 (2019): 196. http://dx.doi.org/10.3390/brainsci9080196.

Full text

Abstract:

Alzheimer’s disease (AD) is the most common form of dementia worldwide. The hallmarks of AD are the extracellular amyloid plaques, which are formed by amyloid β (Aβ) aggregates derived from the processing of the amyloid precursor protein (APP), and the intraneuronal neurofibrillary tangles, which are formed by the hyperphosphorylated tau protein. The aim of this work was to study the effects of α-tocopherol in retinoic acid differentiated SH-SY5Y neuroblastoma cells exposed to Aβ1-42 evaluating the transcriptional profile by next-generation sequencing. We observed that α-tocopherol was able to reduce the cytotoxicity induced by Aβ treatment, as demonstrated by Thiazolyl Blue Tetrazolium Bromide (MTT) assay. Moreover, the transcriptomic analysis evidenced that α-tocopherol treatment upregulated genes involved in the non-amyloidogenic processing of APP, while it downregulated the amyloidogenic pathway. Moreover, α-tocopherol modulated the expression of the genes involved in autophagy and the cell cycle, which are both known to be altered in AD. The treatment with α-tocopherol was also able to reduce oxidative stress, restoring nuclear factor erythroid-derived 2-like 2 (Nrf2) and decreasing inducible nitric oxide synthase (iNOS) levels, as demonstrated by immunocytochemistry.

APA, Harvard, Vancouver, ISO, and other styles

27

BORCHARDT, Thilo, James CAMAKARIS, Roberto CAPPAI, Colin L. MASTERS, Konrad BEYREUTHER та Gerd MULTHAUP. "Copper inhibits β-amyloid production and stimulates the non-amyloidogenic pathway of amyloid-precursor-protein secretion". Biochemical Journal 344, № 2 (1999): 461–67. http://dx.doi.org/10.1042/bj3440461.

Full text

Abstract:

Previous studies have demonstrated that amyloid precursor protein (APP) can bind and reduce Cu(II) to Cu(I), leading to oxidative modification of APP. In the present study we show that adding copper to Chinese-hamster ovary (CHO) cells greatly reduced the levels of amyloid Aβ peptide (Aβ) both in parental CHO-K1 and in copper-resistant CHO-CUR3 cells, which have lower intracellular copper levels. Copper also caused an increase in the secretion of the APP ectodomain, indicating that the large decrease in Aβ release was not due to a general inhibition in protein secretion. There was an increase in intracellular full-length APP levels which paralleled the decrease in Aβ generation, suggesting the existence of two distinct regulating mechanisms, one acting on Aβ production and the other on APP synthesis. Maximal inhibition of Aβ production and stimulation of APP secretion was achieved in CHO-K1 cells at about 10 μM copper and in CHO-CUR3 cells at about 50 μM copper. This dose ‘window of opportunity’ at which copper promoted the non-amyloidogenic pathway of APP was confirmed by an increase in the non-amyloidogenic p3 fragment produced by α-secretase cleavage. Our findings suggest that copper or copper agonists might be useful tools to discover novel targets for anti-Alzheimer drugs and may prove beneficial for the prevention of Alzheimer's disease.

APA, Harvard, Vancouver, ISO, and other styles

28

Yu, Yang, Yang Gao, Bengt Winblad, Lars O. Tjernberg, and 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 (2021): 833–52. http://dx.doi.org/10.3233/jad-215008.

Full text

Abstract:

Background: Processing of the amyloid-β protein precursor (AβPP) is neurophysiologically important due to the resulting fragments that regulate synapse biology, as well as potentially harmful due to generation of the 42 amino acid long amyloid β-peptide (Aβ42), which is a key player in Alzheimer’s disease. Objective: Our aim was to clarify the subcellular locations of the fragments involved in the amyloidogenic pathway in primary neurons with a focus on Aβ42 and its immediate substrate AβPP C-terminal fragment (APP-CTF). To overcome the difficulties of resolving these compartments due to their small size, we used super-resolution microscopy. Methods: Mouse primary hippocampal neurons were immunolabelled and imaged by stimulated emission depletion (STED) microscopy, including three-dimensional three-channel imaging, and quantitative image analyses. Results: The first (β-secretase) and second (γ-secretase) cleavages of AβPP were localized to functionally and distally distinct compartments. The β-secretase cleavage was observed in early endosomes in soma, where we were able to show that the liberated N- and C-terminal fragments were sorted into distinct vesicles budding from the early endosomes. Lack of colocalization of Aβ42 and APP-CTF in soma suggested that γ-secretase cleavage occurs in neurites. Indeed, APP-CTF was, in line with Aβ42 in our previous study, enriched in the presynapse but absent from the postsynapse. In contrast, full-length AβPP was not detected in either the pre- or the postsynaptic side of the synapse. Furthermore, we observed that endogenously produced and endocytosed Aβ42 were localized in different compartments. Conclusion: These findings provide critical super-resolved insight into amyloidogenic AβPP processing in primary neurons.

APA, Harvard, Vancouver, ISO, and other styles

29

Abdul Manap, Aimi Syamima, Priya Madhavan, Shantini Vijayabalan, Adeline Chia та Koji Fukui. "Explicating anti-amyloidogenic role of curcumin and piperine via amyloid beta (Aβ) explicit pathway: recovery and reversal paradigm effects". PeerJ 8 (30 вересня 2020): e10003. http://dx.doi.org/10.7717/peerj.10003.

Full text

Abstract:

Previously, we reported the synergistic effects of curcumin and piperine in cell cultures as potential anti-cholinesterase and anti-amyloidogenic agents. Due to limited findings on the enrolment of these compounds on epigenetic events in AD, we aimed at elucidating the expression profiles of Aβ42-induced SH-SY5Y cells using microarray profiling. In this study, an optimized concentration of 35 µM of curcumin and piperine in combination was used to treat Aβ42 fibril and high-throughput microarray profiling was performed on the extracted RNA. This was then compared to curcumin and piperine used singularly at 49.11 µM and 25 µM, respectively. Our results demonstrated that in the curcumin treated group, from the top 10 upregulated and top 10 downregulated significantly differentially expressed genes (p < 0.05; fold change ≥ 2 or ≤ −2), there were five upregulated and three downregulated genes involved in the amyloidogenic pathway. While from top 10 upregulated and top 10 downregulated significantly differentially expressed genes (p < 0.05; fold change ≥ 2 or ≤ − 2) in the piperine treated group, there were four upregulated and three downregulated genes involved in the same pathway, whereas there were five upregulated and two downregulated genes involved (p < 0.05; fold change ≥ 2 or ≤ − 2) in the curcumin-piperine combined group. Four genes namely GABARAPL1, CTSB, RAB5 and AK5 were expressed significantly in all groups. Other genes such as ITPR1, GSK3B, PPP3CC, ERN1, APH1A, CYCS and CALM2 were novel putative genes that are involved in the pathogenesis of AD. We revealed that curcumin and piperine have displayed their actions against Aβ via the modulation of various mechanistic pathways. Alterations in expression profiles of genes in the neuronal cell model may explain Aβ pathology post-treatment and provide new insights for remedial approaches of a combined treatment using curcumin and piperine.

APA, Harvard, Vancouver, ISO, and other styles

30

Mori, Takashi, Naoki Koyama, Tatsuya Segawa та ін. "Methylene Blue Modulates β-Secretase, Reverses Cerebral Amyloidosis, and Improves Cognition in Transgenic Mice". Journal of Biological Chemistry 289, № 44 (2014): 30303–17. http://dx.doi.org/10.1074/jbc.m114.568212.

Full text

Abstract:

Amyloid precursor protein (APP) proteolysis is required for production of amyloid-β (Aβ) peptides that comprise β-amyloid plaques in the brains of patients with Alzheimer disease (AD). Here, we tested whether the experimental agent methylene blue (MB), used for treatment of methemoglobinemia, might improve AD-like pathology and behavioral deficits. We orally administered MB to the aged transgenic PSAPP mouse model of cerebral amyloidosis and evaluated cognitive function and cerebral amyloid pathology. Beginning at 15 months of age, animals were gavaged with MB (3 mg/kg) or vehicle once daily for 3 months. MB treatment significantly prevented transgene-associated behavioral impairment, including hyperactivity, decreased object recognition, and defective spatial working and reference memory, but it did not alter nontransgenic mouse behavior. Moreover, brain parenchymal and cerebral vascular β-amyloid deposits as well as levels of various Aβ species, including oligomers, were mitigated in MB-treated PSAPP mice. These effects occurred with inhibition of amyloidogenic APP proteolysis. Specifically, β-carboxyl-terminal APP fragment and β-site APP cleaving enzyme 1 protein expression and activity were attenuated. Additionally, treatment of Chinese hamster ovary cells overexpressing human wild-type APP with MB significantly decreased Aβ production and amyloidogenic APP proteolysis. These results underscore the potential for oral MB treatment against AD-related cerebral amyloidosis by modulating the amyloidogenic pathway.

APA, Harvard, Vancouver, ISO, and other styles

31

Ciccone, Lidia, Nicolò Tonali, William Shepard, Susanna Nencetti, and Elisabetta Orlandini. "Physiological Metals Can Induce Conformational Changes in Transthyretin Structure: Neuroprotection or Misfolding Induction?" Crystals 11, no. 4 (2021): 354. http://dx.doi.org/10.3390/cryst11040354.

Full text

Abstract:

Transthyretin (TTR) is a plasma homotetrameric protein that transports thyroxine and retinol. TTR itself, under pathological conditions, dissociates into partially unfolded monomers that aggregate and form fibrils. Metal ions such as Zn2+, Cu2+, Fe2+, Mn2+ and Ca2+ play a controversial role in the TTR amyloidogenic pathway. TTR is also present in cerebrospinal fluid (CSF), where it behaves as one of the major Aβ-binding-proteins. The interaction between TTR and Aβ is stronger in the presence of high concentrations of Cu2+. Crystals of TTR, soaked in solutions of physiological metals such as Cu2+ and Fe2+, but not Mn2+, Zn2+, Fe3+, Al3+, Ni2+, revealed an unusual conformational change. Here, we investigate the effects that physiological metals have on TTR, in order to understand if metals can induce a specific and active conformation of TTR that guides its Aβ-scavenging role. The capability of certain metals to induce and accelerate its amyloidogenic process is also discussed.

APA, Harvard, Vancouver, ISO, and other styles

32

Zhuo, Jia-Min, Warren D. Kruger, and Domenico Praticò. "The Herp Protein Pathway is Not Involved in the Pro-Amyloidogenic Effect of Hyperhomocysteinemia." Journal of Alzheimer's Disease 20, no. 2 (2010): 569–76. http://dx.doi.org/10.3233/jad-2010-1394.

Full text

APA, Harvard, Vancouver, ISO, and other styles

33

Lazic, Divna, Abhay P. Sagare, Angeliki M. Nikolakopoulou, John H. Griffin, Robert Vassar, and Berislav V. Zlokovic. "3K3A-activated protein C blocks amyloidogenic BACE1 pathway and improves functional outcome in mice." Journal of Experimental Medicine 216, no. 2 (2019): 279–93. http://dx.doi.org/10.1084/jem.20181035.

Full text

Abstract:

3K3A-activated protein C (APC), a cell-signaling analogue of endogenous blood serine protease APC, exerts vasculoprotective, neuroprotective, and anti-inflammatory activities in rodent models of stroke, brain injury, and neurodegenerative disorders. 3K3A-APC is currently in development as a neuroprotectant in patients with ischemic stroke. Here, we report that 3K3A-APC inhibits BACE1 amyloidogenic pathway in a mouse model of Alzheimer’s disease (AD). We show that a 4-mo daily treatment of 3-mo-old 5XFAD mice with murine recombinant 3K3A-APC (100 µg/kg/d i.p.) prevents development of parenchymal and cerebrovascular amyloid-β (Aβ) deposits by 40–50%, which is mediated through NFκB–dependent transcriptional inhibition of BACE1, resulting in blockade of Aβ generation in neurons overexpressing human Aβ-precursor protein. Consistent with reduced Aβ deposition, 3K3A-APC normalized hippocampus-dependent behavioral deficits and cerebral blood flow responses, improved cerebrovascular integrity, and diminished neuroinflammatory responses. Our data suggest that 3K3A-APC holds potential as an effective anti-Aβ prevention therapy for early-stage AD.

APA, Harvard, Vancouver, ISO, and other styles

34

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

35

Das, Utpal, Lina Wang, Archan Ganguly, et al. "Visualizing APP and BACE-1 approximation in neurons yields insight into the amyloidogenic pathway." Nature Neuroscience 19, no. 1 (2015): 55–64. http://dx.doi.org/10.1038/nn.4188.

Full text

APA, Harvard, Vancouver, ISO, and other styles

36

Xia, Yiyuan, Zhihao Wang, Jianzhi Wang, Xiaochuan Wang, and Keqiang Ye. "P1-150: DELTA- AND BETA-SECRETASES CROSSTALK AMPLIFIES THE AMYLOIDOGENIC PATHWAY IN ALZHEIMER'S DISEASE." Alzheimer's & Dementia 15 (July 2019): P294—P295. http://dx.doi.org/10.1016/j.jalz.2019.06.705.

Full text

APA, Harvard, Vancouver, ISO, and other styles

37

Yu, W. Haung, Ana Maria Cuervo, Asok Kumar та ін. "Macroautophagy—a novel β-amyloid peptide-generating pathway activated in Alzheimer's disease". Journal of Cell Biology 171, № 1 (2005): 87–98. http://dx.doi.org/10.1083/jcb.200505082.

Full text

Abstract:

Macroautophagy, which is a lysosomal pathway for the turnover of organelles and long-lived proteins, is a key determinant of cell survival and longevity. In this study, we show that neuronal macroautophagy is induced early in Alzheimer's disease (AD) and before β-amyloid (Aβ) deposits extracellularly in the presenilin (PS) 1/Aβ precursor protein (APP) mouse model of β-amyloidosis. Subsequently, autophagosomes and late autophagic vacuoles (AVs) accumulate markedly in dystrophic dendrites, implying an impaired maturation of AVs to lysosomes. Immunolabeling identifies AVs in the brain as a major reservoir of intracellular Aβ. Purified AVs contain APP and β-cleaved APP and are highly enriched in PS1, nicastrin, and PS-dependent γ-secretase activity. Inducing or inhibiting macroautophagy in neuronal and nonneuronal cells by modulating mammalian target of rapamycin kinase elicits parallel changes in AV proliferation and Aβ production. Our results, therefore, link β-amyloidogenic and cell survival pathways through macroautophagy, which is activated and is abnormal in AD.

APA, Harvard, Vancouver, ISO, and other styles

38

Rajput, Rinky, Balasubramani G L, Ankit Srivastava та ін. "Specific keratinase derived designer peptides potently inhibit Aβ aggregation resulting in reduced neuronal toxicity and apoptosis". Biochemical Journal 476, № 12 (2019): 1817–41. http://dx.doi.org/10.1042/bcj20190183.

Full text

Abstract:

Abstract Compelling evidence implicates self-assembly of amyloid-β (Aβ1–42) peptides into soluble oligomers and fibrils as a major underlying event in Alzheimer's disease (AD) pathogenesis. Herein, we employed amyloid-degrading keratinase (kerA) enzyme as a key Aβ1–42-binding scaffold to identify five keratinase-guided peptides (KgPs) capable of interacting with and altering amyloidogenic conversion of Aβ1–42. The KgPs showed micromolar affinities with Aβ1–42 and abolished its sigmoidal amyloidogenic transition, resulting in abrogation of fibrillogenesis. Comprehensive assessment using dynamic light scattering (DLS), atomic force microscopy (AFM) and Fourier-transform infrared (FTIR) spectroscopy showed that KgPs induced the formation of off-pathway oligomers comparatively larger than the native Aβ1–42 oligomers but with a significantly reduced cross-β signature. These off-pathway oligomers exhibited low immunoreactivity against oligomer-specific (A11) and fibril-specific (OC) antibodies and rescued neuronal cells from Aβ1–42 oligomer toxicity as well as neuronal apoptosis. Structural analysis using molecular docking and molecular dynamics (MD) simulations showed two preferred KgP binding sites (Lys16–Phe20 and Leu28–Val39) on the NMR ensembles of monomeric and fibrillar Aβ1–42, indicating an interruption of crucial hydrophobic and aromatic interactions. Overall, our results demonstrate a new approach for designing potential anti-amyloid molecules that could pave way for developing effective therapeutics against AD and other amyloid diseases.

APA, Harvard, Vancouver, ISO, and other styles

39

Marshall, Karen E., Devkee M. Vadukul, Kevin Staras та Louise C. Serpell. "Misfolded amyloid-β-42 impairs the endosomal–lysosomal pathway". Cellular and Molecular Life Sciences 77, № 23 (2020): 5031–43. http://dx.doi.org/10.1007/s00018-020-03464-4.

Full text

Abstract:

Abstract Misfolding and aggregation of proteins is strongly linked to several neurodegenerative diseases, but how such species bring about their cytotoxic actions remains poorly understood. Here we used specifically-designed optical reporter probes and live fluorescence imaging in primary hippocampal neurons to characterise the mechanism by which prefibrillar, oligomeric forms of the Alzheimer’s-associated peptide, Aβ42, exert their detrimental effects. We used a pH-sensitive reporter, Aβ42-CypHer, to track Aβ internalisation in real-time, demonstrating that oligomers are rapidly taken up into cells in a dynamin-dependent manner, and trafficked via the endo-lysosomal pathway resulting in accumulation in lysosomes. In contrast, a non-assembling variant of Aβ42 (vAβ42) assayed in the same way is not internalised. Tracking ovalbumin uptake into cells using CypHer or Alexa Fluor tags shows that preincubation with Aβ42 disrupts protein uptake. Our results identify a potential mechanism by which amyloidogenic aggregates impair cellular function through disruption of the endosomal–lysosomal pathway.

APA, Harvard, Vancouver, ISO, and other styles

40

Li, Hongyun, Genevieve Evin, Andrew F. Hill, Ya Hui Hung, Ashley I. Bush, and Brett Garner. "Dissociation of ERK signalling inhibition from the anti-amyloidogenic action of synthetic ceramide analogues." Clinical Science 122, no. 9 (2012): 409–20. http://dx.doi.org/10.1042/cs20110257.

Full text

Abstract:

Inhibition of GSL (glycosphingolipid) synthesis reduces Aβ (amyloid β-peptide) production in vitro. Previous studies indicate that GCS (glucosylceramide synthase) inhibitors modulate phosphorylation of ERK1/2 (extracellular-signal-regulated kinase 1/2) and that the ERK pathway may regulate some aspects of Aβ production. It is not clear whether there is a causative relationship linking GSL synthesis inhibition, ERK phosphorylation and Aβ production. In the present study, we treated CHO cells (Chinese-hamster ovary cells) and SH-SY5Y neuroblastoma cells, that both constitutively express human wild-type APP (amyloid precursor protein) and process this to produce Aβ, with GSL-modulating agents to explore this relationship. We found that three related ceramide analogue GSL inhibitors, based on the PDMP (D-threo-1-phenyl-2-decanoylamino-3-morpholino-1-propanol) structure, reduced cellular Aβ production and in all cases this was correlated with inhibition of pERK (phosphorylated ERK) formation. Importantly, the L-threo enantiomers of these compounds (that are inferior GSL synthesis inhibitors compared with the D-threo-enantiomers) also reduced ERK phosphorylation to a similar extent without altering Aβ production. Inhibition of ERK activation using either PD98059 [2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one] or U0126 (1,4-diamino-2,3-dicyano-1,4-bis[2-aminophenylthio] butadiene) had no impact on Aβ production, and knockdown of endogenous GCS using small interfering RNA reduced cellular GSL levels without suppressing Aβ production or pERK formation. Our data suggest that the alteration in pERK levels following treatment with these ceramide analogues is not the principal mechanism involved in the inhibition of Aβ generation and that the ERK signalling pathway does not play a crucial role in processing APP through the amyloidogenic pathway.

APA, Harvard, Vancouver, ISO, and other styles

41

Mizuguchi, Chiharu, Fuka Ogata, Shiho Mikawa, et al. "Amyloidogenic Mutation Promotes Fibril Formation of the N-terminal Apolipoprotein A-I on Lipid Membranes." Journal of Biological Chemistry 290, no. 34 (2015): 20947–59. http://dx.doi.org/10.1074/jbc.m115.664227.

Full text

Abstract:

The N-terminal amino acid 1–83 fragment of apolipoprotein A-I (apoA-I) has a strong propensity to form amyloid fibrils at physiological neutral pH. Because apoA-I has an ability to bind to lipid membranes, we examined the effects of the lipid environment on fibril-forming properties of the N-terminal fragment of apoA-I variants. Thioflavin T fluorescence assay as well as fluorescence and transmission microscopies revealed that upon lipid binding, fibril formation by apoA-I 1–83 is strongly inhibited, whereas the G26R mutant still retains the ability to form fibrils. Such distinct effects of lipid binding on fibril formation were also observed for the amyloidogenic prone region-containing peptides, apoA-I 8–33 and 8–33/G26R. This amyloidogenic region shifts from random coil to α-helical structure upon lipid binding. The G26R mutation appears to prevent this helix transition because lower helical propensity and more solvent-exposed conformation of the G26R variant upon lipid binding were observed in the apoA-I 1–83 fragment and 8–33 peptide. With a partially α-helical conformation induced by the presence of 2,2,2-trifluoroethanol, fibril formation by apoA-I 1–83 was strongly inhibited, whereas the G26R variant can form amyloid fibrils. These findings suggest a new possible pathway for amyloid fibril formation by the N-terminal fragment of apoA-I variants: the amyloidogenic mutations partially destabilize the α-helical structure formed upon association with lipid membranes, resulting in physiologically relevant conformations that allow fibril formation.

APA, Harvard, Vancouver, ISO, and other styles

42

Cochet, Maud, Romain Donneger, Elisabeth Cassier, et al. "5-HT4Receptors Constitutively Promote the Non-Amyloidogenic Pathway of APP Cleavage and Interact with ADAM10." ACS Chemical Neuroscience 4, no. 1 (2012): 130–40. http://dx.doi.org/10.1021/cn300095t.

Full text

APA, Harvard, Vancouver, ISO, and other styles

43

Scheuermann, Stefan, Boris Hambsch, Lars Hesse, et al. "Homodimerization of Amyloid Precursor Protein and Its Implication in the Amyloidogenic Pathway of Alzheimer's Disease." Journal of Biological Chemistry 276, no. 36 (2001): 33923–29. http://dx.doi.org/10.1074/jbc.m105410200.

Full text

APA, Harvard, Vancouver, ISO, and other styles

44

Soriano, Salvador, Daniel C. Lu, Sreeganga Chandra, Claus U. Pietrzik, and Edward H. Koo. "The Amyloidogenic Pathway of Amyloid Precursor Protein (APP) Is Independent of Its Cleavage by Caspases." Journal of Biological Chemistry 276, no. 31 (2001): 29045–50. http://dx.doi.org/10.1074/jbc.m102456200.

Full text

APA, Harvard, Vancouver, ISO, and other styles

45

MURAKAMI, Kazuma, Nakaba MURATA, Yoshihiro NODA, Kazuhiro IRIE, Takuji SHIRASAWA, and Takahiko SHIMIZU. "Stimulation of the Amyloidogenic Pathway by Cytoplasmic Superoxide Radicals in an Alzheimer's Disease Mouse Model." Bioscience, Biotechnology, and Biochemistry 76, no. 6 (2012): 1098–103. http://dx.doi.org/10.1271/bbb.110934.

Full text

APA, Harvard, Vancouver, ISO, and other styles

46

Kojima, Kaori, Yasushi Kitaoka, Yasunari Munemasa, and Satoki Ueno. "Axonal Protection via Modulation of the Amyloidogenic Pathway in Tumor Necrosis Factor–Induced Optic Neuropathy." Investigative Opthalmology & Visual Science 53, no. 12 (2012): 7675. http://dx.doi.org/10.1167/iovs.12-10271.

Full text

APA, Harvard, Vancouver, ISO, and other styles

47

Grimm, Marcus, Viola Haupenthal, Tatjana Rothhaar та ін. "Effect of Different Phospholipids on α-Secretase Activity in the Non-Amyloidogenic Pathway of Alzheimer’s Disease". International Journal of Molecular Sciences 14, № 3 (2013): 5879–98. http://dx.doi.org/10.3390/ijms14035879.

Full text

APA, Harvard, Vancouver, ISO, and other styles

48

Shi, J., J. Guan, B. Jiang, et al. "Amyloidogenic light chains induce cardiomyocyte contractile dysfunction and apoptosis via a non-canonical p38 MAPK pathway." Proceedings of the National Academy of Sciences 107, no. 9 (2010): 4188–93. http://dx.doi.org/10.1073/pnas.0912263107.

Full text

APA, Harvard, Vancouver, ISO, and other styles

49

BORCHARDT, Thilo, James CAMAKARIS, Roberto CAPPAI, Colin L. MASTERS, Konrad BEYREUTHER та Gerd MULTHAUP. "Copper inhibits β-amyloid production and stimulates the non-amyloidogenic pathway of amyloid-precursor-protein secretion". Biochemical Journal 344, № 2 (1999): 461. http://dx.doi.org/10.1042/0264-6021:3440461.

Full text

APA, Harvard, Vancouver, ISO, and other styles

50

Dhouafli, Zohra, Manuela Leri, Monica Bucciantini та ін. "A new purified Lawsoniaside remodels amyloid-β42 fibrillation into a less toxic and non-amyloidogenic pathway". International Journal of Biological Macromolecules 114 (липень 2018): 830–35. http://dx.doi.org/10.1016/j.ijbiomac.2018.04.005.

Full text

APA, Harvard, Vancouver, ISO, and other styles

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!