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Showing 1 to 12 of 97 entries
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NADPH Oxidase Mediates β-Amyloid Peptide-Induced Neuronal Death in Mouse Cortical Cultures.

Chonnam medical journal

Chay KO, Nam Koong KY, Hwang S, Kim JK, Bae CS.
PMID: 29026707
Chonnam Med J. 2017 Sep;53(3):196-202. doi: 10.4068/cmj.2017.53.3.196. Epub 2017 Sep 25.

β-Amyloid peptide (Aβ) is the main component of senile plaques in patients with Alzheimer's disease, and is known to be a main pathogenic factor of the disease. Recent evidence indicates that activation of NADPH oxidase (NOX) in microglia or...

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Chay KO, Nam Koong KY, Hwang S, et al. NADPH Oxidase Mediates β-Amyloid Peptide-Induced Neuronal Death in Mouse Cortical Cultures. Chonnam Med J. 2017;53(3):196-202doi: 10.4068/cmj.2017.53.3.196.
Chay, K. O., Nam Koong, K. Y., Hwang, S., Kim, J. K., & Bae, C. S. (2017). NADPH Oxidase Mediates β-Amyloid Peptide-Induced Neuronal Death in Mouse Cortical Cultures. Chonnam medical journal, 53(3), 196-202. https://doi.org/10.4068/cmj.2017.53.3.196
Chay, Kee-Oh, et al. "NADPH Oxidase Mediates β-Amyloid Peptide-Induced Neuronal Death in Mouse Cortical Cultures." Chonnam medical journal vol. 53,3 (2017): 196-202. doi: https://doi.org/10.4068/cmj.2017.53.3.196
Chay KO, Nam Koong KY, Hwang S, Kim JK, Bae CS. NADPH Oxidase Mediates β-Amyloid Peptide-Induced Neuronal Death in Mouse Cortical Cultures. Chonnam Med J. 2017 Sep;53(3):196-202. doi: 10.4068/cmj.2017.53.3.196. Epub 2017 Sep 25. PMID: 29026707; PMCID: PMC5636758.
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Amyloid beta peptide 22-35 induces a negative inotropic effect on isolated rat hearts.

International journal of physiology, pathophysiology and pharmacology

Yousefirad N, Kaygısız Z, Aydın Y.
PMID: 28078053
Int J Physiol Pathophysiol Pharmacol. 2016 Dec 25;8(4):146-151. eCollection 2016.

Evidences indicate that deposition of amyloid beta peptides (Aβs) plays an important role in the pathogenesis of Alzheimer disease. Aβs may influence cardiovascular system and ileum contractions. But the effect of amyloid beta peptide 22-35 (Aβ

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Yousefirad N, Kaygısız Z, Aydın Y. Amyloid beta peptide 22-35 induces a negative inotropic effect on isolated rat hearts. Int J Physiol Pathophysiol Pharmacol. 2016;8(4):146-151
Yousefirad, N., Kaygısız, Z., & Aydın, Y. (2016). Amyloid beta peptide 22-35 induces a negative inotropic effect on isolated rat hearts. International journal of physiology, pathophysiology and pharmacology, 8(4), 146-151.
Yousefirad, Neda, et al. "Amyloid beta peptide 22-35 induces a negative inotropic effect on isolated rat hearts." International journal of physiology, pathophysiology and pharmacology vol. 8,4 (2016): 146-151.
Yousefirad N, Kaygısız Z, Aydın Y. Amyloid beta peptide 22-35 induces a negative inotropic effect on isolated rat hearts. Int J Physiol Pathophysiol Pharmacol. 2016 Dec 25;8(4):146-151. eCollection 2016. PMID: 28078053; PMCID: PMC5209443.
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Cortical Amyloid Beta in Cognitively Normal Elderly Adults is Associated with Decreased Network Efficiency within the Cerebro-Cerebellar System.

Frontiers in aging neuroscience

Steininger SC, Liu X, Gietl A, Wyss M, Schreiner S, Gruber E, Treyer V, Kälin A, Leh S, Buck A, Nitsch RM, Prüssmann KP, Hock C, Unschuld PG.
PMID: 24672483
Front Aging Neurosci. 2014 Mar 18;6:52. doi: 10.3389/fnagi.2014.00052. eCollection 2014.

BACKGROUND: Deposition of cortical amyloid beta (Aβ) is a correlate of aging and a risk factor for Alzheimer disease (AD). While several higher order cognitive processes involve functional interactions between cortex and cerebellum, this study aims to investigate effects...

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Steininger SC, Liu X, Gietl A, et al. Cortical Amyloid Beta in Cognitively Normal Elderly Adults is Associated with Decreased Network Efficiency within the Cerebro-Cerebellar System. Front Aging Neurosci. 2014;6:52doi: 10.3389/fnagi.2014.00052.
Steininger, S. C., Liu, X., Gietl, A., Wyss, M., Schreiner, S., Gruber, E., Treyer, V., Kälin, A., Leh, S., Buck, A., Nitsch, R. M., Prüssmann, K. P., Hock, C., & Unschuld, P. G. (2014). Cortical Amyloid Beta in Cognitively Normal Elderly Adults is Associated with Decreased Network Efficiency within the Cerebro-Cerebellar System. Frontiers in aging neuroscience, 652. https://doi.org/10.3389/fnagi.2014.00052
Steininger, Stefanie C, et al. "Cortical Amyloid Beta in Cognitively Normal Elderly Adults is Associated with Decreased Network Efficiency within the Cerebro-Cerebellar System." Frontiers in aging neuroscience vol. 6 (2014): 52. doi: https://doi.org/10.3389/fnagi.2014.00052
Steininger SC, Liu X, Gietl A, Wyss M, Schreiner S, Gruber E, Treyer V, Kälin A, Leh S, Buck A, Nitsch RM, Prüssmann KP, Hock C, Unschuld PG. Cortical Amyloid Beta in Cognitively Normal Elderly Adults is Associated with Decreased Network Efficiency within the Cerebro-Cerebellar System. Front Aging Neurosci. 2014 Mar 18;6:52. doi: 10.3389/fnagi.2014.00052. eCollection 2014. PMID: 24672483; PMCID: PMC3957491.
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Pyroglutamate-Modified Amyloid Beta Peptides: Emerging Targets for Alzheimer´s Disease Immunotherapy.

Current neuropharmacology

Perez-Garmendia R, Gevorkian G.
PMID: 24403873
Curr Neuropharmacol. 2013 Sep;11(5):491-8. doi: 10.2174/1570159X11311050004.

Extracellular and intraneuronal accumulation of amyloid-beta (Aβ) peptide aggregates in the brain has been hypothesized to play an important role in the neuropathology of Alzheimer's Disease (AD). The main Aβ variants detected in the human brain are Aβ1-40 and...

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Perez-Garmendia R, Gevorkian G. Pyroglutamate-Modified Amyloid Beta Peptides: Emerging Targets for Alzheimer´s Disease Immunotherapy. Curr Neuropharmacol. 2013;11(5):491-8doi: 10.2174/1570159X11311050004.
Perez-Garmendia, R., & Gevorkian, G. (2013). Pyroglutamate-Modified Amyloid Beta Peptides: Emerging Targets for Alzheimer´s Disease Immunotherapy. Current neuropharmacology, 11(5), 491-8. https://doi.org/10.2174/1570159X11311050004
Perez-Garmendia, Roxanna, and Gevorkian, Goar. "Pyroglutamate-Modified Amyloid Beta Peptides: Emerging Targets for Alzheimer´s Disease Immunotherapy." Current neuropharmacology vol. 11,5 (2013): 491-8. doi: https://doi.org/10.2174/1570159X11311050004
Perez-Garmendia R, Gevorkian G. Pyroglutamate-Modified Amyloid Beta Peptides: Emerging Targets for Alzheimer´s Disease Immunotherapy. Curr Neuropharmacol. 2013 Sep;11(5):491-8. doi: 10.2174/1570159X11311050004. PMID: 24403873; PMCID: PMC3763757.
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Theory of amyloid fibril nucleation from folded proteins.

Israel journal of chemistry

Zhang L, Schmit JD.
PMID: 28935998
Isr J Chem. 2017 Jul;57(7):738-749. doi: 10.1002/ijch.201600079. Epub 2017 Jan 30.

We present a theoretical model for the nucleation of amyloid fibrils. In our model we use helix-coil theory to describe the equilibrium between a soluble native state and an aggregation-prone unfolded state. We then extend the theory to include...

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Zhang L, Schmit JD. Theory of amyloid fibril nucleation from folded proteins. Isr J Chem. 2017;57(7):738-749doi: 10.1002/ijch.201600079.
Zhang, L., & Schmit, J. D. (2017). Theory of amyloid fibril nucleation from folded proteins. Israel journal of chemistry, 57(7), 738-749. https://doi.org/10.1002/ijch.201600079
Zhang, Lingyun, and Schmit, Jeremy D. "Theory of amyloid fibril nucleation from folded proteins." Israel journal of chemistry vol. 57,7 (2017): 738-749. doi: https://doi.org/10.1002/ijch.201600079
Zhang L, Schmit JD. Theory of amyloid fibril nucleation from folded proteins. Isr J Chem. 2017 Jul;57(7):738-749. doi: 10.1002/ijch.201600079. Epub 2017 Jan 30. PMID: 28935998; PMCID: PMC5602581.
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Possible role of amyloid-beta, adenine nucleotide translocase and cyclophilin-D interaction in mitochondrial dysfunction of Alzheimer's disease.

Bioinformation

Singh P, Suman S, Chandna S, Das TK.
PMID: 19759867
Bioinformation. 2009 Aug 04;3(10):440-5. doi: 10.6026/97320630003440.

Alzheimer's disease (AD) is a common neurodegenerative disease characterized by both extra- as well as intracellular deposition of amyloid beta peptides (Abeta). The accumulation of Abeta in mitochondria is associated with mitochondrial dysfunction and oxidative stress in AD. Recent...

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Singh P, Suman S, Chandna S, et al. Possible role of amyloid-beta, adenine nucleotide translocase and cyclophilin-D interaction in mitochondrial dysfunction of Alzheimer's disease. Bioinformation. 2009;3(10):440-5doi: 10.6026/97320630003440.
Singh, P., Suman, S., Chandna, S., & Das, T. K. (2009). Possible role of amyloid-beta, adenine nucleotide translocase and cyclophilin-D interaction in mitochondrial dysfunction of Alzheimer's disease. Bioinformation, 3(10), 440-5. https://doi.org/10.6026/97320630003440
Singh, Prabhakar, et al. "Possible role of amyloid-beta, adenine nucleotide translocase and cyclophilin-D interaction in mitochondrial dysfunction of Alzheimer's disease." Bioinformation vol. 3,10 (2009): 440-5. doi: https://doi.org/10.6026/97320630003440
Singh P, Suman S, Chandna S, Das TK. Possible role of amyloid-beta, adenine nucleotide translocase and cyclophilin-D interaction in mitochondrial dysfunction of Alzheimer's disease. Bioinformation. 2009 Aug 04;3(10):440-5. doi: 10.6026/97320630003440. PMID: 19759867; PMCID: PMC2737500.
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Microglia, Alzheimer's disease, and complement.

International journal of Alzheimer's disease

Crehan H, Hardy J, Pocock J.
PMID: 22957298
Int J Alzheimers Dis. 2012;2012:983640. doi: 10.1155/2012/983640. Epub 2012 Aug 21.

Microglia, the immune cell of the brain, are implicated in cascades leading to neuronal loss and cognitive decline in Alzheimer's disease (AD). Recent genome-wide association studies have indicated a number of risk factors for the development of late-onset AD....

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Crehan H, Hardy J, Pocock J. Microglia, Alzheimer's disease, and complement. Int J Alzheimers Dis. 2012;2012:983640doi: 10.1155/2012/983640.
Crehan, H., Hardy, J., & Pocock, J. (2012). Microglia, Alzheimer's disease, and complement. International journal of Alzheimer's disease, 2012983640. https://doi.org/10.1155/2012/983640
Crehan, Helen, et al. "Microglia, Alzheimer's disease, and complement." International journal of Alzheimer's disease vol. 2012 (2012): 983640. doi: https://doi.org/10.1155/2012/983640
Crehan H, Hardy J, Pocock J. Microglia, Alzheimer's disease, and complement. Int J Alzheimers Dis. 2012;2012:983640. doi: 10.1155/2012/983640. Epub 2012 Aug 21. PMID: 22957298; PMCID: PMC3432348.
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Effects of NADPH Oxidase Inhibitors and Mitochondria-Targeted Antioxidants on Amyloid β.

Chonnam medical journal

Hwang S, Kim JK.
PMID: 30288371
Chonnam Med J. 2018 Sep;54(3):159-166. doi: 10.4068/cmj.2018.54.3.159. Epub 2018 Sep 27.

The Amyloid β peptide (Aβ) is a main component of senile plaques in Alzheimer's disease. Currently, NADPH oxidase (NOX) and mitochondria are considered as primary sources of ROS induced by Aβ. However, the contribution of NOX and mitochondria to...

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Hwang S, Kim JK. Effects of NADPH Oxidase Inhibitors and Mitochondria-Targeted Antioxidants on Amyloid β. Chonnam Med J. 2018;54(3):159-166doi: 10.4068/cmj.2018.54.3.159.
Hwang, S., & Kim, J. K. (2018). Effects of NADPH Oxidase Inhibitors and Mitochondria-Targeted Antioxidants on Amyloid β. Chonnam medical journal, 54(3), 159-166. https://doi.org/10.4068/cmj.2018.54.3.159
Hwang, Shinae, and Kim, Jong-Keun. "Effects of NADPH Oxidase Inhibitors and Mitochondria-Targeted Antioxidants on Amyloid β." Chonnam medical journal vol. 54,3 (2018): 159-166. doi: https://doi.org/10.4068/cmj.2018.54.3.159
Hwang S, Kim JK. Effects of NADPH Oxidase Inhibitors and Mitochondria-Targeted Antioxidants on Amyloid β. Chonnam Med J. 2018 Sep;54(3):159-166. doi: 10.4068/cmj.2018.54.3.159. Epub 2018 Sep 27. PMID: 30288371; PMCID: PMC6165920.
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Neuroinflammatory Processes, A1 Astrocyte Activation and Protein Aggregation in the Retina of Alzheimer's Disease Patients, Possible Biomarkers for Early Diagnosis.

Frontiers in neuroscience

Grimaldi A, Pediconi N, Oieni F, Pizzarelli R, Rosito M, Giubettini M, Santini T, Limatola C, Ruocco G, Ragozzino D, Di Angelantonio S.
PMID: 31551688
Front Neurosci. 2019 Sep 04;13:925. doi: 10.3389/fnins.2019.00925. eCollection 2019.

Alzheimer's disease (AD), a primary cause of dementia in the aging population, is characterized by extracellular amyloid-beta peptides aggregation, intracellular deposits of hyperphosphorylated tau, neurodegeneration and glial activation in the brain. It is commonly thought that the lack of...

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Grimaldi A, Pediconi N, Oieni F, et al. Neuroinflammatory Processes, A1 Astrocyte Activation and Protein Aggregation in the Retina of Alzheimer's Disease Patients, Possible Biomarkers for Early Diagnosis. Front Neurosci. 2019;13:925doi: 10.3389/fnins.2019.00925.
Grimaldi, A., Pediconi, N., Oieni, F., Pizzarelli, R., Rosito, M., Giubettini, M., Santini, T., Limatola, C., Ruocco, G., Ragozzino, D., & Di Angelantonio, S. (2019). Neuroinflammatory Processes, A1 Astrocyte Activation and Protein Aggregation in the Retina of Alzheimer's Disease Patients, Possible Biomarkers for Early Diagnosis. Frontiers in neuroscience, 13925. https://doi.org/10.3389/fnins.2019.00925
Grimaldi, Alfonso, et al. "Neuroinflammatory Processes, A1 Astrocyte Activation and Protein Aggregation in the Retina of Alzheimer's Disease Patients, Possible Biomarkers for Early Diagnosis." Frontiers in neuroscience vol. 13 (2019): 925. doi: https://doi.org/10.3389/fnins.2019.00925
Grimaldi A, Pediconi N, Oieni F, Pizzarelli R, Rosito M, Giubettini M, Santini T, Limatola C, Ruocco G, Ragozzino D, Di Angelantonio S. Neuroinflammatory Processes, A1 Astrocyte Activation and Protein Aggregation in the Retina of Alzheimer's Disease Patients, Possible Biomarkers for Early Diagnosis. Front Neurosci. 2019 Sep 04;13:925. doi: 10.3389/fnins.2019.00925. eCollection 2019. PMID: 31551688; PMCID: PMC6737046.
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Immunosenescence of Natural Killer Cells, Inflammation, and Alzheimer's Disease.

International journal of Alzheimer's disease

Solana C, Tarazona R, Solana R.
PMID: 30515321
Int J Alzheimers Dis. 2018 Nov 01;2018:3128758. doi: 10.1155/2018/3128758. eCollection 2018.

Alzheimer's disease (AD) represents the most common cause of dementia in the elderly. AD is a neurodegenerative disorder characterized by progressive memory loss and cognitive decline. Although the aetiology of AD is not clear, both environmental factors and heritable...

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Solana C, Tarazona R, Solana R. Immunosenescence of Natural Killer Cells, Inflammation, and Alzheimer's Disease. Int J Alzheimers Dis. 2018;2018:3128758doi: 10.1155/2018/3128758.
Solana, C., Tarazona, R., & Solana, R. (2018). Immunosenescence of Natural Killer Cells, Inflammation, and Alzheimer's Disease. International journal of Alzheimer's disease, 20183128758. https://doi.org/10.1155/2018/3128758
Solana, Corona, et al. "Immunosenescence of Natural Killer Cells, Inflammation, and Alzheimer's Disease." International journal of Alzheimer's disease vol. 2018 (2018): 3128758. doi: https://doi.org/10.1155/2018/3128758
Solana C, Tarazona R, Solana R. Immunosenescence of Natural Killer Cells, Inflammation, and Alzheimer's Disease. Int J Alzheimers Dis. 2018 Nov 01;2018:3128758. doi: 10.1155/2018/3128758. eCollection 2018. PMID: 30515321; PMCID: PMC6236558.
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Plasma lipocalin-2 levels in the preclinical stage of Alzheimer's disease.

Alzheimer's & dementia (Amsterdam, Netherlands)

Eruysal E, Ravdin L, Kamel H, Iadecola C, Ishii M.
PMID: 31517027
Alzheimers Dement (Amst). 2019 Sep 06;11:646-653. doi: 10.1016/j.dadm.2019.07.004. eCollection 2019 Dec.

INTRODUCTION: Lipocalin-2 is an acute-phase protein with pleotropic functions that has been implicated in several diseases including Alzheimer's disease (AD). However, it is unknown if circulating lipocalin-2 levels are altered in the preclinical stage of AD, where AD pathology...

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Eruysal E, Ravdin L, Kamel H, et al. Plasma lipocalin-2 levels in the preclinical stage of Alzheimer's disease. Alzheimers Dement (Amst). 2019;11:646-653doi: 10.1016/j.dadm.2019.07.004.
Eruysal, E., Ravdin, L., Kamel, H., Iadecola, C., & Ishii, M. (2019). Plasma lipocalin-2 levels in the preclinical stage of Alzheimer's disease. Alzheimer's & dementia (Amsterdam, Netherlands), 11646-653. https://doi.org/10.1016/j.dadm.2019.07.004
Eruysal, Emily, et al. "Plasma lipocalin-2 levels in the preclinical stage of Alzheimer's disease." Alzheimer's & dementia (Amsterdam, Netherlands) vol. 11 (2019): 646-653. doi: https://doi.org/10.1016/j.dadm.2019.07.004
Eruysal E, Ravdin L, Kamel H, Iadecola C, Ishii M. Plasma lipocalin-2 levels in the preclinical stage of Alzheimer's disease. Alzheimers Dement (Amst). 2019 Sep 06;11:646-653. doi: 10.1016/j.dadm.2019.07.004. eCollection 2019 Dec. PMID: 31517027; PMCID: PMC6733778.
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Specific Mutations in Aph1 Cause γ-Secretase Activation.

International journal of molecular sciences

Watanabe H, Yoshida C, Hidaka M, Ogawa T, Tomita T, Futai E.
PMID: 35008932
Int J Mol Sci. 2022 Jan 03;23(1). doi: 10.3390/ijms23010507.

Amyloid beta peptides (Aβs) are generated from amyloid precursor protein (APP) through multiple cleavage steps mediated by γ-secretase, including endoproteolysis and carboxypeptidase-like trimming. The generation of neurotoxic Aβ42/43 species is enhanced by familial Alzheimer's disease (FAD) mutations within the...

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Watanabe H, Yoshida C, Hidaka M, et al. Specific Mutations in Aph1 Cause γ-Secretase Activation. Int J Mol Sci. 2022;23(1)doi: 10.3390/ijms23010507.
Watanabe, H., Yoshida, C., Hidaka, M., Ogawa, T., Tomita, T., & Futai, E. (2022). Specific Mutations in Aph1 Cause γ-Secretase Activation. International journal of molecular sciences, 23(1), . https://doi.org/10.3390/ijms23010507
Watanabe, Hikari, et al. "Specific Mutations in Aph1 Cause γ-Secretase Activation." International journal of molecular sciences vol. 23,1 (2022). doi: https://doi.org/10.3390/ijms23010507
Watanabe H, Yoshida C, Hidaka M, Ogawa T, Tomita T, Futai E. Specific Mutations in Aph1 Cause γ-Secretase Activation. Int J Mol Sci. 2022 Jan 03;23(1). doi: 10.3390/ijms23010507. PMID: 35008932; PMCID: PMC8745412.
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Showing 1 to 12 of 97 entries