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Showing 13 to 24 of 97 entries
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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.
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Structural and Functional Determinants of gamma-Secretase, an Intramembrane Protease Implicated in Alzheimer's Disease.

Current genomics

Fraering PC.
PMID: 19415127
Curr Genomics. 2007 Dec;8(8):531-49. doi: 10.2174/138920207783769521.

Alzheimer's disease is the most common form of neurodegenerative diseases in humans, characterized by the progressive accumulation and aggregation of amyloid-beta peptides (Abeta) in brain regions subserving memory and cognition. These 39-43 amino acids long peptides are generated by...

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Fraering PC. Structural and Functional Determinants of gamma-Secretase, an Intramembrane Protease Implicated in Alzheimer's Disease. Curr Genomics. 2007;8(8):531-49doi: 10.2174/138920207783769521.
Fraering, P. C. (2007). Structural and Functional Determinants of gamma-Secretase, an Intramembrane Protease Implicated in Alzheimer's Disease. Current genomics, 8(8), 531-49. https://doi.org/10.2174/138920207783769521
Fraering, Patrick C. "Structural and Functional Determinants of gamma-Secretase, an Intramembrane Protease Implicated in Alzheimer's Disease." Current genomics vol. 8,8 (2007): 531-49. doi: https://doi.org/10.2174/138920207783769521
Fraering PC. Structural and Functional Determinants of gamma-Secretase, an Intramembrane Protease Implicated in Alzheimer's Disease. Curr Genomics. 2007 Dec;8(8):531-49. doi: 10.2174/138920207783769521. PMID: 19415127; PMCID: PMC2647162.
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The Role of Cathepsin B in the Degradation of Aβ and in the Production of Aβ Peptides Starting With Ala2 in Cultured Astrocytes.

Frontiers in molecular neuroscience

Oberstein TJ, Utz J, Spitzer P, Klafki HW, Wiltfang J, Lewczuk P, Kornhuber J, Maler JM.
PMID: 33510618
Front Mol Neurosci. 2021 Jan 12;13:615740. doi: 10.3389/fnmol.2020.615740. eCollection 2020.

Astrocytes may not only be involved in the clearance of Amyloid beta peptides (Aβ) in Alzheimer's disease (AD), but appear to produce N-terminally truncated Aβ (Aβ

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Oberstein TJ, Utz J, Spitzer P, et al. The Role of Cathepsin B in the Degradation of Aβ and in the Production of Aβ Peptides Starting With Ala2 in Cultured Astrocytes. Front Mol Neurosci. 2021;13:615740doi: 10.3389/fnmol.2020.615740.
Oberstein, T. J., Utz, J., Spitzer, P., Klafki, H. W., Wiltfang, J., Lewczuk, P., Kornhuber, J., & Maler, J. M. (2020). The Role of Cathepsin B in the Degradation of Aβ and in the Production of Aβ Peptides Starting With Ala2 in Cultured Astrocytes. Frontiers in molecular neuroscience, 13615740. https://doi.org/10.3389/fnmol.2020.615740
Oberstein, Timo Jan, et al. "The Role of Cathepsin B in the Degradation of Aβ and in the Production of Aβ Peptides Starting With Ala2 in Cultured Astrocytes." Frontiers in molecular neuroscience vol. 13 (2020): 615740. doi: https://doi.org/10.3389/fnmol.2020.615740
Oberstein TJ, Utz J, Spitzer P, Klafki HW, Wiltfang J, Lewczuk P, Kornhuber J, Maler JM. The Role of Cathepsin B in the Degradation of Aβ and in the Production of Aβ Peptides Starting With Ala2 in Cultured Astrocytes. Front Mol Neurosci. 2021 Jan 12;13:615740. doi: 10.3389/fnmol.2020.615740. eCollection 2020. PMID: 33510618; PMCID: PMC7836726.
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Extensive frontal focused ultrasound mediated blood-brain barrier opening for the treatment of Alzheimer's disease: a proof-of-concept study.

Translational neurodegeneration

Park SH, Baik K, Jeon S, Chang WS, Ye BS, Chang JW.
PMID: 34740367
Transl Neurodegener. 2021 Nov 05;10(1):44. doi: 10.1186/s40035-021-00269-8.

BACKGROUND: Focused ultrasound (FUS)-mediated blood-brain barrier (BBB) opening has shown efficacy in removal of amyloid plaque and improvement of cognitive functions in preclinical studies, but this is rarely reported in clinical studies. This study was conducted to evaluate the...

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Park SH, Baik K, Jeon S, et al. Extensive frontal focused ultrasound mediated blood-brain barrier opening for the treatment of Alzheimer's disease: a proof-of-concept study. Transl Neurodegener. 2021;10(1):44doi: 10.1186/s40035-021-00269-8.
Park, S. H., Baik, K., Jeon, S., Chang, W. S., Ye, B. S., & Chang, J. W. (2021). Extensive frontal focused ultrasound mediated blood-brain barrier opening for the treatment of Alzheimer's disease: a proof-of-concept study. Translational neurodegeneration, 10(1), 44. https://doi.org/10.1186/s40035-021-00269-8
Park, So Hee, et al. "Extensive frontal focused ultrasound mediated blood-brain barrier opening for the treatment of Alzheimer's disease: a proof-of-concept study." Translational neurodegeneration vol. 10,1 (2021): 44. doi: https://doi.org/10.1186/s40035-021-00269-8
Park SH, Baik K, Jeon S, Chang WS, Ye BS, Chang JW. Extensive frontal focused ultrasound mediated blood-brain barrier opening for the treatment of Alzheimer's disease: a proof-of-concept study. Transl Neurodegener. 2021 Nov 05;10(1):44. doi: 10.1186/s40035-021-00269-8. PMID: 34740367; PMCID: PMC8570037.
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Clinical Usefulness of 18F-FC119S Positron-Emission Tomography as an Auxiliary Diagnostic Method for Dementia: An Open-Label, Single-Dose, Evaluator-Blind Clinical Trial.

Journal of clinical neurology (Seoul, Korea)

Lee I, Na HR, Byun BH, Lim I, Kim BI, Choi CW, Ko IO, Lee KC, Kim KM, Park SY, Kim YK, Lee JY, Bu SH, Kim JH, Kil HS, Park C, Chi DY, Ha JH, Lim SM.
PMID: 31942769
J Clin Neurol. 2020 Jan;16(1):131-139. doi: 10.3988/jcn.2020.16.1.131.

BACKGROUND AND PURPOSE: The aim of this study was to determine the diagnostic performance and safety of a new ¹⁸F-labeled amyloid tracer, ¹⁸F-FC119S.METHODS: This study prospectively recruited 105 participants, comprising 53 with Alzheimer's disease (AD) patients, 16 patients with...

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Lee I, Na HR, Byun BH, et al. Clinical Usefulness of 18F-FC119S Positron-Emission Tomography as an Auxiliary Diagnostic Method for Dementia: An Open-Label, Single-Dose, Evaluator-Blind Clinical Trial. J Clin Neurol. 2020;16(1):131-139doi: 10.3988/jcn.2020.16.1.131.
Lee, I., Na, H. R., Byun, B. H., Lim, I., Kim, B. I., Choi, C. W., Ko, I. O., Lee, K. C., Kim, K. M., Park, S. Y., Kim, Y. K., Lee, J. Y., Bu, S. H., Kim, J. H., Kil, H. S., Park, C., Chi, D. Y., Ha, J. H., & Lim, S. M. (2020). Clinical Usefulness of 18F-FC119S Positron-Emission Tomography as an Auxiliary Diagnostic Method for Dementia: An Open-Label, Single-Dose, Evaluator-Blind Clinical Trial. Journal of clinical neurology (Seoul, Korea), 16(1), 131-139. https://doi.org/10.3988/jcn.2020.16.1.131
Lee, Inki, et al. "Clinical Usefulness of 18F-FC119S Positron-Emission Tomography as an Auxiliary Diagnostic Method for Dementia: An Open-Label, Single-Dose, Evaluator-Blind Clinical Trial." Journal of clinical neurology (Seoul, Korea) vol. 16,1 (2020): 131-139. doi: https://doi.org/10.3988/jcn.2020.16.1.131
Lee I, Na HR, Byun BH, Lim I, Kim BI, Choi CW, Ko IO, Lee KC, Kim KM, Park SY, Kim YK, Lee JY, Bu SH, Kim JH, Kil HS, Park C, Chi DY, Ha JH, Lim SM. Clinical Usefulness of 18F-FC119S Positron-Emission Tomography as an Auxiliary Diagnostic Method for Dementia: An Open-Label, Single-Dose, Evaluator-Blind Clinical Trial. J Clin Neurol. 2020 Jan;16(1):131-139. doi: 10.3988/jcn.2020.16.1.131. PMID: 31942769; PMCID: PMC6974833.
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Effects of Amyloid Precursor Protein Overexpression on NF-κB, Rho-GTPase and Pro-Apoptosis Bcl-2 Pathways in Neuronal Cells.

Reports of biochemistry & molecular biology

Chan HH, Leong YQ, Voon SM, Pan ML, Leong CO, Lim CL, Koh RY.
PMID: 33969135
Rep Biochem Mol Biol. 2021 Jan;9(4):417-425. doi: 10.52547/rbmb.9.4.417.

BACKGROUND: Alzheimer's disease (AD) is a neurodegenerative disorder that causes cognitive dysfunction. Previous studies have suggested that amyloid plaques, mainly comprising of amyloid-beta peptides, play a pivotal role in AD pathophysiology. This study focuses on the evaluation of the...

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Chan HH, Leong YQ, Voon SM, et al. Effects of Amyloid Precursor Protein Overexpression on NF-κB, Rho-GTPase and Pro-Apoptosis Bcl-2 Pathways in Neuronal Cells. Rep Biochem Mol Biol. 2021;9(4):417-425doi: 10.52547/rbmb.9.4.417.
Chan, H. H., Leong, Y. Q., Voon, S. M., Pan, M. L., Leong, C. O., Lim, C. L., & Koh, R. Y. (2021). Effects of Amyloid Precursor Protein Overexpression on NF-κB, Rho-GTPase and Pro-Apoptosis Bcl-2 Pathways in Neuronal Cells. Reports of biochemistry & molecular biology, 9(4), 417-425. https://doi.org/10.52547/rbmb.9.4.417
Chan, Hong Hao, et al. "Effects of Amyloid Precursor Protein Overexpression on NF-κB, Rho-GTPase and Pro-Apoptosis Bcl-2 Pathways in Neuronal Cells." Reports of biochemistry & molecular biology vol. 9,4 (2021): 417-425. doi: https://doi.org/10.52547/rbmb.9.4.417
Chan HH, Leong YQ, Voon SM, Pan ML, Leong CO, Lim CL, Koh RY. Effects of Amyloid Precursor Protein Overexpression on NF-κB, Rho-GTPase and Pro-Apoptosis Bcl-2 Pathways in Neuronal Cells. Rep Biochem Mol Biol. 2021 Jan;9(4):417-425. doi: 10.52547/rbmb.9.4.417. PMID: 33969135; PMCID: PMC8068452.
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Thiophene-Based Optical Ligands That Selectively Detect Aβ Pathology in Alzheimer's Disease.

Chembiochem : a European journal of chemical biology

Klingstedt T, Shirani H, Ghetti B, Vidal R, R Nilsson KP.
PMID: 34101954
Chembiochem. 2021 Aug 03;22(15):2568-2581. doi: 10.1002/cbic.202100199. Epub 2021 Jun 21.

In several neurodegenerative diseases, the presence of aggregates of specific proteins in the brain is a significant pathological hallmark; thus, developing ligands able to bind to the aggregated proteins is essential for any effort related to imaging and therapeutics....

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Klingstedt T, Shirani H, Ghetti B, et al. Thiophene-Based Optical Ligands That Selectively Detect Aβ Pathology in Alzheimer's Disease. Chembiochem. 2021;22(15):2568-2581doi: 10.1002/cbic.202100199.
Klingstedt, T., Shirani, H., Ghetti, B., Vidal, R., & R Nilsson, K. P. (2021). Thiophene-Based Optical Ligands That Selectively Detect Aβ Pathology in Alzheimer's Disease. Chembiochem : a European journal of chemical biology, 22(15), 2568-2581. https://doi.org/10.1002/cbic.202100199
Klingstedt, Therése, et al. "Thiophene-Based Optical Ligands That Selectively Detect Aβ Pathology in Alzheimer's Disease." Chembiochem : a European journal of chemical biology vol. 22,15 (2021): 2568-2581. doi: https://doi.org/10.1002/cbic.202100199
Klingstedt T, Shirani H, Ghetti B, Vidal R, R Nilsson KP. Thiophene-Based Optical Ligands That Selectively Detect Aβ Pathology in Alzheimer's Disease. Chembiochem. 2021 Aug 03;22(15):2568-2581. doi: 10.1002/cbic.202100199. Epub 2021 Jun 21. PMID: 34101954; PMCID: PMC8409278.
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Does oxidatively damaged DNA drive amyloid-β generation in Alzheimer's disease? A hypothesis.

Journal of neurogenetics

Sanders OD, Rajagopal L, Rajagopal JA.
PMID: 34282704
J Neurogenet. 2021 Jul 20;1-7. doi: 10.1080/01677063.2021.1954641. Epub 2021 Jul 20.

In Alzheimer's disease (AD), amyloid-β (Aβ) generation and upstream β-secretase 1 (BACE1) expression appear to be driven by oxidative stress via c-Jun N-terminal kinase (JNK), p38, and Interferon-Induced, Double-Stranded RNA-Activated Protein Kinase (PKR). In addition, inflammatory molecules, including lipopolysaccharide...

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Sanders OD, Rajagopal L, Rajagopal JA. Does oxidatively damaged DNA drive amyloid-β generation in Alzheimer's disease? A hypothesis. J Neurogenet. 2021;1-7doi: 10.1080/01677063.2021.1954641.
Sanders, O. D., Rajagopal, L., & Rajagopal, J. A. (2021). Does oxidatively damaged DNA drive amyloid-β generation in Alzheimer's disease? A hypothesis. Journal of neurogenetics, 1-7. https://doi.org/10.1080/01677063.2021.1954641
Sanders, Owen Davis, et al. "Does oxidatively damaged DNA drive amyloid-β generation in Alzheimer's disease? A hypothesis." Journal of neurogenetics vol. (2021): 1-7. doi: https://doi.org/10.1080/01677063.2021.1954641
Sanders OD, Rajagopal L, Rajagopal JA. Does oxidatively damaged DNA drive amyloid-β generation in Alzheimer's disease? A hypothesis. J Neurogenet. 2021 Jul 20;1-7. doi: 10.1080/01677063.2021.1954641. Epub 2021 Jul 20. PMID: 34282704.
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Amyloid-Beta Peptides and Activated Astroglia Impairs Proliferation of Nerve Growth Factor Releasing Cells In Vitro: Implication for Encapsulated Cell Biodelivery-Mediated AD Therapy.

Cells

Mitra S, Turchetto S, Van Os W, Wahlberg LU, Linderoth B, Behbahani H, Eriksdotter M.
PMID: 34831056
Cells. 2021 Oct 21;10(11). doi: 10.3390/cells10112834.

Alzheimer's disease (AD) treatment is constrained due to the inability of peripherally administered therapeutic molecules to cross the blood-brain barrier. Encapsulated cell biodelivery (ECB) devices, a tissue-targeted approach for local drug release, was previously optimized for human mature nerve...

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Mitra S, Turchetto S, Van Os W, et al. Amyloid-Beta Peptides and Activated Astroglia Impairs Proliferation of Nerve Growth Factor Releasing Cells In Vitro: Implication for Encapsulated Cell Biodelivery-Mediated AD Therapy. Cells. 2021;10(11)doi: 10.3390/cells10112834.
Mitra, S., Turchetto, S., Van Os, W., Wahlberg, L. U., Linderoth, B., Behbahani, H., & Eriksdotter, M. (2021). Amyloid-Beta Peptides and Activated Astroglia Impairs Proliferation of Nerve Growth Factor Releasing Cells In Vitro: Implication for Encapsulated Cell Biodelivery-Mediated AD Therapy. Cells, 10(11), . https://doi.org/10.3390/cells10112834
Mitra, Sumonto, et al. "Amyloid-Beta Peptides and Activated Astroglia Impairs Proliferation of Nerve Growth Factor Releasing Cells In Vitro: Implication for Encapsulated Cell Biodelivery-Mediated AD Therapy." Cells vol. 10,11 (2021). doi: https://doi.org/10.3390/cells10112834
Mitra S, Turchetto S, Van Os W, Wahlberg LU, Linderoth B, Behbahani H, Eriksdotter M. Amyloid-Beta Peptides and Activated Astroglia Impairs Proliferation of Nerve Growth Factor Releasing Cells In Vitro: Implication for Encapsulated Cell Biodelivery-Mediated AD Therapy. Cells. 2021 Oct 21;10(11). doi: 10.3390/cells10112834. PMID: 34831056; PMCID: PMC8616486.
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Methyl Salicylate Lactoside Protects Neurons Ameliorating Cognitive Disorder Through Inhibiting Amyloid Beta-Induced Neuroinflammatory Response in Alzheimer's Disease.

Frontiers in aging neuroscience

Li J, Ma X, Wang Y, Chen C, Hu M, Wang L, Fu J, Shi G, Zhang D, Zhang T.
PMID: 29636677
Front Aging Neurosci. 2018 Mar 27;10:85. doi: 10.3389/fnagi.2018.00085. eCollection 2018.

Neuroinflammatory reactions mediated by microglia and astrocytes have been shown to play a key role in early progression of Alzheimer's disease (AD). Increased evidences have demonstrated that neurons exacerbate local inflammatory reactions by producing inflammatory mediators and act as...

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Li J, Ma X, Wang Y, et al. Methyl Salicylate Lactoside Protects Neurons Ameliorating Cognitive Disorder Through Inhibiting Amyloid Beta-Induced Neuroinflammatory Response in Alzheimer's Disease. Front Aging Neurosci. 2018;10:85doi: 10.3389/fnagi.2018.00085.
Li, J., Ma, X., Wang, Y., Chen, C., Hu, M., Wang, L., Fu, J., Shi, G., Zhang, D., & Zhang, T. (2018). Methyl Salicylate Lactoside Protects Neurons Ameliorating Cognitive Disorder Through Inhibiting Amyloid Beta-Induced Neuroinflammatory Response in Alzheimer's Disease. Frontiers in aging neuroscience, 1085. https://doi.org/10.3389/fnagi.2018.00085
Li, Jinze, et al. "Methyl Salicylate Lactoside Protects Neurons Ameliorating Cognitive Disorder Through Inhibiting Amyloid Beta-Induced Neuroinflammatory Response in Alzheimer's Disease." Frontiers in aging neuroscience vol. 10 (2018): 85. doi: https://doi.org/10.3389/fnagi.2018.00085
Li J, Ma X, Wang Y, Chen C, Hu M, Wang L, Fu J, Shi G, Zhang D, Zhang T. Methyl Salicylate Lactoside Protects Neurons Ameliorating Cognitive Disorder Through Inhibiting Amyloid Beta-Induced Neuroinflammatory Response in Alzheimer's Disease. Front Aging Neurosci. 2018 Mar 27;10:85. doi: 10.3389/fnagi.2018.00085. eCollection 2018. PMID: 29636677; PMCID: PMC5880880.
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Tau Pathology of Alzheimer Disease: Possible Role of Sleep Deprivation.

Basic and clinical neuroscience

Ahmadian N, Hejazi S, Mahmoudi J, Talebi M.
PMID: 30719245
Basic Clin Neurosci. 2018 Sep-Oct;9(5):307-316. doi: 10.32598/bcn.9.5.307. Epub 2018 Sep 01.

Sleep deprivation is a common complaint in modern societies. Insufficient sleep has increased the risk of catching neurodegenerative diseases such as Alzheimer's. Several studies have indicated that restricted sleep increases the level of deposition of β-amyloid and formation of...

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Ahmadian N, Hejazi S, Mahmoudi J, et al. Tau Pathology of Alzheimer Disease: Possible Role of Sleep Deprivation. Basic Clin Neurosci. 2018;9(5):307-316doi: 10.32598/bcn.9.5.307.
Ahmadian, N., Hejazi, S., Mahmoudi, J., & Talebi, M. (2018). Tau Pathology of Alzheimer Disease: Possible Role of Sleep Deprivation. Basic and clinical neuroscience, 9(5), 307-316. https://doi.org/10.32598/bcn.9.5.307
Ahmadian, Nahid, et al. "Tau Pathology of Alzheimer Disease: Possible Role of Sleep Deprivation." Basic and clinical neuroscience vol. 9,5 (2018): 307-316. doi: https://doi.org/10.32598/bcn.9.5.307
Ahmadian N, Hejazi S, Mahmoudi J, Talebi M. Tau Pathology of Alzheimer Disease: Possible Role of Sleep Deprivation. Basic Clin Neurosci. 2018 Sep-Oct;9(5):307-316. doi: 10.32598/bcn.9.5.307. Epub 2018 Sep 01. PMID: 30719245; PMCID: PMC6360494.
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A novel copper-chelating strategy for fluorescent proteins to image dynamic copper fluctuations on live cell surfaces.

Chemical science

Choi YA, Keem JO, Kim CY, Yoon HR, Heo WD, Chung BH, Jung Y.
PMID: 29560216
Chem Sci. 2015 Feb 01;6(2):1301-1307. doi: 10.1039/c4sc03027c. Epub 2014 Nov 19.

Copper is indispensable in most aerobic organisms although it is toxic if unregulated as illustrated in many neurodegenerative diseases. To elucidate the mechanisms underlying copper release from cells, a membrane-targeting reporter which can compete with extracellular copper-binding molecules is...

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Choi YA, Keem JO, Kim CY, et al. A novel copper-chelating strategy for fluorescent proteins to image dynamic copper fluctuations on live cell surfaces. Chem Sci. 2014;6(2):1301-1307doi: 10.1039/c4sc03027c.
Choi, Y. A., Keem, J. O., Kim, C. Y., Yoon, H. R., Heo, W. D., Chung, B. H., & Jung, Y. (2015). A novel copper-chelating strategy for fluorescent proteins to image dynamic copper fluctuations on live cell surfaces. Chemical science, 6(2), 1301-1307. https://doi.org/10.1039/c4sc03027c
Choi, Yoon-Aa, et al. "A novel copper-chelating strategy for fluorescent proteins to image dynamic copper fluctuations on live cell surfaces." Chemical science vol. 6,2 (2015): 1301-1307. doi: https://doi.org/10.1039/c4sc03027c
Choi YA, Keem JO, Kim CY, Yoon HR, Heo WD, Chung BH, Jung Y. A novel copper-chelating strategy for fluorescent proteins to image dynamic copper fluctuations on live cell surfaces. Chem Sci. 2015 Feb 01;6(2):1301-1307. doi: 10.1039/c4sc03027c. Epub 2014 Nov 19. PMID: 29560216; PMCID: PMC5811147.
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Showing 13 to 24 of 97 entries