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Quercetin protects human brain microvascular endothelial cells from fibrillar β-amyloid1-40-induced toxicity.

Acta pharmaceutica Sinica. B

Li Y, Zhou S, Li J, Sun Y, Hasimu H, Liu R, Zhang T.
PMID: 26579424
Acta Pharm Sin B. 2015 Jan;5(1):47-54. doi: 10.1016/j.apsb.2014.12.003. Epub 2015 Jan 13.

Amyloid beta-peptides (Aβ) are known to undergo active transport across the blood-brain barrier, and cerebral amyloid angiopathy has been shown to be a prominent feature in the majority of Alzheimer׳s disease. Quercetin is a natural flavonoid molecule and has...

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Li Y, Zhou S, Li J, et al. Quercetin protects human brain microvascular endothelial cells from fibrillar β-amyloid1-40-induced toxicity. Acta Pharm Sin B. 2015;5(1):47-54doi: 10.1016/j.apsb.2014.12.003.
Li, Y., Zhou, S., Li, J., Sun, Y., Hasimu, H., Liu, R., & Zhang, T. (2015). Quercetin protects human brain microvascular endothelial cells from fibrillar β-amyloid1-40-induced toxicity. Acta pharmaceutica Sinica. B, 5(1), 47-54. https://doi.org/10.1016/j.apsb.2014.12.003
Li, Yongjie, et al. "Quercetin protects human brain microvascular endothelial cells from fibrillar β-amyloid1-40-induced toxicity." Acta pharmaceutica Sinica. B vol. 5,1 (2015): 47-54. doi: https://doi.org/10.1016/j.apsb.2014.12.003
Li Y, Zhou S, Li J, Sun Y, Hasimu H, Liu R, Zhang T. Quercetin protects human brain microvascular endothelial cells from fibrillar β-amyloid1-40-induced toxicity. Acta Pharm Sin B. 2015 Jan;5(1):47-54. doi: 10.1016/j.apsb.2014.12.003. Epub 2015 Jan 13. PMID: 26579424; PMCID: PMC4629123.
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Fluorescence imaging of the interaction of amyloid beta 40 peptides with live cells and model membrane.

Biochimica et biophysica acta. Biomembranes

Jamasbi E, Hossain MA, Tan M, Separovic F, Ciccotosto GD.
PMID: 29408451
Biochim Biophys Acta Biomembr. 2018 Sep;1860(9):1609-1615. doi: 10.1016/j.bbamem.2018.01.024. Epub 2018 Feb 07.

Amyloid beta peptides (Aβ) found in plaques in the brain have been widely recognised as a hallmark of Alzheimer's disease although the underlying mechanism is still unknown. Aβ40 and Aβ40(A2T) peptides were synthesized and their effects on neuronal cells...

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Jamasbi E, Hossain MA, Tan M, et al. Fluorescence imaging of the interaction of amyloid beta 40 peptides with live cells and model membrane. Biochim Biophys Acta Biomembr. 2018;1860(9):1609-1615doi: 10.1016/j.bbamem.2018.01.024.
Jamasbi, E., Hossain, M. A., Tan, M., Separovic, F., & Ciccotosto, G. D. (2018). Fluorescence imaging of the interaction of amyloid beta 40 peptides with live cells and model membrane. Biochimica et biophysica acta. Biomembranes, 1860(9), 1609-1615. https://doi.org/10.1016/j.bbamem.2018.01.024
Jamasbi, Elaheh, et al. "Fluorescence imaging of the interaction of amyloid beta 40 peptides with live cells and model membrane." Biochimica et biophysica acta. Biomembranes vol. 1860,9 (2018): 1609-1615. doi: https://doi.org/10.1016/j.bbamem.2018.01.024
Jamasbi E, Hossain MA, Tan M, Separovic F, Ciccotosto GD. Fluorescence imaging of the interaction of amyloid beta 40 peptides with live cells and model membrane. Biochim Biophys Acta Biomembr. 2018 Sep;1860(9):1609-1615. doi: 10.1016/j.bbamem.2018.01.024. Epub 2018 Feb 07. PMID: 29408451.
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Periodontitis and Alzheimer's Disease: A Possible Comorbidity between Oral Chronic Inflammatory Condition and Neuroinflammation.

Frontiers in aging neuroscience

Teixeira FB, Saito MT, Matheus FC, Prediger RD, Yamada ES, Maia CSF, Lima RR.
PMID: 29085294
Front Aging Neurosci. 2017 Oct 10;9:327. doi: 10.3389/fnagi.2017.00327. eCollection 2017.

Periodontitis is an oral chronic infection/inflammatory condition, identified as a source of mediators of inflammation into the blood circulation, which may contribute to exacerbate several diseases. There is increasing evidence that inflammation plays a key role in the pathophysiology...

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Teixeira FB, Saito MT, Matheus FC, et al. Periodontitis and Alzheimer's Disease: A Possible Comorbidity between Oral Chronic Inflammatory Condition and Neuroinflammation. Front Aging Neurosci. 2017;9:327doi: 10.3389/fnagi.2017.00327.
Teixeira, F. B., Saito, M. T., Matheus, F. C., Prediger, R. D., Yamada, E. S., Maia, C. S. F., & Lima, R. R. (2017). Periodontitis and Alzheimer's Disease: A Possible Comorbidity between Oral Chronic Inflammatory Condition and Neuroinflammation. Frontiers in aging neuroscience, 9327. https://doi.org/10.3389/fnagi.2017.00327
Teixeira, Francisco B, et al. "Periodontitis and Alzheimer's Disease: A Possible Comorbidity between Oral Chronic Inflammatory Condition and Neuroinflammation." Frontiers in aging neuroscience vol. 9 (2017): 327. doi: https://doi.org/10.3389/fnagi.2017.00327
Teixeira FB, Saito MT, Matheus FC, Prediger RD, Yamada ES, Maia CSF, Lima RR. Periodontitis and Alzheimer's Disease: A Possible Comorbidity between Oral Chronic Inflammatory Condition and Neuroinflammation. Front Aging Neurosci. 2017 Oct 10;9:327. doi: 10.3389/fnagi.2017.00327. eCollection 2017. PMID: 29085294; PMCID: PMC5649154.
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Evaluation of the amyloid beta-GFP fusion protein as a model of amyloid beta peptides-mediated aggregation: a study of DNAJB6 chaperone.

Frontiers in molecular neuroscience

Hussein RM, Hashem RM, Rashed LA.
PMID: 26283911
Front Mol Neurosci. 2015 Jul 27;8:40. doi: 10.3389/fnmol.2015.00040. eCollection 2015.

Alzheimer's disease (AD) is a progressive neurodegenerative disease characterized by the accumulation and aggregation of extracellular amyloid β (Aβ) peptides and intracellular aggregation of hyper-phosphorylated tau protein. Recent evidence indicates that accumulation and aggregation of intracellular amyloid β peptides...

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Hussein RM, Hashem RM, Rashed LA. Evaluation of the amyloid beta-GFP fusion protein as a model of amyloid beta peptides-mediated aggregation: a study of DNAJB6 chaperone. Front Mol Neurosci. 2015;8:40doi: 10.3389/fnmol.2015.00040.
Hussein, R. M., Hashem, R. M., & Rashed, L. A. (2015). Evaluation of the amyloid beta-GFP fusion protein as a model of amyloid beta peptides-mediated aggregation: a study of DNAJB6 chaperone. Frontiers in molecular neuroscience, 840. https://doi.org/10.3389/fnmol.2015.00040
Hussein, Rasha M, et al. "Evaluation of the amyloid beta-GFP fusion protein as a model of amyloid beta peptides-mediated aggregation: a study of DNAJB6 chaperone." Frontiers in molecular neuroscience vol. 8 (2015): 40. doi: https://doi.org/10.3389/fnmol.2015.00040
Hussein RM, Hashem RM, Rashed LA. Evaluation of the amyloid beta-GFP fusion protein as a model of amyloid beta peptides-mediated aggregation: a study of DNAJB6 chaperone. Front Mol Neurosci. 2015 Jul 27;8:40. doi: 10.3389/fnmol.2015.00040. eCollection 2015. PMID: 26283911; PMCID: PMC4515555.
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Amyloid Beta peptides differentially affect hippocampal theta rhythms in vitro.

International journal of peptides

Gutiérrez-Lerma AI, Ordaz B, Peña-Ortega F.
PMID: 23878547
Int J Pept. 2013;2013:328140. doi: 10.1155/2013/328140. Epub 2013 Jun 25.

Soluble amyloid beta peptide (A β ) is responsible for the early cognitive dysfunction observed in Alzheimer's disease. Both cholinergically and glutamatergically induced hippocampal theta rhythms are related to learning and memory, spatial navigation, and spatial memory. However, these...

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Gutiérrez-Lerma AI, Ordaz B, Peña-Ortega F. Amyloid Beta peptides differentially affect hippocampal theta rhythms in vitro. Int J Pept. 2013;2013:328140doi: 10.1155/2013/328140.
Gutiérrez-Lerma, A. I., Ordaz, B., & Peña-Ortega, F. (2013). Amyloid Beta peptides differentially affect hippocampal theta rhythms in vitro. International journal of peptides, 2013328140. https://doi.org/10.1155/2013/328140
Gutiérrez-Lerma, Armando I, et al. "Amyloid Beta peptides differentially affect hippocampal theta rhythms in vitro." International journal of peptides vol. 2013 (2013): 328140. doi: https://doi.org/10.1155/2013/328140
Gutiérrez-Lerma AI, Ordaz B, Peña-Ortega F. Amyloid Beta peptides differentially affect hippocampal theta rhythms in vitro. Int J Pept. 2013;2013:328140. doi: 10.1155/2013/328140. Epub 2013 Jun 25. PMID: 23878547; PMCID: PMC3708430.
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Blood-brain barrier transport of amyloid beta peptides in efflux pump knock-out animals evaluated by in vivo optical imaging.

Fluids and barriers of the CNS

Zhang W, Xiong H, Callaghan D, Liu H, Jones A, Pei K, Fatehi D, Brunette E, Stanimirovic D.
PMID: 23432917
Fluids Barriers CNS. 2013 Feb 25;10(1):13. doi: 10.1186/2045-8118-10-13.

BACKGROUND: Aβ transport (flux) across the blood-brain barrier (BBB) is thought to contribute to the pathogenesis of Alzheimer's disease as well as to elimination of toxic amyloid from the brain by immunotherapy. Several BBB transporters have been implicated in...

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Zhang W, Xiong H, Callaghan D, et al. Blood-brain barrier transport of amyloid beta peptides in efflux pump knock-out animals evaluated by in vivo optical imaging. Fluids Barriers CNS. 2013;10(1):13doi: 10.1186/2045-8118-10-13.
Zhang, W., Xiong, H., Callaghan, D., Liu, H., Jones, A., Pei, K., Fatehi, D., Brunette, E., & Stanimirovic, D. (2013). Blood-brain barrier transport of amyloid beta peptides in efflux pump knock-out animals evaluated by in vivo optical imaging. Fluids and barriers of the CNS, 10(1), 13. https://doi.org/10.1186/2045-8118-10-13
Zhang, Wandong, et al. "Blood-brain barrier transport of amyloid beta peptides in efflux pump knock-out animals evaluated by in vivo optical imaging." Fluids and barriers of the CNS vol. 10,1 (2013): 13. doi: https://doi.org/10.1186/2045-8118-10-13
Zhang W, Xiong H, Callaghan D, Liu H, Jones A, Pei K, Fatehi D, Brunette E, Stanimirovic D. Blood-brain barrier transport of amyloid beta peptides in efflux pump knock-out animals evaluated by in vivo optical imaging. Fluids Barriers CNS. 2013 Feb 25;10(1):13. doi: 10.1186/2045-8118-10-13. PMID: 23432917; PMCID: PMC3601014.
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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 Sep-Dec;35(4):351-357. 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...

Cite
Sanders OD, Rajagopal L, Rajagopal JA. Does oxidatively damaged DNA drive amyloid-β generation in Alzheimer's disease? A hypothesis. J Neurogenet. 2021;35(4):351-357doi: 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, 35(4), 351-357. 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. 35,4 (2021): 351-357. 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 Sep-Dec;35(4):351-357. doi: 10.1080/01677063.2021.1954641. Epub 2021 Jul 20. PMID: 34282704.
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Synthesis of New Tyrosol-Based Phosphodiester Derivatives: Effect on Amyloid β Aggregation and Metal Chelation Ability.

ChemMedChem

Romanucci V, Giordano M, De Tommaso G, Iuliano M, Bernini R, Clemente M, Garcia-Viñuales S, Milardi D, Zarrelli A, Di Fabio G.
PMID: 33326184
ChemMedChem. 2021 Apr 08;16(7):1172-1183. doi: 10.1002/cmdc.202000807. Epub 2021 Jan 26.

Alzheimer's disease (AD) is a multifactorial pathology that requires multifaceted agents able to address its peculiar nature. Increasing evidence has shown that aggregation of amyloid β (Aβ) and oxidative stress are strictly interconnected, and their modulation might have a...

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Romanucci V, Giordano M, De Tommaso G, et al. Synthesis of New Tyrosol-Based Phosphodiester Derivatives: Effect on Amyloid β Aggregation and Metal Chelation Ability. ChemMedChem. 2021;16(7):1172-1183doi: 10.1002/cmdc.202000807.
Romanucci, V., Giordano, M., De Tommaso, G., Iuliano, M., Bernini, R., Clemente, M., Garcia-Viñuales, S., Milardi, D., Zarrelli, A., & Di Fabio, G. (2021). Synthesis of New Tyrosol-Based Phosphodiester Derivatives: Effect on Amyloid β Aggregation and Metal Chelation Ability. ChemMedChem, 16(7), 1172-1183. https://doi.org/10.1002/cmdc.202000807
Romanucci, Valeria, et al. "Synthesis of New Tyrosol-Based Phosphodiester Derivatives: Effect on Amyloid β Aggregation and Metal Chelation Ability." ChemMedChem vol. 16,7 (2021): 1172-1183. doi: https://doi.org/10.1002/cmdc.202000807
Romanucci V, Giordano M, De Tommaso G, Iuliano M, Bernini R, Clemente M, Garcia-Viñuales S, Milardi D, Zarrelli A, Di Fabio G. Synthesis of New Tyrosol-Based Phosphodiester Derivatives: Effect on Amyloid β Aggregation and Metal Chelation Ability. ChemMedChem. 2021 Apr 08;16(7):1172-1183. doi: 10.1002/cmdc.202000807. Epub 2021 Jan 26. PMID: 33326184.
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Cyclodextrin 3-Functionalized with 8-Hydroxyquinoline as an Antioxidant Inhibitor of Metal-Induced Amyloid Aggregation.

ChemPlusChem

Oliveri V, Bellia F, Vecchio G.
PMID: 31973438
Chempluschem. 2015 Apr;80(4):762-770. doi: 10.1002/cplu.201402450. Epub 2015 Feb 06.

Cyclodextrins are used increasingly in pharmacotherapy. Experimental and clinical data suggest that cyclodextrins can be used not only as excipients for marketed drugs, but also as active pharmaceutical ingredients to treat neurological diseases including Niemann-Pick type C disease. Disruption...

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Oliveri V, Bellia F, Vecchio G. Cyclodextrin 3-Functionalized with 8-Hydroxyquinoline as an Antioxidant Inhibitor of Metal-Induced Amyloid Aggregation. Chempluschem. 2015;80(4):762-770doi: 10.1002/cplu.201402450.
Oliveri, V., Bellia, F., & Vecchio, G. (2015). Cyclodextrin 3-Functionalized with 8-Hydroxyquinoline as an Antioxidant Inhibitor of Metal-Induced Amyloid Aggregation. ChemPlusChem, 80(4), 762-770. https://doi.org/10.1002/cplu.201402450
Oliveri, Valentina, et al. "Cyclodextrin 3-Functionalized with 8-Hydroxyquinoline as an Antioxidant Inhibitor of Metal-Induced Amyloid Aggregation." ChemPlusChem vol. 80,4 (2015): 762-770. doi: https://doi.org/10.1002/cplu.201402450
Oliveri V, Bellia F, Vecchio G. Cyclodextrin 3-Functionalized with 8-Hydroxyquinoline as an Antioxidant Inhibitor of Metal-Induced Amyloid Aggregation. Chempluschem. 2015 Apr;80(4):762-770. doi: 10.1002/cplu.201402450. Epub 2015 Feb 06. PMID: 31973438.
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A Biosynthetic Hybrid Spidroin-Amyloid-Mussel Foot Protein for Underwater Adhesion on Diverse Surfaces.

ACS applied materials & interfaces

Kim E, Jeon J, Zhu Y, Hoppe ED, Jun YS, Genin GM, Zhang F.
PMID: 34633172
ACS Appl Mater Interfaces. 2021 Oct 20;13(41):48457-48468. doi: 10.1021/acsami.1c14182. Epub 2021 Oct 11.

Strong underwater adhesives are attractive materials for biomedical healing and underwater repair, but their success in applications has been limited, owing to challenges with underwater setting and with balancing surface adhesion and cohesion. Here, we applied synthetic biology approaches...

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Kim E, Jeon J, Zhu Y, et al. A Biosynthetic Hybrid Spidroin-Amyloid-Mussel Foot Protein for Underwater Adhesion on Diverse Surfaces. ACS Appl Mater Interfaces. 2021;13(41):48457-48468doi: 10.1021/acsami.1c14182.
Kim, E., Jeon, J., Zhu, Y., Hoppe, E. D., Jun, Y. S., Genin, G. M., & Zhang, F. (2021). A Biosynthetic Hybrid Spidroin-Amyloid-Mussel Foot Protein for Underwater Adhesion on Diverse Surfaces. ACS applied materials & interfaces, 13(41), 48457-48468. https://doi.org/10.1021/acsami.1c14182
Kim, Eugene, et al. "A Biosynthetic Hybrid Spidroin-Amyloid-Mussel Foot Protein for Underwater Adhesion on Diverse Surfaces." ACS applied materials & interfaces vol. 13,41 (2021): 48457-48468. doi: https://doi.org/10.1021/acsami.1c14182
Kim E, Jeon J, Zhu Y, Hoppe ED, Jun YS, Genin GM, Zhang F. A Biosynthetic Hybrid Spidroin-Amyloid-Mussel Foot Protein for Underwater Adhesion on Diverse Surfaces. ACS Appl Mater Interfaces. 2021 Oct 20;13(41):48457-48468. doi: 10.1021/acsami.1c14182. Epub 2021 Oct 11. PMID: 34633172.
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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 Sep-Dec;35(4):351-357. 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...

Cite
Sanders OD, Rajagopal L, Rajagopal JA. Does oxidatively damaged DNA drive amyloid-β generation in Alzheimer's disease? A hypothesis. J Neurogenet. 2021;35(4):351-357doi: 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, 35(4), 351-357. 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. 35,4 (2021): 351-357. 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 Sep-Dec;35(4):351-357. doi: 10.1080/01677063.2021.1954641. Epub 2021 Jul 20. PMID: 34282704.
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The orphan drug dichloroacetate reduces amyloid beta-peptide production whilst promoting non-amyloidogenic proteolysis of the amyloid precursor protein.

PloS one

Parkin ET, Hammond JE, Owens L, Hodges MD.
PMID: 35025874
PLoS One. 2022 Jan 13;17(1):e0255715. doi: 10.1371/journal.pone.0255715. eCollection 2022.

The amyloid cascade hypothesis proposes that excessive accumulation of amyloid beta-peptides is the initiating event in Alzheimer's disease. These neurotoxic peptides are generated from the amyloid precursor protein via sequential cleavage by β- and γ-secretases in the 'amyloidogenic' proteolytic...

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Parkin ET, Hammond JE, Owens L, et al. The orphan drug dichloroacetate reduces amyloid beta-peptide production whilst promoting non-amyloidogenic proteolysis of the amyloid precursor protein. PLoS One. 2022;17(1):e0255715doi: 10.1371/journal.pone.0255715.
Parkin, E. T., Hammond, J. E., Owens, L., & Hodges, M. D. (2022). The orphan drug dichloroacetate reduces amyloid beta-peptide production whilst promoting non-amyloidogenic proteolysis of the amyloid precursor protein. PloS one, 17(1), e0255715. https://doi.org/10.1371/journal.pone.0255715
Parkin, Edward T, et al. "The orphan drug dichloroacetate reduces amyloid beta-peptide production whilst promoting non-amyloidogenic proteolysis of the amyloid precursor protein." PloS one vol. 17,1 (2022): e0255715. doi: https://doi.org/10.1371/journal.pone.0255715
Parkin ET, Hammond JE, Owens L, Hodges MD. The orphan drug dichloroacetate reduces amyloid beta-peptide production whilst promoting non-amyloidogenic proteolysis of the amyloid precursor protein. PLoS One. 2022 Jan 13;17(1):e0255715. doi: 10.1371/journal.pone.0255715. eCollection 2022. PMID: 35025874; PMCID: PMC8757967.
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Showing 25 to 36 of 97 entries