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Showing 1 to 12 of 18 entries
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Cortical neurons transgenic for human Abeta40 or Abeta42 have similar vulnerability to apoptosis despite their different amyloidogenic properties.

International journal of clinical and experimental pathology

Shiwany NA, Xie J, Guo Q.
PMID: 19158991
Int J Clin Exp Pathol. 2009;2(4):339-52. Epub 2008 Nov 26.

Alzheimer's disease (AD) is a leading cause of chronic dementia in the United States. Its incidence is increasing with an attendant increase in associated health care costs. Amyloid beta peptide (Abeta; a 39-42 amino acid molecule) is the major...

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Shiwany NA, Xie J, Guo Q. Cortical neurons transgenic for human Abeta40 or Abeta42 have similar vulnerability to apoptosis despite their different amyloidogenic properties. Int J Clin Exp Pathol. 2008;2(4):339-52
Shiwany, N. A., Xie, J., & Guo, Q. (2009). Cortical neurons transgenic for human Abeta40 or Abeta42 have similar vulnerability to apoptosis despite their different amyloidogenic properties. International journal of clinical and experimental pathology, 2(4), 339-52.
Shiwany, Najeeb A, et al. "Cortical neurons transgenic for human Abeta40 or Abeta42 have similar vulnerability to apoptosis despite their different amyloidogenic properties." International journal of clinical and experimental pathology vol. 2,4 (2009): 339-52.
Shiwany NA, Xie J, Guo Q. Cortical neurons transgenic for human Abeta40 or Abeta42 have similar vulnerability to apoptosis despite their different amyloidogenic properties. Int J Clin Exp Pathol. 2009;2(4):339-52. Epub 2008 Nov 26. PMID: 19158991; PMCID: PMC2615591.
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APP Causes Hyperexcitability in Fragile X Mice.

Frontiers in molecular neuroscience

Westmark CJ, Chuang SC, Hays SA, Filon MJ, Ray BC, Westmark PR, Gibson JR, Huber KM, Wong RK.
PMID: 28018172
Front Mol Neurosci. 2016 Dec 15;9:147. doi: 10.3389/fnmol.2016.00147. eCollection 2016.

Amyloid-beta protein precursor (APP) and metabolite levels are altered in fragile X syndrome (FXS) patients and in the mouse model of the disorder,

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Westmark CJ, Chuang SC, Hays SA, et al. APP Causes Hyperexcitability in Fragile X Mice. Front Mol Neurosci. 2016;9:147doi: 10.3389/fnmol.2016.00147.
Westmark, C. J., Chuang, S. C., Hays, S. A., Filon, M. J., Ray, B. C., Westmark, P. R., Gibson, J. R., Huber, K. M., & Wong, R. K. (2016). APP Causes Hyperexcitability in Fragile X Mice. Frontiers in molecular neuroscience, 9147. https://doi.org/10.3389/fnmol.2016.00147
Westmark, Cara J, et al. "APP Causes Hyperexcitability in Fragile X Mice." Frontiers in molecular neuroscience vol. 9 (2016): 147. doi: https://doi.org/10.3389/fnmol.2016.00147
Westmark CJ, Chuang SC, Hays SA, Filon MJ, Ray BC, Westmark PR, Gibson JR, Huber KM, Wong RK. APP Causes Hyperexcitability in Fragile X Mice. Front Mol Neurosci. 2016 Dec 15;9:147. doi: 10.3389/fnmol.2016.00147. eCollection 2016. PMID: 28018172; PMCID: PMC5156834.
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PAMP and PARL, two novel putative metalloproteases interacting with the COOH-terminus of Presenilin-1 and -2.

Journal of Alzheimer's disease : JAD

Pellegrini L, Passer BJ, Canelles M, Lefterov I, Ganjei JK, Fowlkes BJ, Koonin EV, D'Adamio L.
PMID: 12214059
J Alzheimers Dis. 2001 Apr;3(2):181-190. doi: 10.3233/jad-2001-3203.

The familial Alzheimer's disease gene products, presenilin-1 and presenilin-2 (PS1 and PS2), are involved in amyloid beta-protein precursor processing (AbetaPP), Notch receptor signaling, and programmed cell death. However, the molecular mechanisms by which presenilins regulate these processes remain unknown....

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Pellegrini L, Passer BJ, Canelles M, et al. PAMP and PARL, two novel putative metalloproteases interacting with the COOH-terminus of Presenilin-1 and -2. J Alzheimers Dis. 2001;3(2):181-190doi: 10.3233/jad-2001-3203.
Pellegrini, L., Passer, B. J., Canelles, M., Lefterov, I., Ganjei, J. K., Fowlkes, B. J., Koonin, E. V., & D'Adamio, L. (2001). PAMP and PARL, two novel putative metalloproteases interacting with the COOH-terminus of Presenilin-1 and -2. Journal of Alzheimer's disease : JAD, 3(2), 181-190. https://doi.org/10.3233/jad-2001-3203
Pellegrini, Luca, et al. "PAMP and PARL, two novel putative metalloproteases interacting with the COOH-terminus of Presenilin-1 and -2." Journal of Alzheimer's disease : JAD vol. 3,2 (2001): 181-190. doi: https://doi.org/10.3233/jad-2001-3203
Pellegrini L, Passer BJ, Canelles M, Lefterov I, Ganjei JK, Fowlkes BJ, Koonin EV, D'Adamio L. PAMP and PARL, two novel putative metalloproteases interacting with the COOH-terminus of Presenilin-1 and -2. J Alzheimers Dis. 2001 Apr;3(2):181-190. doi: 10.3233/jad-2001-3203. PMID: 12214059.
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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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Chronic Leptin Supplementation Ameliorates Pathology and Improves Cognitive Performance in a Transgenic Mouse Model of Alzheimer's Disease.

Journal of Alzheimer's disease : JAD

Greco SJ, Bryan KJ, Sarkar S, Zhu X, Smith MA, Ashford JW, Johnston JM, Tezapsidis N, Casadesus G.
PMID: 20009219
J Alzheimers Dis. 2009 Dec 14; doi: 10.3233/JAD-2009-1308. Epub 2009 Dec 14.

We have previously reported anti-amyloidogenic effects of leptin using in vitro and in vivo models and, more recently, demonstrated the ability of leptin to reduce tau phosphorylation in neuronal cells. The present study examined the efficacy of leptin in...

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Greco SJ, Bryan KJ, Sarkar S, et al. Chronic Leptin Supplementation Ameliorates Pathology and Improves Cognitive Performance in a Transgenic Mouse Model of Alzheimer's Disease. J Alzheimers Dis. 2009;doi: 10.3233/JAD-2009-1308.
Greco, S. J., Bryan, K. J., Sarkar, S., Zhu, X., Smith, M. A., Ashford, J. W., Johnston, J. M., Tezapsidis, N., & Casadesus, G. (2009). Chronic Leptin Supplementation Ameliorates Pathology and Improves Cognitive Performance in a Transgenic Mouse Model of Alzheimer's Disease. Journal of Alzheimer's disease : JAD, . https://doi.org/10.3233/JAD-2009-1308
Greco, Steven J, et al. "Chronic Leptin Supplementation Ameliorates Pathology and Improves Cognitive Performance in a Transgenic Mouse Model of Alzheimer's Disease." Journal of Alzheimer's disease : JAD vol. (2009). doi: https://doi.org/10.3233/JAD-2009-1308
Greco SJ, Bryan KJ, Sarkar S, Zhu X, Smith MA, Ashford JW, Johnston JM, Tezapsidis N, Casadesus G. Chronic Leptin Supplementation Ameliorates Pathology and Improves Cognitive Performance in a Transgenic Mouse Model of Alzheimer's Disease. J Alzheimers Dis. 2009 Dec 14; doi: 10.3233/JAD-2009-1308. Epub 2009 Dec 14. PMID: 20009219.
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Abetapp secretases are co-expressed with Abetapp in the pancreatic islets.

Journal of Alzheimer's disease : JAD

Figueroa DJ, Shi XP, Gardell SJ, Austin CP.
PMID: 12214042
J Alzheimers Dis. 2001 Aug;3(4):393-396. doi: 10.3233/jad-2001-3405.

Amyloid beta protein precursor is cleaved by beta- and gamma-secretases to produce Abeta peptides which deposit in amyloid plaques in Alzheimer's disease (AD) brain. A recently identified beta-site cleaving enzyme (BACE) appears to fulfill the requirements for beta-secretase, and...

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Figueroa DJ, Shi XP, Gardell SJ, et al. Abetapp secretases are co-expressed with Abetapp in the pancreatic islets. J Alzheimers Dis. 2001;3(4):393-396doi: 10.3233/jad-2001-3405.
Figueroa, D. J., Shi, X. P., Gardell, S. J., & Austin, C. P. (2001). Abetapp secretases are co-expressed with Abetapp in the pancreatic islets. Journal of Alzheimer's disease : JAD, 3(4), 393-396. https://doi.org/10.3233/jad-2001-3405
Figueroa, David J., et al. "Abetapp secretases are co-expressed with Abetapp in the pancreatic islets." Journal of Alzheimer's disease : JAD vol. 3,4 (2001): 393-396. doi: https://doi.org/10.3233/jad-2001-3405
Figueroa DJ, Shi XP, Gardell SJ, Austin CP. Abetapp secretases are co-expressed with Abetapp in the pancreatic islets. J Alzheimers Dis. 2001 Aug;3(4):393-396. doi: 10.3233/jad-2001-3405. PMID: 12214042.
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Abeta immunoreactive material is present in several intracellular compartments in transfected, neuronally differentiated, P19 cells expressing the human amyloid beta-protein precursor.

Journal of Alzheimer's disease : JAD

Grant SM, Ducatenzeiler A, Szyf M, Cuello AC.
PMID: 12214085
J Alzheimers Dis. 2000 Nov;2(3):207-22. doi: 10.3233/jad-2000-23-403.

Processing of the amyloid beta-protein precursor is believed to play a critical role in the development of Alzheimer's disease neuropathology. The localization of the human Abeta epitope within mature neuroectodermally differentiated embryonal carcinoma (P19) cells, stably transfected with the...

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Grant SM, Ducatenzeiler A, Szyf M, et al. Abeta immunoreactive material is present in several intracellular compartments in transfected, neuronally differentiated, P19 cells expressing the human amyloid beta-protein precursor. J Alzheimers Dis. 2000;2(3):207-22doi: 10.3233/jad-2000-23-403.
Grant, S. M., Ducatenzeiler, A., Szyf, M., & Cuello, A. C. (2000). Abeta immunoreactive material is present in several intracellular compartments in transfected, neuronally differentiated, P19 cells expressing the human amyloid beta-protein precursor. Journal of Alzheimer's disease : JAD, 2(3), 207-22. https://doi.org/10.3233/jad-2000-23-403
Grant, S M, et al. "Abeta immunoreactive material is present in several intracellular compartments in transfected, neuronally differentiated, P19 cells expressing the human amyloid beta-protein precursor." Journal of Alzheimer's disease : JAD vol. 2,3 (2000): 207-22. doi: https://doi.org/10.3233/jad-2000-23-403
Grant SM, Ducatenzeiler A, Szyf M, Cuello AC. Abeta immunoreactive material is present in several intracellular compartments in transfected, neuronally differentiated, P19 cells expressing the human amyloid beta-protein precursor. J Alzheimers Dis. 2000 Nov;2(3):207-22. doi: 10.3233/jad-2000-23-403. PMID: 12214085.
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Using the zebrafish model for Alzheimer's disease research.

Frontiers in genetics

Newman M, Ebrahimie E, Lardelli M.
PMID: 25071820
Front Genet. 2014 Jun 30;5:189. doi: 10.3389/fgene.2014.00189. eCollection 2014.

Rodent models have been extensively used to investigate the cause and mechanisms behind Alzheimer's disease. Despite many years of intensive research using these models we still lack a detailed understanding of the molecular events that lead to neurodegeneration. Although...

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Newman M, Ebrahimie E, Lardelli M. Using the zebrafish model for Alzheimer's disease research. Front Genet. 2014;5:189doi: 10.3389/fgene.2014.00189.
Newman, M., Ebrahimie, E., & Lardelli, M. (2014). Using the zebrafish model for Alzheimer's disease research. Frontiers in genetics, 5189. https://doi.org/10.3389/fgene.2014.00189
Newman, Morgan, et al. "Using the zebrafish model for Alzheimer's disease research." Frontiers in genetics vol. 5 (2014): 189. doi: https://doi.org/10.3389/fgene.2014.00189
Newman M, Ebrahimie E, Lardelli M. Using the zebrafish model for Alzheimer's disease research. Front Genet. 2014 Jun 30;5:189. doi: 10.3389/fgene.2014.00189. eCollection 2014. PMID: 25071820; PMCID: PMC4075077.
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Inter-Dependent Mechanisms Behind Cognitive Dysfunction, Vascular Biology and Alzheimer's Dementia in Down Syndrome: Multi-Faceted Roles of APP.

Frontiers in behavioral neuroscience

Nizetic D, Chen CL, Hong W, Koo EH.
PMID: 26648852
Front Behav Neurosci. 2015 Dec 01;9:299. doi: 10.3389/fnbeh.2015.00299. eCollection 2015.

People with Down syndrome (DS) virtually all develop intellectual disability (ID) of varying degree of severity, and also have a high risk of early Alzheimer's disease (AD). ID prior to the onset of dementia, and its relationship to the...

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Nizetic D, Chen CL, Hong W, et al. Inter-Dependent Mechanisms Behind Cognitive Dysfunction, Vascular Biology and Alzheimer's Dementia in Down Syndrome: Multi-Faceted Roles of APP. Front Behav Neurosci. 2015;9:299doi: 10.3389/fnbeh.2015.00299.
Nizetic, D., Chen, C. L., Hong, W., & Koo, E. H. (2015). Inter-Dependent Mechanisms Behind Cognitive Dysfunction, Vascular Biology and Alzheimer's Dementia in Down Syndrome: Multi-Faceted Roles of APP. Frontiers in behavioral neuroscience, 9299. https://doi.org/10.3389/fnbeh.2015.00299
Nizetic, Dean, et al. "Inter-Dependent Mechanisms Behind Cognitive Dysfunction, Vascular Biology and Alzheimer's Dementia in Down Syndrome: Multi-Faceted Roles of APP." Frontiers in behavioral neuroscience vol. 9 (2015): 299. doi: https://doi.org/10.3389/fnbeh.2015.00299
Nizetic D, Chen CL, Hong W, Koo EH. Inter-Dependent Mechanisms Behind Cognitive Dysfunction, Vascular Biology and Alzheimer's Dementia in Down Syndrome: Multi-Faceted Roles of APP. Front Behav Neurosci. 2015 Dec 01;9:299. doi: 10.3389/fnbeh.2015.00299. eCollection 2015. PMID: 26648852; PMCID: PMC4664698.
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Generation of an apoptotic intracellular peptide by gamma-secretase cleavage of Alzheimer's amyloid beta protein precursor.

Journal of Alzheimer's disease : JAD

Passer B, Pellegrini L, Russo C, Siegel RM, Lenardo MJ, Schettini G, Bachmann M, Tabaton M, D'Adamio L.
PMID: 12214090
J Alzheimers Dis. 2000 Nov;2(3):289-301. doi: 10.3233/jad-2000-23-408.

The amyloid beta protein precursor (AbetaPP) is sequentially processed by beta- and gamma-secretases to generate the Abeta peptide. The biochemical path leading to Abeta formation has been extensively studied since extracellular aggregates of amyloidogenic forms of Abeta peptide (Abeta42)...

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Passer B, Pellegrini L, Russo C, et al. Generation of an apoptotic intracellular peptide by gamma-secretase cleavage of Alzheimer's amyloid beta protein precursor. J Alzheimers Dis. 2000;2(3):289-301doi: 10.3233/jad-2000-23-408.
Passer, B., Pellegrini, L., Russo, C., Siegel, R. M., Lenardo, M. J., Schettini, G., Bachmann, M., Tabaton, M., & D'Adamio, L. (2000). Generation of an apoptotic intracellular peptide by gamma-secretase cleavage of Alzheimer's amyloid beta protein precursor. Journal of Alzheimer's disease : JAD, 2(3), 289-301. https://doi.org/10.3233/jad-2000-23-408
Passer, B, et al. "Generation of an apoptotic intracellular peptide by gamma-secretase cleavage of Alzheimer's amyloid beta protein precursor." Journal of Alzheimer's disease : JAD vol. 2,3 (2000): 289-301. doi: https://doi.org/10.3233/jad-2000-23-408
Passer B, Pellegrini L, Russo C, Siegel RM, Lenardo MJ, Schettini G, Bachmann M, Tabaton M, D'Adamio L. Generation of an apoptotic intracellular peptide by gamma-secretase cleavage of Alzheimer's amyloid beta protein precursor. J Alzheimers Dis. 2000 Nov;2(3):289-301. doi: 10.3233/jad-2000-23-408. PMID: 12214090.
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The quest for fragile X biomarkers.

Molecular and cellular pediatrics

Westmark CJ.
PMID: 26567095
Mol Cell Pediatr. 2014 Dec;1(1):1. doi: 10.1186/s40348-014-0001-3. Epub 2014 Sep 04.

BACKGROUND: Fragile X is the most common form of inherited intellectual disability and the leading known genetic cause of autism. There is currently no cure or approved medication for fragile X although various drugs target specific disease symptoms and...

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Westmark CJ. The quest for fragile X biomarkers. Mol Cell Pediatr. 2014;1(1):1doi: 10.1186/s40348-014-0001-3.
Westmark, C. J. (2014). The quest for fragile X biomarkers. Molecular and cellular pediatrics, 1(1), 1. https://doi.org/10.1186/s40348-014-0001-3
Westmark, Cara J. "The quest for fragile X biomarkers." Molecular and cellular pediatrics vol. 1,1 (2014): 1. doi: https://doi.org/10.1186/s40348-014-0001-3
Westmark CJ. The quest for fragile X biomarkers. Mol Cell Pediatr. 2014 Dec;1(1):1. doi: 10.1186/s40348-014-0001-3. Epub 2014 Sep 04. PMID: 26567095.
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Amyloid beta protein precursor metabolism as a modulator of islet beta-cell function.

Journal of Alzheimer's disease : JAD

Martins RN.
PMID: 12214043
J Alzheimers Dis. 2001 Aug;3(4):397-399. doi: 10.3233/jad-2001-3406.

No abstract available.

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Martins RN. Amyloid beta protein precursor metabolism as a modulator of islet beta-cell function. J Alzheimers Dis. 2001;3(4):397-399doi: 10.3233/jad-2001-3406.
Martins, R. N. (2001). Amyloid beta protein precursor metabolism as a modulator of islet beta-cell function. Journal of Alzheimer's disease : JAD, 3(4), 397-399. https://doi.org/10.3233/jad-2001-3406
Martins, Ralph N.. "Amyloid beta protein precursor metabolism as a modulator of islet beta-cell function." Journal of Alzheimer's disease : JAD vol. 3,4 (2001): 397-399. doi: https://doi.org/10.3233/jad-2001-3406
Martins RN. Amyloid beta protein precursor metabolism as a modulator of islet beta-cell function. J Alzheimers Dis. 2001 Aug;3(4):397-399. doi: 10.3233/jad-2001-3406. PMID: 12214043.
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Showing 1 to 12 of 18 entries