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Extracellular CIRP Activates the IL-6Rα/STAT3/Cdk5 Pathway in Neurons.

Molecular neurobiology

Sharma A, Brenner M, Jacob A, Marambaud P, Wang P.
PMID: 33783711
Mol Neurobiol. 2021 Aug;58(8):3628-3640. doi: 10.1007/s12035-021-02368-z. Epub 2021 Mar 30.

Extracellular cold-inducible RNA-binding protein (eCIRP) stimulates microglial inflammation causing neuronal damage during ischemic stroke and is a critical mediator of alcohol-induced cognitive impairment. However, the precise role of eCIRP in mediating neuroinflammation remains unknown. In this study, we report...

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Sharma A, Brenner M, Jacob A, et al. Extracellular CIRP Activates the IL-6Rα/STAT3/Cdk5 Pathway in Neurons. Mol Neurobiol. 2021;58(8):3628-3640doi: 10.1007/s12035-021-02368-z.
Sharma, A., Brenner, M., Jacob, A., Marambaud, P., & Wang, P. (2021). Extracellular CIRP Activates the IL-6Rα/STAT3/Cdk5 Pathway in Neurons. Molecular neurobiology, 58(8), 3628-3640. https://doi.org/10.1007/s12035-021-02368-z
Sharma, Archna, et al. "Extracellular CIRP Activates the IL-6Rα/STAT3/Cdk5 Pathway in Neurons." Molecular neurobiology vol. 58,8 (2021): 3628-3640. doi: https://doi.org/10.1007/s12035-021-02368-z
Sharma A, Brenner M, Jacob A, Marambaud P, Wang P. Extracellular CIRP Activates the IL-6Rα/STAT3/Cdk5 Pathway in Neurons. Mol Neurobiol. 2021 Aug;58(8):3628-3640. doi: 10.1007/s12035-021-02368-z. Epub 2021 Mar 30. PMID: 33783711.
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Calcium signaling in neurodegeneration.

Molecular neurodegeneration

Marambaud P, Dreses-Werringloer U, Vingtdeux V.
PMID: 19419557
Mol Neurodegener. 2009 May 06;4:20. doi: 10.1186/1750-1326-4-20.

Calcium is a key signaling ion involved in many different intracellular and extracellular processes ranging from synaptic activity to cell-cell communication and adhesion. The exact definition at the molecular level of the versatility of this ion has made overwhelming...

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Marambaud P, Dreses-Werringloer U, Vingtdeux V. Calcium signaling in neurodegeneration. Mol Neurodegener. 2009;4:20doi: 10.1186/1750-1326-4-20.
Marambaud, P., Dreses-Werringloer, U., & Vingtdeux, V. (2009). Calcium signaling in neurodegeneration. Molecular neurodegeneration, 420. https://doi.org/10.1186/1750-1326-4-20
Marambaud, Philippe, et al. "Calcium signaling in neurodegeneration." Molecular neurodegeneration vol. 4 (2009): 20. doi: https://doi.org/10.1186/1750-1326-4-20
Marambaud P, Dreses-Werringloer U, Vingtdeux V. Calcium signaling in neurodegeneration. Mol Neurodegener. 2009 May 06;4:20. doi: 10.1186/1750-1326-4-20. PMID: 19419557; PMCID: PMC2689218.
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A modification-specific peptide-based immunization approach using CRM197 carrier protein: .

Molecular medicine (Cambridge, Mass.)

Vingtdeux V, Zhao H, Chandakkar P, Acker CM, Davies P, Marambaud P.
PMID: 27900387
Mol Med. 2017 Jan;22:841-849. doi: 10.2119/molmed.2016.00218. Epub 2016 Nov 28.

Strategies aimed at reducing cerebral accumulation of the amyloid-β (Aβ) peptides have therapeutic potential in Alzheimer's disease (AD). Aβ immunization has proven to be effective at promoting Aβ clearance in animal models but adverse effects have hampered its clinical...

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Vingtdeux V, Zhao H, Chandakkar P, et al. A modification-specific peptide-based immunization approach using CRM197 carrier protein: . Mol Med. 2016;22:841-849doi: 10.2119/molmed.2016.00218.
Vingtdeux, V., Zhao, H., Chandakkar, P., Acker, C. M., Davies, P., & Marambaud, P. (2017). A modification-specific peptide-based immunization approach using CRM197 carrier protein: . Molecular medicine (Cambridge, Mass.), 22841-849. https://doi.org/10.2119/molmed.2016.00218
Vingtdeux, Valérie, et al. "A modification-specific peptide-based immunization approach using CRM197 carrier protein: ." Molecular medicine (Cambridge, Mass.) vol. 22 (2017): 841-849. doi: https://doi.org/10.2119/molmed.2016.00218
Vingtdeux V, Zhao H, Chandakkar P, Acker CM, Davies P, Marambaud P. A modification-specific peptide-based immunization approach using CRM197 carrier protein: . Mol Med. 2017 Jan;22:841-849. doi: 10.2119/molmed.2016.00218. Epub 2016 Nov 28. PMID: 27900387; PMCID: PMC5263057.
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Haloperidol inactivates AMPK and reduces tau phosphorylation in a tau mouse model of Alzheimer's disease.

Alzheimer's & dementia (New York, N. Y.)

Koppel J, Jimenez H, Adrien L, Greenwald BS, Marambaud P, Cinamon E, Davies P.
PMID: 29067299
Alzheimers Dement (N Y). 2016 Jun 21;2(2):121-130. doi: 10.1016/j.trci.2016.05.003. eCollection 2016 Jun.

INTRODUCTION: The use of antipsychotic medications in Alzheimer's disease has been associated with an increased risk of mortality in clinical trials. However, an older postmortem literature suggests that those with schizophrenia treated in an era of exclusively conventional antipsychotic...

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Koppel J, Jimenez H, Adrien L, et al. Haloperidol inactivates AMPK and reduces tau phosphorylation in a tau mouse model of Alzheimer's disease. Alzheimers Dement (N Y). 2016;2(2):121-130doi: 10.1016/j.trci.2016.05.003.
Koppel, J., Jimenez, H., Adrien, L., Greenwald, B. S., Marambaud, P., Cinamon, E., & Davies, P. (2016). Haloperidol inactivates AMPK and reduces tau phosphorylation in a tau mouse model of Alzheimer's disease. Alzheimer's & dementia (New York, N. Y.), 2(2), 121-130. https://doi.org/10.1016/j.trci.2016.05.003
Koppel, Jeremy, et al. "Haloperidol inactivates AMPK and reduces tau phosphorylation in a tau mouse model of Alzheimer's disease." Alzheimer's & dementia (New York, N. Y.) vol. 2,2 (2016): 121-130. doi: https://doi.org/10.1016/j.trci.2016.05.003
Koppel J, Jimenez H, Adrien L, Greenwald BS, Marambaud P, Cinamon E, Davies P. Haloperidol inactivates AMPK and reduces tau phosphorylation in a tau mouse model of Alzheimer's disease. Alzheimers Dement (N Y). 2016 Jun 21;2(2):121-130. doi: 10.1016/j.trci.2016.05.003. eCollection 2016 Jun. PMID: 29067299; PMCID: PMC5644277.
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Amyloid-beta peptide degradation in cell cultures by mycoplasma contaminants.

BMC research notes

Zhao H, Dreses-Werringloer U, Davies P, Marambaud P.
PMID: 18710491
BMC Res Notes. 2008 Jun 30;1:38. doi: 10.1186/1756-0500-1-38.

BACKGROUND: Cell cultures have become an indispensable tool in Alzheimer's disease research for studying amyloid-beta (Abeta) metabolism. It is estimated that up to 35% of cell cultures in current use are infected with various mycoplasma species. In contrast with...

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Zhao H, Dreses-Werringloer U, Davies P, et al. Amyloid-beta peptide degradation in cell cultures by mycoplasma contaminants. BMC Res Notes. 2008;1:38doi: 10.1186/1756-0500-1-38.
Zhao, H., Dreses-Werringloer, U., Davies, P., & Marambaud, P. (2008). Amyloid-beta peptide degradation in cell cultures by mycoplasma contaminants. BMC research notes, 138. https://doi.org/10.1186/1756-0500-1-38
Zhao, Haitian, et al. "Amyloid-beta peptide degradation in cell cultures by mycoplasma contaminants." BMC research notes vol. 1 (2008): 38. doi: https://doi.org/10.1186/1756-0500-1-38
Zhao H, Dreses-Werringloer U, Davies P, Marambaud P. Amyloid-beta peptide degradation in cell cultures by mycoplasma contaminants. BMC Res Notes. 2008 Jun 30;1:38. doi: 10.1186/1756-0500-1-38. PMID: 18710491; PMCID: PMC2527505.
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Showing 1 to 5 of 5 entries