Publications

Misfolded amyloid β-42 induced impairment of the endosomal-lysosomal pathway revealed by real-time optical monitoring

bioRxiv; https://doi.org/10.1101/598540.

Native Ion Mobility-Mass Spectrometry Reveals the Formation of β-Barrel Shaped Amyloid-β Hexamers in a Membrane-Mimicking Environment

J. Am. Chem. Soc.; https://doi.org/10.1021/jacs.9b04596.

Gedunin Inhibits Oligomeric Aβ1–42-Induced Microglia Activation Via Modulation of Nrf2-NF-κB Signaling.

Mol Neurobiol.; DOI: 10.1007/s12035-019-1636-9.

Facile single-molecule pull-down assay for analysis of endogenous proteins

Physical Biology; doi: 10.1088/1478-3975/ab0792

Influence of Matrix Metallopeptidase 9 on Beta-Amyloid Elimination Across the Blood-Brain Barrier.

Mol Neurobiol.; DOI: 10.1007/s12035-019-01672-z.

Trodusquemine enhances Aβ42 aggregation but suppresses its toxicity by displacing oligomers from cell membranes

Nature Communications; https://doi.org/10.1038/s41467-018-07699-5

In vitro studies of the neuroprotective activities of astaxanthin and fucoxanthin against amyloid beta (Aβ1-42) toxicity and aggregation

Neurochemistry International; https://doi.org/10.1016/j.neuint.2019.01.010

Amyloid-beta impairs insulin signaling by accelerating autophagy-lysosomal degradation of LRP-1 and IR-β in blood-brain barrier endothelial cells in vitro and in 3XTg-AD mice

Molecular and Cellular Neuroscience; https://doi.org/10.1016/j.mcn.2019.103390.

Marine bacterial extracts as a new rich source of drugs against Alzheimer’s disease.

Journal of Neurochemistry; https://doi.org/10.1111/jnc.14847.

Small molecule sequestration of amyloid-β as a drug discovery strategy for Alzheimer’s disease

bioRxiv; doi: https://doi.org/10.1101/729392.

17 Oxo Sparteine and Lupanine, Obtained from Cytisus scoparius, Exert a Neuroprotection against Soluble Oligomers of Amyloid-β Toxicity by Nicotinic Acetylcholine Receptors.

Journal of Alzheimer’s Disease; DOI: 10.3233/JAD-180945.

Resveratrol alleviates motor and cognitive deficits and neuropathology in the A53T α-synuclein mouse model of Parkinson's disease.

Food & Function; DOI: 10.1039/c8fo00964c.

α-synuclein promotes progression of Parkinson's disease by upregulating autophagy signaling pathway to activate NLRP3 inflammasome.

Experimental and Therapeutic Medicine; https://doi.org/10.3892/etm.2019.8297.

Effects of single and combined immunotherapy approach targeting amyloid β protein and α-synuclein in a dementia with Lewy bodies-like model..

Alzheimers Dement.; doi: 10.1016/j.jalz.2019.02.002.

TREM2 deficiency aggravates α-synuclein–induced neurodegeneration and neuroinflammation in Parkinson’s disease models

FASEB J.; DOI: 10.1096/fj.201900992R.

Functionalization of the TMEM175 p.M393T Variant as a risk factor for Parkinson Disease

Hum Mol Genet.; DOI: 10.1093/hmg/ddz136.

Increased Immune Activation by Pathologic α‐Synuclein in Parkinson's Disease.

Annals of Neurology; https://doi.org/10.1002/ana.25557.

Effect of naturally occurring α-synuclein-antibodies on toxic α-synuclein-fragments.

Neuroscience Letters; https://doi.org/10.1016/j.neulet.2019.04.004

Reduction of Immunoreactivity Against the C-Terminal Region of the Intracellular α-Synuclein by Exogenous α-Synuclein Aggregates: Possibility of Conformational Changes..

Journal of Parkinson’s Disease; doi: 10.3233/JPD-160835..

Identification of a New α-Synuclein Aggregation Inhibitor via Mass Spectrometry Based Screening.

ACS Chem. Neurosci.; https://doi.org/10.1021/acschemneuro.9b00092.