about
Alterations of mitochondrial dynamics allow retrograde propagation of locally initiated axonal insultsIdentification of interaction domains of the prion protein with its 37-kDa/67-kDa laminin receptorSequential signaling through Notch1 and erbB receptors mediates radial glia differentiationCombining microfluidics, optogenetics and calcium imaging to study neuronal communication in vitro.Double-Edge Sword of Sustained ROCK Activation in Prion Diseases through Neuritogenesis Defects and Prion AccumulationManipulation of the N-terminal sequence of the Borna disease virus X protein improves its mitochondrial targeting and neuroprotective potential.Microfluidic construction of minimalistic neuronal co-cultures.Magnetic proteinase K reactor as a new tool for reproducible limited protein digestion.β-amyloid induces a dying-back process and remote trans-synaptic alterations in a microfluidic-based reconstructed neuronal network.Corrigendum: Alterations of mitochondrial dynamics allow retrograde propagation of locally initiated axonal insultsNeuron dysfunction is induced by prion protein with an insertional mutation via a Fyn kinase and reversed by sirtuin activation in Caenorhabditis elegans.BDNF stimulates migration of cerebellar granule cells.Activation of the JNK-c-Jun pathway during the early phase of neuronal apoptosis induced by PrP106-126 and prion infection.Axon diodes for the reconstruction of oriented neuronal networks in microfluidic chambers.Neurotoxicity of the Cyanotoxin BMAA Through Axonal Degeneration and Intercellular Spreading.Combination of memantine and vitamin D prevents axon degeneration induced by amyloid-beta and glutamate.In-mold patterning and actionable axo-somatic compartmentalization for on-chip neuron culture.Controlled proteolysis of normal and pathological prion protein in a microfluidic chip.Theoretical analysis of the implication of PrP in neuronal death during transmissible subacute spongiform encephalopathies: hypothesis of a PrP oligomeric channel.Dysregulated Neurotransmission induces Trans-synaptic degeneration in reconstructed Neuronal NetworksGlutamatergic and dopaminergic modulation of cortico-striatal circuits probed by dynamic calcium imaging of networks reconstructed in microfluidic chipsNeurotoxicity of the Putative Transmembrane Domain of the Prion ProteinPropagation of α-Synuclein Strains within Human Reconstructed Neuronal NetworkReconstruction of directed neuronal networks in a microfluidic device with asymmetric microchannelsTransmission of the BSE agent to mice in the absence of detectable abnormal prion proteinEpidemiology of cervical spine abnormalities in asymptomatic adult professional rugby union players using static and dynamic MRI protocols: 2002 to 2006Endogenous prion protein conversion is required for prion-induced neuritic alterations and neuronal deathCellular mechanisms responsible for cell-to-cell spreading of prionsCorrection to: Cellular mechanisms responsible for cell-to-cell spreading of prions
P50
Q27312652-4AE35A18-9E81-427B-8110-608551063A17Q28363055-E3BC648E-8075-4627-B350-54560C2F0CF4Q28577336-49C29E18-CBDB-4C21-A414-AAF5CEF80ED1Q35611436-D2A92109-3E97-45DD-9F38-B39B1760A6CAQ35737668-8E47A5E0-1199-4E9C-9A44-BA47E7056D18Q35877670-80A81704-21AA-4E5C-AE94-6B123ECF388BQ39195565-62ED52E9-3D74-4F0C-9542-6104A3C5011BQ40003307-C84C2294-4EF0-436E-8F32-5A8D9D1B3590Q41861213-E325A104-8AC8-4CBE-B9C1-70357BFE42E0Q42370979-9CFBAED9-2B15-4FB2-B25F-ED80CB7A1E71Q43099242-9D2464A5-7C13-4F8B-AAC5-33831D353C24Q48668885-3DBB5EE7-8403-414F-8F6E-ECD3E47EEE34Q48873095-755C88A6-5FF0-4078-87E8-AE1E7126089BQ48895630-A75CC1BE-EC74-4F0E-BCFD-271F353D55E0Q50495346-D4859EB2-8355-488A-BADA-BDA8018E24C5Q50883284-FDCD9908-0D78-470C-B953-A7FF9BAF915AQ51462814-21F54150-D1C5-4490-B389-8D0686AA762FQ51575758-65178B02-0954-41CB-8CE3-BB5201B6692FQ54054664-1DFBA00A-67D4-40EF-8E68-316057409553Q58803573-755BFDA0-E3B4-43C0-8281-2D0497B9573AQ59802214-04CA66FF-CB16-4D9C-A221-3ABCDCAEE621Q61587543-7710864B-3480-41D0-B0F7-FFC5A21389BEQ64238991-242F26A4-EDEA-459A-877A-630C3AFABFB3Q64814721-D45A038A-D68C-4145-ADC4-70136229E52DQ71970964-3F3483C5-F182-460E-80E5-7AB6C0C3A179Q81006176-19B18E30-CFC4-4E37-BD72-69A526BB53AAQ84282802-7F1B2DC1-8F91-4A9D-8D95-1A80F9B63CEFQ88673114-F798EF7F-3B28-4B38-A670-4FDCD11CEAA1Q89122048-3B3043A0-888F-498D-92FB-0ECED63BAEB0
P50
description
researcher (ORCID 0000-0002-8705-8672)
@en
wetenschapper
@nl
name
Jean-Michel Peyrin
@ast
Jean-Michel Peyrin
@en
Jean-Michel Peyrin
@nl
type
label
Jean-Michel Peyrin
@ast
Jean-Michel Peyrin
@en
Jean-Michel Peyrin
@nl
prefLabel
Jean-Michel Peyrin
@ast
Jean-Michel Peyrin
@en
Jean-Michel Peyrin
@nl
P106
P31
P496
0000-0002-8705-8672