Outeiro, Tiago Fleming

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05.10.2024

The synaptic vesicle cluster as a controller of pre- and postsynaptic structure and function

Authors Reshetniak S, Bogaciu CA, Bonn S, Brose N, Cooper BH, D’Este E, Fauth M, Fernández-Busnadiego R, Fiosins M, Fischer A, Georgiev SV, Jakobs S, Klumpp S, Köster S, Lange F, Lipstein N, Macarrón-Palacios V, Milovanovic D, Moser T, Müller M, Opazo F, Outeiro TF, Pape C, Priesemann V, Rehling
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25.09.2024

A novel alpha-synuclein G14R missense variant is associated with atypical neuropathological features

Authors Brücke C, Al-Azzani M, Ramalingam N, Ramón M, Sousa RL, Buratti F, Zech M, Sicking K, Amaral L, Gelpi E, Chandran A, Agarwal A, Chaves SR, Fernández CO, Dettmer U, Lautenschläger J, Zweckstteter M, Fernandez Busnadiego R, Zimprich A, Outeiro TF Journal MedRxiv Citation medRxiv 2024.09.23.24313864. Abstract Background: Parkinson’s
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12.09.2024

The epitranscriptomic m6A RNA modification modulates synaptic function in ageing and in a mouse model of synucleinopathy

Authors Chopra A, Xylaki M, Yin F, Castro-Hernández R, Merghani M, Grande V, Mollenhauer B, Fischer A, Outeiro TF Journal BioRxiv Citation bioRxiv 2024.09.12.612649. Abstract N6-methyladenosine (m6A) is the most abundant and conserved transcriptional modification in eukaryotic RNA, regulating RNA fate. While the functions of m6A in the development of
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06.08.2024

A versatile yeast model identifies the pesticides cymoxanil and metalaxyl as risk factors for synucleinopathies

Authors Amaral L, Mendes F, Côrte-Real M, Rego A, Outeiro TF, Chaves SR Journal Chemosphere Citation Chemosphere. 2024 Aug 6:143039. Abstract Parkinson’s disease (PD) is a neurodegenerative disorder characterized by the loss of dopaminergic neurons and the presence of Lewy bodies, which predominantly consist of aggregated forms of the protein
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05.07.2024

Synthesis and Semi-Synthesis of Alpha-Synuclein: Insight into the Chemical Complexity of Synucleinopathies

Authors Gatzemeier LM, Meyer F, Outeiro TF Journal ChemBioChem Citation Chembiochem. 2024 Jul 5:e202400253. Abstract The chemical rules governing protein folding have intrigued generations of researchers for decades. With the advent of artificial intelligence (AI), prediction of protein structure has improved tremendously. However, there is still a level of analysis
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02.07.2024

Glycation of alpha-synuclein enhances aggregation and neuroinflammatory responses

Authors Vasili E, Konig A, Al-Azzani M, Bosbach C, Gatzemeier LM, Chegao A, Miranda HV, Erskine D, Outeiro T Journal BioRxiv Citation bioRxiv 2024.06.27.600956. Abstract The risk of developing Parkinson’s disease (PD) is elevated in people with type 2 diabetes, but the precise molecular pathways underlying this connection are still
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22.06.2024

Aging and neurodegeneration: From molecular mechanisms to therapeutic interventions

Authors Outeiro TF, Brocardo PS, Gelain DP Journal Journal of Neurochemistry Citation J Neurochem. 2024 Jun 22. Abstract Protein aggregation is a common age-associated process and can be a pathological hallmark of various neurodegenerative conditions, possibly because of an age-associated decline in the activity of components of the proteostasis network.
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13.04.2024

α-Synuclein triggers cofilin pathology and dendritic spine impairment via a PrPC-CCR5 dependent pathway

Authors Oliveira da Silva MI, Santejo M, Babcock IW, Magalhães A, Minamide LS, Won SJ, Castillo E, Gerhardt E, Fahlbusch C, Swanson RA, Outeiro TF, Taipa R, Ruff M, Bamburg JR, Liz MA Journal Cell Death & Disease Citation Cell Death Dis. 2024 Apr 13;15(4):264. Abstract Cognitive dysfunction and dementia
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04.04.2024

Basic Science in Movement Disorders: Fueling the Engine of Translation into Clinical Practice

Authors Outeiro TF, Kalia LV, Bezard E, Ferrario J, Lin CH, Salama M, Standaert DG, Taiwo L, Takahashi R, Vila M, Mollenhauer B, Svenningsson P; MDS Journal Movement Disorders Citation Mov Disord. 2024 Apr 4. Abstract Basic Science is crucial for the advancement of clinical care for Movement Disorders. Here,
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27.03.2024

Chemical synthesis of site-selective advanced glycation end products in α-synuclein and its fragments

Authors Bosbach C, Gatzemeier LM, Bloch von Blottnitz KI, König A, Diederichsen U, Steinem C, Outeiro TF Journal Organic & Biomolecular Chemistry Citation Org Biomol Chem. 2024 Mar 27;22(13):2670-2676. Abstract Advanced glycation end products (AGEs) arise from the Maillard reaction between dicarbonyls and proteins, nucleic acids, or specific lipids. Notably,
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