Outeiro, Tiago Fleming

Authors Flores-León M, Outeiro TF   Journal FEBS Journal   Citation FEBS J. 2025 Feb 25.   Abstract A possible consequence of the process of protein aggregation in neurodegenerative diseases is the depletion of soluble protein species (proteinopenia), which may, at least in some cases, reduce protein function/activity. This concept,

Authors Outeiro TF, Höglinger G, Lang AE, Vieira TCRG Journal Journal of Neural Transmission Citation J Neural Transm (Vienna). 2025 Feb 11. Abstract Protein misfolding and aggregation is a major pathological hallmark in a variety of human conditions, including cancer, diabetes, and neurodegeneration. However, we still do not fully understand

Authors da Silva IS, Cardoso AR, Reimer L, König A, van Riesen C, Outeiro TF, Jensen PH, Sales MGF Journal Biosensors and Bioelectronics Citation Biosensors and Bioelectronics 268 (2025) 116880. Abstract Aggregation of alpha-synuclein (aSyn) occurs in presynaptic neurons and constitutes a key factor for the progression of Parkinson’s disease,

Authors de Bruyn E, Dorn AE, Rossetti G, Fernandez C, Outeiro TF, Schulz JB, Carloni P Journal Journal of Chemical Information and Modeling Citation J Chem Inf Model. 2024 Oct 27. Abstract Serine 129 can be phosphorylated in pathological inclusions formed by the intrinsically disordered protein human α-synuclein (AS), a

Authors Shaib AH, Chouaib AA, Chowdhury R, Altendorf J, Mihaylov D, Zhang C, Krah D, Imani V, Spencer RKW, Georgiev SV, Mougios N, Monga M, Reshetniak S, Mimoso T, Chen H, Fatehbasharzad P, Crzan D, Saal KA, Alawieh MM, Alawar N, Eilts J, Kang J, Soleimani A, Müller M, Pape

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

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

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

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

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.