M
Maria Soledad Celej
Researcher at National University of Cordoba
Publications - 16
Citations - 901
Maria Soledad Celej is an academic researcher from National University of Cordoba. The author has contributed to research in topics: Alpha-synuclein & Autophagy. The author has an hindex of 11, co-authored 14 publications receiving 740 citations. Previous affiliations of Maria Soledad Celej include National Scientific and Technical Research Council & Max Planck Society.
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Journal ArticleDOI
Toxic prefibrillar α-synuclein amyloid oligomers adopt a distinctive antiparallel β-sheet structure.
Maria Soledad Celej,Rabia Sarroukh,Erik Goormaghtigh,Gerardo D. Fidelio,Jean Marie Ruysschaert,Vincent Raussens +5 more
TL;DR: ATR (attenuated total reflection)-FTIR (Fourier-transform infrared) spectroscopy is used, a technique especially sensitive to β-sheet structure, to get a deeper insight into theβ-sheet organization within oligomers and fibrils and the implications of such conformational arrangement for the pathogenicity associated with AS oligomers are discussed.
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Protein stability induced by ligand binding correlates with changes in protein flexibility
TL;DR: Five conformers are distinguished among the large number of possible states of the conformational dynamic ensemble: BSA1,8‐ANS, BSA2,6‐ANS', BSAfree, B SAbis‐ans, and BSAunfolded among theLarge number of state-based ligand interactions and the relative population of each distinguishable conformer depends on the type and concentration of ligand and the temperature of the system.
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Amyloid fibrils are the molecular trigger of inflammation in Parkinson's disease.
Adelin Gustot,Jose Ignacio Gallea,Rabia Sarroukh,Maria Soledad Celej,Jean Marie Ruysschaert,Vincent Raussens +5 more
TL;DR: It is suggested that the inflammatory properties of α-syn fibrils are linked to their intrinsic structure, most probably to their cross-β structure, and it is proposed that the canonical fibril-specific cross- β structure represents a new generic motif recognized by the innate immune system.
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Neuronal inclusions of α-synuclein contribute to the pathogenesis of Krabbe disease.
Benjamin Smith,Marta B. Santos,Michael S. Marshall,Ludovico Cantuti-Castelvetri,Aurora Lopez-Rosas,Guannan Li,Richard B. van Breemen,Kumiko I. Claycomb,Jose Ignacio Gallea,Maria Soledad Celej,Stephen J. Crocker,Maria I. Givogri,Ernesto R. Bongarzone +12 more
TL;DR: In vitro assays demonstrated that psychosine, the neurotoxic sphingolipid accumulated in Krabbe disease, accelerated the fibrillization of α‐synuclein, identifying Krab be disease as a new α‐ synucleinopathy.
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Autophagy down regulates pro-inflammatory mediators in BV2 microglial cells and rescues both LPS and alpha-synuclein induced neuronal cell death.
Claudio Bussi,Javier María Peralta Ramos,Daniela S. Arroyo,Emilia A. Gaviglio,Jose Ignacio Gallea,Ji Ming Wang,Maria Soledad Celej,Pablo Iribarren +7 more
TL;DR: A novel role for autophagy is demonstrated in the regulation of microglial cell activation and pro-inflammatory molecule secretion, which may be important for the control of inflammatory responses in the CNS and neurotoxicity.