J
Jerson L. Silva
Researcher at Federal University of Rio de Janeiro
Publications - 242
Citations - 9604
Jerson L. Silva is an academic researcher from Federal University of Rio de Janeiro. The author has contributed to research in topics: Hydrostatic pressure & Protein aggregation. The author has an hindex of 51, co-authored 225 publications receiving 8496 citations. Previous affiliations of Jerson L. Silva include Boston Biomedical Research Institute & University of Illinois at Urbana–Champaign.
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Journal ArticleDOI
Pressure stability of proteins
Jerson L. Silva,Gregorio Weber +1 more
TL;DR: Observations of pressure effects ought to precede those of tem perature in order to facilitate the interpretation of the more involved effects of the latter variable.
Journal ArticleDOI
Pressure provides new insights into protein folding, dynamics and structure.
TL;DR: Kinetic studies under pressure enable dissection of the roles of packing and cavities in folding, and in assembly of multimolecular structures such as protein-DNA complexes and viruses.
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DNA Converts Cellular Prion Protein into the β-Sheet Conformation and Inhibits Prion Peptide Aggregation
Yraima Cordeiro,Filipe Machado,Luiz Juliano,Maria A. Juliano,Ricardo R. Brentani,Debora Foguel,Jerson L. Silva +6 more
TL;DR: It is suggested that a macromolecular complex of prion-DNA may act as an intermediate for the formation of the growing fiber, and host nucleic acid may modulate the delicate balance between the cellular and the misfolded conformations by reducing the protein mobility and by making the protein-protein interactions more likely.
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Mutant p53 Aggregates into Prion-like Amyloid Oligomers and Fibrils IMPLICATIONS FOR CANCER
Ana Paula Dinis Ano Bom,Luciana P. Rangel,Danielly C. Ferraz da Costa,Guilherme A. P. de Oliveira,Daniel Sanches,Carolina A. Braga,Lisandra M. Gava,Lisandra M. Gava,Carlos H.I. Ramos,Carlos H.I. Ramos,Ana Oliva Tiroli Cepeda,Ana Carolina Stumbo,Claudia V. De Moura Gallo,Claudia V. De Moura Gallo,Yraima Cordeiro,Jerson L. Silva +15 more
TL;DR: It is concluded that aggregation of p53 into a mixture of oligomers and fibrils sequestrates the native protein into an inactive conformation that is typical of a prionoid.
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The preaggregated state of an amyloidogenic protein: hydrostatic pressure converts native transthyretin into the amyloidogenic state.
TL;DR: It is shown that hydrostatic pressure converts native tetramers of TTR into an altered state that shares properties with a previously described amyloidogenic intermediate, and it may be an intermediate that lies on the aggregation pathway.