Ivan Rosa e Silva
University of São Paulo
9 Papers
14 Citations
Ivan Rosa e Silva is an academic researcher from University of São Paulo. The author has contributed to research in topics: Selenocysteine & Selenoprotein. The author has an hindex of 3, co-authored 6 publications.
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Papers
Structural validation and assessment of AlphaFold2 predictions for centrosomal and centriolar proteins and their complexes
TL;DR: The authors used AlphaFold2 (AF2) to predict the structure of proteins with essential roles in centrosome and centriole biogenesis, and demonstrated the quality and usability of the AF2 prediction models and they can provide important insights into the modular organization of two key players in this process.
Formation of a Ternary Complex for Selenocysteine Biosynthesis in Bacteria
Ivan Rosa e Silva,Vitor Serrão,Vitor Serrão,Livia Regina Manzine,Lívia Maria Faim,Marco Túlio Alves da Silva,Raphaela Makki,Daniel M. Saidemberg,Marinônio Lopes Cornélio,Mario Sergio Palma,Otavio Henrique Thiemann +10 more
TL;DR: This study demonstrates the interaction of SPS with the SelA-tRNASec complex, resulting in a ternary complex that may be involved in avoiding the cellular toxicity of selenium compounds and proposes that this complex is necessary for proper selenocysteine synthesis.
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Proteomic profiling of centrosomes across multiple mammalian cell and tissue types by an affinity capture method.
Sarah Carden,Elisa Vitiello,Ivan Rosa e Silva,James Holder,Valentina Quarantotti,Kamal Kishore,Valar Nila Roamio Franklin,Clive D'Santos,Takashi Ochi,Mark van Breugel,Fanni Gergely +10 more
TL;DR: The development of centrosome affinity capture-mass spectrometry (CAPture-MS) is reported, a powerful one-step purification method to obtain high-resolution centrosomes from mammalian cells and represents a transformative tool to unveil temporal, regulatory, cell-type- and tissue-specific changes inCentrosome proteomes in health and disease.
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Trypanosomatid selenophosphate synthetase structure, function and interaction with selenocysteine lyase
Marco Túlio Alves da Silva,Ivan Rosa e Silva,Lívia Maria Faim,Natália Karla Bellini,Murilo Leão Pereira,Ana Laura Godinho Lima,Teresa Cristina Leandro de Jesus,Fernanda C. Costa,Tatiana Faria Watanabe,Humberto D'Muniz Pereira,Sandro Roberto Valentini,Cleslei Fernando Zanelli,Júlio César Borges,Marcio Vinicius Bertacine Dias,Julia Pinheiro Chagas da Cunha,Bidyottam Mittra,Norma W. Andrews,Otavio Henrique Thiemann +17 more
TL;DR: The results suggest a role for the T. brucei selenophosphate synthetase in regulation of the parasite’s ER stress response and show how the interaction of different proteins leads to the protection of the cell against the toxic effects of seleium compounds during selenocysteine synthesis.
Trypanosomatid selenophosphate synthetase structure, function and interaction with selenocysteine lyase.
Marco Túlio Alves da Silva,Ivan Rosa e Silva,Lívia Maria Faim,Natália Karla Bellini,Murilo Leão Pereira,Ana Laura Godinho Lima,Teresa Cristina Leandro de Jesus,Fernanda C. Costa,Fernanda C. Costa,Tatiana Faria Watanabe,Humberto D'Muniz Pereira,Sandro Roberto Valentini,Cleslei Fernando Zanelli,Júlio César Borges,Marcio Vinicius Bertacine Dias,Julia Pinheiro Chagas da Cunha,Bidyottam Mittra,Norma W. Andrews,Otavio Henrique Thiemann,Otavio Henrique Thiemann +19 more
TL;DR: The crystal structure of the L. major selenophosphate synthetase was solved and it was confirmed that its dimeric organization is functionally important throughout the domains of life, suggesting a role for the T. brucei selenoprotein T in the regulation of the parasite’s ER stress response.