Search Results - "Bigi, Ilaria"

Shank synaptic scaffold proteins: keys to understanding the pathogenesis of autism and other synaptic disorders by Sala, Carlo, Vicidomini, Cinzia, Bigi, Ilaria, Mossa, Adele, Verpelli, Chiara

“…Shank/ProSAP proteins are essential to synaptic formation, development, and function. Mutations in the family of SHANK genes are strongly associated with…”
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A Surveillance Function of the HSPB8-BAG3-HSP70 Chaperone Complex Ensures Stress Granule Integrity and Dynamism by Ganassi, Massimo, Mateju, Daniel, Bigi, Ilaria, Mediani, Laura, Poser, Ina, Lee, Hyun O., Seguin, Samuel J., Morelli, Federica F., Vinet, Jonathan, Leo, Giuseppina, Pansarasa, Orietta, Cereda, Cristina, Poletti, Angelo, Alberti, Simon, Carra, Serena

“…Stress granules (SGs) are ribonucleoprotein complexes induced by stress. They sequester mRNAs and disassemble when the stress subsides, allowing translation…”
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The chaperone HSPB8 reduces the accumulation of truncated TDP-43 species in cells and protects against TDP-43-mediated toxicity by Crippa, Valeria, Cicardi, Maria Elena, Ramesh, Nandini, Seguin, Samuel J, Ganassi, Massimo, Bigi, Ilaria, Diacci, Chiara, Zelotti, Elena, Baratashvili, Madina, Gregory, Jenna M, Dobson, Christopher M, Cereda, Cristina, Pandey, Udai Bhan, Poletti, Angelo, Carra, Serena

“…Aggregation of TAR-DNA-binding protein 43 (TDP-43) and of its fragments TDP-25 and TDP-35 occurs in amyotrophic lateral sclerosis (ALS). TDP-25 and TDP-35 act…”
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BAG3 and BAG6 differentially affect the dynamics of stress granules by targeting distinct subsets of defective polypeptides released from ribosomes by Mediani, Laura, Galli, Veronica, Carrà, Arianna Dorotea, Bigi, Ilaria, Vinet, Jonathan, Ganassi, Massimo, Antoniani, Francesco, Tiago, Tatiana, Cimino, Marco, Mateju, Daniel, Cereda, Cristina, Pansarasa, Orietta, Alberti, Simon, Mandrioli, Jessica, Carra, Serena

“…Stress granules (SGs) are dynamic ribonucleoprotein granules induced by environmental stresses. They play an important role in the stress response by…”
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Defective ribosomal products challenge nuclear function by impairing nuclear condensate dynamics and immobilizing ubiquitin by Mediani, Laura, Guillén‐Boixet, Jordina, Vinet, Jonathan, Franzmann, Titus M, Bigi, Ilaria, Mateju, Daniel, Carrà, Arianna D, Morelli, Federica F, Tiago, Tatiana, Poser, Ina, Alberti, Simon, Carra, Serena

“…Nuclear protein aggregation has been linked to genome instability and disease. The main source of aggregation‐prone proteins in cells is defective ribosomal…”
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Hsp90-mediated regulation of DYRK3 couples stress granule disassembly and growth via mTORC1 signaling by Mediani, Laura, Antoniani, Francesco, Galli, Veronica, Vinet, Jonathan, Carrà, Arianna Dorotea, Bigi, Ilaria, Tripathy, Vadreenath, Tiago, Tatiana, Cimino, Marco, Leo, Giuseppina, Amen, Triana, Kaganovich, Daniel, Cereda, Cristina, Pansarasa, Orietta, Mandrioli, Jessica, Tripathi, Priyanka, Troost, Dirk, Aronica, Eleonora, Buchner, Johannes, Goswami, Anand, Sterneckert, Jared, Alberti, Simon, Carra, Serena

“…Stress granules (SGs) are dynamic condensates associated with protein misfolding diseases. They sequester stalled mRNAs and signaling factors, such as the…”
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An interaction study in mammalian cells demonstrates weak binding of HSPB2 to BAG3, which is regulated by HSPB3 and abrogated by HSPB8 by Morelli, Federica F., Mediani, Laura, Heldens, Lonneke, Bertacchini, Jessika, Bigi, Ilaria, Carrà, Arianna Dorotea, Vinet, Jonathan, Carra, Serena

“…The ten mammalian small heat shock proteins (sHSPs/HSPBs) show a different expression profile, although the majority of them are abundant in skeletal and…”
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