N-Terminal and C-Terminal Domains of Calmodulin Mediate FADD and TRADD Interaction. (Articolo in rivista)

Type

• Prodotto della ricerca (Classe)
• Articolo in rivista (Classe)

Label

• N-Terminal and C-Terminal Domains of Calmodulin Mediate FADD and TRADD Interaction. (Articolo in rivista) (literal)

Anno

• 2015-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

• 10.1371/journal.pone.0116251 (literal)

Alternative label

• Papoff G, Trivieri N, Marsilio S, Crielesi R, Lalli C, Castellani L, Balog EM, Ruberti G. (2015)
  N-Terminal and C-Terminal Domains of Calmodulin Mediate FADD and TRADD Interaction.
  in PloS one
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Papoff G, Trivieri N, Marsilio S, Crielesi R, Lalli C, Castellani L, Balog EM, Ruberti G. (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url

• http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0116251 (literal)

Rivista

• PloS one (Rivista)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• Papoff G, Trivieri N, Marsilio S, Crielesi R, Lalli C, Ruberti G, National Research Council, Institute of Cell Biology and Neurobiology, Campus Adriano Buzzati-Traverso, Monterotondo, Rome, Italy. Castellani L, National Research Council, Institute of Cell Biology and Neurobiology, Campus Adriano Buzzati-Traverso, Monterotondo, Rome, Italy; Department of Human Sciences, Society and Health, University of Cassino, Cassino, Italy. Balog EM, School of Applied Physiology, Georgia Institute of Technology, Atlanta, Georgia, United States of America. (literal)

Titolo

• N-Terminal and C-Terminal Domains of Calmodulin Mediate FADD and TRADD Interaction. (literal)

Abstract

• FADD (Fas-associated death domain) and TRADD (Tumor Necrosis Factor Receptor 1-associated death domain) proteins are important regulators of cell fate in mammalian cells. They are both involved in death receptors mediated signaling pathways and have been linked to the Toll-like receptor family and innate immunity. Here we identify and characterize by database search analysis, mutagenesis and calmodulin (CaM) pull-down assays a calcium-dependent CaM binding site in the ?-helices 1-2 of TRADD death domain. We also show that oxidation of CaM methionines drastically reduces CaM affinity for FADD and TRADD suggesting that oxidation might regulate CaM-FADD and CaM-TRADD interactions. Finally, using Met-to-Leu CaM mutants and binding assays we show that both the N- and C-terminal domains of CaM are important for binding. (literal)

Autore CNR

• Loriana Castellani (Persona)
• NADIA TRIVIERI (Unità di personale esterno)
• GIULIANA PAPOFF (Unità di personale interno)
• CRISTIANA LALLI (Unità di personale esterno)
• GIOVINA RUBERTI (Unità di personale interno)
• Sonia Marsilio (Persona)
• Roberta Crielesi (Unità di personale esterno)

Incoming links:

Autore CNR di

• GIOVINA RUBERTI (Unità di personale interno)
• NADIA TRIVIERI (Unità di personale esterno)
• Loriana Castellani (Persona)
• Roberta Crielesi (Unità di personale esterno)
• GIULIANA PAPOFF (Unità di personale interno)
• CRISTIANA LALLI (Unità di personale esterno)
• Sonia Marsilio (Persona)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• PloS one (Rivista)