13 research outputs found
Systemic and transcardiac platelet activity in acute myocardial infarction in man: resistance to prostacyclin.
Hypersensitivity to ADP of platelets from diabetic rats associated with enhanced fibrinogen binding
Erythrocytes with covalently bound fibrinogen as a cellular replacement for the treatment of thrombocytopenia
Development of glycoprotein IIbâIIIa antagonists: translation of pharmacodynamic effects into clinical benefit
Interactions between RNA-binding proteins and P32 homologues in trypanosomes and human cells
RNA-binding proteins (RBPs) are involved in many aspects of mRNA metabolism such as splicing, nuclear export, translation, silencing, and decay. To cope with these tasks, these proteins use specialized domains such as the RNA recognition motif (RRM), the most abundant and widely spread RNA-binding domain. Although this domain was first described as a dedicated RNA-binding moiety, current evidence indicates these motifs can also engage in direct proteinâprotein interactions. Here, we discuss recent evidence describing the interaction between the RRM of the trypanosomatid RBP UBP1 and P22, the homolog of the human multifunctional protein P32/C1QBP. Human P32 was also identified while performing a similar interaction screening using both RRMs of TDP-43, an RBP involved in splicing regulation and Amyotrophic Lateral Sclerosis. Furthermore, we show that this interaction is mediated by RRM1. The relevance of this interaction is discussed in the context of recent TDP-43 interactomic approaches that identified P32, and the numerous evidences supporting interactions between P32 and RBPs. Finally, we discuss the vast universe of interactions involving P32, supporting its role as a molecular chaperone regulating the function of its ligands.Fil: Polledo, Juan Manuel. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Conicet - La Plata. Instituto de Investigaciones BiotecnolĂłgicas. Instituto de Investigaciones BiotecnolĂłgicas "Dr. RaĂșl AlfonsĂn" (sede ChascomĂșs). Universidad Nacional de San MartĂn. Instituto de Investigaciones BiotecnolĂłgicas. Instituto de Investigaciones BiotecnolĂłgicas "Dr. RaĂșl AlfonsĂn" (sede ChascomĂșs); ArgentinaFil: Cervini Bohm, Gabriela Marta . Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Conicet - La Plata. Instituto de Investigaciones BiotecnolĂłgicas. Instituto de Investigaciones BiotecnolĂłgicas "Dr. RaĂșl AlfonsĂn" (sede ChascomĂșs). Universidad Nacional de San MartĂn. Instituto de Investigaciones BiotecnolĂłgicas. Instituto de Investigaciones BiotecnolĂłgicas "Dr. RaĂșl AlfonsĂn" (sede ChascomĂșs); ArgentinaFil: Romaniuk, MarĂa Albertina. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Conicet - La Plata. Instituto de Investigaciones BiotecnolĂłgicas. Instituto de Investigaciones BiotecnolĂłgicas "Dr. RaĂșl AlfonsĂn" (sede ChascomĂșs). Universidad Nacional de San MartĂn. Instituto de Investigaciones BiotecnolĂłgicas. Instituto de Investigaciones BiotecnolĂłgicas "Dr. RaĂșl AlfonsĂn" (sede ChascomĂșs); ArgentinaFil: Cassola, Alejandro Carlos. Consejo Nacional de Investigaciones CientĂficas y TĂ©cnicas. Centro CientĂfico TecnolĂłgico Conicet - La Plata. Instituto de Investigaciones BiotecnolĂłgicas. Instituto de Investigaciones BiotecnolĂłgicas "Dr. RaĂșl AlfonsĂn" (sede ChascomĂșs). Universidad Nacional de San MartĂn. Instituto de Investigaciones BiotecnolĂłgicas. Instituto de Investigaciones BiotecnolĂłgicas "Dr. RaĂșl AlfonsĂn" (sede ChascomĂșs); Argentin