Carlos Tabernero

TL;DR: TAP, like its yeast homolog Mex67p, is a bona fide mRNA nuclear export mediator and is the second cellular RNA binding protein shown to be directly involved in the export of its target RNA.

TL;DR: It is demonstrated that upon removal of all the utilized splicing sites, the env mRNA is still Rev dependent and Rev responsive for expression in human cells, and it is proposed that elements unrelated to utilized splice sites are responsible for the posttranscriptional regulation of env mRNA.

TL;DR: HTAP is a 619-amino-acid protein extending the previously identified protein by another 60 residues at the N terminus and that hTAP shares high homology with the predicted rat and mouse TAP proteins, which further support hT AP’s role as an export factor of the CTE-containing mRNAs.

TL;DR: Analysis of the molecular and structural requirements for function of a 240-nucleotide RNA element that can functionally replace posttranscriptional activation directed by Rev and the Rev-responsive element when inserted into a Rev- and RRE-deficient molecular clone of human immunodeficiency virus type 1, demonstrates the importance of the sequence and structure of the SRV-1 CTE for appropriate function.

TL;DR: Comparative analysis of the predicted amino acid sequence showed that basidiomycete PM1 laccase I had great similarity to the laccases fromCoriolus versicolor, Coriolus hirsutus, and Phlebia radiata.