J
Javier M. Rodríguez
Researcher at Spanish National Research Council
Publications - 63
Citations - 2823
Javier M. Rodríguez is an academic researcher from Spanish National Research Council. The author has contributed to research in topics: African swine fever virus & Virus. The author has an hindex of 28, co-authored 62 publications receiving 2304 citations. Previous affiliations of Javier M. Rodríguez include Autonomous University of Madrid & Carlos III Health Institute.
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Journal ArticleDOI
African swine fever virus p10 protein exhibits nuclear import capacity and accumulates in the nucleus during viral infection.
Isabel Nunes-Correia,Javier M. Rodríguez,Ana Eulalio,Ana Luísa Carvalho,Vitaly Citovsky,Sérgio Simões,Carlos Faro,María L. Salas,Maria C. Pedroso de Lima +8 more
TL;DR: In ASFV-infected cells, the p10 protein strongly accumulates in the nucleus at late times post-infection, indicating that p10protein may accomplish an important function inside the nucleus during the late phase of the viral replication cycle.
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African Swine Fever Virus trans-Prenyltransferase
TL;DR: The present study describes the characterization of an African swine fever virus gene homologous to prenyltransferases, located within the EcoRI B fragment in the central region of the virus genome, and encodes a polypeptide characterized by the presence of a putative hydrophobic transmembrane domain at the amino end.
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Highly efficient expression of proteins encoded by recombinant vaccinia virus in lymphocytes.
TL;DR: The physiology of T cells appears to be less perturbed by VV than that of B ceils, although the virus is capable of directing expression of recombinant genes to T lymphocytes.
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Mxi2 sustains ERK1/2 phosphorylation in the nucleus by preventing ERK1/2 binding to phosphatases.
TL;DR: It is shown that Mxi2 prevents nuclear but not cytoplasmic phosphatases from binding to and dephosphorylating ERK1/2, disclosing an unprecedented mechanism for the spatial regulation of ERK 1/2 activation.
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The expression of heat shock protein HSP60A reveals a dynamic mitochondrial pattern in Drosophila melanogaster embryos.
TL;DR: Using two-dimensional gel electrophoresis followed by MALDI-TOF to identify and purify heat shock protein HSP60A of Drosophila melanoagaster shows that it is heat-shock inducible and describes two novel antisera, specifically designed to recognize the denatured and native polypeptide, respectively, in Dosophila.