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Juan E. Ludert

Researcher at CINVESTAV

Publications -  97
Citations -  3527

Juan E. Ludert is an academic researcher from CINVESTAV. The author has contributed to research in topics: Dengue virus & Dengue fever. The author has an hindex of 34, co-authored 88 publications receiving 3178 citations. Previous affiliations of Juan E. Ludert include Venezuelan Institute for Scientific Research & National Autonomous University of Mexico.

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Etiology and outcome of diarrhea after marrow transplantation: a prospective study.

TL;DR: Most cases of diarrhea after marrow transplant are not caused by infection, and clinical signs and symptoms of infection and GVHD were similar, and no clear etiology could be found for self-limited diarrhea.
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Diversity and evolution of the envelope gene of dengue virus type 1.

TL;DR: Very low average value of the ratio of nonsynonymous-to-synonymous nucleotide substitutions, relative to the respective sites, indicated that the evolution of the E gene of the DV-1 is subject mostly to purifying selection.
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Rapid antigen tests for dengue virus serotypes and Zika virus in patient serum

Irene Bosch, +58 more
TL;DR: The characterization of monoclonal antibody pairs that have been translated into rapid immunochromatography tests to specifically detect the viral nonstructural 1 (NS1) protein antigen and distinguish the four DENV serotypes (DENV1–4) and ZIKV without cross-reaction are reported.
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Endocytic pathway followed by dengue virus to infect the mosquito cell line C6/36 HT.

TL;DR: Results indicate that dengue virions enter into C6/36 HT cells by clathrin-mediated endocytosis, using the endosomal pathway from early endosomes to acidic lysosomes before viral RNA is released into the cytoplasm.
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Genetic mapping indicates that VP4 is the rotavirus cell attachment protein in vitro and in vivo.

TL;DR: Income and binding assays indicate that gene 4 encodes the rotavirus protein which mediates attachment to cells in culture for both sialic acid-dependent and -independent strains, and VP4 appears to function as the cell attachment protein in vivo as well as in vitro.