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Miguel Vidal

Researcher at Spanish National Research Council

Publications -  84
Citations -  12557

Miguel Vidal is an academic researcher from Spanish National Research Council. The author has contributed to research in topics: Gene & Cellular differentiation. The author has an hindex of 43, co-authored 82 publications receiving 11787 citations. Previous affiliations of Miguel Vidal include Heidelberg University & National Institute for Medical Research.

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Polycomb complexes repress developmental regulators in murine embryonic stem cells

TL;DR: It is shown that PcG proteins directly repress a large cohort of developmental regulators in murine ES cells, the expression of which would otherwise promote differentiation, and dynamic repression of developmental pathways by Polycomb complexes may be required for maintaining ES cell pluripotency and plasticity during embryonic development.
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Role of histone H2A ubiquitination in Polycomb silencing

TL;DR: The purification and functional characterization of an E3 ubiquitin ligase complex that is specific for histone H2A is reported, and it is linked to Polycomb silencing, which is important in regulating chromatin dynamics and transcription.
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Polycomb Group Proteins Ring1A/B Link Ubiquitylation of Histone H2A to Heritable Gene Silencing and X Inactivation

TL;DR: It is demonstrated that uH2A occurs on the inactive X chromosome in female mammals and that this correlates with recruitment of Polycomb group (PcG) proteins belonging to Polycomb repressor complex 1 (PRC1).
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Ring1-mediated ubiquitination of H2A restrains poised RNA polymerase II at bivalent genes in mouse ES cells

TL;DR: It is shown here that this important subset of developmental regulator genes, termed bivalent genes, assemble RNAP complexes phosphorylated on Ser 5 and are transcribed at low levels, providing an insight into the molecular mechanisms that allow ES cells to self-renew and yet retain the ability to generate multiple lineage outcomes.
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RYBP-PRC1 Complexes Mediate H2A Ubiquitylation at Polycomb Target Sites Independently of PRC2 and H3K27me3

TL;DR: It is shown that RING1B, the catalytic subunit of PRC1, and associated monoubiquitylation of histone H2A are targeted to closely overlapping sites in wild-type and PRC2-deficient mouse embryonic stem cells (mESCs), demonstrating an H3K27me3-independent pathway for recruitment ofPRC1 activity.