M
Maribel Parra
Researcher at University of California, San Francisco
Publications - 35
Citations - 2338
Maribel Parra is an academic researcher from University of California, San Francisco. The author has contributed to research in topics: Transcription factor & Plasminogen activator. The author has an hindex of 23, co-authored 34 publications receiving 2085 citations. Previous affiliations of Maribel Parra include Katholieke Universiteit Leuven & Catalan Institution for Research and Advanced Studies.
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Journal ArticleDOI
Histone deacetylases and cancer.
TL;DR: The aim of this review is to summarize the current knowledge concerning the role of HDACs in cancer with special emphasis on what the authors have learned from the analysis of patient samples.
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Control of endothelial cell proliferation and migration by VEGF signaling to histone deacetylase 7
TL;DR: It is shown that VEGF induces the phosphorylation of three conserved serine residues in histone deacetylase 7 (HDAC7) via protein kinase D, which promotes nuclear export of HDAC7 and activation of V EGF-responsive genes in ECs.
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The SWI/SNF chromatin-remodeling complex is a cofactor for Tat transactivation of the HIV promoter.
Tokameh Mahmoudi,Maribel Parra,Robert G.J. Vries,Steven E. Kauder,C. Peter Verrijzer,Melanie Ott,Eric Verdin +6 more
TL;DR: Tat-mediated activation of the HIV promoter requires the SWI/SNF complex in synergy with the coactivator p300, and it is found that INI-1 and BRG-1 synergized with the p300 acetyltransferase to activate the HIV promoters.
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Repressive LTR Nucleosome Positioning by the BAF Complex Is Required for HIV Latency
Haleh Rafati,Maribel Parra,Shweta Hakre,Yuri M. Moshkin,Eric Verdin,Tokameh Mahmoudi,Tokameh Mahmoudi +6 more
TL;DR: The role of SWI/SNF in regulation of the latent HIV LTR before and after transcriptional activation is addressed and a striking reverse correlation is found when compared to the strictly positioned in vivo LTR nucleosomal structure.
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Protein kinase D1 phosphorylates HDAC7 and induces its nuclear export after T-cell receptor activation
TL;DR: It is reported that HDAC7 is exported to the cytoplasm by a calcium-independent signaling pathway after TCR activation, and observations indicate that PKD1 regulates the expression of Nur77 during thymocyte activation at least in part by phosphorylatingHDAC7.