The malaria parasite Plasmodium falciparum histones: organization, expression, and acetylation.

The malaria parasite Plasmodium falciparum histones: organization, expression, and acetylation.

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http://www.wikidata.org/entity/Q46892612
Toxoplasma histone acetylation remodelers as novel drug targetsPlasmodium falciparum histones induce endothelial proinflammatory response and barrier dysfunctionDNA organization by the apicoplast-targeted bacterial histone-like protein of Plasmodium falciparumExpression of P. falciparum var genes involves exchange of the histone variant H2A.Z at the promoterPlasmodium falciparum heterochromatin protein 1 marks genomic loci linked to phenotypic variation of exported virulence factorsThe MYST family histone acetyltransferase regulates gene expression and cell cycle in malaria parasite Plasmodium falciparumIdentification and molecular characterization of an Alba-family protein from human malaria parasite Plasmodium falciparumComprehensive histone phosphorylation analysis and identification of Pf14-3-3 protein as a histone H3 phosphorylation reader in malaria parasitesPlasmodium falciparum heterochromatin protein 1 binds to tri-methylated histone 3 lysine 9 and is linked to mutually exclusive expression of var genesHistone deacetylases play a major role in the transcriptional regulation of the Plasmodium falciparum life cycleH2A.Z demarcates intergenic regions of the plasmodium falciparum epigenome that are dynamically marked by H3K9ac and H3K4me3Plasmodium falciparum centromeres display a unique epigenetic makeup and cluster prior to and during schizogonyBranched tricarboxylic acid metabolism in Plasmodium falciparumH3.3 demarcates GC-rich coding and subtelomeric regions and serves as potential memory mark for virulence gene expression in Plasmodium falciparumCharacterization of PRMT1 from Plasmodium falciparumThe RNA-binding protein Puf1 functions in the maintenance of gametocytes in Plasmodium falciparumThe Puf-family RNA-binding protein PfPuf2 regulates sexual development and sex differentiation in the malaria parasite Plasmodium falciparumA moonlighting function of Plasmodium falciparum histone 3, mono-methylated at lysine 9?H2A.Z/H2B.Z double-variant nucleosomes inhabit the AT-rich promoter regions of the Plasmodium falciparum genomeQuantitative proteomic analysis of histone modificationsA unified phylogeny-based nomenclature for histone variantsGenome-wide nucleosome mapping of Plasmodium falciparum reveals histone-rich coding and histone-poor intergenic regions and chromatin remodeling of core and subtelomeric genesIn silico and biological survey of transcription-associated proteins implicated in the transcriptional machinery during the erythrocytic development of Plasmodium falciparum.One-pot shotgun quantitative mass spectrometry characterization of histonesDesigning synthetic drugs against Plasmodium falciparum: a computational study of histone-lysine N-methyltransferase (PfHKMT)Quantitative chromatin proteomics reveals a dynamic histone post-translational modification landscape that defines asexual and sexual Plasmodium falciparum parasitesRegulation of gene expression in protozoa parasitesEpigenetic control of the variable expression of a Plasmodium falciparum receptor protein for erythrocyte invasionChromatin-mediated epigenetic regulation in the malaria parasite Plasmodium falciparum.Development of diaminoquinazoline histone lysine methyltransferase inhibitors as potent blood-stage antimalarial compoundsDynamic epigenetic regulation of gene expression during the life cycle of malaria parasite Plasmodium falciparum.Puf mediates translation repression of transmission-blocking vaccine candidates in malaria parasitesProtein arginine methylation in parasitic protozoa.Multiple dimensions of epigenetic gene regulation in the malaria parasite Plasmodium falciparum: gene regulation via histone modifications, nucleosome positioning and nuclear architecture in P. falciparumCytotoxic effect of curcumin on malaria parasite Plasmodium falciparum: inhibition of histone acetylation and generation of reactive oxygen species.Profiling the anti-protozoal activity of anti-cancer HDAC inhibitors against Plasmodium and Trypanosoma parasitesChromatin modifications, epigenetics, and how protozoan parasites regulate their lives.PfGCN5-mediated histone H3 acetylation plays a key role in gene expression in Plasmodium falciparum.Lysine acetylation is widespread on proteins of diverse function and localization in the protozoan parasite Toxoplasma gondii.Histone lysine methyltransferases and demethylases in Plasmodium falciparum
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P2860

The malaria parasite Plasmodium falciparum histones: organization, expression, and acetylation.

Item
http://www.wikidata.org/entity/Q46892612
description
2006 nî lūn-bûn
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2006年の論文
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2006年学术文章
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2006年学术文章
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2006年学术文章
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2006年学术文章
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2006年学术文章
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2006年学术文章
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2006年學術文章
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2006年學術文章
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name
The malaria parasite Plasmodiu ...... , expression, and acetylation.
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The malaria parasite Plasmodiu ...... , expression, and acetylation.
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type
label
The malaria parasite Plasmodiu ...... , expression, and acetylation.
@en
The malaria parasite Plasmodiu ...... , expression, and acetylation.
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prefLabel
The malaria parasite Plasmodiu ...... , expression, and acetylation.
@en
The malaria parasite Plasmodiu ...... , expression, and acetylation.
@nl
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The malaria parasite Plasmodiu ...... , expression, and acetylation.
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10.1016/J.GENE.2005.10.022
P407
P478
P50
P577
P5875
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P921