Global ETD Search
Search theses and dissertations gathered from participating repositories worldwide. Every result links back to the library that holds it. No account is needed.
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Showing 1 to 10 of 10 for “"PHD finger"”.
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THE PHD FINGER OF SP140: A STRUCTURAL AND FUNCTIONAL STUDY
… signal, a SAND domain (residues 588-661), a PHD finger (residues 692-734) and a bromodomain (residues 756-859). In this thesis we investigated Sp140 PHD finger both at functional and structural level. Structural determination was performed in solution by means of NMR spectroscopy. Analysis of …
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Structural studies of paired PHD finger-bromodomain chromatin-binding modules: targeting epigenetic readers with chemical probes
… the binding mode of the H3 histone tail by the PHD zinc finger of BAZ2A. A crystal structure of the complex of BAZ2A with the H3 10-mer peptide identified a helical conformation of H3 upon binding with the PHD. This information coupled with further structural and biophysical analysis led to the …
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The PHD finger protein 5 is a part of the spliceosome and acts as a DNA-binding protein
Vier Proteine: U2AF35, SRp40, mDomino und Ddx1 wurden durch Screening Yeast-two hybride-Bibliothek als Partner des PHF 5a-Protein gefunden. Proteininteraktionen wurden in-vitro und in-vivo bestätigt. Die für Bindungen verantwortlichen Domäne wurden als RS Domäne (reich an Arginin-Serin) …
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PHDS, Stress, And Starvation: The Identification Of A New RPD3 Deacetylase Complex Involved In The Yeast Oxidative Stress And Metabolism Pathways
… regulators is the plant homeodomain, or PHD finger, a module that preferentially interacts with either methylated or unmethylated lysines on histones, and has important functions in human health. Despite recent advances in identifying the histone ligands for some PHD fingers as well as …
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Analysis of Plant Homeodomain Proteins and the Inhibitor of Growth Family Proteins in Arabidopsis thaliana
… the open versus closed status of chromatin. The PHD (Plant HomeoDomain) finger is a structural domain primarily found in nuclear proteins across eukaryotes. This domain specifically recognizes the epigenetic marks H3K4me2 and H3K4me3, which are di- and tri-methylated lysine 4 residues of Histone …
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The susceptibility of primordial germ cells to malignant transformation and isolation and characterization of members of a new gene family differentially expressed in invasive and non-invasive immortalized male germ cells
… wurden. Wir bezeichneten dieses Gen Pfcp (PHD-finger ähnlich chromatin proteins) weil die deduzierte Proteinsequenz eine Domäne zeigt,welche bekannt als PHD-finger ähnliche Domäne ist,dafür bekannt ist in die chromatin Bindung integriert zu sein. Die cDNA Sequenz des Pfcp Gens der Maus …
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Trim24-Regulated Estrogen Response Is Dependent On Specific Histone Modifications In Breast Cancer Cells
… In the first</p> <p>part, I proved that TRIM24-PHD finger domain, which recognizes unmethylated</p> <p>histone H3 lysine K4 (H3K4me0), is critical for ERα-regulated transcription.</p> <p>Therefore, when LSD1-mediated demethylation of H3K4 is inhibited, activation of</p> <p>TRIM24-regulated ERα …
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Discovery of Novel Ubiquitin- and Methylation-Dependent Interactions Using Protein Domain Microarrays
… suggesting PLAA's function in DNA damage repair. PHD fingers recognize the histone H3 N-terminal tail harboring either H3K4me3 or H3K4me0. Structural studies have identified common features among different H3K4me3 effector PHDs: Cleaved initiator methionine: a groove that fits the R2 residue, and …
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Molecular Functions of MLL PHD3 Binding to Its Ligands Cyp33 and H3K4Me3
… correlates with active transcription. The 3rd PHD finger of MLL binds to H3K4me3. Thus MLL is a "writer" with an embedded "reader" for H3K4Me3. Cyp33 is another known ligand of MLL PHD3. Over expression of Cyp33 results in transcriptional repression of MLL target genes.</p> <p>The aim of this …
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Functional Analysis of Drosophila Integrator Complex In Snrna 3' End Processing
… acid region and not the highly conserved central PHD finger domain, is required for snRNA 3’ end cleavage. The IntS12 microdomain (1-45) functions autonomously, and is sufficient to interact and stabilize the putative scaffold protein IntS1.</p> <p>Our findings provide more details of the …