Structure of the dimerization domain of DiGeorge Critical Region 8
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The DGCR8 RNA-binding heme domain recognizes primary microRNAs by clamping the hairpinProcessing of microRNA primary transcripts requires heme in mammalian cellsmiRNA and vascular cell movementRibonuclease III mechanisms of double-stranded RNA cleavageBiogenesis and mechanism of action of small non-coding RNAs: insights from the point of view of structural biologyExome sequencing and CRISPR/Cas genome editing identify mutations of ZAK as a cause of limb defects in humans and mice.Dimerization and Heme Binding Are Conserved in Amphibian and Starfish Homologues of the microRNA Processing Protein DGCR8Staphylococcus aureus Uses a Novel Multidomain Receptor to Break Apart Human Hemoglobin and Steal Its HemeCharacterization of the SAM domain of the PKD-related protein ANKS6 and its interaction with ANKS3Versatile communication strategies among tandem WW domain repeatsMolecular mechanisms of RNA interferenceA heterotrimer model of the complete Microprocessor complex revealed by single-molecule subunit countingDGCR8 recognizes primary transcripts of microRNAs through highly cooperative binding and formation of higher-order structures.Homodimerization of HYL1 ensures the correct selection of cleavage sites in primary miRNA.Novel mechanism of hemin capture by Hbp2, the hemoglobin-binding hemophore from Listeria monocytogenes.DiGeorge critical region 8 (DGCR8) is a double-cysteine-ligated heme proteinDeformability in the cleavage site of primary microRNA is not sensed by the double-stranded RNA binding domains in the microprocessor component DGCR8From guide to target: molecular insights into eukaryotic RNA-interference machinery.Ferric, not ferrous, heme activates RNA-binding protein DGCR8 for primary microRNA processing.Quantitative functions of Argonaute proteins in mammalian development.The PRE-Derived NMR Model of the 38.8-kDa Tri-Domain IsdH Protein from Staphylococcus aureus Suggests That It Adaptively Recognizes Human Hemoglobin.Caspases cleave and inhibit the microRNA processing protein DiGeorge Critical Region 8.Structural and functional insights into the fly microRNA biogenesis factor Loquacious.Cobalt(III) Protoporphyrin Activates the DGCR8 Protein and Can Compensate microRNA Processing Deficiency.Primary microRNA processing assay reconstituted using recombinant Drosha and DGCR8.Regulation of iron homeostasis by microRNAs.CO and NO bind to Fe(II) DiGeorge critical region 8 heme but do not restore primary microRNA processing activity.Newcomers to the WW Domain-Mediated Network of the Hippo Tumor Suppressor Pathway.Dynamic origins of differential RNA binding function in two dsRBDs from the miRNA "microprocessor" complex.Energetics underlying hemin extraction from human hemoglobin by Staphylococcus aureus.The microRNA Machinery.
P2860
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P2860
Structure of the dimerization domain of DiGeorge Critical Region 8
description
2010 nî lūn-bûn
@nan
2010 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Structure of the dimerization domain of DiGeorge Critical Region 8
@ast
Structure of the dimerization domain of DiGeorge Critical Region 8
@en
Structure of the dimerization domain of DiGeorge Critical Region 8
@nl
type
label
Structure of the dimerization domain of DiGeorge Critical Region 8
@ast
Structure of the dimerization domain of DiGeorge Critical Region 8
@en
Structure of the dimerization domain of DiGeorge Critical Region 8
@nl
prefLabel
Structure of the dimerization domain of DiGeorge Critical Region 8
@ast
Structure of the dimerization domain of DiGeorge Critical Region 8
@en
Structure of the dimerization domain of DiGeorge Critical Region 8
@nl
P2093
P2860
P356
P1433
P1476
Structure of the dimerization domain of DiGeorge Critical Region 8
@en
P2093
Daniel Hwang
Joseph A Loo
Michael Faller
Rachel Senturia
Robert T Clubb
P2860
P304
P356
10.1002/PRO.414
P577
2010-07-01T00:00:00Z