Crystal structure of Escherichia coli PNPase: Central channel residues are involved in processive RNA degradation - Test2 - elhamkhani - TriplyDB

Crystal structure of Escherichia coli PNPase: Central channel residues are involved in processive RNA degradation

Crystal structure of Escherichia coli PNPase: Central channel residues are involved in processive RNA degradation

http://www.wikidata.org/entity/Q27652277

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Crystal structure of the S. solfataricus archaeal exosome reveals conformational flexibility in the RNA-binding ring Regulation and functions of bacterial PNPase Crystal Structure of Escherichia coli Polynucleotide Phosphorylase Core Bound to RNase E, RNA and Manganese: Implications for Catalytic Mechanism and RNA Degradosome Assembly Structural and biochemical characterization of CRN-5 and Rrp46: An exosome component participating in apoptotic DNA degradation Crystal structure of human polynucleotide phosphorylase: insights into its domain function in RNA binding and degradation Crystal structure of Caulobacter crescentus polynucleotide phosphorylase reveals a mechanism of RNA substrate channelling and RNA degradosome assembly.CryoEM structure of yeast cytoplasmic exosome complex RNase Y in Bacillus subtilis: a Natively disordered protein that is the functional equivalent of RNase E from Escherichia coli From conformational chaos to robust regulation: the structure and function of the multi-enzyme RNA degradosome Inhibition of homologous phosphorolytic ribonucleases by citrate may represent an evolutionarily conserved communicative link between RNA degradation and central metabolism.Bacterial/archaeal/organellar polyadenylation.Structural components and architectures of RNA exosomes PNPASE and RNA trafficking into mitochondria.Polynucleotide phosphorylase is implicated in homologous recombination and DNA repair in Escherichia coli.A mutation in PNPT1, encoding mitochondrial-RNA-import protein PNPase, causes hereditary hearing loss.Crystallization and preliminary X-ray diffraction studies of Xanthomonas campestris PNPase in the presence of c-di-GMP.The Protein Interaction of RNA Helicase B (RhlB) and Polynucleotide Phosphorylase (PNPase) Contributes to the Homeostatic Control of Cysteine in Escherichia coli Human mitochondrial RNA decay mediated by PNPase-hSuv3 complex takes place in distinct foci CvfA protein and polynucleotide phosphorylase act in an opposing manner to regulate Staphylococcus aureus virulence.RNase E forms a complex with polynucleotide phosphorylase in cyanobacteria via a cyanobacterial-specific nonapeptide in the noncatalytic region.Structure and Activities of the Eukaryotic RNA Exosome.The eukaryotic RNA exosome Battle against RNA oxidation: molecular mechanisms for reducing oxidized RNA to protect cells.The critical role of RNA processing and degradation in the control of gene expression.Sensing the messenger: the diverse ways that bacteria signal through c-di-GMP.Structure and function of the archaeal exosome.NanoRNAs: a class of small RNAs that can prime transcription initiation in bacteria.Characterization of components of the Staphylococcus aureus mRNA degradosome holoenzyme-like complex.S1 and KH domains of polynucleotide phosphorylase determine the efficiency of RNA binding and autoregulation.The oligomeric architecture of the archaeal exosome is important for processive and efficient RNA degradation.Distinctive effects of domain deletions on the manganese-dependent DNA polymerase and DNA phosphorylase activities of Mycobacterium smegmatis polynucleotide phosphorylase.Discrimination of RNA from DNA by polynucleotide phosphorylase.Exoribonucleases as modulators of virulence in pathogenic bacteria.Molecular determinants for CRISPR RNA maturation in the Cas10-Csm complex and roles for non-Cas nucleases.RNA degradation by the plant RNA exosome involves both phosphorolytic and hydrolytic activities.Enolase binds to RnpA in competition with PNPase in Staphylococcus aureus.Mutational analysis of Arabidopsis chloroplast polynucleotide phosphorylase reveals roles for both RNase PH core domains in polyadenylation, RNA 3'-end maturation and intron degradation.

P2860

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P2860

Crystal structure of Escherichia coli PNPase: Central channel residues are involved in processive RNA degradation

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2008 nî lūn-bûn

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2008 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

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2008年の論文

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2008年論文

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Crystal structure of Escherich ...... in processive RNA degradation

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Crystal structure of Escherich ...... in processive RNA degradation

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Crystal structure of Escherich ...... in processive RNA degradation

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Crystal structure of Escherich ...... in processive RNA degradation

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Crystal structure of Escherich ...... in processive RNA degradation

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Crystal structure of Escherich ...... in processive RNA degradation

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Crystal structure of Escherich ...... in processive RNA degradation

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Crystal structure of Escherich ...... in processive RNA degradation

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Crystal structure of Escherich ...... in processive RNA degradation

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Hanna S Yuan

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Kin-Fu Chak

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Sue Lin-Chao

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Wei-Zen Yang

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Zhonghao Shi

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P2860

The TCL1 oncoprotein binds the RNase PH domains of the PNPase exoribonuclease without affecting its RNA degrading activity

Mammalian polynucleotide phosphorylase is an intermembrane space RNase that maintains mitochondrial homeostasis

Reconstitution, activities, and structure of the eukaryotic RNA exosome

RNA channelling by the archaeal exosome

Domain analysis of the chloroplast polynucleotide phosphorylase reveals discrete functions in RNA degradation, polyadenylation, and sequence homology with exosome proteins

A duplicated fold is the structural basis for polynucleotide phosphorylase catalytic activity, processivity, and regulation

Insights into the mechanism of progressive RNA degradation by the archaeal exosome

Nucleic acid recognition by OB-fold proteins

RNA-quality control by the exosome

The archaeal exosome core is a hexameric ring structure with three catalytic subunits

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18812438

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Escherichia coli

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2578853

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