NMD: a multifaceted response to premature translational termination. - Test2 - elhamkhani - TriplyDB

NMD: a multifaceted response to premature translational termination.

NMD: a multifaceted response to premature translational termination.

http://www.wikidata.org/entity/Q37675497

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DHX34 and NBAS form part of an autoregulatory NMD circuit that regulates endogenous RNA targets in human cells, zebrafish and Caenorhabditis elegans Current status and new features of the Consensus Coding Sequence database A SWI/SNF-related autism syndrome caused by de novo mutations in ADNP Ribosome-based quality control of mRNA and nascent peptides Mechanism and regulation of the nonsense-mediated decay pathway The combined human sperm proteome: cellular pathways and implications for basic and clinical science Neuronal RNA-binding proteins in health and disease The dharma of nonsense-mediated mRNA decay in mammalian cells Retroviral strategy to stabilize viral RNA The RNA helicase DHX34 functions as a scaffold for SMG1-mediated UPF1 phosphorylation.Deficient and Null Variants of SERPINA1 Are Proteotoxic in a Caenorhabditis elegans Model of α1-Antitrypsin Deficiency Phospho-dependent and phospho-independent interactions of the helicase UPF1 with the NMD factors SMG5–SMG7 and SMG6 Structural basis of mRNA-cap recognition by Dcp1-Dcp2 Cdc48-associated complex bound to 60S particles is required for the clearance of aberrant translation products.SPO24 is a transcriptionally dynamic, small ORF-encoding locus required for efficient sporulation in Saccharomyces cerevisiae.Yeast Edc3 targets RPS28B mRNA for decapping by binding to a 3' untranslated region decay-inducing regulatory element.Saccharomyces cerevisiae Ski7 Is a GTP-Binding Protein Adopting the Characteristic Conformation of Active Translational GTPases.A novel protein, Pho92, has a conserved YTH domain and regulates phosphate metabolism by decreasing the mRNA stability of PHO4 in Saccharomyces cerevisiae.Yeast Upf1 CH domain interacts with Rps26 of the 40S ribosomal subunit.HTLV-1 Rex Tunes the Cellular Environment Favorable for Viral Replication Principles of Virus Uncoating: Cues and the Snooker Ball Cytoplasmic mRNA turnover and ageing Nonsense-Mediated mRNA Decay: Degradation of Defective Transcripts Is Only Part of the Story Integrative analysis of RNA, translation, and protein levels reveals distinct regulatory variation across humans Organizing principles of mammalian nonsense-mediated mRNA decay Mutations in SMG9, Encoding an Essential Component of Nonsense-Mediated Decay Machinery, Cause a Multiple Congenital Anomaly Syndrome in Humans and Mice Chemical-Induced Read-Through at Premature Termination Codons Determined by a Rapid Dual-Fluorescence System Based on S. cerevisiae Homozygous missense and nonsense mutations in BMPR1B cause acromesomelic chondrodysplasia-type Grebe The RNA helicase MOV10L1 binds piRNA precursors to initiate piRNA processing The RNA helicase Ddx5/p68 binds to hUpf3 and enhances NMD of Ddx17/p72 and Smg5 mRNA Plakophilins 1 and 3 bind to FXR1 and thereby influence the mRNA stability of desmosomal proteins Mutant Cohesin in Premature Ovarian Failure Impaired Dendritic Development and Memory in Sorbs2 Knock-Out Mice.The exon junction complex in neural development and neurodevelopmental disease.eMERGE Phenome-Wide Association Study (PheWAS) identifies clinical associations and pleiotropy for stop-gain variants Novel membrane frizzled-related protein gene mutation as cause of posterior microphthalmia resulting in high hyperopia with macular folds Human Upf1 is a highly processive RNA helicase and translocase with RNP remodelling activities Mutation in MEOX1 gene causes a recessive Klippel-Feil syndrome subtype.Transcriptome analysis of the filamentous fungus Aspergillus nidulans directed to the global identification of promoters The CCAAT box-binding transcription factor NF-YA1 controls rhizobial infection.

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NMD: a multifaceted response to premature translational termination.

http://www.wikidata.org/entity/Q37675497

description

article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 17 October 2012

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

NMD: a multifaceted response to premature translational termination.

@en

NMD: a multifaceted response to premature translational termination.

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type

label

NMD: a multifaceted response to premature translational termination.

@en

NMD: a multifaceted response to premature translational termination.

@nl

prefLabel

NMD: a multifaceted response to premature translational termination.

@en

NMD: a multifaceted response to premature translational termination.

@nl

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Nature Reviews Molecular Cell Biology

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NMD: a multifaceted response to premature translational termination.

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Allan Jacobson

http://www.w3.org/2001/XMLSchema#string

Stephanie Kervestin

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P2860

Characterization of the biochemical properties of the human Upf1 gene product that is involved in nonsense-mediated mRNA decay.

Cloning of a novel phosphatidylinositol kinase-related kinase: characterization of the human SMG-1 RNA surveillance protein

Role of the nonsense-mediated decay factor hUpf3 in the splicing-dependent exon-exon junction complex

Communication of the position of exon-exon junctions to the mRNA surveillance machinery by the protein RNPS1

Characterization of human Smg5/7a: a protein with similarities to Caenorhabditis elegans SMG5 and SMG7 that functions in the dephosphorylation of Upf1.

SMG7 is a 14-3-3-like adaptor in the nonsense-mediated mRNA decay pathway

Molecular mechanisms for the RNA-dependent ATPase activity of Upf1 and its regulation by Upf2

The crystal structure of the exon junction complex reveals how it maintains a stable grip on mRNA

Phosphorylation of hUPF1 induces formation of mRNA surveillance complexes containing hSMG-5 and hSMG-7

SMG6 interacts with the exon junction complex via two conserved EJC-binding motifs (EBMs) required for nonsense-mediated mRNA decay

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700-712

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scholarly article

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10.1038/NRM3454

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11

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13

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2012-10-17T00:00:00Z

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1002187607

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23072888

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3970730

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