Phosphorylation of a chloroplast RNA-binding protein changes its affinity to RNA. - Wikidata - awgldk - TriplyDB

Phosphorylation of a chloroplast RNA-binding protein changes its affinity to RNA.

Phosphorylation of a chloroplast RNA-binding protein changes its affinity to RNA.

http://www.wikidata.org/entity/Q40394774

about

Protein tyrosine kinases and protein tyrosine phosphatases are involved in abscisic acid-dependent processes in Arabidopsis seeds and suspension cells.Chloroplast mRNA 3'-end processing by a high molecular weight protein complex is regulated by nuclear encoded RNA binding proteins Post-translational Modifications in Regulation of Chloroplast Function: Recent Advances.Emerging roles of protein kinase CK2 in abscisic acid signaling.Multiple checkpoints for the expression of the chloroplast-encoded splicing factor MatK.Endonucleolytic activation directs dark-induced chloroplast mRNA degradation.Chloroplast endoribonuclease p54 involved in RNA 3'-end processing is regulated by phosphorylation and redox state.The redox state regulates RNA degradation in the chloroplast of Chlamydomonas reinhardtii.Protein kinase a-dependent phosphorylation of serine 119 in the proto-oncogenic serine/arginine-rich splicing factor 1 modulates its activity as a splicing enhancer protein The Role of Polypyrimidine Tract-Binding Proteins and Other hnRNP Proteins in Plant Splicing Regulation.Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks.RNA-stabilization factors in chloroplasts of vascular plants.

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P2860

Phosphorylation of a chloroplast RNA-binding protein changes its affinity to RNA.

http://www.wikidata.org/entity/Q40394774

description

1995 nî lūn-bûn

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1995年の論文

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1995年論文

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1995年論文

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1995年論文

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1995年論文

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1995年論文

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1995年论文

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1995年论文

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1995年论文

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name

Phosphorylation of a chloroplast RNA-binding protein changes its affinity to RNA.

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type

label

Phosphorylation of a chloroplast RNA-binding protein changes its affinity to RNA.

@en

prefLabel

Phosphorylation of a chloroplast RNA-binding protein changes its affinity to RNA.

@en

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Nucleic Acids Research

P1476

Phosphorylation of a chloroplast RNA-binding protein changes its affinity to RNA.

@en

P2093

Lisitsky I

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

Schuster G

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P2860

Analysis of the RNA-recognition motif and RS and RGG domains: conservation in metazoan pre-mRNA splicing factors

hnRNP proteins and the biogenesis of mRNA

RNA recognition: towards identifying determinants of specificity

Mechanism of transcriptional activation by Sp1: evidence for coactivators

RNP-T, a ribonucleoprotein from Arabidopsis thaliana, contains two RNP-80 motifs and a novel acidic repeat arranged in an alpha-helix conformation.

Three distinct ribonucleoproteins from tobacco chloroplasts: each contains a unique amino terminal acidic domain and two ribonucleoprotein consensus motifs.

Identification and characterization of a HeLa nuclear protein that specifically binds to the trans-activation-response (TAR) element of human immunodeficiency virus.

Post-transcriptional steps in the expression of chloroplast genes.

Diversity of a ribonucleoprotein family in tobacco chloroplasts: two new chloroplast ribonucleoproteins and a phylogenetic tree of ten chloroplast RNA-binding domains.

Chloroplast mRNA 3' end processing requires a nuclear-encoded RNA-binding protein.

P304

2506-2511

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scholarly article

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10.1093/NAR/23.13.2506

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13

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23

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1995-07-01T00:00:00Z

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15567877

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7630729

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phosphorylation

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307058

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