The PPR motif - a TPR-related motif prevalent in plant organellar proteins.
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Characterization of unique small RNA populations from rice grainA new and unified nomenclature for male fertility restorer (RF) proteins in higher plantsGenome sequence of the plant pathogen Ralstonia solanacearumSequence analysis of LRPPRC and its SEC1 domain interaction partners suggests roles in cytoskeletal organization, vesicular trafficking, nucleocytosolic shuttling, and chromosome activityHuman U4/U6 snRNP recycling factor p110: mutational analysis reveals the function of the tetratricopeptide repeat domain in recyclingLRP130, a pentatricopeptide motif protein with a noncanonical RNA-binding domain, is bound in vivo to mitochondrial and nuclear RNAsDefects in energy homeostasis in Leigh syndrome French Canadian variant through PGC-1alpha/LRP130 complexMolecular dissection of the eukaryotic initiation factor 4E (eIF4E) export-competent RNPMutations in TTC19 cause mitochondrial complex III deficiency and neurological impairment in humans and fliesSmall glutamine-rich tetratricopeptide repeat-containing protein (SGT) interacts with the ubiquitin-dependent endocytosis (UbE) motif of the growth hormone receptorGenome-wide analysis of Arabidopsis pentatricopeptide repeat proteins reveals their essential role in organelle biogenesisReverse genetic screening identifies five E-class PPR proteins involved in RNA editing in mitochondria of Arabidopsis thalianaProfile-profile comparisons by COMPASS predict intricate homologies between protein familiesCharacterization of two potentially universal turn motifs that shape the repeated five-residues fold--crystal structure of a lumenal pentapeptide repeat protein from Cyanothece 51142A novel multifunctional factor involved in trans-splicing of chloroplast introns in Chlamydomonas.Mechanistic and Structural Studies of Protein-Only RNase P Compared to Ribonucleoproteins Reveal the Two Faces of the Same Enzymatic ActivityExpansion and Function of Repeat Domain Proteins During Stress and Development in PlantsGenomics for greater efficiency in pigeonpea hybrid breedingThe human mitochondrial transcriptome and the RNA-binding proteins that regulate its expressionMitochondrial RNA editing in trypanosomes: small RNAs in controlCrystal structure of ISG54 reveals a novel RNA binding structure and potential functional mechanismsMitochondrial ribonuclease P structure provides insight into the evolution of catalytic strategies for precursor-tRNA 5' processingStructure of human mitochondrial RNA polymeraseStructure of a PLS-class Pentatricopeptide Repeat Protein Provides Insights into Mechanism of RNA RecognitionStructural basis for the modular recognition of single-stranded RNA by PPR proteinsStructural basis for RNA recognition by a dimeric PPR-protein complexStructure of the hypothetical protein Ton1535 from Thermococcus onnurineus NA1 reveals unique structural properties by a left-handed helical turn in normal α-solenoid proteinAn artificial PPR scaffold for programmable RNA recognitionThe design and structural characterization of a synthetic pentatricopeptide repeat proteinThe mitochondrial message-specific mRNA protectors Cbp1 and Pet309 are associated in a high-molecular weight complex.A screen for RNA-binding proteins in yeast indicates dual functions for many enzymes.The Pet309 pentatricopeptide repeat motifs mediate efficient binding to the mitochondrial COX1 transcript in yeast.Ccm1p/Ygr150cp, a pentatricopeptide repeat protein, is essential to remove the fourth intron of both COB and COX1 pre-mRNAs in Saccharomyces cerevisiae.DMR1 (CCM1/YGR150C) of Saccharomyces cerevisiae encodes an RNA-binding protein from the pentatricopeptide repeat family required for the maintenance of the mitochondrial 15S ribosomal RNA.RNA Editing and Its Molecular Mechanism in Plant OrganellesThe Propensity of Pentatricopeptide Repeat Genes to Evolve into Restorers of Cytoplasmic Male SterilityEmerging Roles of RNA-Binding Proteins in Plant Growth, Development, and Stress ResponsesStructure of the nuclease subunit of human mitochondrial RNase PLRP130, a protein containing nine pentatricopeptide repeat motifs, interacts with a single-stranded cytosine-rich sequence of mouse hypervariable minisatellite Pc-1Analyses of RNA-Seq and sRNA-Seq data reveal a complex network of anti-viral defense in TCV-infected Arabidopsis thaliana
P2860
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P2860
The PPR motif - a TPR-related motif prevalent in plant organellar proteins.
description
2000 nî lūn-bûn
@nan
2000 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
The PPR motif - a TPR-related motif prevalent in plant organellar proteins.
@ast
The PPR motif - a TPR-related motif prevalent in plant organellar proteins.
@en
type
label
The PPR motif - a TPR-related motif prevalent in plant organellar proteins.
@ast
The PPR motif - a TPR-related motif prevalent in plant organellar proteins.
@en
prefLabel
The PPR motif - a TPR-related motif prevalent in plant organellar proteins.
@ast
The PPR motif - a TPR-related motif prevalent in plant organellar proteins.
@en
P1476
The PPR motif - a TPR-related motif prevalent in plant organellar proteins.
@en
P2093
P356
10.1016/S0968-0004(99)01520-0
P577
2000-02-01T00:00:00Z