Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Combined Automated Annotation using Multiple IEA Methods
Novel complex integrating mitochondria and the microtubular cytoskeleton with chromosome remodeling and tumor suppressor RASSF1 deduced by in silico homology analysis, interaction cloning in yeast, and colocalization in cultured cells.
LRP130, a pentatricopeptide motif protein with a noncanonical RNA-binding domain, is bound in vivo to mitochondrial and nuclear RNAs.
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Majority of LRPPRC is mitochondrial, directly bound to poly(A) RNAs in vivo
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A fraction is nuclear, bound to some of same RNAs as hnRNP A1
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RNA binding maps to C-terminal domain containing only 2 of 11 PPR motifs
Comprehensive proteomic analysis of interphase and mitotic 14-3-3-binding proteins.
Putative tumor suppressor RASSF1 interactive protein and cell death inducer C19ORF5 is a DNA binding protein.
Defects in energy homeostasis in Leigh syndrome French Canadian variant through PGC-1alpha/LRP130 complex.
Large-scale identification of c-MYC-associated proteins using a combined TAP/MudPIT approach.
Large-scale mapping of human protein-protein interactions by mass spectrometry.
The layered structure of human mitochondrial DNA nucleoids.
Molecular dissection of the eukaryotic initiation factor 4E (eIF4E) export-competent RNP.
Proteomic analysis of increased Parkin expression and its interactants provides evidence for a role in modulation of mitochondrial function.
Defining the membrane proteome of NK cells.
Proteomic profiling of Myc-associated proteins.
PEX14 is required for microtubule-based peroxisome motility in human cells.
LRPPRC is necessary for polyadenylation and coordination of translation of mitochondrial mRNAs.
Insights into RNA biology from an atlas of mammalian mRNA-binding proteins.
LRPPRC/SLIRP suppresses PNPase-mediated mRNA decay and promotes polyadenylation in human mitochondria.
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LRPPRC/SLIRP suppresses 3'-5' mRNA degradation by PNPase/SUV3
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LRPPRC promotes MTPAP-mediated polyadenylation
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Copy numbers of mt-mRNAs range from 6000 to 51000 per cell
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Half-lives of mt-mRNAs range from 68-231 minutes
The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts.
Alternative translation initiation augments the human mitochondrial proteome.
Quantitative interaction proteomics of neurodegenerative disease proteins.
A human interactome in three quantitative dimensions organized by stoichiometries and abundances.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
A central chaperone-like role for 14-3-3 proteins in human cells.
SLIRP:LRPPRC binds mitochondrial RNAs
Deep research summary for LRPPRC including 2024 structural and functional studies
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Cryo-EM structure of LRPPRC-SLIRP on mitoribosome (Singh et al. 2024)
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LRPPRC contacts mS39 and mS31 for mRNA delivery
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SLIRP directly holds mRNA in corridor
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Transcript-specific translation efficiency changes upon LRPPRC loss
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LRPPRC acts as mRNA holdase maintaining proper folding (Moran et al. 2024)
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LRPPRC-SLIRP required throughout mt-mRNA life cycle (Rubalcava-Gracia et al. 2024)