Affinage

POP5

Ribonuclease P/MRP protein subunit POP5 · UniProt Q969H6

Length
163 aa
Mass
18.8 kDa
Annotated
2026-04-28
36 papers in source corpus 19 papers cited in narrative 19 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

POP5 is a conserved protein subunit of both RNase P and RNase MRP ribonucleoprotein complexes that functions as a critical activator of RNA-catalyzed pre-tRNA 5'-end maturation. POP5 adopts an RRM-like α-β sandwich fold and heterodimerizes with RPP30; in solution this pair forms a (POP5·RPP30)₂ heterotetramer that, upon binding the catalytic domain of RNase P/MRP RNA, converts to 1:1 stoichiometry per holoenzyme and is solely responsible for enhancing the RNA catalyst's cleavage rate by ~60–100-fold while also promoting cleavage-site fidelity (~25-fold rescue of mis-cleavage), whereas a second protein pair (RPP21·RPP29) principally increases substrate affinity (PMID:16418270, PMID:18558617, PMID:20705647, PMID:22298511, PMID:25195671). The C-terminal helix α4 of POP5 mediates direct contacts with the RNase P RNA catalytic core, and RPP30 assists POP5 in attaining an active conformation by shielding its hydrophobic surfaces (PMID:24120499, PMID:26152732). In human cells, POP5 localizes to the nucleus and nucleolus, and its overexpression lengthens telomeres, indicating a functional role beyond canonical tRNA processing (PMID:11413139, PMID:38789417).

Mechanistic history

Synthesis pass · year-by-year structured walk · 11 steps
  1. 2001 High

    Establishing POP5 as a shared subunit of RNase P and RNase MRP resolved whether this protein participates in one or both major RNA-processing ribonucleoprotein complexes, and localized it to the nucleus/nucleolus.

    Evidence Co-immunoprecipitation with anti-hPop5 antibodies, immunofluorescence in HeLa cells, and deletion analysis of the C-terminal tail

    PMID:11413139

    Open questions at the time
    • The specific RNA contacts made by human POP5 within the holoenzyme were not mapped
    • Whether POP5 is essential for cell viability was not tested
  2. 2006 High

    Determining POP5's three-dimensional structure as an RRM-like fold homologous to the bacterial RNase P protein revealed the evolutionary link between the bacterial single-protein cofactor and the archaeal/eukaryotic multi-subunit system, and identified POP5–RPP30 as the functional pair acting on the catalytic domain.

    Evidence X-ray crystallography and NMR of archaeal POP5; NMR chemical shift perturbation mapping of the POP5–RPP30 interface; functional reconstitution

    PMID:16418270

    Open questions at the time
    • How POP5–RPP30 contacts the RNA catalytic core at nucleotide resolution was unknown
    • The stoichiometry of the POP5–RPP30 assembly was not yet resolved
  3. 2008 High

    Quantitative kinetics revealed that POP5–RPP30, not RPP21–RPP29, is the protein pair responsible for enhancing the catalytic rate of RNase P RNA (~100-fold), establishing a division of labor among the protein cofactors.

    Evidence In vitro reconstitution with pre-tRNA–RPR conjugate; single-turnover kinetics at defined ionic conditions

    PMID:18558617

    Open questions at the time
    • Whether POP5–RPP30 also controls cleavage-site selection was not examined
    • Rate enhancement mechanism (conformational change vs. chemical step stabilization) was not resolved
  4. 2010 High

    Cross-species reconstitution demonstrated that POP5–RPP30 activates not only cognate archaeal but also bacterial and organellar RNase P RNAs, establishing that POP5–RPP30 recognizes a universally conserved catalytic core, while RPP21–RPP29 contributes substrate affinity; chimeric RNA experiments confirmed POP5–RPP30 acts on the C-domain analogously to bacterial C5 protein.

    Evidence Heterologous in vitro reconstitution across three archaeal species and with bacterial/organellar RNase P RNAs; chimeric C-/S-domain RNA assembly; single-turnover kinetics

    PMID:20139629 PMID:20705647

    Open questions at the time
    • The structural basis for cross-species compatibility was not determined
    • The precise RNA nucleotides contacted by POP5 remained unidentified
  5. 2011 High

    Biophysical characterization revealed that free POP5–RPP30 assembles as a (POP5)₂·(RPP30)₂ heterotetramer, and that this pair binds the conserved catalytic domain of RNase MRP RNA in addition to RNase P RNA, unifying the mechanism across both complexes.

    Evidence NMR, ITC, light scattering, and SEC for stoichiometry; direct RNA-binding assays with RNase MRP RNA

    PMID:21878546 PMID:22162665

    Open questions at the time
    • Whether the heterotetramer rearranges to a heterodimer upon RNA binding was not yet proven
    • Functional consequences of heterotetrameric vs. heterodimeric forms for catalysis were unclear
  6. 2012 High

    POP5–RPP30 was shown to enforce cleavage-site fidelity by selectively enhancing correct cleavage ~11,000-fold over mis-cleavage ~480-fold for a non-consensus pre-tRNA, establishing that POP5–RPP30 is the primary fidelity factor in the holoenzyme; separately, POP5–RPP30 can partially rescue catalytic defects from deletion of a conserved bulged uridine in the RNA, demonstrating cooperative RNA–protein rescue.

    Evidence Single-turnover kinetics with correct vs. mis-cleavage measurements; mutagenesis of RPR bulged U; ITC and NMR for assembly assessment

    PMID:21683084 PMID:22298511

    Open questions at the time
    • Whether fidelity control operates through ground-state substrate positioning or transition-state stabilization was not distinguished
    • The contribution of POP5–RPP30 to fidelity in vivo was not tested
  7. 2013 Medium

    Mutagenesis identified the C-terminal helix α4 of POP5 as the element required for both pre-tRNA cleavage and RNA annealing/strand displacement activities, pinpointing the functional surface that contacts the RNase P RNA.

    Evidence Deletion and point mutant reconstitution assays; FRET-based RNA annealing and strand displacement assays

    PMID:24120499

    Open questions at the time
    • No high-resolution structure of the POP5 α4–RNA interface was obtained
    • Whether α4 contacts are conserved in eukaryotic POP5 was not tested
  8. 2014 High

    Native mass spectrometry resolved that POP5–RPP30 exists as a dimer-of-dimers in solution but adopts 1:1 stoichiometry per subunit when assembled on the cognate RNase P RNA, clarifying the functional stoichiometry of the holoenzyme.

    Evidence Surface-induced dissociation coupled with ion mobility mass spectrometry of Pfu RNase P

    PMID:25195671

    Open questions at the time
    • Whether the stoichiometric switch is driven by RNA binding alone or requires other subunits was not resolved
  9. 2015 High

    Crystal structures of the TkoPop5–TkoRpp30 complex confirmed structural conservation of the RRM-like fold and TIM-barrel pairing across archaea, and SPR quantified that RPP30 enables POP5 to bind SL3 RNA by shielding POP5's hydrophobic surfaces, explaining why POP5 alone has minimal RNA affinity.

    Evidence X-ray crystallography of TkoRpp30 and TkoRpp30–TkoPop5; SPR with wild-type and mutant proteins; cross-species reconstitution

    PMID:25704799 PMID:26152732

    Open questions at the time
    • No structure of POP5–RPP30 bound to full-length RNase P RNA was available
    • Dynamics of the conformational chaperoning by RPP30 were not characterized
  10. 2022 High

    Native MS and mass photometry validated a monomeric holoenzyme (1 RPR + 1 each of POP5, RPP30, RPP21, RPP29, + up to 2 L7Ae) and showed that redundant protein–protein interactions involving POP5 maintain assembly even when all canonical kink-turn–L7Ae contacts are abolished.

    Evidence Native mass spectrometry; mass photometry; kink-turn mutagenesis; activity assays with Mja RNase P

    PMID:35848927

    Open questions at the time
    • Which specific protein–protein contacts between POP5 and L7Ae compensate for kink-turn loss were not mapped
    • Whether this redundancy operates in eukaryotic RNase P was not examined
  11. 2024 Medium

    Overexpression of human POP5 in K562 cells was shown to lengthen telomeres, linking a GWAS telomere-length locus to POP5 transcriptional regulation and revealing a function beyond canonical tRNA processing.

    Evidence POP5 overexpression with telomere length measurement; CRISPR/Cas9 deletion of predicted causal genomic region with expression quantification

    PMID:38789417

    Open questions at the time
    • The molecular mechanism by which POP5 lengthens telomeres is unknown
    • Whether the telomere effect is direct or secondary to RNase MRP processing of telomerase RNA was not determined
    • Independent replication in other cell types is lacking

Open questions

Synthesis pass · forward-looking unresolved questions
  • A high-resolution structure of the eukaryotic/human RNase P holoenzyme showing POP5's contacts with H1 RNA has not been reported, the molecular mechanism connecting POP5 to telomere length regulation remains unresolved, and whether POP5's rate-enhancing and fidelity roles defined in vitro are recapitulated in vivo in human cells is untested.
  • No cryo-EM or crystal structure of the complete human RNase P holoenzyme with POP5 contacts resolved
  • Mechanism of POP5-mediated telomere lengthening is unknown
  • In vivo validation of POP5's rate and fidelity contributions in human cells is lacking

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0003723 RNA binding 3 GO:0005198 structural molecule activity 3 GO:0098772 molecular function regulator activity 3
Localization
GO:0005634 nucleus 1 GO:0005730 nucleolus 1
Pathway
R-HSA-8953854 Metabolism of RNA 4
Partners
L7AERPP1RPP21RPP29RPP30
Complex memberships
RNase MRPRNase P

Evidence

Reading pass · 19 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2001 Human POP5 (hPop5) is a protein subunit of both RNase MRP and RNase P ribonucleoprotein complexes; it is localized to the nucleus and nucleolus in HeLa cells, and the evolutionarily conserved acidic C-terminal tail is not required for complex formation or RNase P activity. Co-immunoprecipitation with polyclonal anti-hPop5 antibodies, partial purification of catalytically active RNase P, immunofluorescence localization, and deletion analysis of C-terminal tail The Journal of biological chemistry High 11413139
2006 Archaeal POP5 (Pfu Pop5) adopts an alpha-beta sandwich fold homologous to the RNA recognition motif (RRM) and to the bacterial RNase P protein subunit; it pairs with RPP30 to functionally reconstitute the catalytic domain of the RNase P RNA, and its interaction surface with RPP30 was mapped by NMR chemical shift perturbations. NMR spectroscopy and X-ray crystallography for structure determination; NMR chemical shift perturbation mapping of POP5–RPP30 interaction; functional reconstitution assay Proceedings of the National Academy of Sciences of the United States of America High 16418270
2008 The POP5–RPP30 binary complex, but not the RPP21–RPP29 complex, enhances the rate of RNase P RNA-catalyzed pre-tRNA cleavage (~100-fold increase in k_obs) while both binary complexes reduce the monovalent and divalent ionic requirements for catalysis. In vitro reconstitution of Methanocaldococcus jannaschii RNase P using a pre-tRNA–RPR conjugate; kinetic assays measuring k_obs at defined pH and temperature Nucleic acids research High 18558617
2010 The archaeal POP5–RPP30 binary complex is solely responsible for enhancing the RNase P RNA's rate of pre-tRNA cleavage (~60-fold), whereas RPP21–RPP29 contributes to increased substrate affinity (~16-fold); POP5–RPP30 can functionally reconstitute with bacterial and organellar RNase P RNAs, reflecting shared recognition of a phylogenetically conserved catalytic core. In vitro reconstitution of archaeal RNase P with recombinant RPP pairs from three archaea; single-turnover kinetics; heterologous assembly with bacterial and organellar RNase P RNAs Nucleic acids research High 20705647
2010 POP5 and RPP29 are among the RNase P protein subunits that directly bind to the H1 RNA moiety of human RNase P in vitro; Rpp21 and Rpp29 are sufficient for reconstitution of endonucleolytic activity and bind to separate regions in the catalytic domain of H1 RNA. In vitro RNA-binding assays with refolded recombinant proteins; nuclease footprinting of H1 RNA Nucleic acids research Medium 21450806
2010 Archaeal POP5 (PhoPop5) and RPP30 (PhoRpp30) function equivalently to the bacterial C5 protein in activating the catalytic C-domain of RNase P RNA, while RPP21 and RPP29 are implicated in stabilizing the specificity (S) domain; demonstrated using chimeric bacterial–archaeal RNase P RNAs. Chimeric RNA assembly combining C- and S-domains of bacterial (M1 RNA) and archaeal (PhopRNA) RNase P RNAs; pre-tRNA cleavage assays with individual and combined protein subunits Bioscience, biotechnology, and biochemistry Medium 20139629
2010 L7Ae, a ribosomal protein, is a subunit of archaeal RNase P and its addition to the POP5–RPP30/RPP21–RPP29 reconstituted complex increases k_cat/K_m by ~360-fold for pre-tRNA cleavage; this stimulation requires conserved nucleotides in a kink-turn (K-turn) in the RNase P RNA and key L7Ae amino acids for K-turn binding. Co-elution of L7Ae with partially purified RNase P activity; in vitro reconstitution of RNase P with five proteins; kinetic assays; site-directed mutagenesis of K-turn and L7Ae residues Proceedings of the National Academy of Sciences of the United States of America High 20675586
2011 Yeast/human Pop5 and Rpp1 (RPP30 homolog) form a heterodimer that binds directly to the conserved putative catalytic domain of RNase MRP RNA at a site corresponding to the protein binding site in bacterial RNase P RNA. Direct RNA-binding assays; structural and biochemical characterization of Pop5/Rpp1 heterodimer interaction with RNase MRP RNA RNA (New York, N.Y.) Medium 21878546
2011 The POP5–RPP30 binary complex forms as a heterotetramer (two copies each of POP5 and RPP30) as revealed by NMR, ITC, light scattering and size exclusion chromatography; chemical shift perturbations on RPP30 upon addition of POP5 define the binding interface. NMR backbone resonance assignment and chemical shift perturbation mapping; isothermal titration calorimetry (ITC); light scattering; size exclusion chromatography Archaea (Vancouver, B.C.) High 22162665
2012 POP5–RPP30 rescues the RNase P RNA's mis-cleavage tendency for a non-consensus pre-tRNA substrate by selectively enhancing correct cleavage (by ~11,140-fold versus ~480-fold for mis-cleavage), showing that POP5–RPP30 promotes cleavage fidelity independently of RPP21–RPP29; together the pairs rescue mis-cleavage by ~25-fold. In vitro single-turnover kinetics using Mja RNase P RNA–pre-tRNA(Gln) conjugate; reconstitution with individual or combined RPP pairs; rate measurements for correct versus mis-cleavage Nucleic acids research High 22298511
2012 POP5–RPP30 (and RPP21–RPP29) can partially compensate for an 80-fold catalytic defect caused by deletion of a universally conserved bulged uridine in archaeal RNase P RNA, demonstrating cooperative protein–RNA rescue of structural defects; similarly, RPR can compensate for an RPP29 assembly-deficient mutant. Site-directed mutagenesis of archaeal RPR (deletion of bulged U); in vitro reconstitution and self-cleavage assays; isothermal titration calorimetry and NMR to assess RPP21–RPP29(ΔN) assembly Journal of molecular biology High 21683084
2013 Extra-structural elements in the RRM fold of archaeal Pop5 (PhoPop5) — specifically C-terminal helices α4 (but not α5 alone) — are required for pre-tRNA cleavage activity and for RNA annealing/strand displacement activities; basic residues in α4 interact with PhopRNA while hydrophobic residues stabilize α4 orientation on the β-sheet. Deletion and point mutant reconstitution assays; FRET-based RNA annealing and strand displacement assays; structural analysis of PhoPop5 mutants Biochemical and biophysical research communications Medium 24120499
2014 Surface-induced dissociation coupled with ion mobility mass spectrometry revealed that Pfu RNase P holoenzyme contains RPP21·RPP29 in 1:1 stoichiometry and POP5·RPP30 as a dimer-of-dimers in solution, but a 1:1 stoichiometry for all subunits when bound to the cognate RNase P RNA. Surface-induced dissociation (SID) mass spectrometry; ion mobility mass spectrometry (IM-MS); native mass spectrometry Angewandte Chemie (International ed. in English) High 25195671
2014 L7Ae binds to two kink-turn motifs located in both the catalytic and specificity domains of Pyrococcus furiosus RNase P RNA, as mapped by site-specific hydroxyl radical-mediated footprinting using single-Cys L7Ae derivatives conjugated with EDTA-Fe; the enzyme assembly for footprinting included POP5, RPP21, RPP29, RPP30, and L7Ae. Site-specific hydroxyl radical footprinting with single-Cys L7Ae–EDTA-Fe conjugates; in vitro reconstitution of RNase P holoenzyme with all five protein cofactors (including POP5) Nucleic acids research High 25361963
2015 The PhoPop5–PhoRpp30 heterotetramer [PhoRpp30-(PhoPop5)2-PhoRpp30] binds strongly to a stem-loop SL3 oligonucleotide in PhopRNA via the C-terminal helix α4 of PhoPop5, whereas PhoPop5 alone has markedly reduced SL3 affinity; PhoRpp30 assists PhoPop5 in attaining a functionally active conformation by shielding its hydrophobic surfaces. Surface plasmon resonance (SPR) analysis of protein–RNA interactions; gel filtration chromatography; SPR with PhoPop5 point mutants Journal of biochemistry Medium 26152732
2015 Crystal structures of Thermococcus kodakarensis TkoRpp30 alone and in complex with TkoPop5 reveal that TkoPop5 folds into an RRM-like fold and TkoRpp30 into a TIM barrel, highly conserved with their Pyrococcus horikoshii counterparts; functional interchangeability was confirmed by in vitro reconstitution. X-ray crystallography of TkoRpp30 and TkoRpp30–TkoPop5 complex; in vitro reconstitution and pre-tRNA cleavage assays with heterologous protein substitutions Bioscience, biotechnology, and biochemistry High 25704799
2022 Native mass spectrometry and mass photometry of Mja RNase P validate a monomeric holoenzyme (one RPR + one copy each of POP5, RPP30, RPP21, RPP29, and up to two copies of L7Ae) in vitro; abolishing all canonical kink-turn–L7Ae interactions by mutagenesis does not impair assembly or activity due to redundant protein–protein interactions between L7Ae and other RPPs including POP5. Native mass spectrometry; mass photometry; mutagenesis of all kink-turns in the RPR; biochemical activity assays Nucleic acids research High 35848927
2024 Overexpression of human POP5 in K562 blood cells lengthens telomeres; CRISPR/Cas9 deletion of the predicted causal genomic region reduces POP5 expression, linking a GWAS locus to transcriptional regulation of POP5 and telomere length regulation. Overexpression of POP5 with telomere length measurement; CRISPR/Cas9 deletion of predicted causal genomic region; expression quantification Nature communications Medium 38789417
2026 The bacterial Escherichia coli RNase P protein (RnpA) can activate the H1 RNA C-domain variants at low Mg2+ concentration, indicating that bacterial RnpA and eukaryotic Pop5 recognize common C-domain core elements in all RNase P RNAs, suggesting functional overlap in their roles in RNA catalytic activation. In vitro reconstitution of H1 RNA variants with E. coli RnpA; Pb2+-probing; UV melting profiles; comparative activity assays Chembiochem : a European journal of chemical biology Medium 41889098

Source papers

Stage 0 corpus · 36 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2003 The enigma of ribonuclease P evolution. Trends in genetics : TIG 108 14550630
2009 Novel biomarkers for prostate cancer including noncoding transcripts. The American journal of pathology 103 19893039
2010 Ribosomal protein L7Ae is a subunit of archaeal RNase P. Proceedings of the National Academy of Sciences of the United States of America 63 20675586
2006 Inventory and analysis of the protein subunits of the ribonucleases P and MRP provides further evidence of homology between the yeast and human enzymes. Nucleic acids research 59 16998185
2019 Structure of ribosome-bound azole-modified peptide phazolicin rationalizes its species-specific mode of bacterial translation inhibition. Nature communications 49 31594941
2010 Dissecting functional cooperation among protein subunits in archaeal RNase P, a catalytic ribonucleoprotein complex. Nucleic acids research 45 20705647
2008 Studies on Methanocaldococcus jannaschii RNase P reveal insights into the roles of RNA and protein cofactors in RNase P catalysis. Nucleic acids research 43 18558617
2006 Structure of Pfu Pop5, an archaeal RNase P protein. Proceedings of the National Academy of Sciences of the United States of America 42 16418270
2001 hPop5, a protein subunit of the human RNase MRP and RNase P endoribonucleases. The Journal of biological chemistry 41 11413139
2009 Solution structure of an archaeal RNase P binary protein complex: formation of the 30-kDa complex between Pyrococcus furiosus RPP21 and RPP29 is accompanied by coupled protein folding and highlights critical features for protein-protein and protein-RNA interactions. Journal of molecular biology 34 19733182
2014 Uncovering the stoichiometry of Pyrococcus furiosus RNase P, a multi-subunit catalytic ribonucleoprotein complex, by surface-induced dissociation and ion mobility mass spectrometry. Angewandte Chemie (International ed. in English) 32 25195671
2010 Cleavage of model substrates by archaeal RNase P: role of protein cofactors in cleavage-site selection. Nucleic acids research 22 20935047
2020 Combination of Linkage Mapping, GWAS, and GP to Dissect the Genetic Basis of Common Rust Resistance in Tropical Maize Germplasm. International journal of molecular sciences 20 32899999
2012 GAMETOPHYTE DEFECTIVE 1, a putative subunit of RNases P/MRP, is essential for female gametogenesis and male competence in Arabidopsis. PloS one 19 22509260
2008 Solution structure of Pyrococcus furiosus RPP21, a component of the archaeal RNase P holoenzyme, and interactions with its RPP29 protein partner. Biochemistry 19 18922021
2010 Archaeal homologs of human RNase P protein pairs Pop5 with Rpp30 and Rpp21 with Rpp29 work on distinct functional domains of the RNA subunit. Bioscience, biotechnology, and biochemistry 18 20139629
2011 RNA binding properties of conserved protein subunits of human RNase P. Nucleic acids research 17 21450806
2012 Fidelity of tRNA 5'-maturation: a possible basis for the functional dependence of archaeal and eukaryal RNase P on multiple protein cofactors. Nucleic acids research 15 22298511
2014 The L7Ae protein binds to two kink-turns in the Pyrococcus furiosus RNase P RNA. Nucleic acids research 14 25361963
2003 Using ancestral sequences to uncover potential gene homologues. Applied bioinformatics 14 15130821
2011 Cooperative RNP assembly: complementary rescue of structural defects by protein and RNA subunits of archaeal RNase P. Journal of molecular biology 11 21683084
2012 Thermodynamics of coupled folding in the interaction of archaeal RNase P proteins RPP21 and RPP29. Biochemistry 9 22243443
2023 Dual-Uptake Mode of the Antibiotic Phazolicin Prevents Resistance Acquisition by Gram-Negative Bacteria. mBio 8 36802165
2022 Elucidation of structure-function relationships in Methanocaldococcus jannaschii RNase P, a multi-subunit catalytic ribonucleoprotein. Nucleic acids research 8 35848927
2011 Interactions of a Pop5/Rpp1 heterodimer with the catalytic domain of RNase MRP. RNA (New York, N.Y.) 8 21878546
2024 Validation of human telomere length multi-ancestry meta-analysis association signals identifies POP5 and KBTBD6 as human telomere length regulation genes. Nature communications 7 38789417
2013 Extra-structural elements in the RNA recognition motif in archaeal Pop5 play a crucial role in the activation of RNase P RNA from Pyrococcus horikoshii OT3. Biochemical and biophysical research communications 7 24120499
2011 Assembly of the complex between archaeal RNase P proteins RPP30 and Pop5. Archaea (Vancouver, B.C.) 7 22162665
2015 Conservation and population genetic diversity of Curcuma wenyujin (Zingiberaceae), a multifunctional medicinal herb. Genetics and molecular research : GMR 6 26400273
2007 Transcriptional linkage of Haloferax volcanii proteasomal genes with non-proteasomal gene neighbours including RNase P, MOSC domain and SAM-methyltransferase homologues. Microbiology (Reading, England) 6 17768244
2015 Functional implication of archaeal homologues of human RNase P protein pair Pop5 and Rpp30. Journal of biochemistry 5 26152732
2015 On archaeal homologs of the human RNase P proteins Pop5 and Rpp30 in the hyperthermophilic archaeon Thermococcus kodakarensis. Bioscience, biotechnology, and biochemistry 4 25704799
2024 miR-571 manipulating termite immune response to fungus and showing potential for green management of Copotermes formosanus (Blattodea: Isoptera). Pesticide biochemistry and physiology 3 40015866
2025 Ribonuclease P/MRP subunit RPP40 coordinates the transcription of pre-rRNA and ribosomal protein genes to promote Hepatocellular carcinoma malignancy. Gene 1 40517827
2026 Resurrecting the Activity of the RNA Subunit of Human RNase P. Chembiochem : a European journal of chemical biology 0 41889098
2014 Genetic diversity and population structure of black Dahe pig based on DNA sequences analyses of mitochondrial and nuclear genes. Mitochondrial DNA. Part A, DNA mapping, sequencing, and analysis 0 24617464