The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The requested target is the fission-yeast gene lsm6, ORF SPAC2F3.17c, encoding Lsm6 (UniProt Q9UUI1), not a similarly named protein from another organism. The supplied UniProt family and domain assignments—snRNP Sm family, SmF/Lsm6; Lsm6/sSmF; Sm/LSM domain—agree with direct structural evidence: recombinant S. pombe Lsm6 adopts the canonical Sm fold and associates with Lsm5 and Lsm7. The primary paper cloned S. pombe lsm6 by RT-PCR, verified its construct by DNA sequencing, and solved the resulting Lsm5/6/7 complex, although it did not print the SPAC2F3.17c or Q9UUI1 identifiers. Thus, the accession-to-locus link relies on the supplied UniProt record, while organism, protein name, fold, and complex membership are independently consistent with the literature. (wu2012crystalstructuresof pages 2-3, wu2012crystalstructuresof pages 7-8)
Primary functional annotation: Lsm6 is a nonenzymatic RNA-binding-complex subunit and structural adaptor. It helps form conserved toroidal Lsm rings that bind U-rich RNA and organize RNA-processing factors. It has no known catalytic reaction or transported substrate. In the nuclear Lsm2–8 ring, its conserved role is U6-snRNP maturation/remodeling and pre-mRNA splicing; in cytoplasmic Lsm1–7, it contributes to decapping-coupled 5′→3′ mRNA turnover. The direct S. pombe evidence is strongest for its Sm-fold structure, Lsm5/6/7 assembly, and oligo(U) binding; complete-ring functions and localization are principally strong orthology-based inferences rather than Q9UUI1-specific in-vivo demonstrations. (wu2012crystalstructuresof pages 1-2)
| Annotation aspect | Best-supported conclusion | Evidence type / organism | Confidence and caveat |
|---|---|---|---|
| Identity and domain | The supplied Q9UUI1 / lsm6 / SPAC2F3.17c assignment is consistent with an S. pombe Lsm6 subunit containing the canonical Sm/LSm fold. Experimentally studied S. pombe lsm6 was RT-PCR cloned, sequence-checked, and incorporated into recombinant Lsm5/6/7; its structure comprises an N-terminal α-helix over a five-stranded β-sheet. (wu2012crystalstructuresof pages 2-3, wu2012crystalstructuresof pages 7-8) | Direct, S. pombe for the named lsm6 product and fold; accession/locus mapping comes from the supplied UniProt record. | High for protein-family identity; moderate-high for exact accession linkage because the primary paper does not print Q9UUI1 or SPAC2F3.17c. |
| Lsm5/6/7 structure and stoichiometry | Lsm6 forms a conserved-interface assembly with Lsm5 and Lsm7. The 2.3 Å crystal structure (PDB 4EMK) contains one Lsm5/6/7 trimer per asymmetric unit; crystallographic twofold symmetry produces a closed heterohexamer—a dimer of trimers. AUC measured approximately 62.7 kDa, close to the calculated 62.5 kDa hexamer. (wu2012crystalstructuresof pages 3-4, wu2012crystalstructuresof pages 2-3, wu2012crystalstructuresof pages 10-11) | Direct structural and solution-biophysical evidence, S. pombe. | High for recombinant subcomplex architecture. It does not demonstrate an endogenous cellular hexamer; Lsm5/6/7 is interpreted as an assembly intermediate within complete heteroheptameric rings. |
| Subunit-interface role | Lsm5 structurally bridges Lsm6 and Lsm7. Buried areas are about 1,741 Ų for Lsm5–Lsm6, 1,777 Ų for Lsm5–Lsm7, and 1,096 Ų for the weaker Lsm6–Lsm7 interface. (wu2012crystalstructuresof pages 6-7) | Direct crystallographic evidence, S. pombe. | High for the purified subcomplex; physiological assembly dynamics were not measured in vivo. |
| U-rich RNA binding | Recombinant Lsm5/6/7 binds synthetic U15 RNA by SPR and fluorescence anisotropy, supporting recognition of oligo(U)/U-rich RNA. The reported fitted Kd is 52.5 ± 10.0, but the article’s displayed unit is questionable and should not be silently corrected. (wu2012crystalstructuresof pages 2-3, wu2012crystalstructuresof pages 8-10, wu2012crystalstructuresof pages 4-6) | Direct biochemical evidence, S. pombe at the subcomplex level. | Moderate-high for U15 binding; low-moderate for physiological substrate specificity because no sequence panel, cellular-target assay, or isolated-Lsm6 binding experiment was reported. |
| Lsm2–8 nuclear U6/splicing role | Lsm6 is inferred to occupy the conserved Lsm2–8 heteroheptamer, which binds the processed, U-rich 3′ end of U6 snRNA, protects/remodels U6, and promotes U4/U6 di-snRNP and U4/U6·U5 tri-snRNP assembly during pre-mRNA splicing. Mature U6 binds within the ring’s central cavity; budding-yeast structures show recognition of a terminal phosphate and four or five terminal uridines. (wu2012crystalstructuresof pages 1-2, montemayor2018architectureofthe pages 1-2, montemayor2018architectureofthe pages 3-4) | Conserved mechanistic inference; the direct structural mechanism is primarily from Saccharomyces cerevisiae, supported by S. pombe Lsm-fold and U-rich-RNA-binding conservation. | High as an orthologous Lsm6-family annotation; moderate for the exact S. pombe mechanism because complete endogenous Lsm2–8/U6 complexes and splicing effects were not directly tested for Q9UUI1. |
| Lsm1–7 cytoplasmic mRNA-decay role | Lsm6 is also inferred to be a shared subunit of Lsm1–7, an RNA-chaperone/adaptor ring that associates with deadenylated or U-rich mRNA 3′ ends and recruits or coordinates decapping and 5′→3′ mRNA degradation, often in processing bodies. It is not itself a nuclease or decapping enzyme. (wu2012crystalstructuresof pages 1-2, mu2025interconversionandmechanisms pages 1-2) | Conserved functional inference from eukaryotic/yeast Lsm1–7 biology; not directly demonstrated for S. pombe Q9UUI1. | Moderate-high for conserved complex membership and pathway; low-moderate for target-specific cellular details because no S. pombe Lsm6 decay kinetics, interactome, or complete-ring experiment was located. |
| Localization | The most defensible assignment is dual-compartment function: nuclear when incorporated into U6-associated Lsm2–8 and cytoplasmic, including possible P-body enrichment, when incorporated into Lsm1–7. Complex-specific subunits Lsm8 and Lsm1 help determine the respective localization and function. (wu2012crystalstructuresof pages 1-2, mu2025interconversionandmechanisms pages 12-13) | Conserved complex-based inference, not direct microscopy of Q9UUI1 in S. pombe. | Moderate. Nuclear/cytoplasmic assignments are well established for the two Lsm rings, but direct endogenous Lsm6 localization in fission yeast was not found. |
| Primary molecular function | Lsm6 is a nonenzymatic structural RNA-binding-complex subunit. Its primary role is to help build Sm-like toroidal RNA-chaperone rings whose central and loop surfaces recognize U-rich RNA and organize partner proteins for U6-snRNP biogenesis/splicing or mRNA decapping/decay. (wu2012crystalstructuresof pages 2-3, wu2012crystalstructuresof pages 1-2, mu2025interconversionandmechanisms pages 1-2) | Direct S. pombe structural evidence plus conserved eukaryotic functional inference. | High for a structural/adaptor rather than catalytic annotation; pathway allocation depends on which complete ring contains Lsm6. |
| Recent-literature status | No 2023–2024 study directly characterizing S. pombe Lsm6/Q9UUI1 was identified. A May 2025 Nucleic Acids Research study reinforces the model of constitutively assembled heteroheptameric Lsm rings, conserved subunit order, uracil-recognition motifs, and RNA-chaperone behavior, but is not S. pombe-specific. (mu2025interconversionandmechanisms pages 1-2, mu2025interconversionandmechanisms pages 12-13) | Negative target-specific literature finding plus recent general mechanistic evidence. | Moderate: absence reflects the searches performed, not proof that no relevant 2023–2024 publication exists. The 2012 S. pombe structure remains the strongest direct evidence. |
Table: This table distinguishes direct evidence for S. pombe Lsm6/Q9UUI1 from functional conclusions inferred through conserved Lsm complexes. It summarizes structural, biochemical, localization, pathway, and recent-literature evidence with quantitative details and explicit caveats.
The S. pombe Lsm5/6/7 structure was determined by SeMet single-wavelength anomalous dispersion at 2.3 Å resolution, with final R = 23.1% and Rfree = 25.4%. Lsm6 contains an N-terminal α-helix spanning residues 4–12 over a twisted, five-stranded antiparallel β-sheet formed by residues 14–21, 24–35, 38–49, 52–63, and 68–72. This is the characteristic Sm fold and directly validates the supplied Sm/LSM-domain annotation; residues 74–75 were disordered in the structure. (wu2012crystalstructuresof pages 2-3)
The deposited Lsm5/6/7 structure is PDB 4EMK. One Lsm5/6/7 trimer occupies the asymmetric unit, while crystallographic twofold symmetry generates a closed heterohexamer—a dimer of Lsm5/6/7 trimers—with an outer diameter of 57.0 Å, central opening of 10.8 Å, and thickness of 32.0 Å. Sedimentation-velocity analytical ultracentrifugation measured approximately 62.7 kDa, essentially matching the 62.5-kDa mass calculated for this recombinant heterohexamer. This does not imply that the physiological endpoint is a six-membered ring: Lsm5/6/7 is best interpreted as a stable assembly module or intermediate incorporated into complete heteroheptameric Lsm1–7 and Lsm2–8 rings. (wu2012crystalstructuresof pages 3-4, wu2012crystalstructuresof pages 6-7)
Lsm6 participates in the standard Sm-family interface, where β4 of one subunit pairs with β5 of its neighbor to extend an antiparallel β-sheet. In the S. pombe subcomplex, Lsm5 bridges Lsm6 and Lsm7. The buried surface areas are approximately 1,741 Ų at Lsm5–Lsm6, 1,777 Ų at Lsm5–Lsm7, and only 1,096 Ų at Lsm6–Lsm7. The smaller Lsm6–Lsm7 interface lacks an ionic interaction and contains only one hydrophobic cluster, supporting a model in which Lsm5 stabilizes this segment during ring assembly. (wu2012crystalstructuresof pages 6-7)
Accordingly, Lsm6 is not an enzyme. Its broader structural role is to supply one segment of a toroidal RNA-binding platform, maintain the correct order and geometry of neighboring subunits, and help present conserved RNA-contacting surfaces. Recent general work describes the conserved ring order as Lsm2–Lsm3–Lsm6–Lsm5–Lsm7–Lsm4–Lsm8, with Lsm1 replacing Lsm8 in the cytoplasmic ring. It further characterizes Lsm rings as dynamic RNA chaperones rather than permanently fixed RNA scaffolds. That 2025 result is mechanistically informative but not direct evidence for Q9UUI1 in fission yeast. (mu2025interconversionandmechanisms pages 1-2)
Recombinant S. pombe Lsm5/6/7 bound synthetic U15 RNA in both surface-plasmon-resonance and fluorescence-anisotropy assays. This directly supports affinity for oligo(U)/U-rich single-stranded RNA. The reported fitted dissociation constant was 52.5 ± 10.0, but the displayed unit in the retrieved article text is questionable; it should not be silently interpreted or converted. Furthermore, only U15 binding was demonstrated: the experiment did not test a broad sequence panel, isolated Lsm6, endogenous RNA targets, or complete Lsm rings. The appropriate annotation is therefore “contributes to U-rich-RNA binding,” not “Lsm6 alone specifically binds U6 snRNA.” (wu2012crystalstructuresof pages 8-10, wu2012crystalstructuresof pages 4-6, wu2012crystalstructuresof pages 10-11)
The conserved nuclear Lsm2–8 ring comprises Lsm2 through Lsm8 and includes Lsm6. It binds and stabilizes the U-rich 3′ end of U6 snRNA, participates in U6 remodeling, and supports formation of the U4/U6 di-snRNP and U4/U6·U5 tri-snRNP required for spliceosome assembly. This provides the most important pathway annotation for nuclear Lsm6: U6-snRNP biogenesis and spliceosomal pre-mRNA processing. These functions are well established for eukaryotic Lsm2–8 and fit the S. pombe structure and oligo(U)-binding data, but the retrieved S. pombe study did not purify endogenous Lsm2–8–U6 or measure splicing after an lsm6 perturbation. (wu2012crystalstructuresof pages 1-2)
A high-resolution Saccharomyces cerevisiae U6-snRNP structure explains the likely conserved mechanism. The processed U6 3′ end binds inside the central Lsm2–8 cavity without threading completely through the ring. The ring accommodates natural U6 ends bearing four or five terminal uridines and preferentially recognizes the terminal phosphate installed during U6 maturation. The terminal nucleotide occupies a pocket formed by Lsm2, Lsm3, and Lsm8; thus substrate discrimination is an emergent property of the complete ring rather than an autonomous activity of Lsm6. Mutating Lsm2 K20 was lethal and strongly reduced U6 affinity, while reversal of Lsm3 R21 charge caused temperature-sensitive growth, demonstrating the biological importance of ring-mediated U6-end recognition in budding yeast. These details should be transferred to S. pombe only as conserved mechanistic inference. (montemayor2018architectureofthe pages 1-2, montemayor2018architectureofthe pages 3-4)
The same budding-yeast structure places Lsm2–8 next to the Prp24 RNA-chaperone surface. Disrupting the Prp24–Lsm2 interface reduced Lsm2–8 affinity for U6/Prp24 and U4/U6 annealing by roughly twofold, supporting a model in which the Lsm ring does more than protect U6: it spatially organizes the RNA-remodeling machinery that prepares U6 for spliceosome assembly. (montemayor2018architectureofthe pages 5-6)
Lsm6 is also a shared component of Lsm1–7, in which Lsm1 replaces nuclear-ring-specific Lsm8. This cytoplasmic ring associates preferentially with deadenylated and/or U-rich mRNA 3′ ends and functions as an RNA chaperone/adaptor promoting decapping and subsequent 5′→3′ exonucleolytic degradation. Lsm6 itself is neither a decapping enzyme nor an exonuclease; its role is structural and organizational, helping the ring bind RNA and engage factors such as Pat1 and the decapping apparatus. Lsm1–7 is also associated with processing bodies, where translationally repressed mRNAs and decay factors accumulate. (wu2012crystalstructuresof pages 1-2, mu2025interconversionandmechanisms pages 1-2)
This pathway assignment is conserved and biologically persuasive, but its evidence level for Q9UUI1 is lower than that of the structural annotation. No S. pombe Lsm6-specific mRNA half-life measurements, decapping kinetics, transcriptome-wide targets, endogenous Lsm1–7 purification, or P-body imaging were located. It should therefore be recorded as orthology-supported participation in mRNA turnover, not as a directly measured fission-yeast phenotype.
The most defensible localization annotation is complex-dependent dual localization:
Lsm8 and Lsm1 are the complex-specific subunits that help confer nuclear versus cytoplasmic identity, respectively. However, this is a conserved complex-based assignment; the retrieved evidence did not include endogenous Q9UUI1 fluorescence microscopy, fractionation, or compartment-specific immunoprecipitation in S. pombe. The localization should consequently be assigned moderate rather than direct experimental confidence. (wu2012crystalstructuresof pages 1-2, mu2025interconversionandmechanisms pages 12-13)
A targeted search did not identify a 2023–2024 study directly characterizing S. pombe Lsm6/Q9UUI1. The 2012 S. pombe crystal/biochemical study remains the strongest target-specific source. This literature scarcity is important: recent papers about human LSM6 or Lsm6 homologues in other organisms should not be treated as direct evidence for SPAC2F3.17c.
The most recent mechanistic source retrieved was published in May 2025, outside the requested priority window. It reinforces three current concepts: Lsm complexes are preassembled heteroheptameric Sm-fold rings; their conserved aromatic and asparagine-containing pockets recognize uracil-rich RNA; and the rings behave as reversible RNA chaperones whose subunit interfaces determine assembly and functional specialization. It places Lsm6 in the conserved third position of the Lsm2–8 architecture and identifies Lsm6/5/7 as one assembly subcomplex. These conclusions sharpen the structural interpretation of the 2012 S. pombe data but remain general rather than Q9UUI1-specific. Published May 2025, DOI/URL: https://doi.org/10.1093/nar/gkaf451. (mu2025interconversionandmechanisms pages 1-2, mu2025interconversionandmechanisms pages 12-13)
The principal target-specific source is Wu et al., “Crystal Structures of Lsm3, Lsm4 and Lsm5/6/7 from Schizosaccharomyces pombe,” published May 2012, PLoS ONE 7:e36768, DOI/URL: https://doi.org/10.1371/journal.pone.0036768. (wu2012crystalstructuresof pages 3-4, wu2012crystalstructuresof pages 2-3)
The key comparative mechanistic source is Montemayor et al., “Architecture of the U6 snRNP reveals specific recognition of 3′-end processed U6 snRNA,” published May 2018, Nature Communications 9, DOI/URL: https://doi.org/10.1038/s41467-018-04145-4. It concerns budding yeast and therefore supports conserved interpretation, not direct fission-yeast annotation. (montemayor2018architectureofthe pages 1-2, montemayor2018architectureofthe pages 3-4)
Lsm6 has no established standalone industrial, diagnostic, or therapeutic application in S. pombe. Its practical value is chiefly as a research-system component:
Recommended concise annotation: “Lsm6 is a conserved Sm-fold, noncatalytic subunit shared by the Lsm2–8 and Lsm1–7 RNA-binding rings. In S. pombe, it directly forms an Lsm5/6/7 assembly module and contributes to oligo(U) binding. By strongly conserved eukaryotic mechanisms, nuclear Lsm2–8 binds the processed U-rich 3′ end of U6 snRNA and promotes U4/U6 and tri-snRNP assembly during pre-mRNA splicing, whereas cytoplasmic Lsm1–7 coordinates deadenylated-mRNA decapping and 5′→3′ decay.” (wu2012crystalstructuresof pages 2-3, wu2012crystalstructuresof pages 1-2)
Confidence is high for identity as an Sm/LSm6-family structural subunit, the Sm fold, Lsm5/6/7 assembly, and U15 binding; moderate-to-high for membership and function in conserved Lsm2–8 and Lsm1–7 pathways; and moderate or lower for precise endogenous localization, physiological RNA targets, and quantitative pathway effects in S. pombe, because target-specific in-vivo experiments were not located.
References
(wu2012crystalstructuresof pages 2-3): Donghui Wu, Shimin Jiang, Matthew W. Bowler, and Haiwei Song. Crystal structures of lsm3, lsm4 and lsm5/6/7 from schizosaccharomyces pombe. PLoS ONE, 7:e36768, May 2012. URL: https://doi.org/10.1371/journal.pone.0036768, doi:10.1371/journal.pone.0036768. This article has 18 citations and is from a peer-reviewed journal.
(wu2012crystalstructuresof pages 7-8): Donghui Wu, Shimin Jiang, Matthew W. Bowler, and Haiwei Song. Crystal structures of lsm3, lsm4 and lsm5/6/7 from schizosaccharomyces pombe. PLoS ONE, 7:e36768, May 2012. URL: https://doi.org/10.1371/journal.pone.0036768, doi:10.1371/journal.pone.0036768. This article has 18 citations and is from a peer-reviewed journal.
(wu2012crystalstructuresof pages 1-2): Donghui Wu, Shimin Jiang, Matthew W. Bowler, and Haiwei Song. Crystal structures of lsm3, lsm4 and lsm5/6/7 from schizosaccharomyces pombe. PLoS ONE, 7:e36768, May 2012. URL: https://doi.org/10.1371/journal.pone.0036768, doi:10.1371/journal.pone.0036768. This article has 18 citations and is from a peer-reviewed journal.
(wu2012crystalstructuresof pages 3-4): Donghui Wu, Shimin Jiang, Matthew W. Bowler, and Haiwei Song. Crystal structures of lsm3, lsm4 and lsm5/6/7 from schizosaccharomyces pombe. PLoS ONE, 7:e36768, May 2012. URL: https://doi.org/10.1371/journal.pone.0036768, doi:10.1371/journal.pone.0036768. This article has 18 citations and is from a peer-reviewed journal.
(wu2012crystalstructuresof pages 10-11): Donghui Wu, Shimin Jiang, Matthew W. Bowler, and Haiwei Song. Crystal structures of lsm3, lsm4 and lsm5/6/7 from schizosaccharomyces pombe. PLoS ONE, 7:e36768, May 2012. URL: https://doi.org/10.1371/journal.pone.0036768, doi:10.1371/journal.pone.0036768. This article has 18 citations and is from a peer-reviewed journal.
(wu2012crystalstructuresof pages 6-7): Donghui Wu, Shimin Jiang, Matthew W. Bowler, and Haiwei Song. Crystal structures of lsm3, lsm4 and lsm5/6/7 from schizosaccharomyces pombe. PLoS ONE, 7:e36768, May 2012. URL: https://doi.org/10.1371/journal.pone.0036768, doi:10.1371/journal.pone.0036768. This article has 18 citations and is from a peer-reviewed journal.
(wu2012crystalstructuresof pages 8-10): Donghui Wu, Shimin Jiang, Matthew W. Bowler, and Haiwei Song. Crystal structures of lsm3, lsm4 and lsm5/6/7 from schizosaccharomyces pombe. PLoS ONE, 7:e36768, May 2012. URL: https://doi.org/10.1371/journal.pone.0036768, doi:10.1371/journal.pone.0036768. This article has 18 citations and is from a peer-reviewed journal.
(wu2012crystalstructuresof pages 4-6): Donghui Wu, Shimin Jiang, Matthew W. Bowler, and Haiwei Song. Crystal structures of lsm3, lsm4 and lsm5/6/7 from schizosaccharomyces pombe. PLoS ONE, 7:e36768, May 2012. URL: https://doi.org/10.1371/journal.pone.0036768, doi:10.1371/journal.pone.0036768. This article has 18 citations and is from a peer-reviewed journal.
(montemayor2018architectureofthe pages 1-2): Eric J. Montemayor, Allison L. Didychuk, Allyson D. Yake, Gurnimrat K. Sidhu, David A. Brow, and Samuel E. Butcher. Architecture of the u6 snrnp reveals specific recognition of 3′-end processed u6 snrna. Nature Communications, May 2018. URL: https://doi.org/10.1038/s41467-018-04145-4, doi:10.1038/s41467-018-04145-4. This article has 30 citations and is from a highest quality peer-reviewed journal.
(montemayor2018architectureofthe pages 3-4): Eric J. Montemayor, Allison L. Didychuk, Allyson D. Yake, Gurnimrat K. Sidhu, David A. Brow, and Samuel E. Butcher. Architecture of the u6 snrnp reveals specific recognition of 3′-end processed u6 snrna. Nature Communications, May 2018. URL: https://doi.org/10.1038/s41467-018-04145-4, doi:10.1038/s41467-018-04145-4. This article has 30 citations and is from a highest quality peer-reviewed journal.
(mu2025interconversionandmechanisms pages 1-2): Li Mu, Yan Hou, Yan Hu, Yingzhi Wang, Congcong Shen, Yongbo Luo, Dan Su, and Rundong Zhang. Interconversion and mechanisms between lsm-type and sm-type heteroheptameric rings: implications for spliceosome evolution and rna metabolism. Nucleic Acids Research, May 2025. URL: https://doi.org/10.1093/nar/gkaf451, doi:10.1093/nar/gkaf451. This article has 2 citations and is from a highest quality peer-reviewed journal.
(mu2025interconversionandmechanisms pages 12-13): Li Mu, Yan Hou, Yan Hu, Yingzhi Wang, Congcong Shen, Yongbo Luo, Dan Su, and Rundong Zhang. Interconversion and mechanisms between lsm-type and sm-type heteroheptameric rings: implications for spliceosome evolution and rna metabolism. Nucleic Acids Research, May 2025. URL: https://doi.org/10.1093/nar/gkaf451, doi:10.1093/nar/gkaf451. This article has 2 citations and is from a highest quality peer-reviewed journal.
(montemayor2018architectureofthe pages 5-6): Eric J. Montemayor, Allison L. Didychuk, Allyson D. Yake, Gurnimrat K. Sidhu, David A. Brow, and Samuel E. Butcher. Architecture of the u6 snrnp reveals specific recognition of 3′-end processed u6 snrna. Nature Communications, May 2018. URL: https://doi.org/10.1038/s41467-018-04145-4, doi:10.1038/s41467-018-04145-4. This article has 30 citations and is from a highest quality peer-reviewed journal.