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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 supplied identity is gene-level correct: D. melanogaster CG6866 is loquacious (loqs), historically also called R3D1, and encodes a double-stranded-RNA-binding protein associated with Dicer complexes. Its primary function is not enzymatic catalysis. Loqs is a noncatalytic substrate-binding/regulatory cofactor that helps Dicer recognize and process structured double-stranded RNA. Alternative isoforms specialize this function: Loqs-PB primarily assists Dicer-1 (Dcr-1) in precursor-miRNA processing, whereas Loqs-PD primarily assists Dicer-2 (Dcr-2) in producing selected endogenous siRNAs. The RNase III cleavage reactions themselves are catalyzed by Dcr-1 or Dcr-2, not Loqs. (forstemann2005normalmicrornamaturation pages 1-2, miyoshi2010molecularmechanismsthat pages 1-2, jiang2009biochemicalanalysisof pages 119-125)
A critical qualification is that the retrieved primary literature uses the names Loqs-PA, -PB, -PC and -PD, or R3D1-L/S. It did not establish a definitive sequence-level mapping between those historical products and the UniProt designation “isoform F” (X2J5X6). Accordingly, the gene-level annotation is secure, but PB- or PD-specific functions should not automatically be assigned to X2J5X6 without reconciling its sequence against current FlyBase transcript models.
The symbol is not being confused with a different organism or protein. Foundational work explicitly identified D. melanogaster CG6866 as loqs and characterized its product as a dsRNA-binding protein related to R2D2. The reported architecture comprised two recognizable dsRNA-binding domains and a third, C-terminal truncated or divergent dsRNA-binding region. This is concordant with the supplied UniProt/InterPro/Pfam annotations dsRBD_dom (IPR014720) and dsrm (PF00035). (forstemann2005normalmicrornamaturation pages 1-2, jiang2009biochemicalanalysisof pages 107-113)
Alternative splicing is functionally consequential. Early studies distinguished PA and PB; later work additionally resolved PC and the Dcr-2-associated PD product. One historical model described PB as a 465-aa protein and PA as a 419-aa protein lacking a 46-aa segment between the final dsRNA-binding regions. Loqs-PD has a different C terminus and primarily retains the first two dsRNA-binding motifs; a short PD-specific tail contributes to Dcr-2 association. (jiang2009biochemicalanalysisof pages 107-113, haac2015thehubprotein pages 4-6, haac2015thehubprotein pages 6-7)
| Topic | Best-supported annotation | Isoform | Evidence type / strength | Key limitation |
|---|---|---|---|---|
| Identity and domains | D. melanogaster CG6866 is loquacious (loqs; R3D1), encoding a double-stranded-RNA-binding protein with two canonical dsRNA-binding domains and a variant/truncated C-terminal dsRNA-binding region. This agrees with the supplied PF00035/IPR014720 annotations for X2J5X6. (forstemann2005normalmicrornamaturation pages 1-2, jiang2009biochemicalanalysisof pages 107-113) | Gene-level; architecture varies among splice products | Strong: direct genetic identification plus sequence/domain analysis | Retrieved literature does not independently curate accession X2J5X6 or every current transcript model. |
| miRNA processing | Loqs-PB binds Dicer-1 and promotes accurate cytoplasmic pre-miRNA cleavage, principally by improving substrate recognition/affinity. Loss of Loqs causes accumulation of ~60-nt pre-miRNAs, although mature-miRNA effects vary by substrate. (forstemann2005normalmicrornamaturation pages 6-8, liu2007dicer1butnot pages 1-2, jiang2009biochemicalanalysisof pages 119-125) | Loqs-PB; PA binds Dicer-1 but is generally less effective | Strong: RNase-resistant co-immunoprecipitation, biochemical processing assays, recombinant reconstitution, knockdown and mutant phenotypes | Loqs is not absolutely required for every miRNA, and measured effects depend on precursor and allele strength. |
| Endogenous-siRNA processing | Loqs-PD binds Dicer-2 and enhances excision of endogenous siRNAs, especially from long, imperfect stem-loop precursors; Dicer-2–Loqs-PD favors longer stems than Dicer-1–Loqs-PB. (miyoshi2010molecularmechanismsthat pages 1-2, miyoshi2010molecularmechanismsthat pages 2-3) | Loqs-PD | Strong: isoform-specific interaction mapping, mutant small-RNA defects and in-vitro substrate processing | Most mechanistic experiments used S2 cells or defined substrates; effects need not extend to every endogenous dsRNA. |
| R2D2 and viral-siRNA distinction | Loqs-PD primarily facilitates Dicer-2 processing of selected endogenous/suboptimal dsRNAs, whereas R2D2 is more closely associated with Dicer-2 stability and transfer/loading of siRNA duplexes into AGO2. Current synthesis indicates Loqs-PD is not generally required for viral-siRNA production. (miyoshi2010molecularmechanismsthat pages 1-2, haac2015thehubprotein pages 9-11, ortola2024rnainterferencein pages 2-4) | Loqs-PD versus R2D2 | Moderate–strong: Drosophila biochemical/genetic evidence, supported by a 2024 insect-RNAi review | The division is not absolute in every experimental system, and antiviral requirements can be virus- or context-dependent. |
| Catalytic status | Loqs is a non-enzymatic RNA-binding Dicer cofactor, not the RNase: catalytic dsRNA/pre-miRNA cleavage is performed by Dicer-1 or Dicer-2. Loqs increases Dicer substrate binding and processing efficiency. (miyoshi2010molecularmechanismsthat pages 1-2, jiang2009biochemicalanalysisof pages 119-125) | PB with Dicer-1; PD with Dicer-2 | Strong: purified-protein binding and cleavage assays plus established domain composition | No independent catalytic active site has been demonstrated for Loqs. |
| Cellular localization | The best-supported site of action is the cytoplasm, where exported pre-miRNAs encounter Dicer-1–Loqs and endogenous dsRNA precursors encounter Dicer-2–Loqs-PD. (miyoshi2010molecularmechanismsthat pages 1-2) | PB and PD | Moderate: pathway topology and cytoplasmic substrate-processing complexes | Direct, isoform-resolved localization data in D. melanogaster were not recovered; mosquito localization must not be substituted. |
| Organismal phenotypes | loqs loss impairs miRNA production, female fertility and ovarian germ-line stem-cell maintenance; it can also compromise inverted-repeat and Stellate silencing. PB rescues miRNA/developmental defects more effectively than PA in tested settings. (forstemann2005normalmicrornamaturation pages 10-11, forstemann2005normalmicrornamaturation pages 12-13, liu2007dicer1butnot pages 1-2) | Predominantly PB for miRNA-linked phenotypes; gene-level alleles may affect several isoforms | Strong: mutant genetics, reporter assays, RNA measurements and ovarian cytology | Broad phenotypes are downstream consequences of small-RNA defects and do not by themselves identify a single direct substrate. |
| UniProt “isoform F” mapping | X2J5X6 is supplied as Loquacious isoform F, but the retrieved primary literature chiefly uses PA, PB, PC and PD or R3D1-L/S nomenclature; a definitive one-to-one mapping was not established. | Isoform F / mapping unresolved | Uncertain: database nomenclature is consistent at the gene level but not reconciled at the transcript/protein level | PB- or PD-specific functions should not be assigned automatically to X2J5X6 without sequence-level transcript mapping. |
Table: Compact assessment of the experimentally supported functions of Drosophila loqs/CG6866, with isoform-specific roles and evidence strength. It highlights the unresolved relationship between UniProt isoform F and historical Loqs isoform nomenclature.
In the canonical fly miRNA pathway, nuclear Drosha–Pasha cleavage releases a hairpin pre-miRNA, which is exported to the cytoplasm. There, Dcr-1 cleaves it into a small-RNA duplex, generally destined for AGO1. Loqs-PB is the principal Dcr-1 cofactor in this step. Loqs and Dcr-1 reciprocally co-immunoprecipitate; their association resists RNase A, supporting direct or RNA-independent protein association. Immunopurified complexes accurately process pre-miRNA, and both PA and PB can associate with Dcr-1, although PB is the stronger functional isoform. (forstemann2005normalmicrornamaturation pages 6-8, miyoshi2010molecularmechanismsthat pages 1-2)
Recombinant-protein studies provide a mechanistic interpretation: Loqs-PB forms a stable complex with Dcr-1, increases pre-miRNA processing dose-dependently, and increases Dcr-1 affinity for pre-miRNA in binding assays conducted without Mg²⁺ to suppress cleavage. Thus Loqs-PB principally improves substrate capture, positioning and cleavage efficiency, rather than contributing an independent nuclease reaction. PA can exert a similar but weaker effect. (jiang2009biochemicalanalysisof pages 119-125)
Loqs is important but not uniformly indispensable for every miRNA. Knockout flies accumulate approximately 60-nt pre-miRNAs, while some mature miRNAs decline and others remain near wild-type abundance. A study examined 33 of the 78 miRNAs then known, although only about half produced clean, detectable Northern-blot signals. These results support precursor-dependent reliance on Loqs rather than an absolute requirement for all miRNA species. Dcr-1, unlike Loqs, remains critical for assembly/loading of miRNA-induced silencing complexes; Loqs therefore acts mainly during precursor processing, not as the essential miRISC-loading factor. (liu2007dicer1butnot pages 1-2)
Loqs depletion or Dcr-1 depletion reduced pre-miRNA-processing activity to approximately 50% of control, while combined depletion reduced it to approximately one-third in the reported S2-cell assays. Precursor accumulation can occur without a commensurate reduction in mature RNA, likely reflecting residual Dcr-1, incomplete depletion, precursor-specific kinetics or partial-loss-of-function alleles. (jiang2009biochemicalanalysisof pages 119-125)
Loqs-PD is functionally distinct. In Drosophila S2 cells, endogenous Loqs-PA and -PB associated selectively with Dcr-1, whereas Loqs-PD associated with Dcr-2 but not Dcr-1; Loqs-PC showed little or no detectable interaction with either enzyme. Dcr-2 binding mapped to approximately Loqs-PD residues Gly206–Ile359, encompassing its second dsRNA-binding domain and flanking sequence, with the specialized C-terminal region helping produce a binding-competent interface. (miyoshi2010molecularmechanismsthat pages 2-3)
The Dcr-2–Loqs-PD complex processes long or imperfect endogenous dsRNA hairpins into endogenous siRNAs (esiRNAs), usually for AGO2. Loqs mutants particularly lose esiRNAs derived from long, mismatched, non-transposon stem-loop precursors. Biochemical substrate comparisons indicate that Dcr-2–Loqs-PD favors longer-stem substrates, while Dcr-1–Loqs-PB favors compact pre-miRNA-like hairpins with stems of roughly 22 nt. Precursor architecture therefore helps route structured RNA between the miRNA and endogenous-siRNA pathways. (miyoshi2010molecularmechanismsthat pages 1-2, miyoshi2010molecularmechanismsthat pages 2-3)
Loqs-PD enhances Dcr-2 excision from selected endogenous or otherwise suboptimal dsRNA substrates. The current synthesis is not that Loqs-PD is universally required for every Dcr-2 reaction: a 2024 review concludes that it is important for certain esiRNAs but generally not required for viral-siRNA production, and may relax Dcr-2 dependence on favorable dsRNA termini. Typical insect siRNA products are approximately 20–22 nt. (ortola2024rnainterferenceina pages 2-4, ortola2024rnainterferencein pages 2-4)
Loqs-PD and R2D2 should not be treated as interchangeable. Loqs-PD primarily promotes Dcr-2 substrate processing in the endogenous-siRNA branch. R2D2 stabilizes Dcr-2 in vivo and participates prominently in recognition or transfer of siRNA duplexes into AGO2-containing RISC; in vitro, R2D2 did not itself enhance Dcr-2 exo-siRNA cleavage in the cited experiments. Viral/exogenous siRNA loading is consequently more closely associated with R2D2 than with an obligatory Loqs-PD requirement. (miyoshi2010molecularmechanismsthat pages 1-2, liu2007dicer1butnot pages 1-2, haac2015thehubprotein pages 9-11)
Earlier literature entertained sequential and partly independent models for Loqs-PD and R2D2. The best-supported working model is a division of labor—Loqs-PD biases processing of selected endogenous/suboptimal precursors, while R2D2 has stronger roles in Dcr-2 stability and productive AGO2 loading—but this boundary may vary with substrate and experimental system. (haac2015thehubprotein pages 1-2, ortola2024rnainterferencein pages 2-4)
Loqs is neither an enzyme nor a transporter. No catalytic active site or Loqs-mediated chemical reaction has been demonstrated. Its dsRNA-binding motifs recognize duplex/structured RNA, while its isoform-specific protein surfaces recruit or tune the corresponding Dicer. The catalytic reactions are endonucleolytic cleavage by Dcr-1 or Dcr-2:
These assignments derive from RNase-resistant co-immunoprecipitation, recombinant reconstitution, RNA-binding assays, defined-substrate cleavage, isoform-specific interaction mapping, RNA depletion, mutant genetics and small-RNA measurements. (forstemann2005normalmicrornamaturation pages 6-8, miyoshi2010molecularmechanismsthat pages 2-3, miyoshi2010molecularmechanismsthat pages 1-2, jiang2009biochemicalanalysisof pages 119-125)
The most defensible functional site is the cytoplasm. Dcr-1–Loqs acts after nuclear Drosha/Pasha processing and export of pre-miRNAs; Dcr-2–Loqs-PD also processes cytoplasmic endogenous dsRNA precursors before AGO2 loading. Thus Loqs is best annotated as an intracellular, cytoplasmic RNA-silencing cofactor rather than a secreted, membrane or organellar protein. (miyoshi2010molecularmechanismsthat pages 1-2)
However, the retrieved evidence did not include decisive, isoform-resolved imaging or fractionation for D. melanogaster. Cytoplasmic localization is therefore strongly supported by pathway topology and complex function but less directly established than the biochemical interactions. Mosquito Loqs proteins have been detected mainly in cytoplasmic fractions, but those data are comparative and must not be substituted for direct Drosophila localization evidence. (haac2015thehubprotein pages 4-6)
Loss or reduction of loqs disrupts miRNA maturation, inverted-repeat-triggered silencing and silencing of the endogenous Stellate locus. The viable loqs f00791 allele caused female sterility, few egg chambers and defective ovarian germ-line stem-cell maintenance; dramatic Stellate derepression occurred despite only an approximately threefold reduction in loqs mRNA. These phenotypes demonstrate biological importance but are downstream, pleiotropic consequences of disturbed small-RNA regulation rather than evidence that Loqs directly controls only those loci. (forstemann2005normalmicrornamaturation pages 10-11, forstemann2005normalmicrornamaturation pages 12-13)
Isoform-rescue data reinforce specialization. Loqs-PB, but not PA, rescued the principal developmental/miRNA defects in one study; later comparative summaries report that PA can restore viability whereas PB is needed to restore fertility. Differences likely reflect allele, construct, expression level and endpoint, but collectively identify PB as the dominant miRNA-processing isoform. (liu2007dicer1butnot pages 1-2, haac2015thehubprotein pages 7-9)
Direct mechanistic annotation of Drosophila Loqs was established chiefly by primary studies from 2005–2012. The retrieved 2023–2024 literature did not materially reassign the function of D. melanogaster loqs. Instead, a February 2024 review consolidates the current view that Loqs-PD expands Dcr-2 processing of selected endogenous/suboptimal dsRNAs but is not generally necessary for viral-siRNA production. Ortolá and Daròs, Biology 13:137, published February 2024, DOI: https://doi.org/10.3390/biology13030137. (ortola2024rnainterferencein pages 2-4)
The practical application is primarily pathway-level rather than use of Loqs itself as a deployed product. Insect RNAi is exploited for experimental knockdown and is being developed for sequence-specific crop protection using plant-produced or externally applied dsRNA. Loqs and related dsRNA-binding cofactors are relevant because their substrate-selection and Dicer-assistance functions can influence RNAi efficiency, precursor design and differences among insect species. Nevertheless, no evidence retrieved here supports a current commercial implementation that directly engineers Drosophila Loqs. (ortola2024rnainterferenceina pages 2-4, ortola2024rnainterferencein pages 2-4)
Comparative studies require particular caution. Aedes mosquitoes do not appear to encode the same conserved Loqs-PD arrangement; their Loqs isoforms divide pathway functions differently. A 2015 mosquito study, for example, found that Loqs-PB depletion reduced 39 of 82 measured miRNAs (48%) and that R2D2 depletion increased 31 of 82 (38%), but these are Aedes, not Drosophila, statistics. They illustrate evolutionary plasticity and must not be used as quantitative annotation of X2J5X6. (haac2015thehubprotein pages 7-9)
Molecular function: Double-stranded-RNA-binding, noncatalytic Dicer cofactor; promotes binding and accurate processing of structured RNA substrates.
Biological processes: miRNA biogenesis through Dcr-1, especially via Loqs-PB; endogenous-siRNA biogenesis through Dcr-2, especially via Loqs-PD; secondary effects on AGO1/AGO2-mediated post-transcriptional silencing, germ-line maintenance and repeat control.
Principal partners: Dcr-1 for PA/PB, with PB functionally dominant; Dcr-2 for PD; pathway-level association with R2D2 and AGO proteins, although Loqs is not the principal obligatory miRISC-loading factor.
Substrates: Structured dsRNA rather than a small-molecule substrate—pre-miRNA hairpins for Dcr-1–Loqs-PB and selected long/imperfect endogenous dsRNA precursors for Dcr-2–Loqs-PD.
Localization: Cytoplasmic site of action, supported principally by pathway topology; direct isoform-resolved localization in Drosophila remains incompletely documented in the retrieved evidence.
Confidence: High for gene identity and Dicer-cofactor function; high for PB-versus-PD pathway specialization; moderate for precise cellular localization; unresolved for mapping UniProt X2J5X6 “isoform F” onto historical PA/PB/PD nomenclature.
References
(forstemann2005normalmicrornamaturation pages 1-2): Klaus Förstemann, Yukihide Tomari, Tingting Du, Vasily V Vagin, Ahmet M Denli, Diana P Bratu, Carla Klattenhoff, William E Theurkauf, and Phillip D Zamore. Normal microrna maturation and germ-line stem cell maintenance requires loquacious, a double-stranded rna-binding domain protein. PLoS Biology, 3:e236, May 2005. URL: https://doi.org/10.1371/journal.pbio.0030236, doi:10.1371/journal.pbio.0030236. This article has 704 citations and is from a highest quality peer-reviewed journal.
(miyoshi2010molecularmechanismsthat pages 1-2): Keita Miyoshi, Tomohiro Miyoshi, Julia Verena Hartig, Haruhiko Siomi, and Mikiko C. Siomi. Molecular mechanisms that funnel rna precursors into endogenous small-interfering rna and microrna biogenesis pathways in drosophila. RNA, 16 3:506-15, Mar 2010. URL: https://doi.org/10.1261/rna.1952110, doi:10.1261/rna.1952110. This article has 129 citations and is from a domain leading peer-reviewed journal.
(jiang2009biochemicalanalysisof pages 119-125): F Jiang. Biochemical analysis of the drosophila rnai pathway. Unknown journal, 2009.
(jiang2009biochemicalanalysisof pages 107-113): F Jiang. Biochemical analysis of the drosophila rnai pathway. Unknown journal, 2009.
(haac2015thehubprotein pages 4-6): Mary Etna Haac, Michelle A.E. Anderson, Heather Eggleston, Kevin M. Myles, and Zach N. Adelman. The hub protein loquacious connects the microrna and short interfering rna pathways in mosquitoes. Nucleic Acids Research, 43:3688-3700, Mar 2015. URL: https://doi.org/10.1093/nar/gkv152, doi:10.1093/nar/gkv152. This article has 47 citations and is from a highest quality peer-reviewed journal.
(haac2015thehubprotein pages 6-7): Mary Etna Haac, Michelle A.E. Anderson, Heather Eggleston, Kevin M. Myles, and Zach N. Adelman. The hub protein loquacious connects the microrna and short interfering rna pathways in mosquitoes. Nucleic Acids Research, 43:3688-3700, Mar 2015. URL: https://doi.org/10.1093/nar/gkv152, doi:10.1093/nar/gkv152. This article has 47 citations and is from a highest quality peer-reviewed journal.
(forstemann2005normalmicrornamaturation pages 6-8): Klaus Förstemann, Yukihide Tomari, Tingting Du, Vasily V Vagin, Ahmet M Denli, Diana P Bratu, Carla Klattenhoff, William E Theurkauf, and Phillip D Zamore. Normal microrna maturation and germ-line stem cell maintenance requires loquacious, a double-stranded rna-binding domain protein. PLoS Biology, 3:e236, May 2005. URL: https://doi.org/10.1371/journal.pbio.0030236, doi:10.1371/journal.pbio.0030236. This article has 704 citations and is from a highest quality peer-reviewed journal.
(liu2007dicer1butnot pages 1-2): Xiang Liu, Joseph K. Park, Feng Jiang, Ying Liu, Dennis McKearin, and Qinghua Liu. Dicer-1, but not loquacious, is critical for assembly of mirna-induced silencing complexes. RNA, 13 12:2324-9, Dec 2007. URL: https://doi.org/10.1261/rna.723707, doi:10.1261/rna.723707. This article has 100 citations and is from a domain leading peer-reviewed journal.
(miyoshi2010molecularmechanismsthat pages 2-3): Keita Miyoshi, Tomohiro Miyoshi, Julia Verena Hartig, Haruhiko Siomi, and Mikiko C. Siomi. Molecular mechanisms that funnel rna precursors into endogenous small-interfering rna and microrna biogenesis pathways in drosophila. RNA, 16 3:506-15, Mar 2010. URL: https://doi.org/10.1261/rna.1952110, doi:10.1261/rna.1952110. This article has 129 citations and is from a domain leading peer-reviewed journal.
(haac2015thehubprotein pages 9-11): Mary Etna Haac, Michelle A.E. Anderson, Heather Eggleston, Kevin M. Myles, and Zach N. Adelman. The hub protein loquacious connects the microrna and short interfering rna pathways in mosquitoes. Nucleic Acids Research, 43:3688-3700, Mar 2015. URL: https://doi.org/10.1093/nar/gkv152, doi:10.1093/nar/gkv152. This article has 47 citations and is from a highest quality peer-reviewed journal.
(ortola2024rnainterferencein pages 2-4): Beltrán Ortolá and José-Antonio Daròs. Rna interference in insects: from a natural mechanism of gene expression regulation to a biotechnological crop protection promise. Biology, 13:137, Feb 2024. URL: https://doi.org/10.3390/biology13030137, doi:10.3390/biology13030137. This article has 54 citations.
(forstemann2005normalmicrornamaturation pages 10-11): Klaus Förstemann, Yukihide Tomari, Tingting Du, Vasily V Vagin, Ahmet M Denli, Diana P Bratu, Carla Klattenhoff, William E Theurkauf, and Phillip D Zamore. Normal microrna maturation and germ-line stem cell maintenance requires loquacious, a double-stranded rna-binding domain protein. PLoS Biology, 3:e236, May 2005. URL: https://doi.org/10.1371/journal.pbio.0030236, doi:10.1371/journal.pbio.0030236. This article has 704 citations and is from a highest quality peer-reviewed journal.
(forstemann2005normalmicrornamaturation pages 12-13): Klaus Förstemann, Yukihide Tomari, Tingting Du, Vasily V Vagin, Ahmet M Denli, Diana P Bratu, Carla Klattenhoff, William E Theurkauf, and Phillip D Zamore. Normal microrna maturation and germ-line stem cell maintenance requires loquacious, a double-stranded rna-binding domain protein. PLoS Biology, 3:e236, May 2005. URL: https://doi.org/10.1371/journal.pbio.0030236, doi:10.1371/journal.pbio.0030236. This article has 704 citations and is from a highest quality peer-reviewed journal.
(ortola2024rnainterferenceina pages 2-4): B Ortolá and JA Daròs. Rna interference in insects: from a natural mechanism of gene expression regulation to a biotechnological crop protection promise. biology (basel). 2024; 13: 3 …. Unknown journal, 2024.
(haac2015thehubprotein pages 1-2): Mary Etna Haac, Michelle A.E. Anderson, Heather Eggleston, Kevin M. Myles, and Zach N. Adelman. The hub protein loquacious connects the microrna and short interfering rna pathways in mosquitoes. Nucleic Acids Research, 43:3688-3700, Mar 2015. URL: https://doi.org/10.1093/nar/gkv152, doi:10.1093/nar/gkv152. This article has 47 citations and is from a highest quality peer-reviewed journal.
(haac2015thehubprotein pages 7-9): Mary Etna Haac, Michelle A.E. Anderson, Heather Eggleston, Kevin M. Myles, and Zach N. Adelman. The hub protein loquacious connects the microrna and short interfering rna pathways in mosquitoes. Nucleic Acids Research, 43:3688-3700, Mar 2015. URL: https://doi.org/10.1093/nar/gkv152, doi:10.1093/nar/gkv152. This article has 47 citations and is from a highest quality peer-reviewed journal.