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This report concerns the Caenorhabditis elegans gene pgl-3, mapped to open reading frame C18G1.4, encoding the P-granule protein PGL-3 (UniProt accession G5EBV6, per user-provided UniProt context). Primary literature explicitly identifies C18G1.4 as pgl-3 and characterizes PGL-3 as a P-granule component closely related to PGL-1, confirming that the gene symbol and organism match the requested target. (kawasaki2004thepglfamily pages 3-4, kawasaki2004thepglfamily pages 4-7)
P granules are germline-enriched, non-membrane ribonucleoprotein (RNP) condensates (“germ granules”) that frequently reside at the nuclear periphery in C. elegans germ cells, where they contribute to post-transcriptional regulation and RNA surveillance. Modern imaging and conceptual models treat the perinuclear germ granule system (“nuage”) as a set of adjacent subcompartments (e.g., P granules, Z granules, Mutator foci, SIMR foci), supporting distinct small-RNA functions. (uebel2023caenorhabditiselegansgerm pages 1-2)
PGL-3 is part of the PGL family (PGL-1, PGL-2, PGL-3) of P-granule proteins. Kawasaki et al. (2004) describe PGL-3 as a 693-aa protein, closely related to PGL-1 (reported 62% identity, 77% similarity) and containing a C-terminal RGG box (an RNA-binding motif) with multiple RGG repeats. (kawasaki2004thepglfamily pages 3-4)
A major conceptual advance was the discovery that PGL proteins possess a base-specific, single-stranded RNase activity. Biochemical work mapped RNase activity to a structured PGL dimerization domain (DD), which forms a positively charged channel compatible with accommodating ssRNA. PGL-family RNase activity shows guanosine specificity and requires RNA (not DNA) and the 2′-OH, consistent with an ssRNA endonuclease mechanism. Although enzymatic characterization is strongest for PGL-1 DD, cleavage activity was also observed for Ce-PGL-3, supporting conserved RNase activity across PGL paralogs. (aoki2016pglgermgranule pages 4-5, aoki2016pglgermgranule pages 2-3, aoki2016pglgermgranule pages 1-2)
Proteolysis and structural work identified a dimerization domain (DD) in PGL-3 (roughly aa 205–447), and analogous PGL-1 DD crystal structures reveal a 13-helix fold forming a homodimer with a central channel (~15 Å diameter) and basic electrostatic surface, consistent with RNA binding and/or catalysis. Dimer-interface residues are highly conserved between PGL-1 and PGL-3 homologs, supporting shared biochemical capabilities. (aoki2016pglgermgranule pages 2-3)
In vitro cleavage by PGL DD is guanosine-dependent: substitution of the guanosine at the cleavage site with U/C/A prevents cleavage; DNA substitution blocks cleavage; and modification of the 2′-OH (e.g., 2′-fluoroguanosine) blocks activity, indicating reliance on RNA-specific chemistry. Cleavage patterns resemble RNase T1-like specificity (guanosine-specific endonuclease). (aoki2016pglgermgranule pages 4-5)
The PGL DD lacks a canonical RNase active-site motif, but mutational analyses in PGL-1 show that a conserved glutamine (reported Q342 in Ce-PGL-1) is essential for cleavage while not disrupting dimerization or RNA binding. Assays suggested metal independence under conditions tested (EDTA; Mg/Mn had no major effect). These findings support a model where PGL DD provides both assembly and enzymatic functions, with PGL-3 likely sharing mechanistic features given conservation and observed cleavage activity. (aoki2016pglgermgranule pages 4-5, aoki2016pglgermgranule pages 5-6)
The PGL DD RNase activity is described as modest compared with classical guanosine-specific RNases such as RNase T1; an illustrative comparison used 3 μM PGL-1 DD vs 1.2 nM RNase T1 to produce similar cleavage patterns (~2,500-fold higher enzyme concentration for PGL DD). (aoki2016pglgermgranule pages 3-4)
pgl-3 mRNA is maternally loaded and retained in germline blastomeres; zygotic expression appears in the germline later in development (larval stages). In larvae and adults, pgl-3 signal is highly concentrated in the germline, particularly in pachytene. (kawasaki2004thepglfamily pages 4-7)
PGL-3 is a constitutive P-granule component “associated with P granules throughout development.” P granules are typically perinuclear for much of germline development and associate with nuclear pores; during oogenesis they can become more cytoplasmic and later reattach during embryogenesis. (kawasaki2004thepglfamily pages 13-14, amini2009theroleof pages 23-28)
PGL-3 functions redundantly with PGL-1 to support germline development. pgl-3 single mutants show little overt germline defect in the cited work, but pgl-1; pgl-3 double mutants show markedly enhanced sterility and germline defects (proliferation/gametogenesis), supporting partial functional redundancy among PGL paralogs. (kawasaki2004thepglfamily pages 1-2, kawasaki2004thepglfamily pages 2-3)
Severe compromise of P granules (simultaneous RNAi depletion of pgl-1, pgl-3, glh-1, glh-4) caused germ cells to express neuronal and muscle markers and develop neurite-like projections, supporting a role for P-granule components (including PGL-3) in maintaining germline identity/totipotency by antagonizing somatic programs. (updike2014germgranulecomponentsprevent pages 1-3)
Recent 2023–2024 work strengthens the model that P granules (PGL-containing) sit at the interface of RNA export and small-RNA compartmentalization.
Uebel et al. (Development, accepted 2023-11-17; published 2023-12) emphasize P granules as liquid-like phase-separated condensates with controlled dissolution/condensation and provide the quantitative estimate that ~75% of nuclear pores associate with P granules, reinforcing their central role as the first perinuclear RNA-surveillance compartment. (uebel2023caenorhabditiselegansgerm pages 1-2)
Price et al. (Nature Communications; accepted 2023-09-08; published 2023-09) establish that loss of EGGD-1 disrupts perinuclear germ granule organization and leads to abnormal cytoplasmic aggregates; their work provides quantitative morphometrics for granule size/volume and links perinuclear granule disruption to altered small-RNA classes and transcriptome programs. While measurements are largely reported for tagged PGL-1, they describe the P-granule system in which PGL-3 participates and directly note prior PGL-3 dispersal upon EGGD-1/MIP-1 depletion. (price2023c.elegansgerm pages 1-2, price2023c.elegansgerm pages 2-3)
Chen et al. (Nature Communications; accepted 2024-06-26; published 2024-07) identify the E granule, positioning it nonrandomly relative to P and Z granules and demonstrating that E-granule assembly controls production of a specialized class of EGO-1-dependent 22G RNAs. This supports the broader view that the germ-granule system is modular, with P granules (containing constitutive factors like PGL proteins) embedded in a multi-compartment framework that orchestrates small-RNA biogenesis. (chen2024germgranulecompartments pages 8-9, chen2024germgranulecompartments pages 1-2)
PGL proteins (including PGL-3) are used as canonical P-granule components in experimental workflows to monitor germ granule integrity and localization, including antibody-based immunostaining and genetic perturbations that test nuage assembly pathways. For example, genome-wide RNAi screens and germ-granule depletion paradigms incorporate PGL-3 as a marker or target to assess P-granule stability/localization and associated phenotypes. (updike2009agenomewidernai pages 2-3, updike2014germgranulecomponentsprevent pages 1-3)
Biochemical dissection of PGL DD (and PGL proteins broadly) provides a tractable system for understanding how structured oligomerization domains can drive condensate assembly while also conferring enzymatic activity, making PGL-family proteins useful for mechanistic studies of biomolecular condensates. (aoki2016pglgermgranule pages 1-2)
The following table consolidates the functional annotation in a single reference.
| Category | Identity | Protein features/domains | Enzymatic activity & specificity | Reaction type/EC context | Localization | Regulators of assembly/disassembly | Genetic phenotypes | Links to small-RNA pathways/nuage organization | Quantitative data points | Key references with year | DOI URL |
|---|---|---|---|---|---|---|---|---|---|---|---|
| pgl-3 / PGL-3 summary | Gene/protein identity: Caenorhabditis elegans pgl-3 = ORF C18G1.4; protein PGL-3; UniProt G5EBV6. Identified as a PGL-family P-granule component and paralog of PGL-1; acts redundantly with PGL-1 in germline development (kawasaki2004thepglfamily pages 3-4, kawasaki2004thepglfamily pages 2-3, kawasaki2004thepglfamily pages 4-7) | 693 aa predicted protein; close to PGL-1 (62% identity, 77% similarity); contains C-terminal RGG box with 59 aa and 6 RGG repeats, consistent with RNA-binding potential. Proteolysis mapped a PGL-3 dimerization domain (DD) to roughly aa 205–447; DD-related interface residues are conserved with PGL-1 (kawasaki2004thepglfamily pages 3-4, kawasaki2004thepglfamily pages 4-7, aoki2016pglgermgranule pages 2-3) | PGL proteins are base-specific, single-stranded RNases. Direct biochemical work established guanosine-specific ssRNA endonuclease activity for PGL-1 DD; Ce-PGL-3 also showed RNA cleavage activity, indicating conserved RNase function in PGL family. Cleavage requires ssRNA, a G residue, and the 2′-OH; DNA or 2′-fluoroguanosine blocks activity. RNase-defective Q342A in PGL-1 abolishes cleavage without disrupting dimerization/RNA binding, supporting DD-centered catalysis (aoki2016pglgermgranule pages 4-5, aoki2016pglgermgranule pages 5-5, aoki2016pglgermgranule pages 5-6, aoki2016pglgermgranule pages 1-2, aoki2016pglgermgranule pages 3-4) | UniProt assigns EC 4.6.1.24 / guanyl-specific ribonuclease context; primary literature supports a guanosine-specific ssRNA endonuclease activity for the PGL family, mechanistically resembling RNase T1-like cleavage specificity but much weaker. Assays were metal-independent under tested conditions (5 mM EDTA, MgCl2, MnCl2 had no major effect) (aoki2016pglgermgranule pages 4-5, aoki2016pglgermgranule pages 5-5, aoki2016pglgermgranule pages 5-6, aoki2016pglgermgranule pages 3-4) | Constitutive component of P granules in embryos and adult germ line; enriched in germline blastomeres after maternal deposition and in larval/adult germ line, especially pachytene region. P granules are typically perinuclear during germline development, become cytoplasmic during oogenesis, and reattach in embryos. P granules contact most nuclear pores; in modern imaging, about 75% of nuclear pores associate with P granules (kawasaki2004thepglfamily pages 4-7, kawasaki2004thepglfamily pages 13-14, amini2009theroleof pages 23-28, uebel2023caenorhabditiselegansgerm pages 1-2) | PGL-3/P granule assembly depends on a broader granule network: PGL-1 and PGL-3 self-associate and nucleate granule formation; GLH-1/GLH-4 promote perinuclear localization; DEPS-1 functions upstream in assembly; MEG-3/MEG-4 promote embryonic assembly, while MEG-1/MEG-2 contribute more to disassembly; MBK-2 kinase and PPTR-1/PP2A regulate dissolution/condensation through phosphorylation pathways. P granules dissolve with heat stress and 1,6-hexanediol (updike2014germgranulecomponentsprevent pages 1-3, amini2009theroleof pages 28-32, wang2014regulationofrna pages 9-11, uebel2023caenorhabditiselegansgerm pages 1-2) | pgl-3 single mutants show little obvious germline defect, but pgl-1; pgl-3 double loss strongly enhances sterility and defects in germline proliferation/gametogenesis. Broad P-granule depletion causes sterile adults and germline-to-soma reprogramming. In quadruple RNAi against pgl-1, pgl-3, glh-1, glh-4, 40/100 F1 adults were sterile (range 27–89%), and sterile germ lines lost detectable perinuclear P-granule organization (kawasaki2004thepglfamily pages 1-2, kawasaki2004thepglfamily pages 13-14, updike2014germgranulecomponentsprevent pages 1-3) | PGL-3 is a constitutive P-compartment factor in perinuclear nuage that interfaces with RNA surveillance/small-RNA pathways. Recent work places P granules as the first compartment receiving newly exported RNA, with adjacent Z, SIMR, Mutator, and E granules handling distinct RNA silencing steps. Disrupting perinuclear germ granules alters piRNA/22G-RNA pathways and transcriptomes; P-granule components including pgl-3 were used in “P-granule RNAi” paradigms to test granule function (uebel2023caenorhabditiselegansgerm pages 1-2, uebel2023caenorhabditiselegansgerm pages 8-9, price2023c.elegansgerm pages 1-2, price2023c.elegansgerm pages 2-3, chen2024germgranulecompartments pages 1-2) | 13.9-fold reduction of pgl-3 transcript in quadruple P-granule RNAi germ lines; paired reductions for pgl-1/glh-1/glh-4 were 24.7-, 2.0-, 3.7-fold. In enzymology, PGL-1 DD cleavage used about 3 μM enzyme versus 1.2 nM RNase T1 for similar pattern (~2,500-fold higher concentration), highlighting modest catalytic power. Recent germ-granule organization work quantified 75% nuclear-pore association with P granules. In eggd-1 mutants, perinuclear PGL-1 granule mean volume dropped from 0.482 to 0.183 μm3 (2.64-fold smaller) and could form rachis aggregates up to 25 μm3; although measured on PGL-1, these values reflect the PGL-3-containing P-granule system. In 2024 E-granule work, 1504 and 1282 genes lost ≥2-fold siRNAs in egc-1(-) and elli-1(-), respectively, underscoring subcompartment specialization adjacent to P granules (aoki2016pglgermgranule pages 4-5, aoki2016pglgermgranule pages 3-4, updike2014germgranulecomponentsprevent pages 1-3, uebel2023caenorhabditiselegansgerm pages 1-2, price2023c.elegansgerm pages 1-2, price2023c.elegansgerm pages 2-3, chen2024germgranulecompartments pages 8-9) | Kawasaki et al. 2004; Updike et al. 2014; Aoki et al. 2016; Uebel et al. 2023; Price et al. 2023; Chen et al. 2024 (kawasaki2004thepglfamily pages 1-2, updike2014germgranulecomponentsprevent pages 1-3, aoki2016pglgermgranule pages 1-2, uebel2023caenorhabditiselegansgerm pages 1-2, price2023c.elegansgerm pages 1-2, chen2024germgranulecompartments pages 1-2) | https://doi.org/10.1534/genetics.103.023093 ; https://doi.org/10.1016/j.cub.2014.03.015 ; https://doi.org/10.1073/pnas.1524400113 ; https://doi.org/10.1242/dev.202284 ; https://doi.org/10.1038/s41467-023-41556-4 ; https://doi.org/10.1038/s41467-024-50027-3 |
Table: This table summarizes the identity, molecular features, enzymatic activity, localization, phenotypes, and modern germ-granule context for C. elegans PGL-3. It condenses both foundational and 2023–2024 evidence into a single citation-linked reference for report writing.
References
(kawasaki2004thepglfamily pages 3-4): Ichiro Kawasaki, Anahita Amiri, Yuan Fan, Nicole Meyer, Steve Dunkelbarger, Tomoko Motohashi, Takeshi Karashima, Olaf Bossinger, and Susan Strome. The pgl family proteins associate with germ granules and function redundantly in caenorhabditis elegans germline development sequence data from this article have been deposited with the ddbj/embl/genbank data libraries under accession nos. ab120729 and ab120730. Genetics, 167:645-661, Jun 2004. URL: https://doi.org/10.1534/genetics.103.023093, doi:10.1534/genetics.103.023093. This article has 174 citations and is from a domain leading peer-reviewed journal.
(kawasaki2004thepglfamily pages 4-7): Ichiro Kawasaki, Anahita Amiri, Yuan Fan, Nicole Meyer, Steve Dunkelbarger, Tomoko Motohashi, Takeshi Karashima, Olaf Bossinger, and Susan Strome. The pgl family proteins associate with germ granules and function redundantly in caenorhabditis elegans germline development sequence data from this article have been deposited with the ddbj/embl/genbank data libraries under accession nos. ab120729 and ab120730. Genetics, 167:645-661, Jun 2004. URL: https://doi.org/10.1534/genetics.103.023093, doi:10.1534/genetics.103.023093. This article has 174 citations and is from a domain leading peer-reviewed journal.
(uebel2023caenorhabditiselegansgerm pages 1-2): Celja J. Uebel, Sanjana Rajeev, and Carolyn M. Phillips. caenorhabditis elegans germ granules are present in distinct configurations and assemble in a hierarchical manner. Development, Dec 2023. URL: https://doi.org/10.1242/dev.202284, doi:10.1242/dev.202284. This article has 22 citations and is from a domain leading peer-reviewed journal.
(aoki2016pglgermgranule pages 4-5): Scott T. Aoki, Aaron M. Kershner, Craig A. Bingman, Marvin Wickens, and Judith Kimble. Pgl germ granule assembly protein is a base-specific, single-stranded rnase. Proceedings of the National Academy of Sciences, 113:1279-1284, Jan 2016. URL: https://doi.org/10.1073/pnas.1524400113, doi:10.1073/pnas.1524400113. This article has 35 citations and is from a highest quality peer-reviewed journal.
(aoki2016pglgermgranule pages 2-3): Scott T. Aoki, Aaron M. Kershner, Craig A. Bingman, Marvin Wickens, and Judith Kimble. Pgl germ granule assembly protein is a base-specific, single-stranded rnase. Proceedings of the National Academy of Sciences, 113:1279-1284, Jan 2016. URL: https://doi.org/10.1073/pnas.1524400113, doi:10.1073/pnas.1524400113. This article has 35 citations and is from a highest quality peer-reviewed journal.
(aoki2016pglgermgranule pages 1-2): Scott T. Aoki, Aaron M. Kershner, Craig A. Bingman, Marvin Wickens, and Judith Kimble. Pgl germ granule assembly protein is a base-specific, single-stranded rnase. Proceedings of the National Academy of Sciences, 113:1279-1284, Jan 2016. URL: https://doi.org/10.1073/pnas.1524400113, doi:10.1073/pnas.1524400113. This article has 35 citations and is from a highest quality peer-reviewed journal.
(aoki2016pglgermgranule pages 5-6): Scott T. Aoki, Aaron M. Kershner, Craig A. Bingman, Marvin Wickens, and Judith Kimble. Pgl germ granule assembly protein is a base-specific, single-stranded rnase. Proceedings of the National Academy of Sciences, 113:1279-1284, Jan 2016. URL: https://doi.org/10.1073/pnas.1524400113, doi:10.1073/pnas.1524400113. This article has 35 citations and is from a highest quality peer-reviewed journal.
(aoki2016pglgermgranule pages 3-4): Scott T. Aoki, Aaron M. Kershner, Craig A. Bingman, Marvin Wickens, and Judith Kimble. Pgl germ granule assembly protein is a base-specific, single-stranded rnase. Proceedings of the National Academy of Sciences, 113:1279-1284, Jan 2016. URL: https://doi.org/10.1073/pnas.1524400113, doi:10.1073/pnas.1524400113. This article has 35 citations and is from a highest quality peer-reviewed journal.
(kawasaki2004thepglfamily pages 13-14): Ichiro Kawasaki, Anahita Amiri, Yuan Fan, Nicole Meyer, Steve Dunkelbarger, Tomoko Motohashi, Takeshi Karashima, Olaf Bossinger, and Susan Strome. The pgl family proteins associate with germ granules and function redundantly in caenorhabditis elegans germline development sequence data from this article have been deposited with the ddbj/embl/genbank data libraries under accession nos. ab120729 and ab120730. Genetics, 167:645-661, Jun 2004. URL: https://doi.org/10.1534/genetics.103.023093, doi:10.1534/genetics.103.023093. This article has 174 citations and is from a domain leading peer-reviewed journal.
(amini2009theroleof pages 23-28): R Amini. The role of nhl-2 in regulating c. elegans p granule function. Unknown journal, 2009.
(kawasaki2004thepglfamily pages 1-2): Ichiro Kawasaki, Anahita Amiri, Yuan Fan, Nicole Meyer, Steve Dunkelbarger, Tomoko Motohashi, Takeshi Karashima, Olaf Bossinger, and Susan Strome. The pgl family proteins associate with germ granules and function redundantly in caenorhabditis elegans germline development sequence data from this article have been deposited with the ddbj/embl/genbank data libraries under accession nos. ab120729 and ab120730. Genetics, 167:645-661, Jun 2004. URL: https://doi.org/10.1534/genetics.103.023093, doi:10.1534/genetics.103.023093. This article has 174 citations and is from a domain leading peer-reviewed journal.
(kawasaki2004thepglfamily pages 2-3): Ichiro Kawasaki, Anahita Amiri, Yuan Fan, Nicole Meyer, Steve Dunkelbarger, Tomoko Motohashi, Takeshi Karashima, Olaf Bossinger, and Susan Strome. The pgl family proteins associate with germ granules and function redundantly in caenorhabditis elegans germline development sequence data from this article have been deposited with the ddbj/embl/genbank data libraries under accession nos. ab120729 and ab120730. Genetics, 167:645-661, Jun 2004. URL: https://doi.org/10.1534/genetics.103.023093, doi:10.1534/genetics.103.023093. This article has 174 citations and is from a domain leading peer-reviewed journal.
(updike2014germgranulecomponentsprevent pages 1-3): Dustin L. Updike, Andrew Kekūpa'a Knutson, Thea A. Egelhofer, Anne C. Campbell, and Susan Strome. Germ-granule components prevent somatic development in the c. elegans germline. Current Biology, 24:970-975, May 2014. URL: https://doi.org/10.1016/j.cub.2014.03.015, doi:10.1016/j.cub.2014.03.015. This article has 156 citations and is from a highest quality peer-reviewed journal.
(uebel2023caenorhabditiselegansgerm pages 8-9): Celja J. Uebel, Sanjana Rajeev, and Carolyn M. Phillips. caenorhabditis elegans germ granules are present in distinct configurations and assemble in a hierarchical manner. Development, Dec 2023. URL: https://doi.org/10.1242/dev.202284, doi:10.1242/dev.202284. This article has 22 citations and is from a domain leading peer-reviewed journal.
(price2023c.elegansgerm pages 2-3): Ian F. Price, Jillian A. Wagner, Benjamin Pastore, Hannah L. Hertz, and Wen Tang. C. elegans germ granules sculpt both germline and somatic rnaome. Nature Communications, Sep 2023. URL: https://doi.org/10.1038/s41467-023-41556-4, doi:10.1038/s41467-023-41556-4. This article has 31 citations and is from a highest quality peer-reviewed journal.
(chen2024germgranulecompartments pages 1-2): Xiangyang Chen, Ke Wang, Farees Ud Din Mufti, Demin Xu, Chengming Zhu, Xinya Huang, Chenming Zeng, Qile Jin, Xiaona Huang, Yong-hong Yan, Meng-qiu Dong, Xuezhu Feng, Yunyu Shi, Scott G. Kennedy, and Shouhong Guang. Germ granule compartments coordinate specialized small rna production. Nature Communications, Jul 2024. URL: https://doi.org/10.1038/s41467-024-50027-3, doi:10.1038/s41467-024-50027-3. This article has 29 citations and is from a highest quality peer-reviewed journal.
(price2023c.elegansgerm pages 1-2): Ian F. Price, Jillian A. Wagner, Benjamin Pastore, Hannah L. Hertz, and Wen Tang. C. elegans germ granules sculpt both germline and somatic rnaome. Nature Communications, Sep 2023. URL: https://doi.org/10.1038/s41467-023-41556-4, doi:10.1038/s41467-023-41556-4. This article has 31 citations and is from a highest quality peer-reviewed journal.
(chen2024germgranulecompartments pages 8-9): Xiangyang Chen, Ke Wang, Farees Ud Din Mufti, Demin Xu, Chengming Zhu, Xinya Huang, Chenming Zeng, Qile Jin, Xiaona Huang, Yong-hong Yan, Meng-qiu Dong, Xuezhu Feng, Yunyu Shi, Scott G. Kennedy, and Shouhong Guang. Germ granule compartments coordinate specialized small rna production. Nature Communications, Jul 2024. URL: https://doi.org/10.1038/s41467-024-50027-3, doi:10.1038/s41467-024-50027-3. This article has 29 citations and is from a highest quality peer-reviewed journal.
(updike2009agenomewidernai pages 2-3): Dustin L Updike and Susan Strome. A genomewide rnai screen for genes that affect the stability, distribution and function of p granules in caenorhabditis elegans. Genetics, 183:1397-1419, Dec 2009. URL: https://doi.org/10.1534/genetics.109.110171, doi:10.1534/genetics.109.110171. This article has 129 citations and is from a domain leading peer-reviewed journal.
(aoki2016pglgermgranule pages 5-5): Scott T. Aoki, Aaron M. Kershner, Craig A. Bingman, Marvin Wickens, and Judith Kimble. Pgl germ granule assembly protein is a base-specific, single-stranded rnase. Proceedings of the National Academy of Sciences, 113:1279-1284, Jan 2016. URL: https://doi.org/10.1073/pnas.1524400113, doi:10.1073/pnas.1524400113. This article has 35 citations and is from a highest quality peer-reviewed journal.
(amini2009theroleof pages 28-32): R Amini. The role of nhl-2 in regulating c. elegans p granule function. Unknown journal, 2009.
(wang2014regulationofrna pages 9-11): Jennifer T Wang, Jarrett Smith, Bi-Chang Chen, Helen Schmidt, Dominique Rasoloson, Alexandre Paix, Bramwell G Lambrus, Deepika Calidas, Eric Betzig, and Geraldine Seydoux. Regulation of rna granule dynamics by phosphorylation of serine-rich, intrinsically disordered proteins in c. elegans. eLife, Dec 2014. URL: https://doi.org/10.7554/elife.04591, doi:10.7554/elife.04591. This article has 438 citations and is from a domain leading peer-reviewed journal.