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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 protein Igo1, formerly designated Mug134 (ORF SPAC10F6.16), from Schizosaccharomyces pombe strain 972. Organism-specific literature consistently identifies Igo1 as the single fission-yeast Endosulfine component of the Greatwall–Endosulfine–PP2A-B55 pathway. No conflicting use of mug134 for another protein was found. The mapping to UniProt P79058 and the InterPro/Pfam Endosulfine-domain annotations derive from the supplied UniProt record; the literature independently corroborates the organism, Igo1 identity, Endosulfine family, and pathway function (perezhidalgo2017couplingtorto pages 3-5, kawamukai2024regulationofsexual pages 8-9).
Igo1 is not an enzyme or transporter. Its primary function is that of a phosphorylation-regulated phosphatase inhibitor. When nutrients become limiting, Greatwall-family kinase activity phosphorylates Igo1—most importantly at Ser64—and activated Igo1 inhibits PP2A-B55, whose B55 regulatory subunit is Pab1. This switch couples reduced TORC1 signaling to cell-cycle remodeling, TORC2–Gad8 activation, sexual differentiation, and entry into G0 quiescence (blanco2021thegreatwallendosulfinepp2ab55pathway pages 123-125, blanco2021thegreatwallendosulfinepp2ab55pathway pages 99-102, perezhidalgo2017couplingtorto pages 3-5, kawamukai2024regulationofsexual pages 8-9).
| Annotation aspect | Best-supported conclusion | Key experimental evidence or quantitative result | Confidence and limitation |
|---|---|---|---|
| Identity | The target is Schizosaccharomyces pombe Igo1, formerly Mug134. The supplied UniProt record maps it to SPAC10F6.16 and P79058. Organism-specific literature identifies Igo1 as the fission-yeast Endosulfine in the Greatwall–Endosulfine–PP2A-B55 pathway. | Genetic studies specifically examine S. pombe igo1Δ and identify Igo1 as Endosulfine (dedo2024thegreatwallendosulfinepp2ab55pathway pages 1-2, perezhidalgo2017couplingtorto pages 3-5, kawamukai2024regulationofsexual pages 8-9). | High for organism and functional identity. The retrieved papers did not independently map every alias to P79058; the accession and SPAC10F6.16 mapping come from the supplied UniProt record. |
| Molecular class | Igo1 is a non-enzymatic, phosphorylation-regulated Endosulfine phosphoprotein rather than a catalyst or transporter. Its primary molecular role is inhibition of PP2A-B55 after activating phosphorylation. | Literature identifies Igo1 as the Endosulfine component and describes phosphorylation-dependent PP2A-B55 inhibition (blanco2021thegreatwallendosulfinepp2ab55pathway pages 123-125, perezhidalgo2017couplingtorto pages 3-5, kawamukai2024regulationofsexual pages 8-9). | High for its regulatory class and lack of a catalytic role. The Endosulphine and Endosulfine domain assignments are database annotations rather than structural determinations in the retrieved studies. |
| Activating phosphorylation and effector | Greatwall-family kinase Ppk18 phosphorylates Igo1 at Ser64. Phosphorylated Igo1 inhibits PP2A-B55, whose B55 regulatory subunit is Pab1. Cek1 contributes to the Greatwall input. | Ser64 phosphorylation and consequent PP2A-B55 inhibition are reported; igo1Δ causes inappropriately high PP2A-B55 activity under nitrogen limitation (blanco2021thegreatwallendosulfinepp2ab55pathway pages 123-125, blanco2021thegreatwallendosulfinepp2ab55pathway pages 99-102, blanco2021thegreatwallendosulfinepp2ab55pathway pages 107-110). | High for Ser64-dependent pathway function. The gathered evidence does not provide a purified Igo1–Pab1 binding constant or complex structure. |
| Additional phosphorylation | Cdk1–Cyclin B can phosphorylate Igo1 at several sites, suggesting cell-cycle modulation in addition to nutrient-responsive Ser64 phosphorylation. | In vitro kinase assays and mass spectrometry identified Cdk1-consensus phosphorylation at Ser31, Ser89 and Ser102. An S31A/S89A/S102A/S118A mutant was not phosphorylated in vitro; Ser76 and Ser115 matched PKA consensus sites in vivo (blanco2021thegreatwallendosulfinepp2ab55pathway pages 123-125). | Moderate–high. Cdk1 phosphorylation is experimentally supported, but its physiological contribution is less firmly resolved than Ppk18–Ser64 signaling. |
| TORC1-to-TORC2 and Gad8 pathway | Igo1 is a phosphatase-inhibitory relay connecting nutrient-responsive TOR signaling. Nitrogen starvation lowers TORC1 activity, activates Greatwall–Igo1, inhibits PP2A-B55/Pab1 and permits TORC2-dependent Gad8-Ser546 phosphorylation. | PP2A/Pab1 associates with Gad8 and opposes Gad8-S546 phosphorylation. igo1Δ lowers both Gad8 abundance and S546 phosphorylation (dedo2024thegreatwallendosulfinepp2ab55pathway pages 1-2, dedo2024thegreatwallendosulfinepp2ab55pathway pages 9-11). | High for pathway placement. Igo1 does not phosphorylate Gad8 directly; its effect is mediated through PP2A-B55 inhibition. |
| Codon-biased translation and tRNA modification | During nitrogen-starvation entry into quiescence, Igo1 supports Elongator and other tRNA-modification systems, sustaining translation of transcripts enriched for AAA rather than AAG lysine codons. | In igo1Δ, polysome-to-monosome ratios were 78% of wild type in nitrogen-rich medium and 27% after four hours of starvation. Translation fell to 40% for rap1 and 30% for ctu1; synonymous all-AAG alleles rescued protein production. The mutant had reduced mcm5s2U34 and a 20–25% reduction in t6A37 after quiescence induction (dedo2024thegreatwallendosulfinepp2ab55pathway pages 11-12, dedo2024thegreatwallendosulfinepp2ab55pathway pages 9-11). | High, based on codon-recoding rescue and quantitative translation and tRNA-modification measurements. These are downstream effects, not evidence that Igo1 binds tRNA or ribosomes directly. |
| G1 arrest, quiescence and differentiation | Igo1 helps convert nitrogen deprivation into G1 extension or arrest, entry into quiescence and sexual differentiation by suppressing PP2A-B55 and promoting TORC2 signaling. | igo1Δ cells fail to execute normal starvation-induced cell-size reduction and G1 arrest and show reduced sporulation (blanco2021thegreatwallendosulfinepp2ab55pathway pages 99-102, perezhidalgo2017couplingtorto pages 3-5, kawamukai2024regulationofsexual pages 8-9). | High for pathway-level physiological function. Differentiation and cell-cycle phenotypes are partly downstream of broad translational and TOR-network changes. |
| Telomere and subtelomere maintenance | Igo1 indirectly preserves telomere attachment and subtelomeric silencing during quiescence entry by maintaining production of Rap1, Lem2, Sgo2, Clr2 and Clr3. | After nitrogen starvation, igo1Δ caused telomere detachment, reduced Rap1 and Sgo2, and greater than tenfold overexpression of a group of subtelomeric genes. Repressing Pab1 restored Rap1 and telomere attachment (moreno2023thegreatwallendosulfinepp2ab55pathway pages 7-10, moreno2023thegreatwallendosulfinepp2ab55pathway pages 10-13). | High for the starvation phenotype and PP2A-B55 dependence. The effect is indirect through codon-sensitive translation rather than evidence that Igo1 is a structural telomere component. |
| Cellular localization | Igo1 acts intracellularly within nutrient-signaling and phosphatase networks, but the retrieved evidence does not support assignment to a specific organelle or compartment. | The studies report localization changes for downstream telomeric proteins and nuclear structures but no direct microscopy or fractionation result establishing Igo1 localization (dedo2024thegreatwallendosulfinepp2ab55pathway pages 11-12, dedo2024thegreatwallendosulfinepp2ab55pathway pages 1-2). | Unresolved. Igo1 should not be annotated as specifically nuclear, cytosolic, telomeric or membrane-associated without independent localization evidence. |
Table: Compact evidence-based annotation of S. pombe Igo1/Mug134, separating its primary phosphatase-inhibitory role from downstream starvation responses and identifying the unresolved localization question.
The functional literature usually uses Igo1, not Mug134. It specifically treats Igo1 as the S. pombe Endosulfine in the conserved Greatwall–Endosulfine–PP2A-B55 module. Thus, studies on budding-yeast Igo1/Igo2 or animal ENSA/ARPP19 are relevant only as evolutionary context and were not substituted for evidence about this target (perezhidalgo2017couplingtorto pages 3-5, kawamukai2024regulationofsexual pages 8-9).
The historical description “mRNA stability protein” is incomplete relative to current evidence. The best-supported primary molecular annotation is phosphorylation-dependent inhibitor of PP2A-B55/Pab1. Effects on RNA abundance, translation, and stability are downstream consequences of this phosphatase switch rather than evidence that Igo1 is an RNA-binding enzyme.
Under nitrogen-rich conditions, TORC1 activity is high, the Greatwall–Endosulfine switch is relatively inactive, and PP2A-B55/Pab1 activity remains high. Nitrogen limitation lowers TORC1 signaling, activates Greatwall-family input, and leads to phosphorylation of Igo1. Phosphorylated Igo1 then strongly suppresses PP2A-B55 activity (perezhidalgo2017couplingtorto pages 3-5, kawamukai2024regulationofsexual pages 8-9).
Ppk18 phosphorylation of Igo1 at Ser64 is the central activating event supported by the mechanistic literature. Loss of igo1 causes abnormally high PP2A-B55 activity under nitrogen-poor or nitrogen-free conditions, while genetically reducing PP2A-B55 can rescue multiple igo1Δ phenotypes. This genetic epistasis strongly supports PP2A-B55 as Igo1’s principal functional effector (blanco2021thegreatwallendosulfinepp2ab55pathway pages 123-125, blanco2021thegreatwallendosulfinepp2ab55pathway pages 99-102, blanco2021thegreatwallendosulfinepp2ab55pathway pages 107-110, moreno2023thegreatwallendosulfinepp2ab55pathway pages 10-13).
There is not yet a retrieved purified-complex structure, dissociation constant, or definitive direct Igo1–Pab1 binding measurement. Accordingly, the strongest formulation is that phosphorylated Igo1 functionally inhibits the PP2A-B55 holoenzyme; claims about a structurally defined binding interface would exceed the evidence.
Cdk1–Cyclin B phosphorylates Igo1 in vitro. Mass spectrometry detected phosphorylation at Cdk1-consensus residues Ser31, Ser89, and Ser102; Ser76 and Ser115 corresponded to PKA-consensus sites. An Igo1-4A protein carrying S31A, S89A, S102A, and S118A substitutions was not phosphorylated by Cdk1–Cyclin B in vitro and produced nutrient-dependent cell-size phenotypes. These findings suggest additional cell-cycle modulation, although their physiological importance is less established than Ppk18-dependent Ser64 phosphorylation (blanco2021thegreatwallendosulfinepp2ab55pathway pages 123-125).
The pathway can be summarized as:
Nitrogen starvation → TORC1 downregulation → Ppk18/Cek1 Greatwall activation → Igo1-Ser64 phosphorylation → PP2A-B55/Pab1 inhibition.
A 2024 review also identifies Ppk31 as part of the broader Greatwall input controlling this switch. In nutrient-rich cells the switch is off and PP2A-B55 is active; under poor nitrogen, phosphorylated Endosulfine suppresses the phosphatase (kawamukai2024regulationofsexual pages 8-9).
PP2A-B55 counteracts Cdk-dependent phosphorylation. Its inhibition therefore permits mitotic entry at lower Cdk activity after TORC1 downregulation. igo1Δ cells do not execute the normal acceleration of G2/M or starvation-associated reduction in division size, placing Igo1 between nutrient sensing and the core cell-cycle machinery (blanco2021thegreatwallendosulfinepp2ab55pathway pages 99-102, perezhidalgo2017couplingtorto pages 3-5).
Igo1 also mediates crosstalk from TORC1 to TORC2. PP2A/Pab1 associates with Gad8 and opposes phosphorylation of Gad8 at Ser546. Inhibiting PP2A-B55 through Igo1 permits accumulation of Gad8-S546 phosphorylation and greater TORC2 output. Conversely, igo1Δ lowers both Gad8 abundance and S546 phosphorylation (dedo2024thegreatwallendosulfinepp2ab55pathway pages 1-2, dedo2024thegreatwallendosulfinepp2ab55pathway pages 9-11).
This is an indirect signaling role: Igo1 does not phosphorylate Gad8. Rather, it prevents PP2A-B55 from reversing the phosphorylation state needed for TORC2–Gad8 signaling.
During nitrogen starvation, the Igo1 switch promotes extension or arrest in G1, sexual differentiation, sporulation, and entry into quiescence. Cells lacking Igo1 fail to arrest normally in G1, show impaired starvation-induced cell-size reduction, and have reduced sporulation. The pathway consequently acts as a nutrient-responsive decision module rather than merely a constitutive mitotic regulator (blanco2021thegreatwallendosulfinepp2ab55pathway pages 99-102, perezhidalgo2017couplingtorto pages 3-5).
For scale, reported wild-type cell lengths were approximately 16.74 ± 0.48 μm in nitrogen-rich medium and 14.29 ± 0.52 μm under nitrogen-poor conditions. Igo1-pathway mutants failed to reproduce the normal nutrient-dependent shortening, although exact values for every mutant were not available in the retrieved text (blanco2021thegreatwallendosulfinepp2ab55pathway pages 99-102).
The principal recent advance is the demonstration that Igo1-dependent PP2A-B55 inhibition sustains a specialized translational program during entry into quiescence. The definitive peer-reviewed paper was published in Nature Communications in December 2024, following a December 2023 preprint: del Dedo et al., “The Greatwall-Endosulfine-PP2A/B55 pathway regulates entry into quiescence by enhancing translation of Elongator-tunable transcripts,” DOI 10.1038/s41467-024-55004-4 (dedo2024thegreatwallendosulfinepp2ab55pathway pages 1-2, dedo2024thegreatwallendosulfinepp2ab55pathway pages 11-12, dedo2024thegreatwallendosulfinepp2ab55pathway pages 9-11).
The proposed chain is:
This mechanism was supported by unusually strong codon-recoding evidence. In igo1Δ cells, polysome-to-monosome ratios were 78% of wild type in nitrogen-rich medium and only 27% after four hours of starvation. Translation fell to approximately 40% for rap1 and 30% for ctu1, whereas low-AAA-bias controls such as fil1 and act1 were minimally affected. Replacing lysine codons with synonymous AAG codons in rap1 and ctu1 rescued protein production, directly implicating codon composition rather than a nonspecific collapse in transcription (dedo2024thegreatwallendosulfinepp2ab55pathway pages 9-11).
The mutant showed reduced mcm5s2U34 and a 20–25% reduction in t6A37 after quiescence induction. It was sensitive to paromomycin, consistent with impaired decoding fidelity. Partial rescue by gsk3Δ or an Elp4-S114A allele further connected TORC2/Gad8 signaling to Elongator control (dedo2024thegreatwallendosulfinepp2ab55pathway pages 11-12, dedo2024thegreatwallendosulfinepp2ab55pathway pages 9-11).
AAA-enriched Igo1-dependent transcripts include genes encoding the telomere-associated proteins Rap1 and Lem2, the subtelomeric regulator Sgo2, SHREC components Clr2 and Clr3, TOR regulators, and tRNA-modification proteins such as Trm112 and Ctu1. Their defective translation explains several apparently pleiotropic igo1Δ phenotypes (dedo2024thegreatwallendosulfinepp2ab55pathway pages 11-12, moreno2023thegreatwallendosulfinepp2ab55pathway pages 1-7).
After nitrogen withdrawal, igo1Δ cells showed reduced Rap1, Lem2, Sgo2, Clr2, and Clr3, detachment of telomeres from the nuclear envelope, and derepression of a group of subtelomeric genes by more than tenfold. Repressing Pab1 restored Rap1 abundance and telomere attachment, demonstrating that these effects arise from excessive PP2A-B55 activity rather than Igo1 being a physical telomere component (moreno2023thegreatwallendosulfinepp2ab55pathway pages 7-10, moreno2023thegreatwallendosulfinepp2ab55pathway pages 10-13).
Igo1-associated and Pab1-associated proteomic datasets also implicated chromatin-remodeling, histone-modification, translation, ribosome, aminoacylation, and tRNA-modification proteins. Some proposed chromatin mechanisms remain provisional: for example, Pab1 proteomics detected Mst2 with 52.6% sequence coverage, but reciprocal co-immunoprecipitation failed, so a direct PP2A-B55–Mst2 interaction was not established (blanco2021thegreatwallendosulfinepp2ab55pathway pages 107-110).
Igo1 loss also reduces autophagic flux, and deletion of the PP2A catalytic subunit gene ppa2 rescues this defect. This places autophagy among the PP2A-dependent starvation responses controlled by the switch, but it remains downstream of Igo1’s primary phosphatase-inhibitory function (blanco2021thegreatwallendosulfinepp2ab55pathway pages 125-126).
The available literature supports an intracellular signaling role but does not establish a specific steady-state localization for Igo1 itself. The retrieved studies report nuclear and telomeric localization changes for downstream proteins, not direct Igo1 microscopy or fractionation. It would therefore be inappropriate to annotate P79058 as specifically nuclear, cytosolic, membrane-associated, or telomeric on present evidence (dedo2024thegreatwallendosulfinepp2ab55pathway pages 11-12, dedo2024thegreatwallendosulfinepp2ab55pathway pages 1-2).
Functionally, Igo1 must act where it can regulate PP2A-B55/Pab1, but the relevant complex may be spatially dynamic. A fluorescently tagged endogenous Igo1 analyzed across nitrogen-rich growth, early starvation, G1 arrest, and quiescence would be needed for a confident compartment-level annotation.
There is no established clinical, agricultural, or deployed industrial application specific to S. pombe igo1. Its current application is as a mechanistic model for understanding how nutrient sensing is coupled to phosphatase control, cell-cycle transitions, quiescence, tRNA epitranscriptomic modification, codon-biased translation, chromatin maintenance, and aging.
The pathway is evolutionarily conserved: fungal Igo proteins correspond functionally to animal ENSA/ARPP19, while PP2A-B55, TOR, and Greatwall-family signaling are broadly conserved. This makes S. pombe Igo1 useful for dissecting general principles of phosphatase regulation. Nevertheless, observations in fission yeast should not be presented as direct evidence for human disease mechanisms without validation in mammalian systems.
High-confidence primary annotation: Igo1/Mug134 is a nutrient-responsive Endosulfine phosphoprotein that, after Greatwall-family phosphorylation at Ser64, inhibits PP2A-B55/Pab1.
High-confidence pathway functions: coupling of TORC1 downregulation to cell-cycle remodeling, TORC2–Gad8 activation, G1/quiescence entry, and sexual differentiation; maintenance of Elongator-dependent tRNA modification and AAA-biased translation during nitrogen starvation (dedo2024thegreatwallendosulfinepp2ab55pathway pages 1-2, perezhidalgo2017couplingtorto pages 3-5, dedo2024thegreatwallendosulfinepp2ab55pathway pages 9-11).
Downstream rather than primary functions: telomere attachment, subtelomeric silencing, autophagy, translational fidelity, and production of Rap1/Sgo2/Clr proteins. Igo1 is not established as a telomere protein, chromatin enzyme, or tRNA-modifying enzyme (dedo2024thegreatwallendosulfinepp2ab55pathway pages 11-12, moreno2023thegreatwallendosulfinepp2ab55pathway pages 7-10, blanco2021thegreatwallendosulfinepp2ab55pathway pages 125-126).
Important unresolved issues: Igo1’s direct subcellular localization, the structural basis and affinity of phospho-Igo1 inhibition of the S. pombe PP2A-B55 holoenzyme, the physiological integration of Cdk1/PKA phosphosites with Ser64 regulation, and whether all proposed chromatin interactors are direct.
References
(perezhidalgo2017couplingtorto pages 3-5): Livia Pérez-Hidalgo and Sergio Moreno. Coupling tor to the cell cycle by the greatwall–endosulfine–pp2a-b55 pathway. Biomolecules, 7:59, Aug 2017. URL: https://doi.org/10.3390/biom7030059, doi:10.3390/biom7030059. This article has 40 citations.
(kawamukai2024regulationofsexual pages 8-9): Makoto Kawamukai. Regulation of sexual differentiation initiation in schizosaccharomyces pombe. Bioscience, biotechnology, and biochemistry, 88:475-492, Mar 2024. URL: https://doi.org/10.1093/bbb/zbae019, doi:10.1093/bbb/zbae019. This article has 17 citations.
(blanco2021thegreatwallendosulfinepp2ab55pathway pages 123-125): Natalia García Blanco. The greatwall-endosulfine-pp2a/b55 pathway in schizosaccharomyces pombe: regulatory mechanisms and roles in cell differentiation and ageing. ArXiv, 2021. URL: https://doi.org/10.14201/gredos.149314, doi:10.14201/gredos.149314. This article has 1 citations.
(blanco2021thegreatwallendosulfinepp2ab55pathway pages 99-102): Natalia García Blanco. The greatwall-endosulfine-pp2a/b55 pathway in schizosaccharomyces pombe: regulatory mechanisms and roles in cell differentiation and ageing. ArXiv, 2021. URL: https://doi.org/10.14201/gredos.149314, doi:10.14201/gredos.149314. This article has 1 citations.
(dedo2024thegreatwallendosulfinepp2ab55pathway pages 1-2): Javier Encinar del Dedo, M. Belén Suárez, Rafael López-San Segundo, Alicia Vázquez-Bolado, Jingjing Sun, Natalia García-Blanco, Patricia García, Pauline Tricquet, Jun-Song Chen, Peter C. Dedon, Kathleen L. Gould, Elena Hidalgo, Damien Hermand, and Sergio Moreno. The greatwall-endosulfine-pp2a/b55 pathway regulates entry into quiescence by enhancing translation of elongator-tunable transcripts. Nature Communications, Dec 2024. URL: https://doi.org/10.1038/s41467-024-55004-4, doi:10.1038/s41467-024-55004-4. This article has 6 citations and is from a highest quality peer-reviewed journal.
(blanco2021thegreatwallendosulfinepp2ab55pathway pages 107-110): Natalia García Blanco. The greatwall-endosulfine-pp2a/b55 pathway in schizosaccharomyces pombe: regulatory mechanisms and roles in cell differentiation and ageing. ArXiv, 2021. URL: https://doi.org/10.14201/gredos.149314, doi:10.14201/gredos.149314. This article has 1 citations.
(dedo2024thegreatwallendosulfinepp2ab55pathway pages 9-11): Javier Encinar del Dedo, M. Belén Suárez, Rafael López-San Segundo, Alicia Vázquez-Bolado, Jingjing Sun, Natalia García-Blanco, Patricia García, Pauline Tricquet, Jun-Song Chen, Peter C. Dedon, Kathleen L. Gould, Elena Hidalgo, Damien Hermand, and Sergio Moreno. The greatwall-endosulfine-pp2a/b55 pathway regulates entry into quiescence by enhancing translation of elongator-tunable transcripts. Nature Communications, Dec 2024. URL: https://doi.org/10.1038/s41467-024-55004-4, doi:10.1038/s41467-024-55004-4. This article has 6 citations and is from a highest quality peer-reviewed journal.
(dedo2024thegreatwallendosulfinepp2ab55pathway pages 11-12): Javier Encinar del Dedo, M. Belén Suárez, Rafael López-San Segundo, Alicia Vázquez-Bolado, Jingjing Sun, Natalia García-Blanco, Patricia García, Pauline Tricquet, Jun-Song Chen, Peter C. Dedon, Kathleen L. Gould, Elena Hidalgo, Damien Hermand, and Sergio Moreno. The greatwall-endosulfine-pp2a/b55 pathway regulates entry into quiescence by enhancing translation of elongator-tunable transcripts. Nature Communications, Dec 2024. URL: https://doi.org/10.1038/s41467-024-55004-4, doi:10.1038/s41467-024-55004-4. This article has 6 citations and is from a highest quality peer-reviewed journal.
(moreno2023thegreatwallendosulfinepp2ab55pathway pages 7-10): Sergio Moreno, Javier Encinar del Dedo, Rafael López-San Segundo, Alicia Vázquez-Bolado, Jingjing Sun, Natalia García-Blanco, M. Belén Suárez, Patricia García, Pauline Tricquet, Jun-Song Chen, Peter Dedon, Kathleen Gould, Elena Hidalgo, and Damien Hermand. The greatwall-endosulfine-pp2a/b55 pathway controls entry into quiescence by promoting translation of elongator-tuneable transcripts. Research Square, Dec 2023. URL: https://doi.org/10.21203/rs.3.rs-3616701/v1, doi:10.21203/rs.3.rs-3616701/v1. This article has 0 citations.
(moreno2023thegreatwallendosulfinepp2ab55pathway pages 10-13): Sergio Moreno, Javier Encinar del Dedo, Rafael López-San Segundo, Alicia Vázquez-Bolado, Jingjing Sun, Natalia García-Blanco, M. Belén Suárez, Patricia García, Pauline Tricquet, Jun-Song Chen, Peter Dedon, Kathleen Gould, Elena Hidalgo, and Damien Hermand. The greatwall-endosulfine-pp2a/b55 pathway controls entry into quiescence by promoting translation of elongator-tuneable transcripts. Research Square, Dec 2023. URL: https://doi.org/10.21203/rs.3.rs-3616701/v1, doi:10.21203/rs.3.rs-3616701/v1. This article has 0 citations.
(moreno2023thegreatwallendosulfinepp2ab55pathway pages 1-7): Sergio Moreno, Javier Encinar del Dedo, Rafael López-San Segundo, Alicia Vázquez-Bolado, Jingjing Sun, Natalia García-Blanco, M. Belén Suárez, Patricia García, Pauline Tricquet, Jun-Song Chen, Peter Dedon, Kathleen Gould, Elena Hidalgo, and Damien Hermand. The greatwall-endosulfine-pp2a/b55 pathway controls entry into quiescence by promoting translation of elongator-tuneable transcripts. Research Square, Dec 2023. URL: https://doi.org/10.21203/rs.3.rs-3616701/v1, doi:10.21203/rs.3.rs-3616701/v1. This article has 0 citations.
(blanco2021thegreatwallendosulfinepp2ab55pathway pages 125-126): Natalia García Blanco. The greatwall-endosulfine-pp2a/b55 pathway in schizosaccharomyces pombe: regulatory mechanisms and roles in cell differentiation and ageing. ArXiv, 2021. URL: https://doi.org/10.14201/gredos.149314, doi:10.14201/gredos.149314. This article has 1 citations.