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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.
Identity check. The specified UniProt record identifies cup (also fs(2)cup, CG11181) as the D. melanogaster protein Cup, alternatively described as an Oskar ribonucleoprotein-complex subunit. This agrees with experimental literature identifying Drosophila Cup as an eIF4E-binding, 4E-T/EIF4E-T-family translational regulator; the research below concerns that fly protein, not another gene named “cup.” The accession, synonyms and InterPro/Pfam identifiers are those supplied in the question; the functional identification is independently supported by fly protein–interaction, genetic and structural studies. (nakamura2004drosophilacupis pages 1-2, kinkelin2012crystalstructureof pages 1-2, meyer2024exploringthedynamics pages 3-4)
Primary annotation: Cup is a cytoplasmic messenger-ribonucleoprotein (mRNP) adaptor and translational repressor, not a known enzyme or membrane transporter. It helps keep selected maternal mRNAs untranslated—and, in some settings, intact—until protein synthesis is appropriate. RNA-associated proteins confer much of its target specificity: Bruno 1 (Bru1) links Cup to oskar (osk) mRNA, whereas Smaug links it to nanos (nos) mRNA. Cup binds the cap-binding initiation factor eIF4E and antagonizes recruitment of eIF4G, a step required for efficient cap-dependent initiation. It also participates in assemblies that regulate poly(A)-tail shortening and mRNA storage. Thus, its relevant “substrates” are regulated mRNPs, rather than molecules chemically converted by Cup itself. (nakamura2004drosophilacupis pages 1-2, nelson2009translationalregulationina pages 47-51, igreja2011cuppromotesdeadenylation pages 1-2, igreja2011cuppromotesdeadenylation pages 6-7)
The following matrix distinguishes molecular interactions from genetic phenotypes and from mechanisms that remain inferential.
| Biological context | Molecular interaction or action | Evidence and qualification |
|---|---|---|
| Bruno–oskar during early oogenesis | Bruno binds response elements in the oskar 3′ UTR and recruits Cup. Cup directly binds eIF4E and opposes eIF4G recruitment. | The cup212 mutant disrupts Cup–eIF4E binding and causes premature Oskar production. Nevertheless, oskar RNA still reaches the posterior pole from late stage 8, although its particles and residual cytoplasmic distribution are abnormal. Cup–Bruno association was RNA-independent in ovarian extracts, while direct Cup–eIF4E binding was demonstrated biochemically. (nakamura2004drosophilacupis pages 3-4, nakamura2004drosophilacupis pages 4-5, nakamura2004drosophilacupis pages 5-7) |
| Smaug–nanos in the early embryo | Smaug binds recognition elements in the nanos 3′ UTR and recruits a repressive complex containing Cup, eIF4E, Me31B, Trailer hitch and Belle. Cup connects 3′-UTR regulation to cap-dependent initiation control. | The 2004 work established Cup association with Smaug and Cup-dependent repression, but extract-based association alone does not prove direct binary binding. A 2017 biochemical study recovered the SRE-dependent complex and found stoichiometric Cup association with SRE-containing RNA; Me31B–Trailer hitch coating was proposed as an additional repression mechanism. (nelson2009translationalregulationina pages 47-51, nelson2009translationalregulationin pages 51-55, gotze2017translationalrepressionof pages 1-2) |
| General effector function and storage of repressed mRNAs | Cup’s middle and glutamine-rich C-terminal regions form an effector domain that represses translation, promotes deadenylation and associates with decapping factors and CAF1–CCR4–NOT. Its N-terminal region protects associated deadenylated RNAs from decapping and complete degradation. | S2-cell tethering and oskar-UTR reporters showed that repression and deadenylation can persist when canonical eIF4E binding is impaired. RNase-resistant co-immunoprecipitation demonstrated physical association with CCR4–NOT components, but a 2024 direct-pair ReLo assay detected no Cup interaction with individual NOT core subunits. Direct Cup–CCR4–NOT binding therefore remains unproven and may require bridging factors. (igreja2011cuppromotesdeadenylation pages 1-2, igreja2011cuppromotesdeadenylation pages 6-7, salgania2024reloisa pages 6-8) |
| Nurse-cell P-bodies and Cyclin A/B control during oogenesis | Cup and Bruno 1 associate spatially with cycA and cycB mRNAs in large nurse-cell cytoplasmic condensates and help recruit or retain them in Me31B-marked P-bodies. | Super-resolution imaging demonstrated colocalization rather than direct RNA binding. RNAi depletion of Cup or Bruno 1 caused ectopic Cyclin B from early egg-chamber stages and later Cyclin A accumulation. Cup depletion also weakened both transcripts’ association with Me31B condensates, whereas Cup-containing mRNP association persisted after Me31B depletion. (bayer2025posttranscriptionalregulationof pages 5-7, bayer2025posttranscriptionalregulationof pages 13-15, bayer2025posttranscriptionalregulationof pages 1-3) |
| Cup clearance during the maternal-to-zygotic transition | Maternal Cup, Me31B and Trailer hitch are ubiquitylated by the CTLH E3-ligase system and cleared as developmental control shifts to zygotic products. | Earlier work established CTLH-dependent turnover of the three repressors. A 2024 preprint, subsequently published in 2025, identified Muskelin as the CTLH substrate adaptor and found few targets beyond this repressor trio. This demonstrates regulated Cup proteolysis, not ubiquitin-catalytic activity by Cup itself. (briney2024muskelinactsas pages 1-4, briney2025muskelinisa pages 17-18, wang2017me31bgloballyrepresses pages 1-2) |
Table: Evidence matrix summarizing experimentally supported functions of Drosophila Cup (Q9VMA3) while distinguishing direct binding, complex association, functional genetics and mechanistic inference.
Cup is a large, approximately 1,132-amino-acid protein with an N-terminal eIF4E-interaction region and middle and glutamine-rich C-terminal regions. The C-terminal region interacts with Bruno. In the original ovarian study, Cup–eIF4E association survived RNase treatment, mutations in Cup’s conserved YxxxxLφ eIF4E-binding motif sharply reduced association, and mutation of the corresponding eIF4E contact residue W117 abolished the tested interaction. These experiments establish direct eIF4E binding more strongly than co-localization alone would. (nakamura2004drosophilacupis pages 3-4, nakamura2004drosophilacupis pages 2-3, nakamura2004drosophilacupis pages 5-7)
Structural analysis subsequently resolved a 2.8-Å crystal structure of an eIF4E–Cup minimal complex. Cup contributes two eIF4E-binding segments: a canonical site modeled at residues 318–339 and a noncanonical site at 362–376. They contact different surfaces of eIF4E, consistent with Cup opposing eIF4G association; the structure establishes the interface of a fragment, not the complete architecture of full-length Cup or an intact ovarian granule. The cropped structural evidence is the original study’s Figure 2. (kinkelin2012crystalstructureof pages 2-4, kinkelin2012crystalstructureof pages 1-2, kinkelin2012crystalstructureof media abf926a3)
eIF4E competition is important, but is not Cup’s only activity. In Drosophila S2-cell tethering and osk-3′-UTR reporter experiments, Cup’s middle plus C-terminal effector domain repressed expression and promoted deadenylation even when canonical eIF4E binding was impaired. Full-length Cup allowed repressed, deadenylated RNA to accumulate, whereas its isolated effector domain promoted degradation. The N-terminal region, particularly its noncanonical eIF4E-binding motif, counteracted subsequent decapping and decay. Cup therefore couples translational inhibition to regulated mRNA stability, rather than simply destroying every transcript it silences. This domain dissection also qualifies the early interpretation that all Cup-dependent repression strictly requires its canonical eIF4E site: that site was essential for repression in the tested cup mutant oocyte context, but not for every repression mechanism measured with S2 reporters. (igreja2011cuppromotesdeadenylation pages 1-2, igreja2011cuppromotesdeadenylation pages 6-7, nakamura2004drosophilacupis pages 5-7)
Cup co-immunoprecipitates, even after RNase treatment, with components of the CAF1–CCR4–NOT deadenylase machinery. However, a 2024 pairwise protein-interaction assay detected Cup binding to eIF4E and Me31B but not to individual CCR4–NOT core subunits. The defensible conclusion is that Cup is associated with a deadenylation-competent complex; direct Cup binding to a particular NOT-core protein is not established by those observations. Cup itself has not been shown to catalyze deadenylation, decapping or ubiquitination. (igreja2011cuppromotesdeadenylation pages 6-7, salgania2024reloisa pages 6-8)
In nurse cells and the developing oocyte, Bruno recognizes response elements in the osk 3′ UTR and associates with Cup; Cup’s C-terminal glutamine-rich region is sufficient for their interaction in yeast assays, and Bruno remains associated with the ovarian Cup–eIF4E complex after RNase treatment. This provides a plausible physical bridge from a transcript-specific 3′-UTR regulator to the cap-dependent initiation machinery. Oskar protein is subsequently required to establish posterior germ plasm and germ-cell determinants; untimely expression is therefore consequential even if osk RNA still reaches the right region. (nakamura2004drosophilacupis pages 1-2, nakamura2004drosophilacupis pages 2-3, nakamura2004drosophilacupis pages 5-7)
The clearest separation of repression from RNA localization comes from the cup212 mutant, which produces a truncated protein lacking a functional canonical eIF4E-binding region. Oskar protein appeared prematurely in early egg chambers, yet osk RNA still enriched at the oocyte posterior from approximately stage 8 onward. Its particles were abnormally large and some RNA persisted elsewhere, so localization was not fully normal. In the same mutant, measured microtubule-polarity markers and gurken RNA/protein localization were largely preserved. The principal demonstrated defect in this experiment is therefore premature osk translation, not a general collapse of oocyte polarity. (nakamura2004drosophilacupis pages 3-4, nakamura2004drosophilacupis pages 4-5, nakamura2004drosophilacupis pages 5-7)
In the early embryo, Smaug recognizes elements in the nos 3′ UTR and forms a repression assembly containing Cup and eIF4E. Experiments established Cup association with Smaug, interference with eIF4G–eIF4E binding and a requirement for Cup in tested Smaug-dependent repression. Later biochemical recovery of an element-dependent nos repressor complex also identified Cup, Smaug, Me31B, Trailer hitch, Belle and eIF4E. In that analysis, Cup associated with the recognition-element-containing complex, whereas Me31B–Trailer hitch coating of RNA was proposed as an additional repression mechanism. Consequently, Cup is an important component of nos regulation, not necessarily its sole effector. (nelson2009translationalregulationina pages 47-51, nelson2009translationalregulationin pages 47-51, gotze2017translationalrepressionof pages 1-2)
A 2024 single-molecule imaging study refined where nos is activated: posterior embryonic germ granules supported active translation preferentially at their surface, while the nos 3′ UTR lay within the granule. Oskar-dependent sequestration of Smaug was implicated in relieving repression. This directly establishes the spatial translation pattern and a role for Smaug–Oskar compartmentalization; it should not be read as direct visualization of Cup dissociating from individual nos molecules. (chen2024directobservationof pages 1-2)
Cup associates with Orb-containing ovarian complexes and restrains premature activation of the orb mRNA/Orb-protein positive-feedback loop. cup mutants accumulate Orb abnormally in nurse cells and retain orb RNAs with longer poly(A) tails, although those RNAs can be mislocalized and less abundant. These findings support a regulatory role in Orb-associated mRNPs, without proving that Cup directly binds orb RNA or enzymatically changes its tail. (wong2011cupblocksthe pages 2-3, wong2011cupblocksthe pages 1-2)
More recent work identifies cyclin A and cyclin B mRNAs as additional ovarian contexts. Tagged Cup and Bru1 occur with cycA and cycB RNA in large nurse-cell cytoplasmic assemblies; Cup or Bru1 depletion causes ectopic Cyclin B protein beginning around egg-chamber stage 2, with the strongest early Cyclin A increase around stage 4. Their mRNAs also associate with Me31B-marked P-bodies. This is strong genetic and spatial evidence for Cup-mediated post-transcriptional control, although microscopic overlap alone does not establish direct Cup–RNA binding for either cyclin. (bayer2025posttranscriptionalregulationof pages 5-7, bayer2025posttranscriptionalregulationof pages 1-3, bayer2025posttranscriptionalregulationof pages 13-15)
Cup’s experimentally well-supported site of action is the intracellular germline cytoplasm: punctate mRNPs in ovarian nurse cells and the oocyte, including Me31B-associated processing bodies (P-bodies), and maternally supplied complexes in the early embryo. Original ovarian immunostaining found Cup co-localized with Me31B particles throughout oogenesis; more recent tagged-protein imaging places it with cyclin-associated condensates in nurse-cell cytoplasm. P-bodies are non-membrane-bound cytoplasmic mRNP compartments, not extracellular structures or evidence that Cup is an ER-resident membrane protein. Older work has also reported nucleocytoplasmic shuttling, but the best-established functional reactions described here—translation control and protection of stored mRNAs—occur in cytoplasmic mRNPs. (nakamura2004drosophilacupis pages 2-3, bayer2025posttranscriptionalregulationof pages 5-7, nelson2009translationalregulationina pages 137-139, milano2024theroleof pages 1-4)
Ovarian P-body organization depends in part on proximity to ER exit sites. In a study first posted in July 2024 and published online in EMBO Reports on 9 December 2024 (January 2025 issue), ER-exit-site-associated P-bodies were larger and less mobile than other cytoplasmic P-bodies. Perturbing exit sites redistributed P-body components, including Cup, and compromised osk mRNA stability and translational repression. This identifies a relevant cellular environment for Cup-containing complexes; it does not establish that Cup itself mediates ER export or directly binds ER-exit-site proteins. (milano2024theroleof pages 9-11, milano2024theroleof pages 1-2)
Functional conclusion. The strongest assignment for Q9VMA3 is a 4E-T-family mRNP scaffold/effector that links transcript-selective RNA-binding regulators to translation-initiation inhibition, deadenylation-associated silencing and protection of selected maternal mRNAs. Its best-demonstrated pathway is Bruno-dependent restriction of osk translation during oogenesis; Smaug-dependent nos regulation, P-body-associated RNA storage and timed embryonic clearance extend that role. Important unresolved questions include exactly how a given Cup-bound mRNP is switched back on and which molecular bridges connect Cup to CCR4–NOT in vivo. (nakamura2004drosophilacupis pages 5-7, igreja2011cuppromotesdeadenylation pages 1-2, salgania2024reloisa pages 6-8, chen2024directobservationof pages 1-2)
References
(nakamura2004drosophilacupis pages 1-2): Akira Nakamura, Keiji Sato, and Kazuko Hanyu-Nakamura. Drosophila cup is an eif4e binding protein that associates with bruno and regulates oskar mrna translation in oogenesis. Developmental cell, 6 1:69-78, Jan 2004. URL: https://doi.org/10.1016/s1534-5807(03)00400-3, doi:10.1016/s1534-5807(03)00400-3. This article has 470 citations and is from a highest quality peer-reviewed journal.
(kinkelin2012crystalstructureof pages 1-2): Kerstin Kinkelin, Katharina Veith, Marlene Grünwald, and Fulvia Bono. Crystal structure of a minimal eif4e-cup complex reveals a general mechanism of eif4e regulation in translational repression. RNA, 18 9:1624-34, Sep 2012. URL: https://doi.org/10.1261/rna.033639.112, doi:10.1261/rna.033639.112. This article has 81 citations and is from a domain leading peer-reviewed journal.
(meyer2024exploringthedynamics pages 3-4): Julia Meyer, Marco Payr, Olivier Duss, and Janosch Hennig. Exploring the dynamics of messenger ribonucleoprotein-mediated translation repression. Biochemical Society Transactions, 52:2267-2279, Nov 2024. URL: https://doi.org/10.1042/bst20231240, doi:10.1042/bst20231240. This article has 5 citations and is from a peer-reviewed journal.
(nelson2009translationalregulationina pages 47-51): M Nelson. Translational regulation in the early drosophila embryo. Unknown journal, 2009.
(igreja2011cuppromotesdeadenylation pages 1-2): Catia Igreja and Elisa Izaurralde. Cup promotes deadenylation and inhibits decapping of mrna targets. Genes & development, 25 18:1955-67, Sep 2011. URL: https://doi.org/10.1101/gad.17136311, doi:10.1101/gad.17136311. This article has 113 citations and is from a highest quality peer-reviewed journal.
(igreja2011cuppromotesdeadenylation pages 6-7): Catia Igreja and Elisa Izaurralde. Cup promotes deadenylation and inhibits decapping of mrna targets. Genes & development, 25 18:1955-67, Sep 2011. URL: https://doi.org/10.1101/gad.17136311, doi:10.1101/gad.17136311. This article has 113 citations and is from a highest quality peer-reviewed journal.
(nakamura2004drosophilacupis pages 3-4): Akira Nakamura, Keiji Sato, and Kazuko Hanyu-Nakamura. Drosophila cup is an eif4e binding protein that associates with bruno and regulates oskar mrna translation in oogenesis. Developmental cell, 6 1:69-78, Jan 2004. URL: https://doi.org/10.1016/s1534-5807(03)00400-3, doi:10.1016/s1534-5807(03)00400-3. This article has 470 citations and is from a highest quality peer-reviewed journal.
(nakamura2004drosophilacupis pages 4-5): Akira Nakamura, Keiji Sato, and Kazuko Hanyu-Nakamura. Drosophila cup is an eif4e binding protein that associates with bruno and regulates oskar mrna translation in oogenesis. Developmental cell, 6 1:69-78, Jan 2004. URL: https://doi.org/10.1016/s1534-5807(03)00400-3, doi:10.1016/s1534-5807(03)00400-3. This article has 470 citations and is from a highest quality peer-reviewed journal.
(nakamura2004drosophilacupis pages 5-7): Akira Nakamura, Keiji Sato, and Kazuko Hanyu-Nakamura. Drosophila cup is an eif4e binding protein that associates with bruno and regulates oskar mrna translation in oogenesis. Developmental cell, 6 1:69-78, Jan 2004. URL: https://doi.org/10.1016/s1534-5807(03)00400-3, doi:10.1016/s1534-5807(03)00400-3. This article has 470 citations and is from a highest quality peer-reviewed journal.
(nelson2009translationalregulationin pages 51-55): M Nelson. Translational regulation in the early drosophila embryo. Unknown journal, 2009.
(gotze2017translationalrepressionof pages 1-2): Michael Götze, Jérémy Dufourt, Christian Ihling, Christiane Rammelt, Stephanie Pierson, Nagraj Sambrani, Claudia Temme, Andrea Sinz, Martine Simonelig, and Elmar Wahle. Translational repression of the drosophila nanos mrna involves the rna helicase belle and rna coating by me31b and trailer hitch. RNA, 23:1552-1568, Jul 2017. URL: https://doi.org/10.1261/rna.062208.117, doi:10.1261/rna.062208.117. This article has 81 citations and is from a domain leading peer-reviewed journal.
(salgania2024reloisa pages 6-8): Harpreet Kaur Salgania, Jutta Metz, and Mandy Jeske. Relo is a simple and rapid colocalization assay to identify and characterize direct protein–protein interactions. Nature Communications, Apr 2024. URL: https://doi.org/10.1038/s41467-024-47233-4, doi:10.1038/s41467-024-47233-4. This article has 22 citations and is from a highest quality peer-reviewed journal.
(bayer2025posttranscriptionalregulationof pages 5-7): Livia V. Bayer, Samantha N. Milano, Harpreet Kaur, Zara Kumar, and Diana P. Bratu. Post-transcriptional regulation of cyclin a and b mrnas by bruno 1, cup, and p-bodies. iScience, 28:112727, Jun 2025. URL: https://doi.org/10.1016/j.isci.2025.112727, doi:10.1016/j.isci.2025.112727. This article has 5 citations and is from a peer-reviewed journal.
(bayer2025posttranscriptionalregulationof pages 13-15): Livia V. Bayer, Samantha N. Milano, Harpreet Kaur, Zara Kumar, and Diana P. Bratu. Post-transcriptional regulation of cyclin a and b mrnas by bruno 1, cup, and p-bodies. iScience, 28:112727, Jun 2025. URL: https://doi.org/10.1016/j.isci.2025.112727, doi:10.1016/j.isci.2025.112727. This article has 5 citations and is from a peer-reviewed journal.
(bayer2025posttranscriptionalregulationof pages 1-3): Livia V. Bayer, Samantha N. Milano, Harpreet Kaur, Zara Kumar, and Diana P. Bratu. Post-transcriptional regulation of cyclin a and b mrnas by bruno 1, cup, and p-bodies. iScience, 28:112727, Jun 2025. URL: https://doi.org/10.1016/j.isci.2025.112727, doi:10.1016/j.isci.2025.112727. This article has 5 citations and is from a peer-reviewed journal.
(briney2024muskelinactsas pages 1-4): Chloe A. Briney, Jesslyn C. Henriksen, Chenwei Lin, Lisa A. Jones, Leif Benner, Addison B. Rains, Roxana Gutierrez, Philip R. Gafken, and Olivia S. Rissland. Muskelin acts as a substrate receptor of the highly regulated drosophila ctlh e3 ligase during the maternal-to-zygotic transition. bioRxiv, Jul 2024. URL: https://doi.org/10.1101/2024.06.28.601265, doi:10.1101/2024.06.28.601265. This article has 1 citations.
(briney2025muskelinisa pages 17-18): Chloe A Briney, Jesslyn C Henriksen, Chenwei Lin, Lisa A. Jones, Leif Benner, Addison B. Rains, Roxana Gutierrez, Philip R. Gafken, and Olivia S. Rissland. Muskelin is a substrate adaptor of the highly regulated drosophila embryonic ctlh e3 ligase. EMBO Reports, 26:1647-1669, Feb 2025. URL: https://doi.org/10.1038/s44319-025-00397-6, doi:10.1038/s44319-025-00397-6. This article has 11 citations and is from a highest quality peer-reviewed journal.
(wang2017me31bgloballyrepresses pages 1-2): Miranda Wang, Michael Ly, Andrew Lugowski, John D Laver, Howard D Lipshitz, Craig A Smibert, and Olivia S Rissland. Me31b globally represses maternal mrnas by two distinct mechanisms during the drosophila maternal-to-zygotic transition. eLife, Sep 2017. URL: https://doi.org/10.7554/elife.27891, doi:10.7554/elife.27891. This article has 97 citations and is from a domain leading peer-reviewed journal.
(nakamura2004drosophilacupis pages 2-3): Akira Nakamura, Keiji Sato, and Kazuko Hanyu-Nakamura. Drosophila cup is an eif4e binding protein that associates with bruno and regulates oskar mrna translation in oogenesis. Developmental cell, 6 1:69-78, Jan 2004. URL: https://doi.org/10.1016/s1534-5807(03)00400-3, doi:10.1016/s1534-5807(03)00400-3. This article has 470 citations and is from a highest quality peer-reviewed journal.
(kinkelin2012crystalstructureof pages 2-4): Kerstin Kinkelin, Katharina Veith, Marlene Grünwald, and Fulvia Bono. Crystal structure of a minimal eif4e-cup complex reveals a general mechanism of eif4e regulation in translational repression. RNA, 18 9:1624-34, Sep 2012. URL: https://doi.org/10.1261/rna.033639.112, doi:10.1261/rna.033639.112. This article has 81 citations and is from a domain leading peer-reviewed journal.
(kinkelin2012crystalstructureof media abf926a3): Kerstin Kinkelin, Katharina Veith, Marlene Grünwald, and Fulvia Bono. Crystal structure of a minimal eif4e-cup complex reveals a general mechanism of eif4e regulation in translational repression. RNA, 18 9:1624-34, Sep 2012. URL: https://doi.org/10.1261/rna.033639.112, doi:10.1261/rna.033639.112. This article has 81 citations and is from a domain leading peer-reviewed journal.
(nelson2009translationalregulationin pages 47-51): M Nelson. Translational regulation in the early drosophila embryo. Unknown journal, 2009.
(chen2024directobservationof pages 1-2): Ruoyu Chen, William Stainier, Jeremy Dufourt, Mounia Lagha, and Ruth Lehmann. Direct observation of translational activation by a ribonucleoprotein granule. Nature Cell Biology, 26:1322-1335, Jul 2024. URL: https://doi.org/10.1038/s41556-024-01452-5, doi:10.1038/s41556-024-01452-5. This article has 64 citations and is from a highest quality peer-reviewed journal.
(wong2011cupblocksthe pages 2-3): Li Chin Wong and Paul Schedl. Cup blocks the precocious activation of the orb autoregulatory loop. PLoS ONE, 6:e28261, Dec 2011. URL: https://doi.org/10.1371/journal.pone.0028261, doi:10.1371/journal.pone.0028261. This article has 33 citations and is from a peer-reviewed journal.
(wong2011cupblocksthe pages 1-2): Li Chin Wong and Paul Schedl. Cup blocks the precocious activation of the orb autoregulatory loop. PLoS ONE, 6:e28261, Dec 2011. URL: https://doi.org/10.1371/journal.pone.0028261, doi:10.1371/journal.pone.0028261. This article has 33 citations and is from a peer-reviewed journal.
(nelson2009translationalregulationina pages 137-139): M Nelson. Translational regulation in the early drosophila embryo. Unknown journal, 2009.
(milano2024theroleof pages 1-4): Samantha N. Milano, Livia V. Bayer, Julie J. Ko, Caroline E. Casella, and Diana P. Bratu. The role of er exit sites in maintaining p-body organization and transmitting er stress response during drosophila melanogaster oogenesis. bioRxiv, Jul 2024. URL: https://doi.org/10.1101/2024.07.03.601952, doi:10.1101/2024.07.03.601952. This article has 2 citations.
(milano2024theroleof pages 9-11): Samantha N. Milano, Livia V. Bayer, Julie J. Ko, Caroline E. Casella, and Diana P. Bratu. The role of er exit sites in maintaining p-body organization and transmitting er stress response during drosophila melanogaster oogenesis. bioRxiv, Jul 2024. URL: https://doi.org/10.1101/2024.07.03.601952, doi:10.1101/2024.07.03.601952. This article has 2 citations.
(milano2024theroleof pages 1-2): Samantha N Milano, Livia V Bayer, Julie J Ko, Caroline E Casella, and Diana P Bratu. The role of er exit sites in maintaining p-body organization and integrity during drosophila melanogaster oogenesis. EMBO Reports, 26:494-520, Dec 2025. URL: https://doi.org/10.1038/s44319-024-00344-x, doi:10.1038/s44319-024-00344-x. This article has 13 citations and is from a highest quality peer-reviewed journal.