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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 protein is correctly identified as Orb/Oo18/CG10868 from Drosophila melanogaster, not the distinct fly protein Orb2 or an ORB-named protein from another organism. The literature explicitly describes Orb as a founding fly homolog of cytoplasmic polyadenylation element-binding protein (CPEB), consistent with the supplied UniProt assignment to the RRM-CPEB family and its C-terminal RNA-recognition architecture. The isoform labels C and E in Q8IMZ2 are therefore compatible with the intended orb locus, although the available literature does not resolve isoform-specific functions. (lipshitz2000mechanismsofrna pages 12-13, barr2019thecpebtranslational pages 2-4, chang1999thedrosophilacpeb pages 1-2)
Orb is not an enzyme or transporter. Its primary function is that of a germline-enriched, cytoplasmic RNA-binding translational regulator: it recognizes selected mRNA 3′ untranslated regions and promotes spatially and temporally restricted protein synthesis, often by recruiting or coordinating cytoplasmic poly(A)-tail extension. The strongest direct targets are oskar (osk) and gurken (grk). Orb also regulates its own mRNA through a positive 3′UTR-dependent feedback loop and functions with the Par–actin–microtubule polarity machinery. (sottolano2023anevolutionarystudy pages 30-34, barr2019thedrosophilacpeb pages 1-2, barr2019thecpebtranslational pages 1-2, chang1999thedrosophilacpeb pages 1-2)
| Functional claim | Molecular/cellular site | Evidence type | Key quantitative or mechanistic observation | Confidence/caveat | Key source DOI/URL |
|---|---|---|---|---|---|
| Identity and architecture: Q8IMZ2 is Drosophila melanogaster Orb/Oo18/CG10868, a germline CPEB-family RNA-binding protein with two C-terminal RRM-like domains; supplied InterPro annotations also identify CPEB and CEBP_ZZ-related regions. | Female germline; predominantly cytoplasmic in germline cysts and oocytes | Sequence homology, domain annotation, and germline-expression studies | Literature identifies Orb as the fly homolog of Xenopus CPEB and reports two C-terminal RNA-recognition-motif-like domains. This agrees with the supplied UniProt/InterPro record. (lipshitz2000mechanismsofrna pages 12-13, barr2019thecpebtranslational pages 2-4, chang1999thedrosophilacpeb pages 1-2) | High for identity, organism, CPEB membership, and two RRMs. Exact domain boundaries and isoform-specific architecture were not independently validated here. Orb2 and proteins from other organisms are excluded. | 10.1006/dbio.1999.9444; 10.1016/S0959-437X(00)00116-7 |
| Primary molecular function: Orb binds selected mRNA 3′UTRs and controls translation, commonly by promoting cytoplasmic poly(A)-tail extension rather than catalyzing polymerization itself. | Cytoplasmic messenger ribonucleoprotein complexes in developing oocytes | Biochemical association, mutant poly(A)-tail analysis, and CPEB-family inference | Orb-associated transcripts lose poly(A)-tail length and protein output when Orb activity is impaired; the polymerase activity is supplied by partners such as Wispy, not Orb. (lipshitz2000mechanismsofrna pages 7-8, lipshitz2000mechanismsofrna pages 12-13, sottolano2023anevolutionarystudy pages 30-34) | High that Orb is a nonenzymatic translational regulator; target outcome can be context dependent, because CPEBs may activate or repress translation. | 10.1016/S0959-437X(00)00116-7; 10.7282/t3-fftx-nn74 |
| Direct target—oskar: Orb binds osk RNA and is required for polyadenylation-dependent Oskar translation. | Oocyte cytoplasm; ultimately the posterior cortex during mid-to-late oogenesis | Co-immunoprecipitation, UV cross-linking, poly(A)-tail assays, mutant genetics, and protein localization | osk RNA co-immunoprecipitates with Orb, and its 3′UTR UV-cross-links to Orb in ovarian extract. Strong orb mutants lack detectable Oskar; hypomorphic orb mutants show little or no posterior Oskar and shortened osk poly(A) tails. (lipshitz2000mechanismsofrna pages 7-8, chang1999thedrosophilacpeb pages 1-2) | Very high for physical association and functional requirement. Severe alleles also impair osk localization, so some downstream patterning defects combine transport and translation failures. | 10.1006/dbio.1999.9444; 10.1016/S0959-437X(00)00116-7 |
| Direct pathway—gurken–Wispy: Orb cooperates with the GLD-2-family cytoplasmic poly(A) polymerase Wispy to activate localized grk translation. | Dorsal-anterior cytoplasm of the oocyte, where localized grk is translated | Primary-study synthesis involving RNA binding, phosphorylation, poly(A)-tail analysis, and genetic cooperation | Orb binds the grk 3′UTR; phosphorylated Orb recruits/cooperates with Wispy, increasing the reported tail from about 30 to 90 adenosines, thereby favoring PABP and translation-initiation-complex recruitment. (sottolano2023anevolutionarystudy pages 30-34, sottolano2023anevolutionarystudy pages 133-136, barr2019thecpebtranslational pages 25-26) | High for Orb–Wispy cooperation and localized grk polyadenylation. The numerical tail estimate here is recovered through a 2023 synthesis rather than directly from the primary paper text. | 10.1002/dvdy.24311; 10.7282/t3-fftx-nn74 |
| Positive autoregulation: the orb 3′UTR drives localization and Orb-dependent translation of orb mRNA, forming a threshold-dependent positive-feedback loop. | Initially two pro-oocytes in germarial region 2a; then one selected oocyte in region 2b and later egg chambers | 3′UTR deletion/replacement, reporter assays, dosage tests, localization imaging, and transgenic rescue | The major ovarian transcript is approximately 4.9 kb with a 1.2-kb 3′UTR; an 815-nt fragment recapitulates localization. Removing the 3′UTR abolishes oocyte enrichment, whereas reducing a partially functional replacement allele to one copy prevents loop activation, supporting an Orb-concentration threshold. (barr2019thedrosophilacpeb pages 13-14, barr2019thedrosophilacpeb pages 4-5) | Very high for 3′UTR-dependent autoregulation and dosage sensitivity. The exact direct RNA contacts within the endogenous 3′UTR remain less completely resolved. | 10.1534/genetics.119.302687 |
| Oocyte specification and maintenance: localized Orb activity selects and continually maintains one oocyte among the 16 cyst cells. | Germarium and early egg chamber | Loss-of-function genetics, cell-fate markers, delayed rescue, and full-length cDNA rescue | Deleting the orb 3′UTR yields chambers with 16 polyploid nurse cells, sterility, and no eggs. With a partially functional replacement, specification is delayed until stage 2 and occurs in only about 50% of chambers; full-length orb cDNA restores organization and fertility. (barr2019thedrosophilacpeb pages 4-5, barr2019thedrosophilacpeb pages 1-2) | Very high for necessity. Some effects on BicD/Egl/Dynein localization may be downstream of failed fate specification rather than independent direct Orb targets. | 10.1534/genetics.119.302687 |
| Par–actin–microtubule polarity: Orb functions with aPKC/Cdc42 and Par proteins to establish cortical polarity and repolarize the oocyte microtubule network. | Anterior/anterior-lateral and posterior oocyte cortex around stage 7 | Genetic interactions, RNA/protein localization, cortical-actin imaging, and microtubule-organization phenotypes | Orb impairment mislocalizes anterior aPKC and posterior Par-1, fragments cortical actin, and disrupts Shot/Patronin-dependent microtubule repolarization. Ventralized eggs increase from about 5% in orb heterozygotes to nearly 50% with an aPKC allele and about 70% with a cdc42 allele. (barr2019thecpebtranslational pages 18-19, barr2019thecpebtranslational pages 1-2) | High for pathway-level functional interaction. Direct translational regulation is clearest for aPKC RNA association; several cytoskeletal consequences may be indirect. | 10.1371/journal.pgen.1008012 |
| aPKC as a likely direct regulatory target: Orb associates with CPE-containing aPKC mRNA and is required for its normal oocyte distribution. | Oocyte cortex and cytoplasm during repolarization | CPE analysis, binding in ovary extracts, mutant RNA localization, and genetic interaction | aPKC mRNA contains CPEs, binds Orb in ovarian extracts, and becomes mislocalized when Orb is compromised; aPKC protein localization is also defective. (barr2019thecpebtranslational pages 18-19) | Moderate-to-high. Physical association and functional dependence are established, but transcript-specific poly(A)-tail extension and translational activation were not demonstrated as completely as for osk or grk. | 10.1371/journal.pgen.1008012 |
| Candidate Orb targets in polarity/cytoskeletal control: cdc42, baz, par-6, capu, spir, Cip4, WASp, shot, and patronin may be Orb-regulated transcripts. | Oocyte cortical-polarity, actin, and microtubule-organizing systems | CPE prediction and binding to ectopically expressed Orb in cultured cells, with genetic/cytological pathway consistency | These transcripts contain candidate CPEs and associated with ectopically expressed Orb; corresponding pathways are perturbed in orb mutants. (barr2019thecpebtranslational pages 18-19) | Provisional. These are candidate—not fully validated direct—targets. Endogenous ovarian binding, Orb-dependent tail changes, target-specific translation effects, and rescue remain necessary for definitive annotation. | 10.1371/journal.pgen.1008012 |
Table: Evidence-ranked summary of the identity, molecular activity, cellular sites, validated targets, developmental pathways, and candidate targets of Drosophila Orb. It separates direct biochemical and genetic findings from pathway inference and provisional RNA-target assignments.
The identities agree across the supplied record and the retrieved literature:
The literature explicitly calls Orb a homolog of Xenopus CPEB and a germline-specific CPEB protein. Chang and colleagues further reported two C-terminal RNA-recognition-motif-like domains, matching the supplied RRM/CPEB-family annotation. (lipshitz2000mechanismsofrna pages 12-13, barr2019thecpebtranslational pages 2-4, chang1999thedrosophilacpeb pages 1-2)
The supplied UniProt/InterPro annotations—CPEB, CPEB1_RRM1, CEBP_ZZ/CEBP_ZZ_sf, and nucleotide-binding α/β-plait fold—are consistent with the conserved CPEB RNA-binding region. Functionally, the paired C-terminal RRM-like domains provide the structural basis for sequence-selective 3′UTR binding. The available retrieved papers do not independently establish exact residue boundaries or differences between isoforms C and E; those details should therefore remain database-level annotations rather than experimentally demonstrated isoform-specific properties.
Orb is best annotated as a sequence-selective mRNA 3′UTR-binding regulator of cytoplasmic polyadenylation, translation, RNA localization, and oocyte polarity. It does not itself catalyze adenylate addition. Instead, it serves as the target-recognition/regulatory component of messenger ribonucleoprotein complexes and can cooperate with a cytoplasmic poly(A) polymerase such as Wispy. Poly(A)-tail extension promotes poly(A)-binding-protein recruitment and productive communication with cap-associated translation-initiation factors. (lipshitz2000mechanismsofrna pages 7-8, sottolano2023anevolutionarystudy pages 30-34)
CPEB-family activity can be activating or repressive depending on transcript, developmental stage, phosphorylation state, and associated proteins. For Orb, however, the best-characterized ovarian functions are translational activation of localized osk and grk mRNAs. Thus, “RNA-binding translational regulator” is more accurate than assigning Orb a poly(A) polymerase activity. (lipshitz2000mechanismsofrna pages 7-8, sottolano2023anevolutionarystudy pages 30-34, barr2019thedrosophilacpeb pages 1-2)
The case for direct regulation of osk is supported by complementary biochemistry and genetics. Ovarian osk RNA co-immunoprecipitates with Orb, and the osk 3′UTR UV-cross-links to Orb in ovarian extracts. Strong orb mutants have undetectable Oskar protein, whereas the hypomorphic orb^mel allele produces little or no posterior Oskar. These defects correlate with shorter osk poly(A) tails, supporting translational activation through cytoplasmic polyadenylation. (lipshitz2000mechanismsofrna pages 7-8, chang1999thedrosophilacpeb pages 1-2)
Orb acts within the polarized oocyte: osk normally enters the oocyte, accumulates posteriorly around stage 8, and forms a posterior cap by stage 10. Severe orb disruption can impair both initial RNA localization and subsequent translation, so the final posterior-patterning phenotype is not attributable solely to translational failure. Nonetheless, direct Orb–osk association and Orb-dependent poly(A)-tail length establish a specific translational mechanism. (chang1999thedrosophilacpeb pages 1-2)
Biological output: posterior Oskar production establishes posterior embryonic determinants and germ-plasm assembly. Orb therefore connects localized mRNA transport to translation at the correct cortical destination.
Primary source: Chang JS, Tan L, Schedl P. “The Drosophila CPEB homolog, Orb, is required for oskar protein expression in oocytes.” Developmental Biology, published November 1999. DOI/URL: https://doi.org/10.1006/dbio.1999.9444. (chang1999thedrosophilacpeb pages 1-2)
Orb cooperates with Wispy, the Drosophila GLD-2-related cytoplasmic poly(A) polymerase, in polyadenylating localized grk mRNA. A recent synthesis describes Orb binding the grk 3′UTR and phosphorylated Orb recruiting/cooperating with Wispy, increasing the tail from approximately 30 to 90 adenosines. This favors poly(A)-binding protein and translation-initiation-complex recruitment. (sottolano2023anevolutionarystudy pages 30-34, sottolano2023anevolutionarystudy pages 133-136)
Spatial regulation is crucial: grk translation is activated in the dorsal-anterior oocyte, where Gurken signals to adjacent follicle cells through the Drosophila EGFR pathway to establish dorsoventral polarity. The 2023 synthesis proposes repression of Orb activity in nurse cells and localized activation, including CK2-associated phosphorylation, in the oocyte. The exact 30-to-90-adenosine value was recovered through this synthesis rather than direct inspection of the 2015 primary paper and should be interpreted accordingly. (sottolano2023anevolutionarystudy pages 30-34)
Primary source: Norvell A et al. “Wispy and Orb cooperate in the cytoplasmic polyadenylation of localized gurken mRNA.” Developmental Dynamics 244:1276–1285, published 2015. DOI/URL: https://doi.org/10.1002/dvdy.24311. (sottolano2023anevolutionarystudy pages 133-136, barr2019thecpebtranslational pages 25-26)
Orb also regulates its own expression. The major ovarian orb transcript is approximately 4.9 kb, including an approximately 1.2-kb 3′UTR. An 815-nt 3′UTR fragment is sufficient to reproduce the endogenous localization pattern in a reporter, and reporter localization/translation depends on Orb, supporting positive autoregulation. (barr2019thedrosophilacpeb pages 4-5)
Deleting the endogenous 3′UTR eliminates normal enrichment of orb mRNA and protein in the pro-oocytes and selected oocyte while preserving more basal nurse-cell expression. Full-length orb cDNA rescues localization, egg-chamber organization, and fertility, tying the phenotype specifically to disrupted 3′UTR-dependent regulation. A partially functional 3′UTR replacement delays specification until stage 2, when only approximately 50% of chambers activate the loop and establish an oocyte. Halving the dose of this replacement prevents loop activation, indicating a threshold-dependent positive-feedback mechanism. (barr2019thedrosophilacpeb pages 13-14, barr2019thedrosophilacpeb pages 4-5, barr2019thedrosophilacpeb pages 1-2)
Primary source: Barr J et al. “The Drosophila CPEB Protein Orb Specifies Oocyte Fate by a 3′UTR-Dependent Autoregulatory Loop.” Genetics 213:1431–1446, published December 2019. DOI/URL: https://doi.org/10.1534/genetics.119.302687. (barr2019thedrosophilacpeb pages 13-14, barr2019thedrosophilacpeb pages 4-5, barr2019thedrosophilacpeb pages 1-2)
Orb carries out its established functions inside female germline cells, predominantly in cytoplasmic RNPs rather than as a secreted, membrane, or nuclear structural protein.
During early oogenesis, a 16-cell cyst contains two pro-oocytes. orb mRNA and Orb protein first become enriched in these cells and then concentrate in one cell in germarial region 2b. This asymmetry coincides with concentration of other oocyte markers and commitment of one cell to oocyte identity, while the remaining 15 become nurse cells. (barr2019thedrosophilacpeb pages 13-14, barr2019thedrosophilacpeb pages 1-2)
Later, Orb distribution is dynamic rather than uniformly cytoplasmic. During oocyte repolarization, orb mRNA moves from the posterior toward the anterior-lateral margin. Functionally relevant Orb complexes act at localized osk and grk RNA domains—the posterior cortex for Oskar production and dorsal-anterior cytoplasm for Gurken production. (sottolano2023anevolutionarystudy pages 30-34, barr2019thecpebtranslational pages 2-4, chang1999thedrosophilacpeb pages 1-2)
These data support the annotation cytoplasm; germline cyst; oocyte; stage-specific cortical RNP compartments, with localization changing across development.
Orb is both an early fate determinant and a continuously required maintenance factor. Removal of its 3′UTR produces chambers containing 16 polyploid nurse cells, female sterility, and no egg laying. Earlier/stronger alleles can block cyst development or cause degeneration, while alleles that permit formation of a 16-cell cyst may still fail to specify an oocyte. Continuous Orb activity is needed after initial specification, indicating that it maintains the oocyte translation program rather than acting as a one-time developmental switch. (barr2019thedrosophilacpeb pages 4-5, barr2019thecpebtranslational pages 2-4, barr2019thedrosophilacpeb pages 1-2)
The Orb feedback loop intersects the BicD–Egl–dynein RNA-transport system. Without normal Orb regulation, progressive restriction of BicD, Egl, dynein, osk, and other oocyte markers fails. For example, BicD is unlocalized or retained in two cells in about 60% of stage-1 mutant chambers; Egl remains abnormal in more than 80% of late region-2b cysts and 95% of stage-1 chambers. These effects support reciprocal coupling between Orb-dependent translation and polarized RNA/protein transport, although not every affected component is necessarily a direct Orb target. (barr2019thedrosophilacpeb pages 13-14, barr2019thedrosophilacpeb pages 4-5)
Around stage 7, the posterior microtubule-organizing center is dismantled and a centrosome-independent network is established along the anterior and lateral cortex. Orb functions upstream of or in feedback with this transition. Reduced Orb activity mislocalizes posterior Par-1 and anterior/anterior-lateral aPKC, disrupts cortical actin, and prevents proper cortical localization of the spectraplakin Shot and microtubule minus-end factor Patronin. These defects compromise microtubule repolarization and consequently the localization of axis-determining RNAs. (barr2019thecpebtranslational pages 1-2, barr2019thecpebtranslational pages 18-19)
Genetic interactions are strong. Approximately 5% of eggs from orb^343/+ females are ventralized; combining the sensitized orb background with an aPKC allele increases this to nearly 50%, and combining it with cdc42 raises it to approximately 70%. aPKC and cdc42 single heterozygotes do not produce the phenotype, whereas the aPKC/cdc42 double heterozygote yields nearly 40% ventralized eggs. These nonadditive effects place Orb functionally within the Par–Cdc42 polarity network. (barr2019thecpebtranslational pages 18-19)
Primary source: Barr J et al. “The CPEB translational regulator, Orb, functions together with Par proteins to polarize the Drosophila oocyte.” PLOS Genetics 15:e1008012, published March 2019. DOI/URL: https://doi.org/10.1371/journal.pgen.1008012. (barr2019thecpebtranslational pages 18-19, barr2019thecpebtranslational pages 1-2)
aPKC mRNA is the best-supported polarity-pathway target: it contains candidate CPEs, binds Orb in ovarian extracts, and changes distribution when Orb is compromised. Its protein is also mislocalized, and orb genetically interacts with aPKC. Nevertheless, Orb-dependent aPKC poly(A)-tail extension and transcript-specific translational output are less completely demonstrated than for osk and grk. (barr2019thecpebtranslational pages 18-19)
Other CPE-containing transcripts—cdc42, baz, par-6, capu, spir, Cip4, WASp, shot, and patronin—associated with ectopically expressed Orb in cultured cells. They are plausible direct links between Orb and cortical polarity, actin assembly, or microtubule organization, but they remain candidate targets pending endogenous ovarian binding, Orb-dependent poly(A)-tail measurements, target-specific translation assays, and rescue experiments. (barr2019thecpebtranslational pages 18-19)
The classic orb phenotype is female sterility accompanied by failures in germline-cyst development, oocyte selection/maintenance, cytoskeletal polarization, localized determinant translation, and embryonic axis patterning. Classic genetic work identified requirements for both anterior-posterior and dorsoventral patterning. (barr2019thecpebtranslational pages 25-26)
These broad phenotypes should not obscure the more precise molecular hierarchy:
Thus, the developmental abnormalities are mechanistically coherent consequences of disrupted spatial translational control rather than evidence that Orb is itself a structural cytoskeletal component or signaling ligand.
A targeted search of 2023–2024 literature did not recover a major new Orb-specific mechanistic primary study comparable to the 1999, 2015, or 2019 papers. Recent work primarily places Orb’s established mechanism into broader analyses of oogenesis, RNA localization, meiosis, or Gurken evolution. A 2023 synthesis reiterates the current model in which phosphorylated Orb acts with Wispy to polyadenylate localized grk and activate translation. (sottolano2023anevolutionarystudy pages 30-34)
The principal 2023 source retrieved was Christopher J. Sottolano, “An evolutionary study of gurken and its effects on axis formation in Drosophila,” published January 2023, DOI/URL: https://doi.org/10.7282/t3-fftx-nn74. It is useful as a recent synthesis but is not a substitute for the underlying primary Orb–Wispy experiments. (sottolano2023anevolutionarystudy pages 30-34, sottolano2023anevolutionarystudy pages 133-136)
Accordingly, the current understanding remains anchored in well-supported foundational and 2015–2019 mechanistic work, rather than having been materially revised in 2023–2024. This is itself informative: no credible recent evidence was found that changes Orb’s primary annotation as a germline CPEB translational regulator.
Orb is chiefly a basic-research model, not a current therapeutic or industrial target. Its practical applications include:
These applications are supported by precise genetic tools: 3′UTR deletion and replacement alleles, sensitized orb hypomorphs, localization reporters, transgenic rescue, RNA–protein association assays, and quantitative egg-patterning phenotypes. (barr2019thecpebtranslational pages 18-19, barr2019thedrosophilacpeb pages 4-5, barr2019thedrosophilacpeb pages 1-2)
Molecular function: cytoplasmic polyadenylation-element/3′UTR RNA binding; translational regulation; recruitment or coordination of cytoplasmic polyadenylation machinery.
Primary biological role: spatial activation of maternal-mRNA translation and maintenance of oocyte identity.
Best-validated substrates/targets: oskar, gurken, and orb mRNAs. aPKC is a likely additional direct regulatory target; other Par, actin, and microtubule transcripts remain provisional.
Cellular location: cytoplasmic RNPs in the female germline, enriched first in pro-oocytes and the selected oocyte and later at developmentally regulated cortical RNA domains.
Principal pathways: Orb autoregulatory oocyte-fate circuit; BicD–Egl–dynein polarized transport; Par/aPKC/Cdc42–actin–Shot/Patronin microtubule polarity; Oskar-dependent posterior/germ-plasm specification; Gurken–EGFR dorsoventral signaling.
Evidence confidence: high for identity, CPEB/RRM classification, osk binding and translational activation, grk–Wispy cooperation, autoregulation, and oocyte-fate requirement; moderate for aPKC as a direct transcript-level target; provisional for the wider proposed polarity/cytoskeletal target set.
References
(lipshitz2000mechanismsofrna pages 12-13): Howard D Lipshitz and Craig A Smibert. Mechanisms of rna localization and translational regulation. Current opinion in genetics & development, 10 5:476-88, Oct 2000. URL: https://doi.org/10.1016/s0959-437x(00)00116-7, doi:10.1016/s0959-437x(00)00116-7. This article has 255 citations and is from a peer-reviewed journal.
(barr2019thecpebtranslational pages 2-4): Justinn Barr, Sofia Charania, Rudolf Gilmutdinov, Konstantin Yakovlev, Yulii Shidlovskii, and Paul Schedl. The cpeb translational regulator, orb, functions together with par proteins to polarize the drosophila oocyte. Mar 2019. URL: https://doi.org/10.1371/journal.pgen.1008012, doi:10.1371/journal.pgen.1008012. This article has 14 citations and is from a domain leading peer-reviewed journal.
(chang1999thedrosophilacpeb pages 1-2): Jacqueline S. Chang, Lihua Tan, and Paul Schedl. The drosophila cpeb homolog, orb, is required for oskar protein expression in oocytes. Developmental biology, 215 1:91-106, Nov 1999. URL: https://doi.org/10.1006/dbio.1999.9444, doi:10.1006/dbio.1999.9444. This article has 167 citations and is from a peer-reviewed journal.
(sottolano2023anevolutionarystudy pages 30-34): Christopher James Sottolano. An evolutionary study of gurken and its effects on axis formation in drosophila. Text, Jan 2023. URL: https://doi.org/10.7282/t3-fftx-nn74, doi:10.7282/t3-fftx-nn74. This article has 0 citations and is from a peer-reviewed journal.
(barr2019thedrosophilacpeb pages 1-2): Justinn Barr, Rudolf Gilmutdinov, Linus Wang, Yulii Shidlovskii, and Paul Schedl. The drosophila cpeb protein orb specifies oocyte fate by a 3′utr-dependent autoregulatory loop. Dec 2019. URL: https://doi.org/10.1534/genetics.119.302687, doi:10.1534/genetics.119.302687. This article has 43 citations and is from a domain leading peer-reviewed journal.
(barr2019thecpebtranslational pages 1-2): Justinn Barr, Sofia Charania, Rudolf Gilmutdinov, Konstantin Yakovlev, Yulii Shidlovskii, and Paul Schedl. The cpeb translational regulator, orb, functions together with par proteins to polarize the drosophila oocyte. Mar 2019. URL: https://doi.org/10.1371/journal.pgen.1008012, doi:10.1371/journal.pgen.1008012. This article has 14 citations and is from a domain leading peer-reviewed journal.
(lipshitz2000mechanismsofrna pages 7-8): Howard D Lipshitz and Craig A Smibert. Mechanisms of rna localization and translational regulation. Current opinion in genetics & development, 10 5:476-88, Oct 2000. URL: https://doi.org/10.1016/s0959-437x(00)00116-7, doi:10.1016/s0959-437x(00)00116-7. This article has 255 citations and is from a peer-reviewed journal.
(sottolano2023anevolutionarystudy pages 133-136): Christopher James Sottolano. An evolutionary study of gurken and its effects on axis formation in drosophila. Text, Jan 2023. URL: https://doi.org/10.7282/t3-fftx-nn74, doi:10.7282/t3-fftx-nn74. This article has 0 citations and is from a peer-reviewed journal.
(barr2019thecpebtranslational pages 25-26): Justinn Barr, Sofia Charania, Rudolf Gilmutdinov, Konstantin Yakovlev, Yulii Shidlovskii, and Paul Schedl. The cpeb translational regulator, orb, functions together with par proteins to polarize the drosophila oocyte. Mar 2019. URL: https://doi.org/10.1371/journal.pgen.1008012, doi:10.1371/journal.pgen.1008012. This article has 14 citations and is from a domain leading peer-reviewed journal.
(barr2019thedrosophilacpeb pages 13-14): Justinn Barr, Rudolf Gilmutdinov, Linus Wang, Yulii Shidlovskii, and Paul Schedl. The drosophila cpeb protein orb specifies oocyte fate by a 3′utr-dependent autoregulatory loop. Dec 2019. URL: https://doi.org/10.1534/genetics.119.302687, doi:10.1534/genetics.119.302687. This article has 43 citations and is from a domain leading peer-reviewed journal.
(barr2019thedrosophilacpeb pages 4-5): Justinn Barr, Rudolf Gilmutdinov, Linus Wang, Yulii Shidlovskii, and Paul Schedl. The drosophila cpeb protein orb specifies oocyte fate by a 3′utr-dependent autoregulatory loop. Dec 2019. URL: https://doi.org/10.1534/genetics.119.302687, doi:10.1534/genetics.119.302687. This article has 43 citations and is from a domain leading peer-reviewed journal.
(barr2019thecpebtranslational pages 18-19): Justinn Barr, Sofia Charania, Rudolf Gilmutdinov, Konstantin Yakovlev, Yulii Shidlovskii, and Paul Schedl. The cpeb translational regulator, orb, functions together with par proteins to polarize the drosophila oocyte. Mar 2019. URL: https://doi.org/10.1371/journal.pgen.1008012, doi:10.1371/journal.pgen.1008012. This article has 14 citations and is from a domain leading peer-reviewed journal.